Growth factor receptor-bound protein 2 (GRB2, also called ASH) is a ubiquitously expressed, non-catalytic 25 kDa adaptor built from an N-terminal SH3 domain, a central SH2 domain and a C-terminal SH3 domain. The SH2 domain binds phosphotyrosine in pY-x-N-x motifs on activated receptor tyrosine kinases (EGFR pY1068/pY1086, KIT, AXL, EPHB1) and on tyrosine-phosphorylated docking proteins and phosphatases (SHC1, IRS1, LAT, LAT2, LAX1, BLNK, SHP2/PTPN11, FAK, BCR), while the SH3 domains bind proline-rich motifs in effectors, most importantly the Ras guanine nucleotide exchange factors SOS1 and SOS2, and also GAB1/GAB2, CBL, dynamin, THEMIS and others. By bridging these two classes of partner, cytosolic GRB2 relocates SOS to the inner face of the plasma membrane when receptors are activated, coupling receptor tyrosine kinases and antigen/immune receptors to Ras activation and the RAF-MEK-ERK cascade. The same adaptor role links receptors to GAB-PI3K signalling, to CBL-mediated receptor ubiquitination and endocytosis, and to multivalent LAT signalling clusters in T cells. Smaller nuclear and endosomal pools of GRB2 have been reported. An alternatively spliced isoform with a truncated SH2 domain (GRB3-3) cannot bind phosphorylated EGFR and acts as a dominant negative. GRB2 can also homodimerize, and dimeric GRB2 bound to the FGFR2 C-terminus restrains basal receptor signalling.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001784 phosphotyrosine residue binding | IBA GO_REF:0000033 | ACCEPT | Summary: GRB2's central SH2 domain recognises phosphotyrosine motifs (pY-x-N-x) on activated receptor tyrosine kinases and phosphorylated docking proteins; this is the informative binding activity underlying its recruitment to activated receptors. Reason: Phylogenetic inference at PANTHER:PTN005273574 (GRB2 clade of PTHR46037); the WITH/FROM includes fly drk, rat Grb2 and human GRB2 itself, all with experimental SH2-phosphotyrosine binding. The function is ancestral to the SEM-5/DRK/GRB2 clade and is supported by abundant direct evidence for human GRB2 (e.g. EGFR pY1068, Shc pY317, IRS-1 pY895). Core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. PMID:7518560 Grb2 binds directly to the EGFR at Y-1068, to a lesser extent at Y-1086, and indirectly at Y-1173 |
| GO:0001784 phosphotyrosine residue binding | IPI PMID:20624904 Tarp regulates early Chlamydia-induced host cell survival th... | ACCEPT | Summary: Human SH2/PTB-domain microarray profiling against tyrosine-phosphorylated peptides of the Chlamydia trachomatis effector Tarp (WITH/FROM Q6GX35) identified GRB2 SH2 among the binders. Reason: Quantitative SH2-domain binding to Tarp phosphopeptides is direct evidence of GRB2 phosphotyrosine residue binding; the partner being a bacterial effector does not change the activity asserted. Consistent with the core SH2 function. Supporting Evidence: PMID:20624904 We discovered numerous novel interactions between human SH2 domains and phosphopeptides derived from Tarp file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | MARK AS OVER ANNOTATED | Summary: GRB2 was recovered in a proteome-wide mRNA interactome capture screen (HDA). Reason: GRB2 has no RNA-binding domain; it is an SH3-SH2-SH3 protein adaptor, and its reported role in miRNA biogenesis is via protein-protein binding to AGO2 (PMID:37328606), not RNA binding. Recovery in a high-throughput UV-crosslink capture screen is not sufficient to establish RNA binding as a GRB2 function; kept as over-annotation rather than removed because it is experimental HDA evidence. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 does not itself exchange the nucleotide or phosphorylate a substrate PMID:37328606 The N-terminal SH3 domain of GRB2 is recruited to the PAZ domain of AGO2 forming a ternary complex containing GRB2, AGO2 and DICER1 |
| GO:0005068 transmembrane receptor protein tyrosine kinase adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer from mouse Grb2 of transmembrane receptor protein tyrosine kinase adaptor activity. Reason: This is the best summary MF for GRB2: it binds activated RTKs (EGFR, Kit, Axl, EphB1, FGFR2) through its SH2 domain and links them to SOS, Gab, Cbl, PI3K-C2beta and HPK1 through its SH3 domains. Directly supported for human GRB2 by several small-scale studies reviewed here. Core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. PMID:11533253 Using immobilized, phosphorylated EGF receptor, recombinant PI3K-C2beta was only purified in the presence of Grb2 |
| GO:0005091 guanyl-nucleotide exchange factor adaptor activity | IDA PMID:8386805 Grb2 mediates the EGF-dependent activation of guanine nucleo... | ACCEPT | Summary: Classic study showing GRB2 overexpression potentiates EGF-induced Ras activation by enhancing guanine nucleotide exchange, via a GRB2-exchange factor complex that binds the activated EGFR. Reason: Direct evidence that GRB2 couples a Ras GEF (SOS) to the activated receptor; the canonical GRB2 function. Core. Supporting Evidence: PMID:8386805 Cellular Grb2 appears to form a complex with a guanine-nucleotide-exchange factor for Ras, which binds to the ligand-activated EGF receptor, allowing the tyrosine kinase to modulate Ras activity file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005091 guanyl-nucleotide exchange factor adaptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated annotation (ARBA/ortholog) of guanyl-nucleotide exchange factor adaptor activity. Reason: Consistent with direct human evidence (PMID:8386805) and the conserved GRB2-SOS mechanism. Core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. file:human/GRB2/GRB2-uniprot.txt GRB2 establishes a a connection with SOS1 that acts as a guanine nucleotide exchange factor and serves as a critical regulator of KRAS/RAF1 |
| GO:0005154 epidermal growth factor receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: GRB2 SH2 binds the activated EGFR at pY1068/pY1086 (and indirectly via Shc at pY1173); the canonical recruitment event for EGFR-Ras signalling. Reason: Phylogenetic inference at PANTHER:PTN005273574 (GRB2 clade of PTHR46037) (seeds include fly drk, worm sem-5 with let-23/EGFR, rat and human GRB2). EGFR binding is conserved from SEM-5/LET-23 to human GRB2/EGFR and is directly shown for human GRB2. Core. Supporting Evidence: PMID:7518560 Grb2 binds directly to the EGFR at Y-1068, to a lesser extent at Y-1086, and indirectly at Y-1173 file:human/GRB2/GRB2-uniprot.txt Associates (via SH2 domain) with activated EGF and PDGF receptors (tyrosine phosphorylated) |
| GO:0005154 epidermal growth factor receptor binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | ACCEPT | Summary: SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells shows EGF-dependent, direct binding of EGFR to the SH2 bait. Reason: Direct, stimulation-dependent binding of EGFR to the GRB2 SH2 domain; supports EGFR binding as a core GRB2 activity (more specifically, SH2 phosphotyrosine binding). Supporting Evidence: PMID:12577067 EGFR and Shc, which interact directly with the bait, had large differential ratios file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005168 neurotrophin TRKA receptor binding | IPI PMID:15488758 TrkA alternative splicing: a regulated tumor-promoting switc... | KEEP AS NON CORE | Summary: IPI for GRB2 binding to TrkA (WITH/FROM P04629) from a study of the oncogenic TrkAIII splice variant in neuroblastoma. Reason: GRB2 is recruited to activated TrkA (directly and via Shc) as for other RTKs, so the annotation is plausible; the cached abstract concerns TrkAIII signalling and does not describe the GRB2 measurement, so the curator's full-text reading is deferred to. Partner-specific receptor binding is secondary to the general SH2 phosphotyrosine-binding/RTK adaptor function; kept as non-core. Supporting Evidence: PMID:15488758 resulting from spontaneous tyrosine kinase activity and IP3K/Akt/NF-kappaB but not Ras/MAPK signaling file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domai... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): study of the Nck-related adaptor Grb4/Nckbeta; the GRB2-EGFR association is not characterised as a GRB2 activity in the cached abstract. Reason: The cited study (study of the Nck-related adaptor Grb4/Nckbeta; the GRB2-EGFR association is not characterised as a GRB2 activity in the cached abstract) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:10026169 Both Nck and Grb4 proteins could associate with receptor tyrosine kinases and the SH3-binding proteins PAK, Sos1, and PRK2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:10206341 Characterization of interactions of Nck with Sos and dynamin... | REMOVE | Summary: GRB2 interaction with DNM1 (Q05193): study of Nck SH3 binding to Sos and dynamin; GRB2-dynamin binding is not characterised in the cached abstract. Reason: The cited study (study of Nck SH3 binding to Sos and dynamin; GRB2-dynamin binding is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward DNM1 beyond physical association. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:10206341 This protein was identified as dynamin, a GTP-binding protein that has been implicated in clathrin-coated vesicle formation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:10229072 Association of Nck with tyrosine-phosphorylated SLP-76 in ac... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): study of Nck binding to SLP-76; the GRB2-EGFR association is not characterised in the cached abstract. Reason: The cited study (study of Nck binding to SLP-76; the GRB2-EGFR association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:10229072 the interaction between Nck and SLP-76 is mediated via the Nck SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:10318918 NS5A, a nonstructural protein of hepatitis C virus, binds gr... | MODIFY | Summary: GRB2 interaction with HCV NS5A (genome polyprotein) (P26662-PRO_0000037647), Hepatitis C virus genotype 1b (isolate Japanese) protein: HCV NS5A binds the GRB2 SH3 domains through a conserved proline-rich motif and perturbs GRB2-mediated ERK activation. Reason: The study maps the GRB2-HCV NS5A (genome polyprotein) association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:10318918 mutational analysis of NS5A assigned the SH3-binding region to a proline-rich motif that is highly conserved among HCV genotypes file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:10356320 Solution structure of the SH2 domain of Grb2 complexed with ... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): NMR structure of the GRB2 SH2 domain bound to a Shc-derived phosphotyrosine peptide. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10356320 The solution structure of growth factor receptor-bound protein 2 (Grb2) SH2 complexed with a Shc-derived phosphotyrosine (pTyr)-containing peptide was determined by nuclear magnetic resonance (NMR) spectroscopy file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10377264 Identification of Tyr-703 and Tyr-936 as the primary associa... | MODIFY | Summary: GRB2 interaction with KIT (P10721): GRB2 binds the c-Kit autophosphorylation sites pTyr-703 and pTyr-936 through its SH2 domain. Reason: The study shows that GRB2 binding to KIT depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10377264 the adapter protein Grb2 is a specific binding partner for both phosphorylated Tyr-703 and phosphorylated Tyr-936 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10660596 Tyrosine dephosphorylation and deactivation of insulin recep... | MODIFY | Summary: GRB2 interaction with PTPN1 (P18031): GRB2 SH2 binding to IRS-1 is lost as PTP1B dephosphorylates IRS-1; GRB2 also promotes a stable IRS-1/PTP1B complex. Reason: The study shows GRB2 bridging PTPN1 to another signalling protein (SH3-mediated partner binding combined with SH2-mediated recruitment to LAT), i.e. protein-macromolecule adaptor activity. For the PTP1B (PTPN1) partner the paper shows GRB2 promoting the formation of a stable complex between tyrosine-phosphorylated IRS-1 and PTP1B, i.e. a bridging (adaptor) activity rather than simple binding. Proposed replacements: protein-macromolecule adaptor activity Supporting Evidence: PMID:10660596 the adaptor protein GRB2 strongly promoted the formation of a stable protein complex between tyrosine-phosphorylated IRS-1 and catalytically inactive PTP1B file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:10660596 Tyrosine dephosphorylation and deactivation of insulin recep... | MODIFY | Summary: GRB2 interaction with Irs1 (P35570), Rattus norvegicus protein: GRB2 SH2 binding to IRS-1 is lost as PTP1B dephosphorylates IRS-1; GRB2 also promotes a stable IRS-1/PTP1B complex. Reason: The study shows that GRB2 binding to Irs1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10660596 Overlay blots with recombinant Src homology 2 domains of IRS-1 adaptor proteins showed that the loss of IRS-1 binding of Crk, GRB2, SHP-2, and the p85 subunit of phosphatidylinositol 3'-kinase paralleled the rate of overall IRS-1 dephosphorylation file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10660620 PILRalpha, a novel immunoreceptor tyrosine-based inhibitory ... | REMOVE | Summary: GRB2 interaction with PTPN6 (P29350): identification of PILRalpha as an SHP-1 ligand; the GRB2-SHP-1 association is not characterised in the cached abstract. Reason: The cited study (identification of PILRalpha as an SHP-1 ligand; the GRB2-SHP-1 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward PTPN6 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:10660620 PILRalpha associates with SHP-1 in vivo upon tyrosine phosphorylation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:10811803 Association of Grb2, Gads, and phospholipase C-gamma 1 with ... | MODIFY | Summary: GRB2 interaction with LAT (O43561): GRB2 binds the phosphorylated distal tyrosines of LAT via its SH2 domain. Reason: The study shows that GRB2 binding to LAT depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10811803 three distal tyrosines, Tyr(171), Tyr(191), and Tyr(226), are responsible for Grb2-binding file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10887132 The Grb2 binding site is required for the induction of chron... | MODIFY | Summary: GRB2 interaction with BCR (P11274): GRB2 SH2 binding to BCR-ABL pTyr177 is required for efficient CML-like disease. Reason: The study shows that GRB2 binding to BCR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10887132 activation of Ras through direct binding of the SH2-containing adapter protein Grb2 to Bcr tyrosine 177 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:10980613 Generation of novel cytoplasmic forms of protein tyrosine ph... | REMOVE | Summary: GRB2 interaction with PTPRE (P23469): characterisation of cytoplasmic PTPepsilon isoforms; the abstract reports GRB2 association only for phosphorylatable full-length forms without mapping the binding mode. Reason: The cited study (characterisation of cytoplasmic PTPepsilon isoforms; the abstract reports GRB2 association only for phosphorylatable full-length forms without mapping the binding mode) does not establish a specific GRB2 molecular activity toward PTPRE beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:10980613 p67 and p65 are exclusively cytoplasmic, are not phosphorylated by Neu, and do not associate with Grb2 in unstimulated cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:11278465 The tyrosine kinase Hck is an inhibitor of HIV-1 replication... | REMOVE | Summary: GRB2 interaction with KHDRBS1 (Q07666): study of HIV-1 Vif binding to Hck; the GRB2-Sam68 association is not characterised in the cached abstract. Reason: The cited study (study of HIV-1 Vif binding to Hck; the GRB2-Sam68 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward KHDRBS1 beyond physical association. KHDRBS1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:11278465 Using a glutathione S-transferase pull-down assay, we identified that Vif binds specifically to the Src homology 3 domain of Hck file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:11432792 Analysis of tyrosine phosphorylation-dependent protein-prote... | MODIFY | Summary: GRB2 interaction with Ptpn11 (P35235), Mus musculus protein: yeast two-and-a-half-hybrid shows SHP2-GRB2 binding dependent on TrkB-mediated tyrosine phosphorylation. Reason: The study shows that GRB2 binding to Ptpn11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:11432792 Shp2 interacts directly with BIT/SHPS-1 (also called SIRP) and Grb2 depending on tyrosine phosphorylation mediated by TrkB file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:11533253 Recruitment of the class II phosphoinositide 3-kinase C2beta... | MODIFY | Summary: GRB2 interaction with PIK3C2B (O00750): GRB2 SH3 domains bind PI3K-C2beta proline-rich motifs and bridge the lipid kinase to the activated EGF receptor. Reason: The study shows GRB2 physically linking PIK3C2B to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:11533253 Using immobilized, phosphorylated EGF receptor, recombinant PI3K-C2beta was only purified in the presence of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:11684012 Site-specific incorporation of a phosphotyrosine mimetic rev... | MODIFY | Summary: GRB2 interaction with Ptpn11 (P35235), Mus musculus protein: semisynthetic SHP2 carrying non-hydrolysable phosphotyrosine mimetics at its C-terminal tail tyrosines (Tyr542/Tyr580), the known GRB2 SH2 docking sites of SHP2; the cached abstract does not itself describe the GRB2 measurement, so this rests partly on the partner site. Reason: The study shows that GRB2 binding to Ptpn11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:11684012 a phosphonate at Tyr542 interacts intramolecularly with the N-terminal SH2 domain to relieve basal inhibition of the PTPase file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:11741929 Phosphorylation-dependent interactions between ADAM15 cytopl... | MODIFY | Summary: GRB2 interaction with ADAM15 (Q13444): ADAM15 cytoplasmic proline-rich motifs mediate GRB2 binding, enhanced by ADAM15 tyrosine phosphorylation. Reason: The study maps the GRB2-ADAM15 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:11741929 confirmed the importance of the proline-rich motifs for Grb2 and Lck binding file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:11827484 Crystal structures of the SH2 domain of Grb2: highlight on t... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): crystal structures of the GRB2 SH2 domain with Shc-derived pYVNV peptides. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:11827484 we have solved the crystal structure of complexes between the Grb2-SH2 domain and peptides corresponding to Shc-derived sequences file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:11882361 The lymphoid protein tyrosine phosphatase Lyp interacts with... | REMOVE | Summary: GRB2 interaction with PTPN22 (Q9Y2R2): GRB2 N-SH3 binds the phosphatase Lyp (PTPN22); the Lyp binding motif is not mapped in the abstract and no GRB2 activity beyond association is shown. Reason: The cited study (GRB2 N-SH3 binds the phosphatase Lyp (PTPN22); the Lyp binding motif is not mapped in the abstract and no GRB2 activity beyond association is shown) does not establish a specific GRB2 molecular activity toward PTPN22 beyond physical association. PTPN22 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:11882361 the N-terminal SH3-containing fusion bound to the protein tyrosine phosphatase Lyp file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): engineered Tpr-Met variants carrying RTK-derived phosphotyrosine docking sites that recruit GRB2 are sufficient for transformation and metastasis. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:11896612 We have generated variant forms of the Tpr-Met oncoprotein with the ability to bind individually to the p85 subunit of PI3'K, PLCgamma, or to the Grb2 or Shc adaptor proteins file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:11923305 Mitotic activation of protein-tyrosine phosphatase alpha and... | MODIFY | Summary: GRB2 interaction with PTPRA (P18433): PTPalpha pTyr789 is bound by the GRB2 SH2 domain, and serine phosphorylation modulates this affinity. Reason: The study shows that GRB2 binding to PTPRA depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:11923305 modulation of the affinity of Tyr(P)789 for the Src and Grb2 SH2 domains file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:12091307 unc-53 controls longitudinal migration in C. elegans. | REMOVE | Summary: GRB2 interaction with unc-53 (C8JQR2), Caenorhabditis elegans protein: C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity. Reason: The cited study (C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity) does not establish a specific GRB2 molecular activity toward unc-53 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12091307 we demonstrated a direct interaction in vitro between UNC-53 and the SH2-SH3 adaptor protein SEM-5/GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12091307 unc-53 controls longitudinal migration in C. elegans. | REMOVE | Summary: GRB2 interaction with unc-53 (G5EBX1), Caenorhabditis elegans protein: C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity. Reason: The cited study (C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity) does not establish a specific GRB2 molecular activity toward unc-53 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12091307 we demonstrated a direct interaction in vitro between UNC-53 and the SH2-SH3 adaptor protein SEM-5/GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12091307 unc-53 controls longitudinal migration in C. elegans. | REMOVE | Summary: GRB2 interaction with unc-53 (G5EEU6), Caenorhabditis elegans protein: C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity. Reason: The cited study (C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity) does not establish a specific GRB2 molecular activity toward unc-53 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12091307 we demonstrated a direct interaction in vitro between UNC-53 and the SH2-SH3 adaptor protein SEM-5/GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12091307 unc-53 controls longitudinal migration in C. elegans. | REMOVE | Summary: GRB2 interaction with unc-53 (Q7YSI9), Caenorhabditis elegans protein: C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity. Reason: The cited study (C. elegans UNC-53 binds SEM-5/GRB2 in vitro; a cross-species association without a characterised GRB2 activity) does not establish a specific GRB2 molecular activity toward unc-53 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12091307 we demonstrated a direct interaction in vitro between UNC-53 and the SH2-SH3 adaptor protein SEM-5/GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12213123 Novel peptide inhibitors for Grb2 SH2 domain and their detec... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): SPR study of peptide inhibitors of the GRB2 SH2 domain, benchmarked against pTyr-motif (Shc-type) ligands. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:12213123 binding of the Grb2 SH2 domain to the phosphotyrosine (pTyr) motifs on growth factor receptors file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:12359715 Molecular cloning of a novel gene encoding a membrane-associ... | MODIFY | Summary: GRB2 interaction with LAX1 (Q8IWV1): the transmembrane adaptor LAX is tyrosine phosphorylated on receptor stimulation and then binds GRB2 through its tyrosine motifs. Reason: The study shows that GRB2 binding to LAX1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:12359715 like LAT, LAX has tyrosine motifs for binding Grb2, Gads, and the p85 subunit of phosphatidylinositol 3-kinase file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with PRMT5 (O14744): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward PRMT5 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with FLNB (O75369): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward FLNB beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. EGFR is one of the two proteins the authors state interact directly with the GRB2 SH2 bait in an EGF-dependent manner. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:12577067 EGFR and Shc, which interact directly with the bait, had large differential ratios file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with KRT8 (P05787): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward KRT8 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with HSPA5 (P11021): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward HSPA5 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with FLNA (P21333): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward FLNA beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Shc is one of the two proteins the authors state interact directly with the GRB2 SH2 bait in an EGF-dependent manner. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:12577067 EGFR and Shc, which interact directly with the bait, had large differential ratios file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with MYH9 (P35579): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward MYH9 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with HNRNPK (P61978): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward HNRNPK beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with PTPN11 (Q06124): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward PTPN11 beyond physical association. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with SOS1 (Q07889): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward SOS1 beyond physical association. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with PPP3CA (Q08209): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward PPP3CA beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with CBLB (Q13191): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward CBLB beyond physical association. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with DBN1 (Q16643): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward DBN1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: GRB2 interaction with VAV3 (Q9UKW4): SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes. Reason: The cited study (SILAC affinity purification over the GRB2 SH2 domain from EGF-stimulated cells; most retrieved proteins are indirect components of EGFR-Shc complexes) does not establish a specific GRB2 molecular activity toward VAV3 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:12577067 Many signaling molecules specifically formed complexes with the activated EGFR-Shc file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:12852788 Adaptor signalling proteins Grb2 and Grb7 are recruited by h... | MODIFY | Summary: GRB2 interaction with LY6G6F (Q5SQ64): GRB2 SH2 binds phosphorylated Tyr281 (YXN motif) of G6f (LY6G6F). Reason: The study shows that GRB2 binding to LY6G6F depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:12852788 the interaction of G6f with both Grb2 and Grb7 is mediated through the Src homology 2 domains of these two proteins and is dependent on the phosphorylation of G6f file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:14679214 A novel proteomic screen for peptide-protein interactions. | MODIFY | Summary: GRB2 interaction with EGFR (P00533): SILAC peptide pull-downs: an EGFR phosphopeptide retrieves GRB2 and a Sos proline-rich peptide also binds GRB2. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:14679214 A tyrosine-phosphorylated peptide of the epidermal growth factor receptor specifically retrieved the Src homology domain (SH) 2- and SH3 domain-containing adapter protein Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:14679214 A novel proteomic screen for peptide-protein interactions. | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): SILAC peptide pull-downs: an EGFR phosphopeptide retrieves GRB2 and a Sos proline-rich peptide also binds GRB2. Reason: The study maps the GRB2-SOS1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. For the SOS partners the bait is a Sos proline-rich peptide, so the informative GRB2 activity is recognition of a proline-rich region by its SH3 domains. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:14679214 A proline-rich sequence of Son of Sevenless also specifically bound Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:14679214 A novel proteomic screen for peptide-protein interactions. | MODIFY | Summary: GRB2 interaction with SOS2 (Q07890): SILAC peptide pull-downs: an EGFR phosphopeptide retrieves GRB2 and a Sos proline-rich peptide also binds GRB2. Reason: The study maps the GRB2-SOS2 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. For the SOS partners the bait is a Sos proline-rich peptide, so the informative GRB2 activity is recognition of a proline-rich region by its SH3 domains. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:14679214 A proline-rich sequence of Son of Sevenless also specifically bound Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:14722116 The importance of three membrane-distal tyrosines in the ada... | MODIFY | Summary: GRB2 interaction with LAT2 (Q9GZY6): GRB2 binds three phosphorylated membrane-distal tyrosines of NTAL/LAB (LAT2). Reason: The study shows that GRB2 binding to LAT2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:14722116 Mutation of these three tyrosines abolished Grb2 binding and LAB function file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:14993658 The hepatitis C virus NS5A protein binds to members of the S... | MODIFY | Summary: GRB2 interaction with HCV NS5A (genome polyprotein) (O92972), Hepatitis C virus genotype 1b (strain HC-J4) protein: HCV NS5A binds GRB2 through a polyproline motif also used for Src-family SH3 domains. Reason: The study maps the GRB2-HCV NS5A (genome polyprotein) association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:14993658 Mutational analysis confirmed that the polyproline motif responsible for binding to Grb2 also bound to the SH3 domains of Hck, Lck, Lyn and Fyn file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:14993658 The hepatitis C virus NS5A protein binds to members of the S... | MODIFY | Summary: GRB2 interaction with HCV NS5A (genome polyprotein) (P27958), Hepatitis C virus genotype 1a (isolate H77) protein: HCV NS5A binds GRB2 through a polyproline motif also used for Src-family SH3 domains. Reason: The study maps the GRB2-HCV NS5A (genome polyprotein) association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:14993658 Mutational analysis confirmed that the polyproline motif responsible for binding to Grb2 also bound to the SH3 domains of Hck, Lck, Lyn and Fyn file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:15467741 Magicin, a novel cytoskeletal protein associates with the NF... | REMOVE | Summary: GRB2 interaction with MED28 (Q9H204): magicin/MED28 associates with GRB2 and merlin; the binding mode is not mapped in the abstract. Reason: The cited study (magicin/MED28 associates with GRB2 and merlin; the binding mode is not mapped in the abstract) does not establish a specific GRB2 molecular activity toward MED28 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15467741 we demonstrate an interaction between Grb2 and magicin file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:15558030 Characterization of VIK-1: a new Vav-interacting Kruppel-lik... | REMOVE | Summary: GRB2 interaction with VAV1 (P15498): study of the Vav-1 partner VIK-1; the GRB2-Vav1 association is not characterised in the cached abstract. Reason: The cited study (study of the Vav-1 partner VIK-1; the GRB2-Vav1 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward VAV1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15558030 VIK-1 interacted both with Vav-1 and cyclin-dependent kinase 4 through two independent domains file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (phosphotyrosine proteomics of EGFR-overexpressing cells). Reason: Detected in a phosphotyrosine proteomics of EGFR-overexpressing cells; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15657067 The functional interactions between IGF-1 receptor, lysophosphatidic acid (LPA) signaling, and EGF receptor were observed file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:15784897 Further studies on hepatitis C virus NS5A-SH3 domain interac... | REMOVE | Summary: GRB2 interaction with HCV NS5A (genome polyprotein) (O92972), Hepatitis C virus genotype 1b (strain HC-J4) protein: further mapping of HCV NS5A polyproline (PP2.2) motif-SH3 interactions; the cached abstract section does not describe the GRB2 measurement specifically. Reason: The cited study (further mapping of HCV NS5A polyproline (PP2.2) motif-SH3 interactions; the cached abstract section does not describe the GRB2 measurement specifically) does not establish a specific GRB2 molecular activity toward HCV NS5A (genome polyprotein) beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15784897 The highly conserved nature of the PP2.2 motif within NS5A suggests that functions involving this motif are of importance file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:15784897 Further studies on hepatitis C virus NS5A-SH3 domain interac... | REMOVE | Summary: GRB2 interaction with HCV NS5A (genome polyprotein) (P27958), Hepatitis C virus genotype 1a (isolate H77) protein: further mapping of HCV NS5A polyproline (PP2.2) motif-SH3 interactions; the cached abstract section does not describe the GRB2 measurement specifically. Reason: The cited study (further mapping of HCV NS5A polyproline (PP2.2) motif-SH3 interactions; the cached abstract section does not describe the GRB2 measurement specifically) does not establish a specific GRB2 molecular activity toward HCV NS5A (genome polyprotein) beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15784897 The highly conserved nature of the PP2.2 motif within NS5A suggests that functions involving this motif are of importance file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:15929943 Novel Src homology 3 domain-binding motifs identified from p... | REMOVE | Summary: GRB2 interaction with LCP2 (Q13094): SLP-76 binds the GRB2 C-SH3 domain through non-conventional (including non-PXXP) peptides. Reason: The cited study (SLP-76 binds the GRB2 C-SH3 domain through non-conventional (including non-PXXP) peptides) does not establish a specific GRB2 molecular activity toward LCP2 beyond physical association. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:15929943 mutation of critical residues for the three sites not only affected binding of SLP-76 to the PLC-gamma1 SH3 domain but also to the Grb2 C-terminal SH3 domain file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16253990 Increased proliferation and altered growth factor dependence... | REMOVE | Summary: GRB2 interaction with GAB2 (Q9UQC2): Gab2 overexpression in mammary epithelial cells; the Gab2-GRB2 binding is required for the phenotype but no distinct GRB2 activity is characterised. Reason: The cited study (Gab2 overexpression in mammary epithelial cells; the Gab2-GRB2 binding is required for the phenotype but no distinct GRB2 activity is characterised) does not establish a specific GRB2 molecular activity toward GAB2 beyond physical association. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16253990 an effect dependent on Gab2 binding to Grb2 and Shp2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): quantitative SH2/PTB-domain microarray measurement of affinities for ErbB receptor phosphotyrosine peptides. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:16273093 we use protein microarrays comprising virtually every Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded in the human genome to measure the equilibrium dissociation constant of each domain for 61 peptides representing physiological sites of tyrosine phosphorylation on the four ErbB receptors file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: GRB2 interaction with ERBB2 (P04626): quantitative SH2/PTB-domain microarray measurement of affinities for ErbB receptor phosphotyrosine peptides. Reason: The study shows that GRB2 binding to ERBB2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:16273093 we use protein microarrays comprising virtually every Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded in the human genome to measure the equilibrium dissociation constant of each domain for 61 peptides representing physiological sites of tyrosine phosphorylation on the four ErbB receptors file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:16374509 Identification of preferred protein interactions by phage-di... | REMOVE | Summary: GRB2 interaction with PAK2 (Q13177): phage display of the human SH3 proteome against PAK2 and ADAM15 ligands; a screening study. Reason: The cited study (phage display of the human SH3 proteome against PAK2 and ADAM15 ligands; a screening study) does not establish a specific GRB2 molecular activity toward PAK2 beyond physical association. PAK2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16374509 We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16374509 Identification of preferred protein interactions by phage-di... | REMOVE | Summary: GRB2 interaction with ADAM15 (Q13444): phage display of the human SH3 proteome against PAK2 and ADAM15 ligands; a screening study. Reason: The cited study (phage display of the human SH3 proteome against PAK2 and ADAM15 ligands; a screening study) does not establish a specific GRB2 molecular activity toward ADAM15 beyond physical association. ADAM15 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16374509 We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16407827 The elucidation of novel SH2 binding sites on PLD2. | MODIFY | Summary: GRB2 interaction with PLD2 (O14939): GRB2 binds PLD2 phosphotyrosines Y169/Y179 through its SH2 domain; these sites also recruit Sos. Reason: The study shows that GRB2 binding to PLD2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:16407827 Phenylalanine replacement of Y(169) (PLD2 Y169F) or Y(179) (PLD2 Y179F) reduced Grb2 binding while simultaneous mutation completely abolished it file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:16520382 Sos-mediated activation of rac1 by p66shc. | MODIFY | Summary: GRB2 interaction with SHC1 (P29353-1): the p66Shc CH2 PPLP motif binds the GRB2 C-SH3 domain and competes with the Sos1 proline-rich region, releasing Sos1 for Rac activation. Reason: The study maps the GRB2-SHC1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:16520382 A proline-rich motif (PPLP) in the CH2 domain mediates this association file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:16520382 Sos-mediated activation of rac1 by p66shc. | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): the p66Shc CH2 PPLP motif binds the GRB2 C-SH3 domain and competes with the Sos1 proline-rich region, releasing Sos1 for Rac activation. Reason: The study maps the GRB2-SOS1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:16520382 The CH2 domain competes with the proline-rich COOH-terminal region of sos1 for the C-SH3 domain of grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:16696976 Two mechanistically distinct forms of endocytosis in adrenal... | REMOVE | Summary: GRB2 interaction with DNM2 (P50570): GRB2 N-SH3 was inactive on dynamin-dependent endocytosis in chromaffin cells, so the paper argues against a functional role for this interaction. Reason: The cited study (GRB2 N-SH3 was inactive on dynamin-dependent endocytosis in chromaffin cells, so the paper argues against a functional role for this interaction) does not establish a specific GRB2 molecular activity toward DNM2 beyond physical association. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16696976 Grb2-SH3 (N-terminal) or a mutant of amphiphysin-1-SH3 was inactive on either process file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16730941 A systematic analysis of human CHMP protein interactions: ad... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (systematic yeast two-hybrid analysis of human CHMP protein interactions). Reason: Detected in a systematic yeast two-hybrid analysis of human CHMP protein interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16730941 Our results describe novel interactions between known components of the human ESCRT III complex and identify a range of putative binding partners file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (proteomic profiling of EGFR post-translational modifications and interaction partners). Reason: Detected in a proteomic profiling of EGFR post-translational modifications and interaction partners; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16799092 Finally potential binding partners to EGFR were identified based on changes in the amount of protein pulled down with EGFR as a function of time of stimulation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16893902 A Src homology 3-binding sequence on the C terminus of Sprou... | MODIFY | Summary: GRB2 interaction with SPRY2 (O43597): the Spry2 C-terminal PXXPXR motif binds the GRB2 N-SH3 domain and competes with SOS1. Reason: The study maps the GRB2-SPRY2 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:16893902 This PXXPXR motif binds directly to the N-terminal Src homology domain 3 of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:16899217 Magicin associates with the Src-family kinases and is phosph... | MODIFY | Summary: GRB2 interaction with MED28 (Q9H204): Lck phosphorylation of magicin/MED28 Tyr64 creates a GRB2 SH2 binding motif. Reason: The study shows that GRB2 binding to MED28 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:16899217 Y64 of magicin is phosphorylated by Lck creating a SH2-Grb2 binding motif file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:16912232 Human SLP-65 isoforms contribute differently to activation a... | REMOVE | Summary: GRB2 interaction with BLNK (Q8WV28): an atypical SH3-binding motif of long-isoform SLP-65/BLNK mediates GRB2 association. Reason: The cited study (an atypical SH3-binding motif of long-isoform SLP-65/BLNK mediates GRB2 association) does not establish a specific GRB2 molecular activity toward BLNK beyond physical association. BLNK is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:16912232 an atypical SH3 domain-binding motif, which is present in the long but not in the short SLP-65 isoform, mediates association to Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:16938345 Evidence of LAT as a dual substrate for Lck and Syk in T lym... | MODIFY | Summary: GRB2 interaction with LAT (O43561): LAT Y171/Y191 phosphorylation by Lck and Syk is required for GRB2 recruitment. Reason: The study shows that GRB2 binding to LAT depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:16938345 Both Lck and Syk, phosphorylate the ITAM-like motifs on LAT at Y171Y191, which is essential for induction of the interaction of LAT with downstream signaling molecules such as Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:17094785 Identification and functional characterization of an Src hom... | REMOVE | Summary: GRB2 interaction with CBL (P22681): mapping of the Src SH3-binding site on Cbl; the GRB2-Cbl association is not characterised in the cached abstract. Reason: The cited study (mapping of the Src SH3-binding site on Cbl; the GRB2-Cbl association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward CBL beyond physical association. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17094785 These data indicate that the Cbl RDLPPPP(540-546) sequence is a functionally important binding site for Src file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17235283 Efficient T-cell receptor signaling requires a high-affinity... | REMOVE | Summary: GRB2 interaction with LCP2 (Q13094): affinity and specificity of the Gads C-SH3 for SLP-76; GRB2 appears only as a cross-reactivity comparator. Reason: The cited study (affinity and specificity of the Gads C-SH3 for SLP-76; GRB2 appears only as a cross-reactivity comparator) does not establish a specific GRB2 molecular activity toward LCP2 beyond physical association. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17235283 the Gads C-terminal SH3 domain binds a core RxxK sequence motif in the SLP-76 scaffold file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17276458 The Grb2/PLD2 interaction is essential for lipase activity, ... | MODIFY | Summary: GRB2 interaction with PLD2 (O14939): GRB2 SH2 binding to phospho-PLD2 is required for PLD2 activity and Golgi relocalization. Reason: The study shows that GRB2 binding to PLD2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:17276458 Grb2 serves to hijack PLD2 to the perinuclear Golgi region through its SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with PIK3C2B (O00750) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DLGAP1 (O14490) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DLGAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SYNJ2 (O15056) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SYNJ2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with FANCA (O15360) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with ASAP2 (O43150) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with BRD4 (O60885) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with FLNB (O75369) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DARS1 (P14868) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with FLNA (P21333) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with ABL2 (P42684) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with LEPR (P48357) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DAB2 (P98082) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with ANK2 (Q01484) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DNM1 (Q05193) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with PPP3CA (Q08209) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with MAP2K5 (Q13163) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with FLNC (Q14315) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with ACAP1 (Q15027) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with AGER (Q15109) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SF3B4 (Q15427) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with UGP2 (Q16851) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with MAP4K3 (Q8IVH8) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K3 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with NELFB (Q8WX92) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with MAP4K1 (Q92918) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with TNPO1 (Q92973) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SHANK3 (Q9BYB0) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHANK3 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DLGAP2 (Q9P1A6) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DLGAP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with TPX2 (Q9ULW0) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with SHANK2 (Q9UPX8) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHANK2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with PALM2AKAP2 (Q9Y2D5) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with DLGAP4 (Q9Y2H0) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DLGAP4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides). Reason: Detected in a peptide-array (PATS) screen of GRB2 and other SH3 domains against 1536 candidate ligand peptides; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17474147 A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:17974561 Tesk1 interacts with Spry2 to abrogate its inhibition of ERK... | REMOVE | Summary: GRB2 interaction with SPRY2 (O43597): Tesk1 blocks the Spry2-GRB2 interaction; no distinct GRB2 activity is characterised. Reason: The cited study (Tesk1 blocks the Spry2-GRB2 interaction; no distinct GRB2 activity is characterised) does not establish a specific GRB2 molecular activity toward SPRY2 beyond physical association. SPRY2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:17974561 Tesk1 nullifies the inhibitory effect of Spry2 by abrogating its interaction with the adaptor protein Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:18273061 Structural basis for a novel intrapeptidyl H-bond and revers... | REMOVE | Summary: GRB2 interaction with CBL (P22681): structures of the Cbl TKB domain; the GRB2-Cbl association is not characterised in the cached abstract. Reason: The cited study (structures of the Cbl TKB domain; the GRB2-Cbl association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward CBL beyond physical association. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:18273061 we compared crystal structures of the Cbl-TKB domain complexed with phosphorylated peptides file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:18624398 Protein interaction data set highlighted with human Ras-MAPK... | REMOVE | Summary: GRB2 association with PRKAB1 (Q9Y478) reported in a high-throughput study (yeast two-hybrid data set centred on Ras-MAPK/PI3K signalling proteins). Reason: Detected in a yeast two-hybrid data set centred on Ras-MAPK/PI3K signalling proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:18624398 This protein interaction network provides further insights into the molecular mechanism of Ras-MAPK/PI3K signaling pathways file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:18647389 The central proline rich region of POB1/REPS2 plays a regula... | MODIFY | Summary: GRB2 interaction with REPS2 (Q8NFH8): the POB1/REPS2 proline-rich domain carries a GRB2 SH3-binding motif involved in EGFR endocytosis. Reason: The study maps the GRB2-REPS2 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:18647389 we have identified two closely spaced binding motifs for 14-3-3 and for the SH3 of the proteins Amphiphysin II and Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:18654987 Identification of multi-SH3 domain-containing protein intera... | REMOVE | Summary: GRB2 association with VAV3 (Q9UKW4) reported in a high-throughput study (multi-SH3 domain protein interactome in pancreatic cancer cells). Reason: Detected in a multi-SH3 domain protein interactome in pancreatic cancer cells; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:18654987 Our results indicate that interactions mediated by multi-SH3 domain-containing proteins could lead to the formation of dynamic protein complexes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:18692475 A protein domain-based interactome network for C. elegans ea... | REMOVE | Summary: GRB2 association with VAV1 (P15498) reported in a high-throughput study (domain-based yeast two-hybrid interactome for C. elegans early embryogenesis). Reason: Detected in a domain-based yeast two-hybrid interactome for C. elegans early embryogenesis; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:18692475 Furthermore, our approach increased the sensitivity of the two-hybrid system, resulting in a more complete interactome network file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19172738 Phosphorylation-dependent binding of 14-3-3 terminates signa... | MODIFY | Summary: GRB2 interaction with GAB2 (Q9UQC2): GRB2 couples Gab2 to activated receptors; 14-3-3 binding to Gab2 terminates signalling by dissociating Gab2 from GRB2. Reason: The study shows GRB2 physically linking GAB2 to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:19172738 Gab2 signalling is promoted by its association with specific receptors through the adaptor Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:19323566 SH3 domains of Grb2 adaptor bind to PXpsiPXR motifs within t... | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): ITC analysis of GRB2 SH3 domain binding to the four PXpsiPXR sites of Sos1. Reason: The study maps the GRB2-SOS1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:19323566 the Grb2-Sos1 interaction is mediated through the combinatorial binding of nSH3 and cSH3 domains of Grb2 to various sites containing PXpsiPXR motifs within Sos1 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with PIK3R2 (O00459) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with DARS1 (P14868) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with PIK3R1 (P27986) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with PTPN11 (Q06124) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with LCP2 (Q13094) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with GAB1 (Q13480) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: GRB2 association with CD2AP (Q9Y5K6) reported in a high-throughput study (TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components). Reason: Detected in a TAP/AP-MS network around Bcr-Abl, with GRB2 as one of seven core components; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CD2AP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19380743 The resulting network revealed a high degree of interconnection of 7 "core" components around Bcr-Abl (Grb2, Shc1, Crk-I, c-Cbl, p85, Sts-1, and SHIP-2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19509291 GAREM, a novel adaptor protein for growth factor receptor-bo... | MODIFY | Summary: GRB2 interaction with GAREM1 (Q9H706): GAREM1 proline-rich motifs are recognized by both GRB2 SH3 domains (binding also requires GAREM tyrosine phosphorylation). Reason: The study maps the GRB2-GAREM1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:19509291 the proline-rich motifs of GAREM are recognized by the N- and C-terminal SH3 domains of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (AP-MS deubiquitinating-enzyme interaction landscape). Reason: Detected in a AP-MS deubiquitinating-enzyme interaction landscape; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19615732 This work provides the first glimpse into the Dub interaction landscape file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:19798056 Participation of Tom1L1 in EGF-stimulated endocytosis of EGF... | MODIFY | Summary: GRB2 interaction with TOM1L1 (O75674): GRB2 (with Shc) bridges tyrosine-phosphorylated Tom1L1 to the activated EGFR for endocytosis. Reason: The study shows GRB2 physically linking TOM1L1 to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:19798056 resulting in transient interaction of Tom1L1 with the activated EGFR bridged by Grb2 and Shc file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:19914172 KIF26A is an unconventional kinesin and regulates GDNF-Ret s... | REMOVE | Summary: GRB2 interaction with Kif26a (Q52KG5), Mus musculus protein: mouse KIF26A binds and inhibits GRB2; GRB2 is the target of the inhibition rather than contributing an activity. Reason: The cited study (mouse KIF26A binds and inhibits GRB2; GRB2 is the target of the inhibition rather than contributing an activity) does not establish a specific GRB2 molecular activity toward Kif26a beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:19914172 KIF26A suppressed GDNF-Ret signaling by direct binding and inhibition of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved. Reason: The cited study (co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20473329 We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: GRB2 interaction with PTK2 (Q05397): co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved. Reason: The cited study (co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved) does not establish a specific GRB2 molecular activity toward PTK2 beyond physical association. PTK2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20473329 We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: GRB2 interaction with PTPN11 (Q06124): co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved. Reason: The cited study (co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved) does not establish a specific GRB2 molecular activity toward PTPN11 beyond physical association. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20473329 We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: GRB2 interaction with SOS1 (Q07889): co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved. Reason: The cited study (co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved) does not establish a specific GRB2 molecular activity toward SOS1 beyond physical association. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20473329 We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: GRB2 interaction with GAB1 (Q13480): co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved. Reason: The cited study (co-immunoprecipitation of the EGFRvIII signalosome (EGFRvIII/SHP-2/Gab1/GRB2/Sos-1/FAK) modulated by SIRPalpha1; binary contacts are not resolved) does not establish a specific GRB2 molecular activity toward GAB1 beyond physical association. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20473329 We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20933011 FCRL6 receptor: expression and associated proteins. | MODIFY | Summary: GRB2 interaction with FCRL6 (Q6DN72): FCRL6 recruits GRB2 through its phosphorylated cytoplasmic tyrosines. Reason: The study shows that GRB2 binding to FCRL6 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:20933011 adaptor protein Grb2 through phosphorylated cytoplasmic tyrosines file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with PIK3R2 (O00459) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with DLGAP1 (O14490) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DLGAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with SYNJ2 (O15056) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SYNJ2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with ASAP2 (O43150) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with WIPF1 (O43516) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with KRT8 (P05787) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with HSPA5 (P11021) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with PIK3R1 (P27986) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with MYH9 (P35579) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with HNRNPK (P61978) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with DAB2 (P98082) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with KHDRBS1 (Q07666) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. KHDRBS1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with TNK2 (Q07912) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with LCP2 (Q13094) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with GAB1 (Q13480) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with MAP4K3 (Q8IVH8) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K3 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with PTPN23 (Q9H3S7) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN23 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with SH2D4A (Q9H788) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with VAV3 (Q9UKW4) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (yeast two-hybrid human MAP kinase pathway interactome). Reason: Detected in a yeast two-hybrid human MAP kinase pathway interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:20936779 This study makes available a large resource of MAPK interactions and clone libraries file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21179510 Histidine domain-protein tyrosine phosphatase interacts with... | MODIFY | Summary: GRB2 interaction with PTPN23 (Q9H3S7): HD-PTP (PTPN23) binds GRB2 through its central proline-rich domain. Reason: The study maps the GRB2-PTPN23 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:21179510 We also discovered that the central proline-rich and histidine-rich domain of HD-PTP is responsible for these interactions file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:21189249 T cell receptor (TCR)-induced tyrosine phosphorylation dynam... | REMOVE | Summary: GRB2 interaction with THEMIS (Q8N1K5): TCR phosphoproteomics; THEMIS association with LAT is presumed to be GRB2-mediated but not demonstrated here. Reason: The cited study (TCR phosphoproteomics; THEMIS association with LAT is presumed to be GRB2-mediated but not demonstrated here) does not establish a specific GRB2 molecular activity toward THEMIS beyond physical association. THEMIS is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21189249 THEMIS associates with LAT, presumably via the adapter growth factor receptor-bound protein 2 (Grb2) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): PI3K inhibition in HER2+ breast cancer increases adaptor binding to HER receptors; the GRB2 binding mode is not characterised. Reason: The cited study (PI3K inhibition in HER2+ breast cancer increases adaptor binding to HER receptors; the GRB2 binding mode is not characterised) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21278786 increased expression of HER3 and binding of adaptor molecules to HER2 and HER3 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: GRB2 interaction with ERBB2 (P04626): PI3K inhibition in HER2+ breast cancer increases adaptor binding to HER receptors; the GRB2 binding mode is not characterised. Reason: The cited study (PI3K inhibition in HER2+ breast cancer increases adaptor binding to HER receptors; the GRB2 binding mode is not characterised) does not establish a specific GRB2 molecular activity toward ERBB2 beyond physical association. ERBB2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21278786 increased expression of HER3 and binding of adaptor molecules to HER2 and HER3 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21278788 Translationally controlled tumor protein induces human breas... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): TCTP-induced EGFR transactivation; the GRB2-EGFR association is not characterised as a GRB2 activity in the cached abstract. Reason: The cited study (TCTP-induced EGFR transactivation; the GRB2-EGFR association is not characterised as a GRB2 activity in the cached abstract) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21278788 These findings suggest that TCTP induces tumorigenesis through distinct multicellular signaling pathways involving Src-dependent EGFR transactivation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with WASL (O00401): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward WASL beyond physical association. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3R2 (O00459): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3R2 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3C2B (O00750): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3C2B beyond physical association. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with ASAP2 (O43150): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward ASAP2 beyond physical association. ASAP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with WIPF1 (O43516): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward WIPF1 beyond physical association. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with STAMBP (O95630): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward STAMBP beyond physical association. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with BCR (P11274): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward BCR beyond physical association. BCR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PLCG1 (P19174): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PLCG1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with CBL (P22681): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward CBL beyond physical association. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3R1 (P27986): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3R1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3CA (P42336): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3CA beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with DNM2 (P50570): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward DNM2 beyond physical association. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with DNM1 (Q05193): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward DNM1 beyond physical association. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PTPN11 (Q06124): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PTPN11 beyond physical association. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with KHDRBS1 (Q07666): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward KHDRBS1 beyond physical association. KHDRBS1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with SOS1 (Q07889): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward SOS1 beyond physical association. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with SOS2 (Q07890): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward SOS2 beyond physical association. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with CBLB (Q13191): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward CBLB beyond physical association. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with AGER (Q15109): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward AGER beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3AP1 (Q6ZUJ8): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3AP1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with DOCK4 (Q8N1I0): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward DOCK4 beyond physical association. DOCK4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with WIPF2 (Q8TF74): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward WIPF2 beyond physical association. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with PIK3R3 (Q92569): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward PIK3R3 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with GAREM1 (Q9H706): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward GAREM1 beyond physical association. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with ERRFI1 (Q9UJM3): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward ERRFI1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with VAV3 (Q9UKW4): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward VAV3 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with ASAP1 (Q9ULH1): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward ASAP1 beyond physical association. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with GAB2 (Q9UQC2): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward GAB2 beyond physical association. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with GIT1 (Q9Y2X7): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward GIT1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with MAP4K5 (Q9Y4K4): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward MAP4K5 beyond physical association. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: GRB2 interaction with CD2AP (Q9Y5K6): AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract. Reason: The cited study (AP-SRM mass spectrometry of time-resolved GRB2 complexes after growth-factor stimulation (90 GRB2-associated proteins); direct versus indirect contacts and binding modes are not resolved for individual partners in the cached abstract) does not establish a specific GRB2 molecular activity toward CD2AP beyond physical association. CD2AP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21706016 which we used to comprehensively and quantitatively investigate changes in protein interactions with GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21725282 Activation of Src and transformation by an RPTPΞ± splice muta... | REMOVE | Summary: GRB2 interaction with PTPRT (O14522): an RPTPalpha splice mutant reduces endogenous RPTPalpha-GRB2 binding; the GOA WITH/FROM partner here is PTPRT (O14522), which the cached abstract does not mention. Reason: The cited study (an RPTPalpha splice mutant reduces endogenous RPTPalpha-GRB2 binding; the GOA WITH/FROM partner here is PTPRT (O14522), which the cached abstract does not mention) does not establish a specific GRB2 molecular activity toward PTPRT beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21725282 which decreased eRPTPΞ±-Grb2 binding and increased eRPTPΞ± dephosphorylation of Src file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21725358 The SRC-associated protein CUB Domain-Containing Protein-1 r... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): CDCP1/SFK signalling study; the GRB2-SHC1 association is not characterised in the cached abstract. Reason: The cited study (CDCP1/SFK signalling study; the GRB2-SHC1 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21725358 Here we show that increased SFK and CDCP1 tyrosine phosphorylation is, surprisingly, associated with a decrease in FAK phosphorylation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21822214 The B-cell antigen receptor signals through a preformed tran... | REMOVE | Summary: GRB2 interaction with BLNK (Q8WV28): mass-spectrometric SLP65/BLNK interactome. Reason: The cited study (mass-spectrometric SLP65/BLNK interactome) does not establish a specific GRB2 molecular activity toward BLNK beyond physical association. BLNK is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21822214 We have now determined and quantified the in vivo interactomes of SLP65 in resting and stimulated B cells by mass spectrometry file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: GRB2 association with PTK2 (Q05397) reported in a high-throughput study (directed yeast two-hybrid network of EGF/ERK signalling proteins). Reason: Detected in a directed yeast two-hybrid network of EGF/ERK signalling proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTK2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21900206 This generic experimental and computational approach provides a framework for elucidating causal connections between signaling proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: GRB2 association with PPP3CA (Q08209) reported in a high-throughput study (directed yeast two-hybrid network of EGF/ERK signalling proteins). Reason: Detected in a directed yeast two-hybrid network of EGF/ERK signalling proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21900206 This generic experimental and computational approach provides a framework for elucidating causal connections between signaling proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (directed yeast two-hybrid network of EGF/ERK signalling proteins). Reason: Detected in a directed yeast two-hybrid network of EGF/ERK signalling proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21900206 This generic experimental and computational approach provides a framework for elucidating causal connections between signaling proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: GRB2 association with GIT1 (Q9Y2X7) reported in a high-throughput study (directed yeast two-hybrid network of EGF/ERK signalling proteins). Reason: Detected in a directed yeast two-hybrid network of EGF/ERK signalling proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21900206 This generic experimental and computational approach provides a framework for elucidating causal connections between signaling proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21930792 SCIMP, a transmembrane adaptor protein involved in major his... | REMOVE | Summary: GRB2 interaction with SCIMP (Q6UWF3): identification of the transmembrane adaptor SCIMP; UniProt records GRB2 SH2 binding to SCIMP pTyr69 from this paper, but the cached abstract does not describe it. Reason: The cited study (identification of the transmembrane adaptor SCIMP; UniProt records GRB2 SH2 binding to SCIMP pTyr69 from this paper, but the cached abstract does not describe it) does not establish a specific GRB2 molecular activity toward SCIMP beyond physical association. SCIMP is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21930792 When phosphorylated, SCIMP binds to the SLP65 adaptor protein and also to the inhibitory kinase Csk file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with WIPF1 (O43516) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with HNRNPK (P61978) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with KHDRBS1 (Q07666) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. KHDRBS1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with ARHGEF5 (Q12774) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ARHGEF5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with SF3B4 (Q15427) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with PIK3AP1 (Q6ZUJ8) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with DOCK4 (Q8N1I0) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with SHANK3 (Q9BYB0) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHANK3 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with WBP11 (Q9Y2W2) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: GRB2 association with CD2AP (Q9Y5K6) reported in a high-throughput study (yeast two-hybrid human liver protein network). Reason: Detected in a yeast two-hybrid human liver protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CD2AP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:21988832 Our data represent the first comprehensive description of a HLPN file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:22057045 Phosphotyrosine mediated protein interactions of the discoid... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): proteomic map of DDR1 phosphotyrosine interactors; the GRB2-SHC1 pair is not resolved as direct. Reason: The cited study (proteomic map of DDR1 phosphotyrosine interactors; the GRB2-SHC1 pair is not resolved as direct) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:22057045 All known interactors of DDR1 were identified and localized to specific phosphotyrosine residues on the receptor file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:22323290 FCH domain only-2 organizes clathrin-coated structures and i... | REMOVE | Summary: GRB2 interaction with Dab2 (P98078), Mus musculus protein: Dab2-FCHO2 study; the GRB2-Dab2 association is not characterised in the cached abstract. Reason: The cited study (Dab2-FCHO2 study; the GRB2-Dab2 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward Dab2 beyond physical association. Dab2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:22323290 We identified one such accessory protein, the F-BAR protein FCH domain only-2 (FCHO2), as a major Dab2-interacting protein file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:22536782 Bivalent binding drives the formation of the Grb2-Gab1 signa... | MODIFY | Summary: GRB2 interaction with GAB1 (Q13480): biophysical analysis of GRB2 cSH3 binding to two RXXK motifs in the GAB1 proline-rich domain. Reason: The study maps the GRB2-GAB1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:22536782 the formation of the Grb2-Gab1 signaling complex is driven via a bivalent interaction through the binding of the C-terminal homology 3 (cSH3) domain within each monomer of Grb2 homodimer to two distinct RXXK motifs file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:22726438 Inhibition of basal FGF receptor signaling by dimeric Grb2. | REMOVE | Summary: GRB2 interaction with FGFR2 (P21802): dimeric GRB2 binds the FGFR2 C-terminus in unstimulated cells and restrains receptor activation until FGFR2 phosphorylates GRB2; this regulatory binding is not captured by a more specific MF term. Reason: The cited study (dimeric GRB2 binds the FGFR2 C-terminus in unstimulated cells and restrains receptor activation until FGFR2 phosphorylates GRB2; this regulatory binding is not captured by a more specific MF term) does not establish a specific GRB2 molecular activity toward FGFR2 beyond physical association. FGFR2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:22726438 Dimeric Grb2 binds to the C termini of two FGFR2 molecules file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:22801373 Protein tyrosine phosphatase Ξ± phosphotyrosyl-789 binds BCAR... | REMOVE | Summary: GRB2 interaction with PTPRA (P18433): PTPalpha pTyr789 recruits BCAR3; the GRB2-PTPalpha association is not characterised in the cached abstract. Reason: The cited study (PTPalpha pTyr789 recruits BCAR3; the GRB2-PTPalpha association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward PTPRA beyond physical association. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:22801373 phospho-Tyr789 PTPΞ± serving as the first defined cellular ligand for the BCAR3 SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:23178716 SnoN/SkiL expression is modulated via arsenic trioxide-induc... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): arsenic trioxide modulates EGFR-Shc/GRB2 association in ovarian cancer cells; binding mode not characterised. Reason: The cited study (arsenic trioxide modulates EGFR-Shc/GRB2 association in ovarian cancer cells; binding mode not characterised) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:23178716 modulates EGFR activation, its interaction with Shc/Grb2, and p-AKT file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:23178716 SnoN/SkiL expression is modulated via arsenic trioxide-induc... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): arsenic trioxide modulates EGFR-Shc/GRB2 association in ovarian cancer cells; binding mode not characterised. Reason: The cited study (arsenic trioxide modulates EGFR-Shc/GRB2 association in ovarian cancer cells; binding mode not characterised) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:23178716 modulates EGFR activation, its interaction with Shc/Grb2, and p-AKT file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:23460737 GRB2-mediated recruitment of THEMIS to LAT is essential for ... | MODIFY | Summary: GRB2 interaction with THEMIS (Q8N1K5-1): GRB2 C-SH3 binds a THEMIS PxRPxK motif and recruits THEMIS to LAT at the immunological synapse. Reason: The study shows GRB2 bridging THEMIS to another signalling protein (SH3-mediated partner binding combined with SH2-mediated recruitment to LAT), i.e. protein-macromolecule adaptor activity. Proposed replacements: protein-macromolecule adaptor activity Supporting Evidence: PMID:23460737 This association is indispensable for THEMIS recruitment to the immunological synapse via the transmembrane adapter linker for activation of T cells (LAT) file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): cooperative recruitment of a Cbl-GRB2 complex to EGFR requires pY1045 plus pY1068 or pY1086 (the GRB2 SH2 sites). Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:23799367 The ubiquitination threshold is mechanistically determined by the cooperative recruitment of the E3 ligase Cbl, in complex with Grb2, to the EGFR file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | MODIFY | Summary: GRB2 interaction with CBL (P22681): cooperative recruitment of a Cbl-GRB2 complex to EGFR requires pY1045 plus pY1068 or pY1086 (the GRB2 SH2 sites). Reason: The study shows GRB2 physically linking CBL to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. For the Cbl partner, GRB2 carries Cbl to the EGFR phosphotyrosines, i.e. it acts as the adaptor linking the E3 ligase to the receptor. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:23799367 The ubiquitination threshold is mechanistically determined by the cooperative recruitment of the E3 ligase Cbl, in complex with Grb2, to the EGFR file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with ERBB2 (P04626) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with ERBB3 (P21860) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB3 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with MYH9 (P35579) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with ARHGEF5 (Q12774) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ARHGEF5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (AP-MS interactome of lung-cancer EGFR mutants). Reason: Detected in a AP-MS interactome of lung-cancer EGFR mutants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24189400 Here, we describe an EGFR interactome of 263 proteins and offer a 14-protein core network critical to the viability of multiple EGFR-mutated lung cancer cells file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (MaMTH membrane two-hybrid method paper using ErbB receptors as test cases). Reason: Detected in a MaMTH membrane two-hybrid method paper using ErbB receptors as test cases; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24658140 We present a split ubiquitin-based method for detection of integral membrane protein-protein interactions (PPIs) in human cells, termed mammalian-membrane two-hybrid assay (MaMTH) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: GRB2 association with ERBB2 (P04626) reported in a high-throughput study (MaMTH membrane two-hybrid method paper using ErbB receptors as test cases). Reason: Detected in a MaMTH membrane two-hybrid method paper using ErbB receptors as test cases; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24658140 We present a split ubiquitin-based method for detection of integral membrane protein-protein interactions (PPIs) in human cells, termed mammalian-membrane two-hybrid assay (MaMTH) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: GRB2 association with ERBB3 (P21860) reported in a high-throughput study (MaMTH membrane two-hybrid method paper using ErbB receptors as test cases). Reason: Detected in a MaMTH membrane two-hybrid method paper using ErbB receptors as test cases; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB3 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24658140 We present a split ubiquitin-based method for detection of integral membrane protein-protein interactions (PPIs) in human cells, termed mammalian-membrane two-hybrid assay (MaMTH) file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: GRB2 interaction with KIT (P10721): high-throughput SH2 domain-phosphopeptide affinity measurements including c-Kit phosphopeptides. Reason: The study shows that GRB2 binding to KIT depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:24728074 We employed a high throughput interaction assay system to empirically determine the affinity between 93 human SH2 domains and phosphopeptides abstracted from several receptor tyrosine kinases and signaling proteins file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:24902122 The Haemophilus ducreyi LspA1 protein inhibits phagocytosis ... | REMOVE | Summary: GRB2 interaction with lspA1 (Q7VLE8), Haemophilus ducreyi (strain 35000HP / ATCC 700724) protein: Haemophilus ducreyi LspA1 targets Csk; the GRB2-LspA1 association is not characterised in the cached abstract. Reason: The cited study (Haemophilus ducreyi LspA1 targets Csk; the GRB2-LspA1 association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward lspA1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:24902122 we show that a 294-aa domain within this bacterial protein binds to C-terminal Src kinase (Csk) and stimulates its catalytic activity file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25036101 Identification of SH3 domain proteins interacting with the c... | REMOVE | Summary: GRB2 interaction with ADAM10 (O14672): SH3 phage-display screen with the ADAM10 cytoplasmic tail. Reason: The cited study (SH3 phage-display screen with the ADAM10 cytoplasmic tail) does not establish a specific GRB2 molecular activity toward ADAM10 beyond physical association. ADAM10 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25036101 we screened the All SH3 Domain Phager library comprising 305 human SH3 domains using a GST fusion protein with the intracellular region of human ADAM10 as a bait for selection file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (quantitative chaperone interaction network). Reason: Detected in a quantitative chaperone interaction network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25036637 We provide a framework for deciphering the proteostasis network and its regulation in development and disease file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25092874 RHEX, a novel regulator of human erythroid progenitor cell e... | REMOVE | Summary: GRB2 interaction with RHEX (Q6ZWK4): RHEX couples to GRB2 in EPO signalling; binding mode not characterised. Reason: The cited study (RHEX couples to GRB2 in EPO signalling; binding mode not characterised) does not establish a specific GRB2 molecular activity toward RHEX beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25092874 This was associated with extracellular signal-regulated kinase 1,2 (ERK1,2) modulation, and RHEX coupling to GRB2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with FAM22F (B7ZLH0) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with ZBTB7B (O15156) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with TRIM27 (P14373) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with LMO2 (P25791) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with PIK3R1 (P27986) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with HNRNPK (P61978) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with REL (Q04864) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with TLE5 (Q08117) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with INCA1 (Q0VD86) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with EPS8 (Q12929) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with LCP2 (Q13094) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with TP53BP2 (Q13625-3) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with C1orf94 (Q6P1W5) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with DPPA4 (Q7L190) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with HOMEZ (Q8IX15-3) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with LNX1 (Q8TBB1) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with DDX17 (Q92841) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with PNMA5 (Q96PV4) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with LZTS2 (Q9BRK4) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with ARHGAP9 (Q9BRR9) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with NIF3L1 (Q9GZT8) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with ABI3 (Q9P2A4) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with IKZF3 (Q9UKT9) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: GRB2 association with WBP11 (Q9Y2W2) reported in a high-throughput study (HI-II-14 proteome-scale binary yeast two-hybrid map). Reason: Detected in a HI-II-14 proteome-scale binary yeast two-hybrid map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25416956 our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25535246 A THEMIS:SHP1 complex promotes T-cell survival. | MODIFY | Summary: GRB2 interaction with PTPN6 (P29350): GRB2 bridges SHP1 to THEMIS and recruits the complex onto LAT. Reason: The study shows GRB2 bridging PTPN6 to another signalling protein (SH3-mediated partner binding combined with SH2-mediated recruitment to LAT), i.e. protein-macromolecule adaptor activity. Proposed replacements: protein-macromolecule adaptor activity Supporting Evidence: PMID:25535246 SHP1 and THEMIS engage with the N-SH3 and C-SH3 domains of GRB2, respectively, a configuration that allows GRB2-SH2 to recruit the complex onto LAT file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:25535246 A THEMIS:SHP1 complex promotes T-cell survival. | MODIFY | Summary: GRB2 interaction with THEMIS (Q8N1K5): GRB2 bridges SHP1 to THEMIS and recruits the complex onto LAT. Reason: The study shows GRB2 bridging THEMIS to another signalling protein (SH3-mediated partner binding combined with SH2-mediated recruitment to LAT), i.e. protein-macromolecule adaptor activity. Proposed replacements: protein-macromolecule adaptor activity Supporting Evidence: PMID:25535246 SHP1 and THEMIS engage with the N-SH3 and C-SH3 domains of GRB2, respectively, a configuration that allows GRB2-SH2 to recruit the complex onto LAT file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | MODIFY | Summary: GRB2 interaction with TSPAN2 (O60636): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The study shows that GRB2 binding to TSPAN2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. TSPAN2 is the pair the authors characterised in detail: GRB2 binding requires a pY-competent SH2 domain and TSPAN2 phospho-Tyr124. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:25814554 TSPAN2 was co-immunoprecipitated with GRB2 requiring an SH2 domain capable of pY binding file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with RB1 (P06400): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward RB1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with CBL (P22681): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward CBL beyond physical association. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with VCP (P55072): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward VCP beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with PPARA (Q07869): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward PPARA beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with ACAP1 (Q15027): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward ACAP1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with DBN1 (Q16643): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward DBN1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with TMEM128 (Q5BJH2-2): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward TMEM128 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with PLEKHS1 (Q5SXH7-1): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward PLEKHS1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with ARL6IP4 (Q66PJ3-4): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward ARL6IP4 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with LMX1A (Q8TE12): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward LMX1A beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with SOCS4 (Q8WXH5): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward SOCS4 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | REMOVE | Summary: GRB2 interaction with PARD6A (Q9NPB6-2): large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs. Reason: The cited study (large-scale kinase-coupled yeast two-hybrid screen for phosphotyrosine-dependent interactions; which partner carries the phosphotyrosine and which reads it was characterised only for selected pairs) does not establish a specific GRB2 molecular activity toward PARD6A beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25814554 We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:25819436 A single PXXP motif in the C-terminal region of srGAP3 media... | MODIFY | Summary: GRB2 interaction with SRGAP3 (O43295): srGAP3 binds GRB2 SH3 through a single C-terminal proline-rich motif. Reason: The study maps the GRB2-SRGAP3 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:25819436 All these interactions depend on a single proline-rich motif in the CTR and the Src-homology 3 domains of the binding partners file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:25825872 Preferred SH3 domain partners of ADAM metalloproteases inclu... | REMOVE | Summary: GRB2 interaction with ADAM15 (Q13444): systematic SH3-binding survey of ADAM cytoplasmic tails. Reason: The cited study (systematic SH3-binding survey of ADAM cytoplasmic tails) does not establish a specific GRB2 molecular activity toward ADAM15 beyond physical association. ADAM15 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:25825872 Here we present a comprehensive characterization of SH3 binding capacity and preferences of the catalytically active ADAMs 8, 9, 10, 12, 15, 17, and 19 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:27059931 Weak binding to E3 ubiquitin ligase c-Cbl increases EGFRvA p... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): GRB2 mediates EGFR-c-Cbl association; the EGFRvA isoform that cannot bind GRB2 binds less Cbl and is stabilised. Reason: The study shows GRB2 physically linking EGFR to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:27059931 EGFRvA cannot bind to Grb2, an important binding mediator between EGFR and c-Cbl file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (Barcode Fusion Genetics pooled yeast two-hybrid matrix screen). Reason: Detected in a Barcode Fusion Genetics pooled yeast two-hybrid matrix screen; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:27107012 BFG-Y2H increases the efficiency of protein matrix screening, with quality that is on par with state-of-the-art Y2H methods file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (Barcode Fusion Genetics pooled yeast two-hybrid matrix screen). Reason: Detected in a Barcode Fusion Genetics pooled yeast two-hybrid matrix screen; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:27107012 BFG-Y2H increases the efficiency of protein matrix screening, with quality that is on par with state-of-the-art Y2H methods file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (Barcode Fusion Genetics pooled yeast two-hybrid matrix screen). Reason: Detected in a Barcode Fusion Genetics pooled yeast two-hybrid matrix screen; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:27107012 BFG-Y2H increases the efficiency of protein matrix screening, with quality that is on par with state-of-the-art Y2H methods file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: GRB2 association with IKZF3 (Q9UKT9) reported in a high-throughput study (Barcode Fusion Genetics pooled yeast two-hybrid matrix screen). Reason: Detected in a Barcode Fusion Genetics pooled yeast two-hybrid matrix screen; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:27107012 BFG-Y2H increases the efficiency of protein matrix screening, with quality that is on par with state-of-the-art Y2H methods file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28046066 HTLV-1 bZIP Factor Enhances T-Cell Proliferation by Impeding... | REMOVE | Summary: GRB2 interaction with THEMIS (Q8N1K5): HTLV-1 HBZ targets the THEMIS/GRB2/SHP-2 complex; the GRB2-THEMIS association is referenced rather than characterised. Reason: The cited study (HTLV-1 HBZ targets the THEMIS/GRB2/SHP-2 complex; the GRB2-THEMIS association is referenced rather than characterised) does not establish a specific GRB2 molecular activity toward THEMIS beyond physical association. THEMIS is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28046066 HBZ does this by interacting with THEMIS, which associates with Grb2 and SHP-2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (global receptor tyrosine kinase-phosphatase interactome (split-ubiquitin two-hybrid)). Reason: Detected in a global receptor tyrosine kinase-phosphatase interactome (split-ubiquitin two-hybrid); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28065597 This comprehensive RTK-phosphatase interactome study provides a broad and deep view of RTK signaling file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (systematic AP-MS analysis of human protein phosphatase interactions). Reason: Detected in a systematic AP-MS analysis of human protein phosphatase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28330616 Our study provides an initial glimpse of the protein interaction landscape of phosphatases and their functions in cellular regulation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with PIK3C2B (O00750) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with WIPF1 (O43516) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with BCR (P11274) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. BCR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with PIK3CA (P42336) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with PIK3AP1 (Q6ZUJ8) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with SPATA2L (Q8IUW3) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with PTPN23 (Q9H3S7) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN23 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (BioPlex 2.0 AP-MS interactome). Reason: Detected in a BioPlex 2.0 AP-MS interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:28514442 BioPlex 2.0 exceeds previous experimentally derived interaction networks in depth and breadth file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | REMOVE | Summary: GRB2 association with LNX1 (Q8TBB1) reported in a high-throughput study (interactome-perturbation screen of missense mutations). Reason: Detected in a interactome-perturbation screen of missense mutations; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:29892012 we demonstrate that our interactome perturbation approach offers a generalizable framework for identifying and prioritizing missense mutations that contribute to the risk of human disease file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec... | REMOVE | Summary: GRB2 association with VAV1 (P15498) reported in a high-throughput study (LuTHy bioluminescence two-hybrid method paper with benchmark interaction sets). Reason: Detected in a LuTHy bioluminescence two-hybrid method paper with benchmark interaction sets; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:29997244 Our study presents a robust, sensitive research tool with high utility for investigating the molecular mechanisms by which disease-associated mutations impair protein activity in biological systems file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (LuTHy bioluminescence two-hybrid method paper with benchmark interaction sets). Reason: Detected in a LuTHy bioluminescence two-hybrid method paper with benchmark interaction sets; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:29997244 Our study presents a robust, sensitive research tool with high utility for investigating the molecular mechanisms by which disease-associated mutations impair protein activity in biological systems file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (binary interactome assay-benchmarking study). Reason: Detected in a binary interactome assay-benchmarking study; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31467278 The resulting union of N2H versions recovers as many PPIs as 10 distinct assays combined file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (yeast two-hybrid profiling of interaction disruption by genetic variants). Reason: Detected in a yeast two-hybrid profiling of interaction disruption by genetic variants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31515488 Furthermore, these results suggest that 10.5% of missense variants carried per individual are disruptive file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: GRB2 association with INCA1 (Q0VD86) reported in a high-throughput study (yeast two-hybrid profiling of interaction disruption by genetic variants). Reason: Detected in a yeast two-hybrid profiling of interaction disruption by genetic variants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31515488 Furthermore, these results suggest that 10.5% of missense variants carried per individual are disruptive file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (yeast two-hybrid profiling of interaction disruption by genetic variants). Reason: Detected in a yeast two-hybrid profiling of interaction disruption by genetic variants; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31515488 Furthermore, these results suggest that 10.5% of missense variants carried per individual are disruptive file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): phosphopeptide pulldowns identify the proteins recruited to EGF-regulated phosphotyrosine sites; GRB2 is retrieved by partner phosphopeptides. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:31585087 we performed >1,000 phosphopeptide pulldowns and analyzed them by rapid mass spectrometric analysis file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | MODIFY | Summary: GRB2 interaction with PTPN11 (Q06124): phosphopeptide pulldowns identify the proteins recruited to EGF-regulated phosphotyrosine sites; GRB2 is retrieved by partner phosphopeptides. Reason: The study shows that GRB2 binding to PTPN11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:31585087 we performed >1,000 phosphopeptide pulldowns and analyzed them by rapid mass spectrometric analysis file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:31820037 Elucidation of protein interactions necessary for the mainte... | REMOVE | Summary: GRB2 interaction with PIK3R1 (P27986): mapping of BCR-ABL core complex interactions; GRB2, SOS1 and CBL are recruited via BCR pTyr177. Reason: The cited study (mapping of BCR-ABL core complex interactions; GRB2, SOS1 and CBL are recruited via BCR pTyr177) does not establish a specific GRB2 molecular activity toward PIK3R1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31820037 BCR-ABL sequence motif located in disordered region around phosphorylated tyrosine 177 mediates binding of three core complex members, i.e., GRB2, SOS1, and cCBL file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31820037 Elucidation of protein interactions necessary for the mainte... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): mapping of BCR-ABL core complex interactions; GRB2, SOS1 and CBL are recruited via BCR pTyr177. Reason: The cited study (mapping of BCR-ABL core complex interactions; GRB2, SOS1 and CBL are recruited via BCR pTyr177) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31820037 BCR-ABL sequence motif located in disordered region around phosphorylated tyrosine 177 mediates binding of three core complex members, i.e., GRB2, SOS1, and cCBL file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31820037 Elucidation of protein interactions necessary for the mainte... | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): mapping of BCR-ABL core complex interactions; GRB2, SOS1 and CBL are recruited via BCR pTyr177. Reason: The study places the GRB2-SOS1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. For the SOS1 partner, SOS1 is recruited to BCR-ABL pTyr177 together with GRB2, i.e. GRB2 bridging SOS1 to a phosphotyrosine docking site. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:31820037 BCR-ABL sequence motif located in disordered region around phosphorylated tyrosine 177 mediates binding of three core complex members, i.e., GRB2, SOS1, and cCBL file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with PIK3C2B (O00750) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with ERBB2 (P04626) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with HSPA5 (P11021) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with PTPN1 (P18031) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with HNRNPK (P61978) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with DNM1 (Q05193) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with PTPN11 (Q06124) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with ARHGEF5 (Q12774) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ARHGEF5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with GAB1 (Q13480) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with PIK3AP1 (Q6ZUJ8) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with DOCK4 (Q8N1I0) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: GRB2 association with GIT1 (Q9Y2X7) reported in a high-throughput study (AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS). Reason: Detected in a AP-MS EGFR network in colorectal cancer cells with or without mutant KRAS; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:31980649 PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32203420 Systems analysis of RhoGEF and RhoGAP regulatory proteins re... | REMOVE | Summary: GRB2 association with ARHGEF5 (Q12774) reported in a high-throughput study (systematic AP-MS/BioID analysis of RhoGEF and RhoGAP regulatory proteins). Reason: Detected in a systematic AP-MS/BioID analysis of RhoGEF and RhoGAP regulatory proteins; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ARHGEF5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32203420 Our systems analysis of Rho regulators is key to revealing emergent organization principles of Rho signalling file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with MED19 (A0JLT2-2) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with VPS37C (A5D8V6) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with MEI4 (A8MW99) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with PRR5-ARHGAP8 (B1AHC3) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with FAM22F (B7ZLH0) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with SOCS7 (O14512) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with AGR2 (O95994) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with TXK (P42681) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with BTG1 (P62324) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ARID5A (Q03989) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with TYRO3 (Q06418) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. TYRO3 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with LCP2 (Q13094) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. LCP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with SF3A2 (Q15428) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with EFHC2 (Q5JST6) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with TBC1D3G (Q6DHY5) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with PLEKHA7 (Q6IQ23-2) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ZNF474 (Q6S9Z5) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ZNF620 (Q6ZNG0) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with KIAA0408 (Q6ZU52) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with UniProtKB:Q7Z783 (Q7Z783) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ANKRD23 (Q86SG2) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with GGN (Q86UU5) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with SPATA2L (Q8IUW3) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with PHETA1 (Q8N4B1-4) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with CPSF7 (Q8N684-3) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with DTX3 (Q8N9I9) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with WASF1 (Q92558) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with PIK3R3 (Q92569) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with DDIT4L (Q96D03) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with TRIB3 (Q96RU7) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with CCDC28B (Q9BUN5-3) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ZNF341 (Q9BYN7) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with RNF208 (Q9H0X6) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with SH2D4A (Q9H788) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with MYG1 (Q9HB07) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with SH2B1 (Q9NRF2-2) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with IKZF3 (Q9UKT9) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with VAV3 (Q9UKW4) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: GRB2 association with ZBTB12 (Q9Y330) reported in a high-throughput study (HuRI proteome-scale binary yeast two-hybrid interactome map). Reason: Detected in a HuRI proteome-scale binary yeast two-hybrid interactome map; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32296183 HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: GRB2 association with MAP4K1 (Q92918) reported in a high-throughput study (AP-MS kinase interaction network). Reason: Detected in a AP-MS kinase interaction network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32707033 The interaction dataset is a high-quality resource with more than 5,000 previously unreported interactions file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (AP-MS kinase interaction network). Reason: Detected in a AP-MS kinase interaction network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32707033 The interaction dataset is a high-quality resource with more than 5,000 previously unreported interactions file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with PRMT5 (O14744) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with PIK3R1 (P27986-2) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with PIK3CA (P42336) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ARHGDIB (P52566) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with GRB10 (Q13322-4) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ITGB3BP (Q13352) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with TNFAIP1 (Q13829) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with BECN1 (Q14457) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with LPIN1 (Q14693) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with RAB11B (Q15907) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with KRTAP19-5 (Q3LI72) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ADAMTSL4 (Q6UY14-3) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ASCL4 (Q6XD76) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with TMEM185A (Q8NFB2) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ZNG1A (Q9BRT8) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with RBM4 (Q9BWF3-2) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with JADE2 (Q9NQC1-2) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with EIF2B4 (Q9UI10) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with KLF15 (Q9UIH9) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: GRB2 association with ZNF232 (Q9UNY5) reported in a high-throughput study (yeast two-hybrid neurodegenerative-disease protein network). Reason: Detected in a yeast two-hybrid neurodegenerative-disease protein network; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:32911434 A functionally defined high-density NRF2 interactome reveals... | REMOVE | Summary: GRB2 association with NFE2L2 (Q16236) reported in a high-throughput study (high-density NRF2 interactome). Reason: Detected in a high-density NRF2 interactome; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:32911434 This experimentally defined binary NRF2 interactome provides a new vision of the complex molecular networks file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PIK3C2B (O00750) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with ASAP2 (O43150) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with WIPF1 (O43516) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with BCR (P11274) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. BCR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PIK3CA (P42336) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with DNM1 (Q05193) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PTPN11 (Q06124) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with TNK2 (Q07912) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with ARHGEF5 (Q12774) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ARHGEF5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with GAB1 (Q13480) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PIK3AP1 (Q6ZUJ8) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with SPATA2L (Q8IUW3) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with DOCK4 (Q8N1I0) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with THEMIS (Q8N1K5) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. THEMIS is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with PTPN23 (Q9H3S7) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN23 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines). Reason: Detected in a BioPlex 3.0 AP-MS proteome-scale interactome in two cell lines; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:33961781 Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (AP-MS protein network of head and neck cancer). Reason: Detected in a AP-MS protein network of head and neck cancer; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:34591642 We anticipate that the application of this framework will be valuable for translating genetic alterations into a molecular and clinical understanding file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (OpenCell endogenous-tagging IP-MS resource). Reason: Detected in a OpenCell endogenous-tagging IP-MS resource; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35271311 Paired with a fully interactive website (opencell.czbiohub.org), our work constitutes a resource for the quantitative cartography of human cellular organization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (OpenCell endogenous-tagging IP-MS resource). Reason: Detected in a OpenCell endogenous-tagging IP-MS resource; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35271311 Paired with a fully interactive website (opencell.czbiohub.org), our work constitutes a resource for the quantitative cartography of human cellular organization file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: GRB2 association with EGFR (P00533) reported in a high-throughput study (AP-MS/BioID atlas of receptor tyrosine kinase interactions). Reason: Detected in a AP-MS/BioID atlas of receptor tyrosine kinase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35384245 Our data represent a comprehensive, systemic mapping of RTK interactions and substrates file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: GRB2 association with ERBB2 (P04626) reported in a high-throughput study (AP-MS/BioID atlas of receptor tyrosine kinase interactions). Reason: Detected in a AP-MS/BioID atlas of receptor tyrosine kinase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ERBB2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35384245 Our data represent a comprehensive, systemic mapping of RTK interactions and substrates file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: GRB2 association with FGFR2 (P21802) reported in a high-throughput study (AP-MS/BioID atlas of receptor tyrosine kinase interactions). Reason: Detected in a AP-MS/BioID atlas of receptor tyrosine kinase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. FGFR2 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35384245 Our data represent a comprehensive, systemic mapping of RTK interactions and substrates file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: GRB2 association with AXL (P30530) reported in a high-throughput study (AP-MS/BioID atlas of receptor tyrosine kinase interactions). Reason: Detected in a AP-MS/BioID atlas of receptor tyrosine kinase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. AXL is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35384245 Our data represent a comprehensive, systemic mapping of RTK interactions and substrates file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: GRB2 association with TYRO3 (Q06418) reported in a high-throughput study (AP-MS/BioID atlas of receptor tyrosine kinase interactions). Reason: Detected in a AP-MS/BioID atlas of receptor tyrosine kinase interactions; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. TYRO3 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:35384245 Our data represent a comprehensive, systemic mapping of RTK interactions and substrates file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:37398436 AI-guided pipeline for protein-protein interaction drug disc... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (AI-guided PPI drug-discovery screen). Reason: Detected in a AI-guided PPI drug-discovery screen; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:37398436 this pipeline will help to prioritize PPI targets to accelerate the discovery of early-stage drug candidates targeting protein complexes and pathways file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:37776851 Analysis of proteome-wide degradation dynamics in ALS SOD1 i... | REMOVE | Summary: GRB2 association with VCP (P55072) reported in a high-throughput study (proteome-wide degradation/interaction profiling in ALS iPSC neurons). Reason: Detected in a proteome-wide degradation/interaction profiling in ALS iPSC neurons; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:37776851 Our results demonstrate that VCP contributes to mutSOD1-dependent degeneration file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:38182563 GRB2 is a BECN1 interacting protein that regulates autophagy... | REMOVE | Summary: GRB2 interaction with BECN1 (Q14457): GRB2 co-immunoprecipitates with BECN1 and regulates autophagy via VPS34 activity; no informative MF beyond association is established. Reason: The cited study (GRB2 co-immunoprecipitates with BECN1 and regulates autophagy via VPS34 activity; no informative MF beyond association is established) does not establish a specific GRB2 molecular activity toward BECN1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:38182563 GRB2 co-immunoprecipitated with BECN1 in several breast cancer cell lines file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: GRB2 association with SF3B4 (Q15427) reported in a high-throughput study (systematic screen for post-transcriptional regulatory modules). Reason: Detected in a systematic screen for post-transcriptional regulatory modules; the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:39251607 This study provides a detailed map of RBP interactions and deconvolves them into distinct regulatory modules with annotated functions and target regulons file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with WASL (O00401) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WASL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PIK3R2 (O00459) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PIK3C2B (O00750) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PIK3C2B is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with SYNJ2 (O15056) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SYNJ2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with WIPF1 (O43516) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with STAMBP (O95630) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. STAMBP is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PTPN1 (P18031) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PTPRA (P18433) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPRA is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with CBL (P22681) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBL is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with SHC1 (P29353) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with DNM2 (P50570) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with DNM1 (Q05193) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PTPN11 (Q06124) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN11 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with SOS1 (Q07889) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with SOS2 (Q07890) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with TNK2 (Q07912) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with CBLB (Q13191) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. CBLB is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with GAB1 (Q13480) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with DOCK1 (Q14185) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PIK3AP1 (Q6ZUJ8) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with MAP4K3 (Q8IVH8) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K3 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with DOCK4 (Q8N1I0) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. DOCK4 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with THEMIS (Q8N1K5) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. THEMIS is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with WIPF2 (Q8TF74) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. WIPF2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PTPN23 (Q9H3S7) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. PTPN23 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with GAREM1 (Q9H706) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAREM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with ERRFI1 (Q9UJM3) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with ASAP1 (Q9ULH1) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. ASAP1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with GAB2 (Q9UQC2) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. GAB2 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with PALM2AKAP2 (Q9Y2D5) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: GRB2 association with MAP4K5 (Q9Y4K4) reported in a high-throughput study (multimodal proteome-scale cell map (AP-MS and imaging)). Reason: Detected in a multimodal proteome-scale cell map (AP-MS and imaging); the screen does not resolve the binding mode, directness or any GRB2 activity for this pair, so no informative molecular function can be assigned from this row. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:40205054 The associated Cell Visualization Portal and Mapping Toolkit provide a reference platform for structural and functional cell biology file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:7504175 Pleiotropic insulin signals are engaged by multisite phospho... | MODIFY | Summary: GRB2 interaction with Irs1 (P35570), Rattus norvegicus protein: the GRB2 SH2 domain binds IRS-1 pTyr895 (YVNI motif). Reason: The study shows that GRB2 binding to Irs1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7504175 the SH2 domain in GRB2 and the amino-terminal SH2 domain in SHPTP2 (Syp) specifically bind to Tyr(P)-895 and Tyr(P)-1172, respectively file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7518560 Hierarchy of binding sites for Grb2 and Shc on the epidermal... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): GRB2 SH2 binds EGFR pY1068/pY1086 directly and pY1173 indirectly via Shc. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7518560 Grb2 binds directly to the EGFR at Y-1068, to a lesser extent at Y-1086, and indirectly at Y-1173 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7518772 Phosphorylation of receptor protein-tyrosine phosphatase alp... | MODIFY | Summary: GRB2 interaction with PTPRA (P18433): RPTPalpha pTyr789 (YANF) is a GRB2 SH2 docking site. Reason: The study shows that GRB2 binding to PTPRA depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7518772 We show that RPTP alpha, but not a mutant of RPTP alpha with a Tyr-->Phe mutation at position 789, bound to GRB2 in vitro file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7522233 Interleukin (IL)-3 and granulocyte/macrophage colony-stimula... | MODIFY | Summary: GRB2 interaction with Ptpn11 (P35235), Mus musculus protein: GRB2 SH2 binds tyrosine-phosphorylated SHP2 after IL-3/GM-CSF stimulation. Reason: The study shows that GRB2 binding to Ptpn11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7522233 The Src homology 2 (SH2) domain of the adaptor protein Grb2 bound with high affinity to tyrosine-phosphorylated SHPTP2 following treatment of cells with IL-3 or GM-CSF file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7523381 The ubiquitously expressed Syp phosphatase interacts with c-... | REMOVE | Summary: GRB2 interaction with KIT (P10721): tyrosine-phosphorylated SHP2 (Syp) complexes with GRB2 downstream of c-Kit. Reason: The cited study (tyrosine-phosphorylated SHP2 (Syp) complexes with GRB2 downstream of c-Kit) does not establish a specific GRB2 molecular activity toward KIT beyond physical association. For the c-Kit partner this paper documents Syp binding to activated c-Kit; the GRB2-c-Kit association is not characterised as a distinct GRB2 activity here. KIT is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:7523381 We found that Syp, a phosphotyrosine phosphatase widely expressed in all the tissues in mammals, associates with c-kit receptor after activation with its ligand file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:7523381 The ubiquitously expressed Syp phosphatase interacts with c-... | MODIFY | Summary: GRB2 interaction with Ptpn11 (P35235), Mus musculus protein: tyrosine-phosphorylated SHP2 (Syp) complexes with GRB2 downstream of c-Kit. Reason: The study shows that GRB2 binding to Ptpn11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7523381 tyrosine-phosphorylated Syp was found to be complexed with Grb2 in steel factor-stimulated M07e cells file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7523381 The ubiquitously expressed Syp phosphatase interacts with c-... | MODIFY | Summary: GRB2 interaction with PTPN11 (Q06124): tyrosine-phosphorylated SHP2 (Syp) complexes with GRB2 downstream of c-Kit. Reason: The study shows that GRB2 binding to PTPN11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7523381 tyrosine-phosphorylated Syp was found to be complexed with Grb2 in steel factor-stimulated M07e cells file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7527391 Independent binding of peptide ligands to the SH2 and SH3 do... | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): intact GRB2 binds an EGFR phosphopeptide and a Sos proline-rich peptide simultaneously, consistent with recruitment of Sos to the receptor. Reason: The study places the GRB2-SOS1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:7527391 Saturation of the SH2 domain of Grb2 with the EGFR phosphopeptide was found not to affect its subsequent binding to the Sos peptide file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:7537265 Functional interaction between c-Src and its mitotic target,... | MODIFY | Summary: GRB2 interaction with KHDRBS1 (Q07666): tyrosine-phosphorylated Sam68 (KHDRBS1) binds recombinant SH2 domains including that of GRB2. Reason: The study shows that GRB2 binding to KHDRBS1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7537265 Mitotic, tyrosine-phosphorylated Sam 68 bound selectively to recombinant SH2 domains with significantly different affinities file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7597091 Stimulation of human monocytes with macrophage colony-stimul... | MODIFY | Summary: GRB2 interaction with PTK2 (Q05397): GRB2 SH2 binds FAK pTyr925 (pYENV) after M-CSF stimulation. Reason: The study shows that GRB2 binding to PTK2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7597091 tyrosine-phosphorylated pp125FAK directly interacts with the SH2 domain of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:7629138 Differential interactions of human Sos1 and Sos2 with Grb2. | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): hSos1 and hSos2 both bind GRB2 via their proline-rich C-termini in an SH3-dependent manner, hSos2 with higher affinity. Reason: The study places the GRB2-SOS1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:7629138 These results suggest that Sos1 and Sos2 may differentially contribute to receptor-mediated Ras activation file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:7629138 Differential interactions of human Sos1 and Sos2 with Grb2. | MODIFY | Summary: GRB2 interaction with SOS2 (Q07890): hSos1 and hSos2 both bind GRB2 via their proline-rich C-termini in an SH3-dependent manner, hSos2 with higher affinity. Reason: The study places the GRB2-SOS2 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:7629138 These results suggest that Sos1 and Sos2 may differentially contribute to receptor-mediated Ras activation file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:7773779 NMR structure of the N-terminal SH3 domain of GRB2 and its c... | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): NMR structure of the GRB2 N-SH3 domain bound to a Sos proline-rich peptide. Reason: The study maps the GRB2-SOS1 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:7773779 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:7929073 5-Lipoxygenase contains a functional Src homology 3-binding ... | MODIFY | Summary: GRB2 interaction with ALOX5 (P09917): 5-lipoxygenase binds GRB2 SH3 domains through a proline-rich SH3-binding motif. Reason: The study maps the GRB2-ALOX5 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:7929073 SH3-binding motif inhibited formation of the 5-lipoxygenase.Grb2 complex in vitro file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:8112292 Bcr-Abl oncoproteins bind directly to activators of the Ras ... | MODIFY | Summary: GRB2 interaction with BCR (P11274): GRB2 SH2 binds BCR pTyr177 (YVNV) of Bcr-Abl. Reason: The study shows that GRB2 binding to BCR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8112292 the Grb2 SH2 domain bound Bcr-Abl through recognition of a tyrosine phosphorylation site within the amino-terminal bcr-encoded sequence file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8491186 The SH2/SH3 domain-containing protein GRB2 interacts with ty... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): GRB2 SH2 binds insulin-stimulated phosphotyrosines on IRS-1 and Shc (YV/IN motif). Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8491186 mediated by the binding of the SH2 domain of GRB2 to phosphotyrosines on both IRS-1 and Shc file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8491186 The SH2/SH3 domain-containing protein GRB2 interacts with ty... | MODIFY | Summary: GRB2 interaction with Irs1 (P35570), Rattus norvegicus protein: GRB2 SH2 binds insulin-stimulated phosphotyrosines on IRS-1 and Shc (YV/IN motif). Reason: The study shows that GRB2 binding to Irs1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8491186 mediated by the binding of the SH2 domain of GRB2 to phosphotyrosines on both IRS-1 and Shc file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8663178 Rapid identification of phosphopeptide ligands for SH2 domai... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): phosphopeptide library screen defining GRB2 SH2 pY-x-N specificity. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8663178 the SH2 domain of the adapter protein Grb2 predominantly selected beads with the sequence Y*ENDP file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8798570 Ligand activation of ELK receptor tyrosine kinase promotes i... | MODIFY | Summary: GRB2 interaction with EPHB1 (P54762): GRB2 SH2 binds autophosphorylated EphB1 (ELK) but not unphosphorylated receptor. Reason: The study shows that GRB2 binding to EPHB1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8798570 These findings define ligand-activated interaction between ELK and the SH2 domains of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8816475 Evidence for in vivo phosphorylation of the Grb2 SH2-domain ... | MODIFY | Summary: GRB2 interaction with Ptk2 (P34152), Mus musculus protein: Src phosphorylation of FAK Tyr925 creates the GRB2 SH2 binding site. Reason: The study shows that GRB2 binding to Ptk2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8816475 Src-family binding and phosphorylation of FAK at Tyr-925 creates a Grb2 SH2-domain binding site file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8887653 The phosphotyrosine interaction domains of X11 and FE65 bind... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): X11/FE65 PI-domain binding to APP; the GRB2-EGFR association is not characterised in the cached abstract. Reason: The cited study (X11/FE65 PI-domain binding to APP; the GRB2-EGFR association is not characterised in the cached abstract) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:8887653 We have found that the X11 PI domain binds a YENPTY motif in the intracellular domain of (beta)APP file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:8892607 Evidence that the Wiskott-Aldrich syndrome protein may be in... | MODIFY | Summary: GRB2 interaction with WAS (P42768): the proline-rich WASP binds the SH3 domains of GRB2 and Tec-family kinases. Reason: The study maps the GRB2-WAS association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:8892607 we show binding of WASP to the Src homology 3 domains of Btk, Itk, Tec, Grb2, and phospholipase C-gamma file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:8939605 The Shc adaptor protein is highly phosphorylated at conserve... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): Shc phosphotyrosines Y239/240 contribute to GRB2 binding. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8939605 Mutagenesis studies indicate that Y239/240 make an important contribution to the association of Shc with Grb2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher aff... | MODIFY | Summary: GRB2 interaction with EGFR (P00533): GRB2 (alone or in complex with mSos1) binds EGFR- and Shc-derived phosphopeptides. Reason: The study shows that GRB2 binding to EGFR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8940013 Grb2-mSos1 bound to both EGFR- and Shc-derived phosphopeptides with higher affinities file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher aff... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): GRB2 (alone or in complex with mSos1) binds EGFR- and Shc-derived phosphopeptides. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8940013 Grb2-mSos1 bound to both EGFR- and Shc-derived phosphopeptides with higher affinities file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher aff... | MODIFY | Summary: GRB2 interaction with Sos1 (Q62245), Mus musculus protein: GRB2 (alone or in complex with mSos1) binds EGFR- and Shc-derived phosphopeptides. Reason: The study places the GRB2-Sos1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. For the mSos1 partner the paper shows that the preformed Grb2-mSos1 complex binds receptor and Shc phosphopeptides, i.e. GRB2 bridging SOS1 to phosphotyrosine docking sites. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:8940013 Grb2-mSos1 bound to both EGFR- and Shc-derived phosphopeptides with higher affinities file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:8955135 Co-expression with BCR induces activation of the FES tyrosin... | MODIFY | Summary: GRB2 interaction with BCR (P11274): FES phosphorylation of BCR Tyr177 creates a GRB2 SH2 binding site. Reason: The study shows that GRB2 binding to BCR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8955135 Mutagenesis of BCR Tyr-177 to Phe completely abolished FES-induced BCR binding to the GRB2 SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8959326 Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 e... | MODIFY | Summary: GRB2 interaction with Ptpn11 (P35235), Mus musculus protein: GRB2 binding to SHP2 requires SHP2 pTyr584 (pY-X-N-X). Reason: The study shows that GRB2 binding to Ptpn11 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8959326 mutation of tyrosine 584, but not tyrosine 546, to phenylalanine totally abolished the binding of Grb2 to SHP-2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:8995379 The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 pro... | REMOVE | Summary: GRB2 interaction with BCR (P11274): characterisation of the GRB2-like adaptor Grap; GRB2 appears as a comparator. Reason: The cited study (characterisation of the GRB2-like adaptor Grap; GRB2 appears as a comparator) does not establish a specific GRB2 molecular activity toward BCR beyond physical association. BCR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:8995379 This interaction is mediated by the Grap SH2 domain, which has similar binding specificity to the Grb2 SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:8995379 The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 pro... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): characterisation of the GRB2-like adaptor Grap; GRB2 appears as a comparator. Reason: The cited study (characterisation of the GRB2-like adaptor Grap; GRB2 appears as a comparator) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:8995379 This interaction is mediated by the Grap SH2 domain, which has similar binding specificity to the Grb2 SH2 domain file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: GRB2 interaction with EGFR (P00533): subpopulations of EGF receptors differ in associated effectors (less GRB2 on pTyr992 receptors); co-precipitation without mapped GRB2 binding. Reason: The cited study (subpopulations of EGF receptors differ in associated effectors (less GRB2 on pTyr992 receptors); co-precipitation without mapped GRB2 binding) does not establish a specific GRB2 molecular activity toward EGFR beyond physical association. EGFR is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9020117 Tyr(P)992 receptors were associated with more SOS, Ras-GTPase activating protein, phosphatidylinositol 3-kinase, and SHPTP2/syp, but less Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: GRB2 interaction with PLCG1 (P19174): subpopulations of EGF receptors differ in associated effectors (less GRB2 on pTyr992 receptors); co-precipitation without mapped GRB2 binding. Reason: The cited study (subpopulations of EGF receptors differ in associated effectors (less GRB2 on pTyr992 receptors); co-precipitation without mapped GRB2 binding) does not establish a specific GRB2 molecular activity toward PLCG1 beyond physical association. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9020117 Tyr(P)992 receptors were associated with more SOS, Ras-GTPase activating protein, phosphatidylinositol 3-kinase, and SHPTP2/syp, but less Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9045636 Interaction between Sam68 and Src family tyrosine kinases, F... | REMOVE | Summary: GRB2 interaction with KHDRBS1 (Q07666): Sam68 (KHDRBS1) co-immunoprecipitates with many signalling proteins including GRB2 in HTLV-1-infected T cells. Reason: The cited study (Sam68 (KHDRBS1) co-immunoprecipitates with many signalling proteins including GRB2 in HTLV-1-infected T cells) does not establish a specific GRB2 molecular activity toward KHDRBS1 beyond physical association. KHDRBS1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9045636 The 68-kDa protein was coimmunoprecipitated with various signaling proteins such as phospholipase C gamma1, the phosphatidylinositol 3-kinase p85 subunit, Grb2, SHP-1, Cbl, and Jak3 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9148935 Focal adhesion kinase overexpression enhances ras-dependent ... | MODIFY | Summary: GRB2 interaction with Ptk2 (P34152), Mus musculus protein: FAK pTyr925 is the GRB2 binding site; fibronectin also induces GRB2-Shc association. Reason: The study shows that GRB2 binding to Ptk2 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9148935 Expression of the Grb2 binding site Phe-925 mutant of FAK enhanced activation of ERK2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9174058 Tyrosine phosphorylation of p120cbl in BCR/abl transformed h... | MODIFY | Summary: GRB2 interaction with BCR (P11274): GRB2 binding to BCR/abl depends on BCR Tyr177; GRB2 SH3 domains also bind Cbl. Reason: The study shows that GRB2 binding to BCR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9174058 p190Y177F BCR/abl mutant which is unable to bind GRB2 file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9175774 An alternative to phosphotyrosine-containing motifs for bind... | REMOVE | Summary: GRB2 interaction with SHC1 (P29353): non-phosphorylated Shc Tyr317-region peptides bind the GRB2 SH2 domain independently of phosphorylation, so a phosphotyrosine-binding term would misrepresent this particular result. Reason: The cited study (non-phosphorylated Shc Tyr317-region peptides bind the GRB2 SH2 domain independently of phosphorylation, so a phosphotyrosine-binding term would misrepresent this particular result) does not establish a specific GRB2 molecular activity toward SHC1 beyond physical association. SHC1 is a phosphotyrosine-bearing GRB2 docking partner; GRB2 SH2-mediated recognition of such partners is captured by the GO:0001784 phosphotyrosine residue binding rows (IBA and experimental) and by the MODIFY proposals on small-scale studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9175774 can bind to the SH2 domain of Grb2 regardless of the state of tyrosine phosphorylation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9178760 Intracellular signaling of the Ufo/Axl receptor tyrosine kin... | MODIFY | Summary: GRB2 interaction with AXL (P30530): Axl/Ufo pTyr821 (pYVNM) is a GRB2 docking site. Reason: The study shows that GRB2 binding to AXL depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9178760 revealed C-terminal tyrosine 821 (EILpYVNMDEG) as a docking site for multiple effectors, namely PLCgamma, p85 proteins, GRB2, c-src and lck file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9178913 Bcr phosphorylated on tyrosine 177 binds Grb2. | MODIFY | Summary: GRB2 interaction with BCR (P11274): Bcr pTyr177 binds the GRB2 SH2 domain. Reason: The study shows that GRB2 binding to BCR depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9178913 Studies with GST-SH2 (Grb2) revealed that tyrosine phosphorylated Bcr was able to bind to GST SH2 (Grb2) but tyrosine phosphorylated Bcr Y177F was deficient in binding file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9254595 Thermodynamic and structural analysis of phosphotyrosine pol... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): calorimetry of GRB2 SH2 binding to Shc-derived phosphopeptides. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9254595 The thermodynamic and structural data are consistent with a Grb2-SH2 recognition motif of pY-hydrophobic-N-X file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9346925 SH2/SH3 adaptor proteins can link tyrosine kinases to a Ste2... | MODIFY | Summary: GRB2 interaction with MAP4K1 (Q92918): GRB2 SH3 domains bind HPK1 (MAP4K1) proline-rich motifs and GRB2 brings HPK1 to the autophosphorylated EGF receptor. Reason: The study shows GRB2 physically linking MAP4K1 to an activated receptor tyrosine kinase (or its phosphorylated docking protein), which is the definition of transmembrane receptor protein tyrosine kinase adaptor activity. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:9346925 induced recruitment of the Grb2.HPK1 complex to the autophosphorylated EGF receptor and to the Shc docking protein file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0005515 protein binding | IPI PMID:9447984 Regulation of Sos activity by intramolecular interactions. | REMOVE | Summary: GRB2 interaction with SOS1 (Q07889): intramolecular regulation of hSos1 catalytic activity; the cached abstract does not describe the GRB2 interaction. Reason: The cited study (intramolecular regulation of hSos1 catalytic activity; the cached abstract does not describe the GRB2 interaction) does not establish a specific GRB2 molecular activity toward SOS1 beyond physical association. SOS coupling by GRB2 is captured by the GO:0005091 guanyl-nucleotide exchange factor adaptor activity rows (IDA, IEA) and by MODIFY proposals on small-scale SOS studies in this review. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9447984 The guanine nucleotide exchange factor Sos mediates the coupling of receptor tyrosine kinases to Ras activation file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9489702 LAT: the ZAP-70 tyrosine kinase substrate that links T cell ... | MODIFY | Summary: GRB2 interaction with LAT (O43561): LAT, phosphorylated by ZAP-70/Syk, recruits GRB2 and other SH2 proteins. Reason: The study shows that GRB2 binding to LAT depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9489702 this protein is phosphorylated by ZAP-70/Syk protein tyrosine kinases leading to recruitment of multiple signaling molecules file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9544989 Shc phosphotyrosine-binding domain dominantly interacts with... | MODIFY | Summary: GRB2 interaction with SHC1 (P29353): receptor-bound, tyrosine-phosphorylated Shc recruits the Grb2-Sos complex. Reason: The study shows that GRB2 binding to SHC1 depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9544989 Shc bound to the activated EGF receptor via the PTB domain dominantly interacts with Grb2-Sos complex and plays a major role in the Ras-signaling pathway file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9569023 Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2. | MODIFY | Summary: GRB2 interaction with Dab2 (P98078), Mus musculus protein: Dab2 binds GRB2 SH3 domains via C-terminal proline-rich sequences and competes with Sos. Reason: The study maps the GRB2-Dab2 association to a proline-rich motif of the partner recognised by the GRB2 SH3 domain(s), so proline-rich region binding is the informative MF. GO:0017124 SH3 domain binding is not appropriate: it would describe the partner (which binds GRB2's SH3 domain), not GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:9569023 These data indicate that Dab2 binds to the SH3 domains of Grb2 via its C-terminal proline-rich sequences file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0005515 protein binding | IPI PMID:9569023 Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2. | MODIFY | Summary: GRB2 interaction with SOS1 (Q07889): Dab2 binds GRB2 SH3 domains via C-terminal proline-rich sequences and competes with Sos. Reason: The study places the GRB2-SOS1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. For the Sos partner the paper characterises the Grb2-Sos complex whose disruption by Dab2 is proposed to modulate growth factor/Ras signalling, i.e. GRB2 acting as the SOS adaptor. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:9569023 Dab2 may modulate growth factor/Ras pathways by competing with Sos for binding to Grb2 file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:9569023 Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2. | MODIFY | Summary: GRB2 interaction with Sos1 (Q62245), Mus musculus protein: Dab2 binds GRB2 SH3 domains via C-terminal proline-rich sequences and competes with Sos. Reason: The study places the GRB2-Sos1 complex in receptor-to-Ras coupling (GRB2 SH3 domains recruiting the Ras exchange factor to phosphotyrosine docking sites), which is GRB2's guanyl-nucleotide exchange factor adaptor activity. For the Sos partner the paper characterises the Grb2-Sos complex whose disruption by Dab2 is proposed to modulate growth factor/Ras signalling, i.e. GRB2 acting as the SOS adaptor. Proposed replacements: guanyl-nucleotide exchange factor adaptor activity Supporting Evidence: PMID:9569023 Dab2 may modulate growth factor/Ras pathways by competing with Sos for binding to Grb2 file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0005515 protein binding | IPI PMID:9697839 BLNK: a central linker protein in B cell activation. | MODIFY | Summary: GRB2 interaction with BLNK (Q8WV28): Syk-phosphorylated BLNK provides SH2 docking sites for GRB2. Reason: The study shows that GRB2 binding to BLNK depends on tyrosine phosphorylation of the partner and/or is mediated by the GRB2 SH2 domain, so the informative MF is SH2-mediated phosphotyrosine residue binding rather than bare protein binding. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:9697839 Tyrosine phosphorylation of BLNK by Syk provides docking sites for these SH2-containing effector molecules file:human/GRB2/GRB2-deep-research-falcon.md The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as **pY-x-N-x** motifs. |
| GO:0005515 protein binding | IPI PMID:9788432 The germinal center kinase (GCK)-related protein kinases HPK... | REMOVE | Summary: GRB2 interaction with MAP4K5 (Q9Y4K4): HPK1 and KHS bind Crk-family SH3 domains; the abstract states KHS (MAP4K5, the WITH/FROM partner) bound exclusively to Crk-family proteins. Reason: The cited study (HPK1 and KHS bind Crk-family SH3 domains; the abstract states KHS (MAP4K5, the WITH/FROM partner) bound exclusively to Crk-family proteins) does not establish a specific GRB2 molecular activity toward MAP4K5 beyond physical association. MAP4K5 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9788432 While KHS bound exclusively to Crk family proteins, HPK1 also interacted with both SH3 domains of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005515 protein binding | IPI PMID:9922133 Dual function C-terminal domain of dynamin-1: modulation of ... | REMOVE | Summary: GRB2 interaction with DNM1 (Q05193): dynamin C-terminal proline motifs bind SH3 proteins and regulate self-assembly; GRB2 is one of the SH3 probes. Reason: The cited study (dynamin C-terminal proline motifs bind SH3 proteins and regulate self-assembly; GRB2 is one of the SH3 probes) does not establish a specific GRB2 molecular activity toward DNM1 beyond physical association. DNM1 is a known ligand of the GRB2 SH3 domains; where the proline-rich binding motif is mapped in a small-scale study this review proposes GO:0070064 proline-rich region binding instead. Removal does not mean the reported interaction is false; the bare protein binding term simply carries no functional information about GRB2. Supporting Evidence: PMID:9922133 Receptor endocytosis is modulated by SH3 (src homology 3) domain proteins, which directly bind to dynamin C-terminal proline motif sequences file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0005634 nucleus | EXP PMID:37328606 Regulation of microRNA expression by the adaptor protein GRB... | KEEP AS NON CORE | Summary: A nuclear pool of GRB2 was reported in the study describing a GRB2-AGO2-DICER1 complex regulating miRNA biogenesis. Reason: Nuclear GRB2 is reported in several contexts (miRNA biogenesis, replication-fork protection) but GRB2's principal signalling function is at the plasma membrane/cytosol; kept as a secondary localization. Supporting Evidence: file:human/GRB2/GRB2-uniprot.txt Nucleus file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0005634 nucleus | IDA PMID:21179510 Histidine domain-protein tyrosine phosphatase interacts with... | KEEP AS NON CORE | Summary: Immunocytochemistry in the HD-PTP study detected GRB2 in the nucleus as well as cytoplasm and endosomes. Reason: Secondary, context-dependent nuclear pool; not where GRB2's core adaptor function is exerted. Non-core. Supporting Evidence: PMID:21179510 Co-immunoprecipitation, pull-down and immunocytochemistry experiments confirmed the interactions file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular-location mapping (Nucleus) derived from the experimental reports above. Reason: Consistent with reported nuclear pools; secondary localization. Non-core. Supporting Evidence: file:human/GRB2/GRB2-uniprot.txt Nucleus file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0005654 nucleoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic inference of nucleoplasm activity for GRB2-clade proteins. Reason: The node (PANTHER:PTN005273574 (GRB2 clade of PTHR46037)) is seeded here by GRAP2/GADS (UniProtKB:O75791); nuclear GRB2 is documented experimentally (PMID:37328606, PMID:21179510), so the transfer is not contradicted, but the nucleoplasm is a secondary site relative to receptor-proximal membrane signalling. Non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. file:human/GRB2/GRB2-uniprot.txt Nucleus |
| GO:0005737 cytoplasm | EXP PMID:30282717 The 11-Kilodalton Nonstructural Protein of Human Parvovirus ... | KEEP AS NON CORE | Summary: GRB2 detected predominantly in the cytoplasm in the study of parvovirus B19 11-kDa protein binding GRB2. Reason: Correct but less specific than cytosol (GO:0005829), where the soluble pool of GRB2 resides before recruitment to membranes; retained as a broader, non-core localization. Supporting Evidence: PMID:30282717 interacting with a host protein that is predominately expressed in the cytoplasm file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. file:human/GRB2/GRB2-uniprot.txt Cytoplasm |
| GO:0005737 cytoplasm | EXP PMID:37328606 Regulation of microRNA expression by the adaptor protein GRB... | KEEP AS NON CORE | Summary: GRB2 detected in the cytoplasm (and nucleus) in the GRB2-AGO2 miRNA biogenesis study. Reason: Correct but less specific than cytosol (GO:0005829), where the soluble pool of GRB2 resides before recruitment to membranes; retained as a broader, non-core localization. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. file:human/GRB2/GRB2-uniprot.txt Cytoplasm |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic inference that GRB2-clade adaptors are active in the cytoplasm. Reason: Sound transfer at PANTHER:PTN005273574 (GRB2 clade of PTHR46037) (seeds include mouse Grb2 and human GRB2 themselves), but cytoplasm is less specific than the cytosol and plasma-membrane locations where the adaptor acts; non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005737 cytoplasm | IDA PMID:21179510 Histidine domain-protein tyrosine phosphatase interacts with... | KEEP AS NON CORE | Summary: GRB2 detected in the cytoplasm by immunocytochemistry in the HD-PTP interaction study. Reason: Correct but less specific than cytosol (GO:0005829), where the soluble pool of GRB2 resides before recruitment to membranes; retained as a broader, non-core localization. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. file:human/GRB2/GRB2-uniprot.txt Cytoplasm |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Combined automated cytoplasm annotation from ortholog and subcellular-location mapping. Reason: Correct but less specific than cytosol (GO:0005829), where the soluble pool of GRB2 resides before recruitment to membranes; retained as a broader, non-core localization. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. file:human/GRB2/GRB2-uniprot.txt Cytoplasm |
| GO:0005768 endosome | IDA PMID:21179510 Histidine domain-protein tyrosine phosphatase interacts with... | KEEP AS NON CORE | Summary: GRB2 detected on endosomes together with HD-PTP (PTPN23), an ESCRT-associated phosphatase. Reason: GRB2 accompanies activated EGFR into endosomes and participates in Cbl-dependent receptor trafficking; endosomal localization is real but secondary to its plasma-membrane signalling role. Non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. file:human/GRB2/GRB2-uniprot.txt Endosome |
| GO:0005768 endosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular-location mapping (Endosome). Reason: Consistent with endosomal GRB2 in receptor trafficking; non-core. Supporting Evidence: file:human/GRB2/GRB2-uniprot.txt Endosome file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular-location mapping (Golgi apparatus), itself based on similarity to mouse Grb2. Reason: GRB2 relocalises with PLD2 to perinuclear Golgi-like structures after EGF stimulation (PMID:17276458); a context-specific, secondary location. Non-core. Supporting Evidence: PMID:17276458 Grb2 serves to hijack PLD2 to the perinuclear Golgi region through its SH2 domain file:human/GRB2/GRB2-uniprot.txt Golgi apparatus |
| GO:0005794 Golgi apparatus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Golgi apparatus localization transferred by sequence similarity from mouse Grb2. Reason: Human GRB2 itself co-localizes with PLD2 in the perinuclear Golgi region of HUVEC after EGF (PMID:17276458); secondary, context-dependent location. Non-core. Supporting Evidence: PMID:17276458 Grb2 serves to hijack PLD2 to the perinuclear Golgi region through its SH2 domain |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Human Protein Atlas immunofluorescence places GRB2 in the cytosol. Reason: GRB2 is a soluble protein that resides in the cytosol (often pre-complexed with SOS) before recruitment to activated receptors; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA machine-learning annotation to cytosol. Reason: Consistent with the experimentally established cytosolic pool of GRB2; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS PMID:14722116 The importance of three membrane-distal tyrosines in the ada... | ACCEPT | Summary: Cytosol (TAS) from the NTAL/LAB tyrosine-mapping study, in which phosphorylated LAB recruits GRB2 from the cytoplasm to the membrane adaptor. Reason: GRB2 is a soluble cytosolic adaptor recruited to phosphorylated transmembrane adaptors such as LAB/NTAL; the cytosolic assignment is correct. Core location. Supporting Evidence: PMID:14722116 Upon engagement of the B cell receptor or Fc receptors, it is phosphorylated and interacts with Grb2 file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109699 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K-containing complexes phosphorylate PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109813 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1 binds SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109822 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'MAPK3,(MAPK1) phosphorylates GRB2-1:SOS1:p-Y427-SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109823 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'MAPK3,(MAPK1) phosphorylates GRB2-1:SOS1:p-Y-IRS1,p-Y-IRS2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225950 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2:SOS1 complex to phosphorylated ligand-responsive EGFR mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225951 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with ligand-responsive p-6Y-EGFR mutants)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225957 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and ligand-responsive p-6Y-EGFR mutants)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225961 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated SHC1 in complex with ligand-responsive p-6Y-EGFR mutants recruits GRB2:SOS1 complex'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226012 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of PI3K to complex of GRB2:GAB1 and ligand-responsive p-6Y-EGFR mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226014 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Conversion of PIP2 to PIP3 by PI3K bound to ligand-responsive p-6Y-EGFR mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226016 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2:GAB1 complex to ligand-responsive p-6Y-EGFR mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250380 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2:SOS1 to phosphorylated SHC1 in complex with phosphorylated ERBB4 homodimers'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250383 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-Y349,350-SHC1:p-ERBB4'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1295613 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SPRY2 binds GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306957 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PIP2 to PIP3 conversion by PI3K bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306963 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2:GAB1 to p-ERBB2:p-EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of PI3K to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306969 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 complex binds phosphorylated ERBB4:ERBB2 heterodimers'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306972 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl nucleotide exchange mediated by SOS1 bound to GRB2 in complex with phosphorylated ERBB4:ERBB2 heterodimers'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1433428 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2 is indirectly recruited to p-KIT through SHP2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1433454 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of GAB2 by SFKs'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1433471 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of RAS by p-KIT bound SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1433514 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Synthesis of PIP3 from PIP2 by PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1549564 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PPTN11 dephosphorylates SPRY2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1562641 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Indirect recruitment of PI3K to KIT via p(Y)-GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177920 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2 to GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177923 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Sustained activation of SRC kinase by SHP2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177924 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Dephosphorylation of Gab1 by SHP2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177926 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Dephosphorylation of PAG by SHP2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177927 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K binds to EGF:EGFR:GRB2:GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177930 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GAB1 phosphorylation by EGFR kinase'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177931 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of PIK3 regulatory alpha subunit to GRB2:GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177935 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SHP2 dephosphorylates Tyr 992 on EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177936 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 binds to phosphorylated SHC1 in complex with EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177938 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:GRB2:SOS1)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177939 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K converts phosphatidylinositol-4,5-bisphosphate (PIP2) to phosphatidylinositol-3,4,5-trisphosphate (PIP3)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177941 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:GAB1 binds to phosphorylated EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177943 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 complex binds to EGF:EGFR complex'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177944 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of SHP2 through the binding to phospho-Gab1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177945 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:SHC1:GRB2:SOS1)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-179467 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GAB1 binds phosphatidylinositol-3,4,5-trisphosphate'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-182994 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Assembly of EGFR complex in clathrin-coated vesicles'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183002 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Beta-Pix:CDC42:GTP binds CBL in EGF:p-6Y-EGFR:CBL:CIN85'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183036 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Ubiquitination of stimulated EGFR (CBL:GRB2)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183052 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL binds to GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183058 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of CBL (EGFR:GRB2:CBL)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183067 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Localization of CBL:GRB2 to the membrane'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-183084 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL escapes CDC42-mediated inhibition by down-regulating the adaptor molecule Beta-Pix'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839095 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-BCR-pFGFR1 binds GRB2:GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839102 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'BCR-FGFR1 fusion:GRB2:p-GAB2:PIK3R1 binds PIK3CA '. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839107 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'BCR-FGFR1-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839110 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-BCR-p-FGFR1 phosphorylates GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839114 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'BCR-FGFR1:GRB2:p-GAB2 binds PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-186826 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 complex binds to the active receptor'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-186834 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange on RAS (PDGF receptor:GRB2:SOS)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029466 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway '(WASPs, WAVE):G-actin:ARP2/3 binds F-actin'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-204871 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Interaction of Tie2 and Grb2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-205234 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Indirect recruitment of GAB2 to p-KIT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-205244 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of CBL to KIT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-205286 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS interacts with p-KIT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-210974 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Interaction of SOS-1 to Tie2 bound Grb2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-210977 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Sos-mediated nucleotide exchange of Ras (Tie2 receptor:Grb2:Sos)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2179407 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS1-mediated nucleotide exchange of RAS (HB-EFG-initiated)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2179415 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 binds to HBEGF:p-Y-EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2197690 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Detachment of WASP/WAVE'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2197691 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'WIP binds WASP,N-WASP, activating them'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2197698 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Src phosphorylate WASP,N-WASP'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396561 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GADS:SLP-76 to p-5Y-LAT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396594 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of SLP-76 by p-SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396599 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2:SOS to p-5Y-LAT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396606 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of PLC-gamma to SLP-76 and p-5Y-LAT'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K inhibitors block PI3K catalytic activity'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424476 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of RAC1 by VAV2/3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424477 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS mediated nucleotide exchange of RAS (SHC)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424481 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of VAV and BTK to p-SLP-76'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424484 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of BTK by p-SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424485 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Release of p-PLCG1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424486 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation and activation of VAV2/VAV3 by SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424487 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of PLC-gamma by p-BTK/p-SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730833 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of TEC kinases by p-SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730837 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2:SOS to p-10Y-NTAL'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730840 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of RAC1 by VAV'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730841 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation and activation of VAV'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730842 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K associates with phosphorylated GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730844 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Interaction of GRB2:SOS complex with p-SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730847 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Hydrolysis of PIP2 by PLCG'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730851 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of SLP-76 by p-SYK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730856 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Autophosphorylation of PAK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730858 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Autophosphorylation of BTK/ITK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730870 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylation of PIP2 to PIP3 by PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730889 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of PAK to the membrane by binding active RAC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730892 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of VAV to p-SLP-76'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-354087 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2 to p-PTK2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-354165 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Interaction of SOS with GRB2 bound to FADK1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-388814 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Grb2 binds CD28'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389348 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of Rac1 by pVav1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389350 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of Cdc42 by pVav1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389352 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Translocation of Vav1 to CD28'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389354 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activation of Vav1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389919 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Grb2 binds pBTLA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-391153 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-4Y-SIRPA:CD47 binds GRB2-1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392051 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of Grb2 to pFAK:NCAM1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392053 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS binds Grb2 bound to pFAK:NCAM1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392054 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'NCAM1:pFAK:Grb2:Sos-mediated nucleotide exchange of Ras'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-453104 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated SHC1 recruits GRB2:GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-453111 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated SHC recruits GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-508247 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Gab2 binds the p85 subunit of Class 1A PI3 kinases'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637764 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2:GAB1 complex to p-EGFRvIII mutant'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637765 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of PI3K to complex of GRB2:GAB1 and p-EGFRvIII'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637770 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Binding of GRB2:SOS1 complex to phosphorylated EGFRvIII'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637798 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated SHC1 in complex with p-5Y-EGFRvIII recruits GRB2:SOS1 complex'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637801 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Conversion of PIP2 to PIP3 by PI3K bound to phosphorylated EGFRvIII'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637806 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with p-EGFRvIII)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637808 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654392 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654402 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654406 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-SHC1 binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654413 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654416 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:pFRS binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654423 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-SHC1 binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654426 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654586 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654591 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS2:GRB2:GAB1:PI3KR1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654592 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654594 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS2:p-PPTN11 binds GRB2:GAB1:PI3KR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654596 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-FRS2:p-PPTN11:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654597 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-SHC1 binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654600 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654612 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654614 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-FRS2:GRB2:GAB1:PI3KR1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654615 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:pFRS binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654618 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654620 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-FRS2:p-PPTN11 binds GRB2:GAB1:PI3KR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654622 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2:p-FRS2:p-PPTN11:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654637 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654640 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-FRS2:GRB2:GAB1:PI3KR1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654641 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-FRS2:p-PPTN11 binds GRB2:GAB1:PI3KR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654643 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-FRS2:p-PPTN11:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654646 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-SHC1 binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654647 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654659 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654662 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS2:GRB2:GAB1:PI3KR1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654663 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654664 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS binds GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654667 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS2:p-PPTN11 binds GRB2:GAB1:PI3KR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654669 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4:p-FRS2:p-PPTN11:GRB2:GAB1:PIK3R1binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654672 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL ubiquitinates FRS2 and FGFR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654673 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-CBL:GRB2 binds p-FRS2:activated FGFR1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654677 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL ubiquitinates FRS2 and FGFR2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654679 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL ubiquitinates FRS2 and FGFR3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654684 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL ubiquitinates FRS2 and FGFR4'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654690 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR1-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654692 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR1- and PTPN11- associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654697 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR2- and PTPN11- associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654701 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR2-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654705 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR3-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654709 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR3- and PTPN11-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654714 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR4- and PTPN11-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654717 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FGFR4-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654729 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-CBL:GRB2 binds p-FRS2:activated FGFR2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654730 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-CBL:GRB2 binds p-FRS2:activated FGFR3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654734 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-CBL:GRB2 binds p-FRS2:activated FGFR4'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655233 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2 mutants:p-FRS2 binds GRB2-SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655235 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4 mutant-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655240 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1 mutants:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655241 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655245 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2 mutants:p-FRS2:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655248 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4 mutants:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655252 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4 mutants:p-FRS2:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655263 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1 mutants:p-FRS2:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655266 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1 mutants:p-FRS2 binds GRB2-SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655277 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3 point, translocation and fusion mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655285 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3 point, translocation and fusion mutants:p-FRS2:GRB2:GAB1:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655289 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3 point, translocation and fusion mutant-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655290 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1 mutant-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655295 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3 point, translocation and fusion mutants:p-FRS2 binds GRB2-SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655315 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR3 point, translocation and fusion mutants:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655320 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2 mutants:p-FRS2 binds GRB2:GAB1:PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655323 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR2 mutant-associated PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655326 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR1 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655347 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655348 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated FGFR4 mutants:p-FRS2 binds GRB2-SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS GEFs promote RAS nucleotide exchange'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5685366 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1:SOS1 binds p-Y-SHC'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5686073 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1:SOS1 binds p-3Y-SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5686074 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1:p-4S-SOS1:p-Y427-SHC1 dissociates'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5686315 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:p-4S-SOS1:p-Y-IRS1,p-Y-IRS2 dissociates'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-74736 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1:SOS1 binds p-IRS1,p-IRS2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-74746 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2-1:SOS1 binds p-Y427-SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-879917 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL, GRB2, FYN and PI3K p85 subunit are constitutively associated'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851804 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated MET recruits GRB2-1:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851827 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl nucleotide exchange by MET-bound GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851899 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl nucleotide exchange by SOS1 bound to GRB2, SCH1-2 and MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851900 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SHC1-2 bound to MET recruits GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851919 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Activated MET binds GAB1 and GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851933 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'MET phosphorylates GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851954 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated GAB1 recruits PI3K to MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8852019 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'MET bound PI3K generates PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853734 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway '2x p-5Y-RET:GDNF:GFRA complexes:p-Y349,Y350,Y427-SHC1 binds GRB2-1:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853774 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GAB in p-5Y-RET:GDNF:GFRA complexes is phosphorylated'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853793 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-5Y-RET complexes bind GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854897 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-5Y-RET-GRB2-containing complexes bind GAB1,GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854899 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway '2x p-5Y-RET:GDNF:GFRA complexes bind GRB2-1:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854905 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-5Y-GAB in the RET-GRB2-GAB complexes binds p85-PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8855508 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-5Y-GAB in RET-GRB2-GAB complexes binds PTPN11'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8865994 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GAB1 binds PTPN11'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8866279 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Epsin family proteins bind ubiquitinated cargo'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867041 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'EGFR phosphorylates EPS15'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867044 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'EGFR binds EPS15, EPN1, EPS15L1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867047 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PTPN3 dephosphorylates EPS15'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867754 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'F- and N- BAR domain proteins bind the clathrin-coated pit'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867756 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CLASP proteins and cargo are recruited to the nascent clathrin-coated pit'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868071 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Clathrin recruits PIK3C2A'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868072 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Clathrin-associated PIK3C2A phosphorylates PI(4)P to PI(3,4)P2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868230 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SNX9 recruits components of the actin polymerizing machinery'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868236 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'BAR domain proteins recruit dynamin'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868648 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SYNJ hydrolyze PI(4,5)P2 to PI(4)P'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868651 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Endophilins recruit synaptojanins to the clathrin-coated pit'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868658 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'HSPA8-mediated ATP hydrolysis promotes vesicle uncoating'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868659 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Clathrin recruits auxilins to the clathrin-coated vesicle'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868660 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Dynamin-mediated GTP hydrolysis promotes vesicle scission'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8869438 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Dissociation of clathrin-associated proteins'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8871193 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Dissociation of AAK1 and dephosphorylation of AP-2 mu2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8871194 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAB5 and GAPVD1 bind AP-2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8874685 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL binds MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875183 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL monoubiquitinates activated MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875451 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'MET phosphorylates CBL'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875482 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL recruits CIN85:endophilin to ubiquitinated MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875490 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'EPS15 and HGS bind ubiquitinated MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875540 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GAB1 recruits CRK,CRKL to MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875558 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAPGEF1 binds CRK,CRKL'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875568 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAPGEF1 activates RAP1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875576 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CRK,CRKL recruits RAC1 GEF to activated MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875591 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'DOCK7 activates RAC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875659 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAB4:GTP promotes recycling of activated MET receptor to the plasma membrane'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8875661 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GGA3 associates with activated MET receptor'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8876240 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL binds InlB-activated MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8876258 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL monoubiquitinates InlB-bound MET'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8951490 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CIN85 dissociates from EGF:p-6Y-EGFR:CBL:Beta-Pix:CDC42:GTP:CIN85'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8983384 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'IL15:IL15RA:p-Y-IL2RB:p-Y-JAK1:p-Y-IL2RG:p-Y-JAK3:p-Y-SHC1:GRB2 binds SOS1,SOS2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9018766 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RHOU binds effectors at the plasma membrane'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9029150 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:VAV1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9032073 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'NTRK2-phosphorylated FRS2 binds GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-912527 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SHC1 mediates cytokine-induced phosphorylation of GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-912627 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'CBL ubiquitinates PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-913424 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'The SHC1:SHIP1 complex is stabilized by GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9606887 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-CD19:VAV binds PI3K and GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9607301 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Active FLT3:GRB2 binds SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9607304 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS1-mediated nucleotide exchange of RAS downstream of FLT3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9634402 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 homodimer'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9634418 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664918 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664933 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664940 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664983 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664991 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665000 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665009 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665404 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665407 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665408 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665409 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665413 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665415 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665417 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665698 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665699 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665700 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665707 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9670428 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'KIT mutants bind GRB2-SOS'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9670436 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-KIT mutants:GRB2:SOS catalyzes nucleotide exchange on RAS'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672158 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 complex binds to PDGFRA extracellular domain dimers'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672163 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange on RAS downstream of PDGFRA extracellular domain dimers'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672164 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'GRB2:SOS1 complex binds to mutant PDGFR receptor'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672170 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS-mediated nucleotide exchange of RAS downstream of mutant PDGFR receptors'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9674816 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-Y546,Y584-PTPN11 (in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:SHC:GRB2:PTPN11) dephosphorylates KRAS'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9695841 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutant dimers bind GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9695845 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutant dimers:GRB2 bind SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9695853 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutants:GRB2:SOS1-mediated nucleotide exchange on RAS'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698000 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutants:GRB2 bind GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698003 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutants phosphorylate GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698005 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 ITD mutants phosphorylate STAT5'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698007 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 ITD mutants bind STAT5 through GAB2:PTPN11'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698008 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutants:GRB2:p-Y-GAB2 binds PTPN11'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698013 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'PTPN11:p-STAT5 dissociates from mutant FLT3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698029 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-STAT5 dissociates from mutant FLT3'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698170 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Active FLT3:GRB2:p-GAB2:PIK3R1 binds PIK3CA'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698174 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 mutants recruit PIK3CA through PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9703430 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 fusions:GRB2 bind SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9703434 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 fusions recruit PIK3CA through PIK3R1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9703438 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'FLT3 fusions phosphorylate GAB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9703441 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'SOS1-mediated nucleotide exchange of RAS downstream of FLT3 fusion mutants'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9710914 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'ALK fusions bind GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9724099 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'ALK mutants:p-3Y SHC binds GRB2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983703 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'p-6Y-SYK phosphorylates BLNK (SLP65)'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9842655 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'IRS1 recruits GRB2 to active LTK'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9842665 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Active LTK binds GRB2:TNK2'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9842669 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Active LTK recruits GRB2:SOS1'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-1250468 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Ras guanyl-nucleotide exchange mediated by Sos1 in complex with GRB2 and P-Erbb2mut'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-1250472 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Ras guanyl-nucleotide exchange mediated by Sos1 bound to GRB2 in complex with P-Shc1:P-Erbb2mut'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-1250475 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Direct recruitment of GRB2:Sos1 to P-Erbb2mut dimer'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-1250500 | ACCEPT | Summary: Reactome places GRB2 (or a GRB2-containing complex) in the cytosol in the reaction/pathway 'Recruitment of GRB2:Sos1 to P-Shc1:P-Erbb2mut complex'. Reason: GRB2 is a soluble cytosolic adaptor that is recruited from the cytosol to activated receptors; Reactome's cytosolic compartment assignment for this GRB2 entity is consistent. Core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: GRB2-clade adaptors act at the plasma membrane, where they are recruited to activated receptors and scaffolds. Reason: Sound phylogenetic transfer at PANTHER:PTN005273574 (GRB2 clade of PTHR46037); the plasma membrane is the principal site of GRB2-SOS-Ras coupling. Core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer from mouse Grb2 of plasma membrane localization. Reason: Consistent with receptor-induced recruitment of GRB2 to the inner plasma membrane; core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1112666 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'BLNK (SLP-65) Signalosome hydrolyzes phosphatidyinositol bisphosphate forming diacylglycerol and inositol-1,4,5-trisphosphate'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2076220 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'CD19 Signalosome phosphorylates PI(4,5)P2 forming PI(3,4,5)P3'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'PI3K phosphorylates PIP2 to PIP3'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'PI3K inhibitors block PI3K catalytic activity'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9606151 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'Phosphorylated BLNK (SLP65, in Antigen:p-BCR:p-SYK:p-BLNK:CIN85:GRB2:SOS1) binds BTK, PLCG2, VAV1, NCK1'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9606887 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'p-CD19:VAV binds PI3K and GRB2'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9691421 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'BTK binds BTK inhibitors'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-983703 | ACCEPT | Summary: Reactome places GRB2 at the plasma membrane in 'p-6Y-SYK phosphorylates BLNK (SLP65)'. Reason: GRB2 is recruited to the cytoplasmic face of the plasma membrane by activated receptors and transmembrane adaptors, where it acts; core location. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0005911 cell-cell junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of cell-cell junction localization. Reason: Mouse Grb2 has experimental cell-cell junction localization; plausible as a site of receptor/adhesion signalling but not the defining location. Non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0005938 cell cortex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of cell cortex activity. Reason: Reflects cortical recruitment of GRB2 in actin/adhesion signalling (e.g. N-WASP-dependent processes); plausible but secondary. Non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0007165 signal transduction | IBA GO_REF:0000033 | MODIFY | Summary: The bare 'signal transduction' is correct but too broad; GRB2's conserved role is coupling activated receptor tyrosine kinases to Ras through SOS. Reason: Sound phylogenetic transfer at PANTHER:PTN005273574 (GRB2 clade of PTHR46037) (seeds: fly drk, worm sem-5, mouse, rat and human GRB2, all of which couple RTKs to Ras). The more informative child GO:0007265 Ras protein signal transduction captures the ancestral function; consistent with the mouse Grb2 review. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN005273574 SUPPORTS TRANSFER GRB2-clade node of PTHR46037; seeds are GRB2 orthologs (fly drk FB:FBgn0004638, worm sem-5 WB:WBGene00004774, mouse, rat and human GRB2), all of which couple receptor tyrosine kinases to Ras. The transfer is sound; only the term is broader than the conserved function, so the child GO:0007265 is proposed. UniProtKB:P62993 Β· GRB2 SUPPORTS TRANSFER The target itself as an IBD seed: human GRB2 has direct experimental evidence for EGFR signalling and Ras coupling (PMID:8386805, PMID:8253073), which is expected grounding for the node, not circularity. Proposed replacements: Ras protein signal transduction Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. PMID:1322798 These results suggest that GRB2/sem-5 plays a crucial role in a highly conserved mechanism for growth factor control of ras signaling |
| GO:0007173 epidermal growth factor receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer from mouse Grb2 of EGF receptor signaling pathway. Reason: GRB2 is a direct, necessary adaptor of EGFR signalling (binds EGFR pY1068/1086 and recruits SOS); core process. Supporting Evidence: PMID:7518560 Grb2 binds directly to the EGFR at Y-1068, to a lesser extent at Y-1086, and indirectly at Y-1173 |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:8253073 Ash/Grb-2, a SH2/SH3-containing protein, couples to signalin... | ACCEPT | Summary: Microinjection of anti-Ash/GRB2 antibody abolished EGF- and PDGF-induced S-phase entry and membrane ruffling; GRB2 co-precipitated with the EGF receptor. Reason: GRB2 performs a step of EGFR signalling (receptor-to-Ras/Rac coupling as an SH2/SH3 linker), not merely being required for it. Core. Supporting Evidence: PMID:8253073 the findings strongly suggest that Ash plays a critical role in the signaling of both pathways downstream from growth factor receptors to Ras and Rac |
| GO:0007173 epidermal growth factor receptor signaling pathway | TAS PMID:1322798 The SH2 and SH3 domain-containing protein GRB2 links recepto... | ACCEPT | Summary: The GRB2 cloning paper showing SH2-mediated association with tyrosine-phosphorylated EGF and PDGF receptors and cooperation with Ras in mitogenesis. Reason: Founding evidence for GRB2 in EGFR signalling; core. Supporting Evidence: PMID:1322798 GRB2 associates with tyrosine-phosphorylated epidermal growth factor receptors (EGFRs) and platelet-derived growth factor receptors (PDGFRs) via its SH2 domain |
| GO:0007265 Ras protein signal transduction | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA annotation to Ras protein signal transduction. Reason: GRB2 is the canonical adaptor linking receptors to Ras via SOS; core process. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. file:human/GRB2/GRB2-deep-research-falcon.md RAS-GTP activates the RAFβMEKβERK cascade |
| GO:0007265 Ras protein signal transduction | TAS PMID:8253073 Ash/Grb-2, a SH2/SH3-containing protein, couples to signalin... | ACCEPT | Summary: GRB2/Ash antibody microinjection blocks growth-factor-induced Ras-dependent S-phase entry; GRB2 described as a linker to Ras. Reason: Core process of GRB2. Supporting Evidence: PMID:8253073 suggesting a role of Ash as a linker molecule in signal transduction downstream of growth factor receptors |
| GO:0008180 COP9 signalosome | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetic transfer of COP9 signalosome membership among GRB2 orthologs. Reason: The WITH/FROM is only mouse Grb2 and human GRB2 at PANTHER:PTN005273574 (GRB2 clade of PTHR46037); no CSN subunit family is involved, so the propagation is faithful but the source assertion is over-scoped. GRB2 is a 25 kDa SH3-SH2-SH3 adaptor, not one of the eight canonical CSN subunits (COPS1-COPS8), so a part_of COP9 signalosome assertion over-states what is documented (association), and says nothing about GRB2's adaptor function. Handled as over-annotation, consistent with the mouse Grb2 review; not removed because the source is experimental (IDA) and its full text is not available here. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: ROLE CONFLATION Sources checked: PANTHER:PTN005273574 SUPPORTS TRANSFER WITH/FROM is only mouse Grb2 (MGI:MGI:95805) and human GRB2 at the GRB2-clade node; no COP9 signalosome subunit family is involved, so the propagation step is a faithful ortholog transfer. The reservation is the scope of the source assertion (part_of the CSN for an adaptor that is at most associated). MGI:MGI:95805 Β· Grb2 SUPPORTS TRANSFER Mouse Grb2 carries its own IDA for GO:0008180 (PMID:22561606, a Tespa1/TCR-signalosome study, abstract only); handled as over-annotation in the mouse review for the same reason. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0008180 COP9 signalosome | IDA PMID:22561606 Tespa1 is involved in late thymocyte development through the... | MARK AS OVER ANNOTATED | Summary: IDA from the Tespa1 thymocyte-development study, which reports Tespa1 association with PLC-gamma1 and GRB2 in the TCR signalosome. Reason: The cached abstract describes Tespa1 as a TCR-signalosome component associating with GRB2, not GRB2 as a COP9 signalosome subunit. GRB2 is a 25 kDa SH3-SH2-SH3 adaptor, not one of the eight canonical CSN subunits (COPS1-COPS8), so a part_of COP9 signalosome assertion over-states what is documented (association), and says nothing about GRB2's adaptor function. Handled as over-annotation, consistent with the mouse Grb2 review; not removed because the source is experimental (IDA) and its full text is not available here. Supporting Evidence: PMID:22561606 Tespa1 associated with the TCR signaling components PLC-Ξ³1 and Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0008180 COP9 signalosome | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara transfer of COP9 signalosome from mouse Grb2. Reason: GRB2 is a 25 kDa SH3-SH2-SH3 adaptor, not one of the eight canonical CSN subunits (COPS1-COPS8), so a part_of COP9 signalosome assertion over-states what is documented (association), and says nothing about GRB2's adaptor function. Handled as over-annotation, consistent with the mouse Grb2 review; not removed because the source is experimental (IDA) and its full text is not available here. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0008286 insulin receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of insulin receptor signaling pathway. Reason: GRB2 binds insulin-stimulated tyrosine-phosphorylated IRS-1 and Shc and links them to Ras; a genuine but receptor-specific instance of its general RTK adaptor function. Non-core (consistent with mouse review). Supporting Evidence: PMID:8491186 mediated by the binding of the SH2 domain of GRB2 to phosphotyrosines on both IRS-1 and Shc |
| GO:0008286 insulin receptor signaling pathway | IPI PMID:8388384 Insulin stimulates association of insulin receptor substrate... | KEEP AS NON CORE | Summary: Insulin stimulates formation of an IRS-1/ASH(GRB2) complex; GRB2 binds tyrosine-phosphorylated IRS-1 directly (WITH/FROM P35568). Reason: Supports GRB2 participation in insulin receptor signalling as the IRS-1-to-Ras adaptor; receptor-specific instance of the core RTK adaptor function, kept as non-core. Supporting Evidence: PMID:8388384 These data suggest that IRS-1.ASH complex formation may play a role in coupling the insulin receptor kinase to a Ras signaling pathway |
| GO:0012506 vesicle membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of vesicle membrane. Reason: Consistent with GRB2 accompanying receptors into endocytic vesicles; secondary location. Non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. |
| GO:0014044 Schwann cell development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 (IMP) of Schwann cell development. Reason: A developmental consequence of GRB2's role in ErbB/neuregulin receptor signalling in mouse; pleiotropic, non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0016020 membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of membrane localization. Reason: Correct but uninformative parent of the plasma membrane, endosome and vesicle membrane locations; non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Upon receptor phosphorylation it becomes enriched at the **cytoplasmic face of the plasma membrane**, where it forms transient RTKβGRB2βSOS assemblies or larger two-dimensional signaling clusters. |
| GO:0017124 SH3 domain binding | IDA PMID:19509291 GAREM, a novel adaptor protein for growth factor receptor-bo... | MODIFY | Summary: GAREM1 proline-rich motifs are recognised by both GRB2 SH3 domains (IDA). Reason: SH3 domain binding (GO:0017124) describes a protein that binds an SH3 domain; here GRB2 contributes the SH3 domains and binds the proline-rich motifs of GAREM1, so the annotation has the direction reversed. The evidence supports GO:0070064 proline-rich region binding for GRB2. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:19509291 the proline-rich motifs of GAREM are recognized by the N- and C-terminal SH3 domains of Grb2 file:human/GRB2/GRB2-deep-research-falcon.md Current reviews summarize N-SH3 preference as **PxxPxR**, whereas C-SH3 favors approximately **PxxxRxxKP/PxxRxxKP** sequences. |
| GO:0019901 protein kinase binding | IPI PMID:20086093 HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regul... | MARK AS OVER ANNOTATED | Summary: IPI with mouse Ack1/Tnk2 (WITH/FROM O54967) from a study of Nedd4-1-mediated ACK ubiquitination and EGFR degradation. Reason: The cached abstract does not describe the GRB2 measurement; the interaction is plausible (ACK1 is an SH3 ligand of GRB2 and is found in GRB2 complexes in interactome studies) but 'protein kinase binding' is uninformative about GRB2's activity. Not removed because the full text (which the curator read) is not available here; over-annotation, consistent with the mouse review. Supporting Evidence: PMID:20086093 Our findings suggest an essential role of Nedd4-1 in regulation of EGFR degradation through interaction with and ubiquitination of ACK file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0019903 protein phosphatase binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara transfer from mouse Grb2 of protein phosphatase binding. Reason: GRB2 binds several phosphatases (SHP2 via pTyr542/580, RPTPalpha pTyr789, PTP-epsilon, Lyp, HD-PTP), but the informative activities are phosphotyrosine binding and proline-rich region binding; 'phosphatase binding' describes the partner class rather than GRB2's function. Supporting Evidence: PMID:7518772 We show that RPTP alpha, but not a mutant of RPTP alpha with a Tyr-->Phe mutation at position 789, bound to GRB2 in vitro |
| GO:0019904 protein domain specific binding | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Combined automated annotation of protein domain specific binding. Reason: GRB2's own domains (SH2, SH3) bind phosphotyrosine and proline-rich linear motifs of partners; it does not characteristically bind a specific domain of its partners, so the term is at best vague. The informative MFs are GO:0001784 and GO:0070064. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0030036 actin cytoskeleton organization | IMP PMID:8253073 Ash/Grb-2, a SH2/SH3-containing protein, couples to signalin... | KEEP AS NON CORE | Summary: Anti-Ash/GRB2 antibody microinjection blocked growth-factor-induced membrane ruffling (acts_upstream_of_or_within actin cytoskeleton organization). Reason: GRB2 acts upstream of Rac-dependent ruffling via SOS; the effect on actin is indirect. Non-core. Supporting Evidence: PMID:8253073 The antibody abolished both S phase entry and the reorganization of actin assembly to ruffle formation upon stimulation with epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:25870599 GRB2 Nucleates T Cell Receptor-Mediated LAT Clusters That Co... | ACCEPT | Summary: GRB2 knockdown in human CD4+ T cells impairs LAT microcluster formation, PLC-gamma1 recruitment and cytokine production; rescue requires the GRB2 N-SH3 domain. Reason: Direct evidence that GRB2 acts as a multivalent adaptor organising LAT signalling clusters (SH2 to pLAT, SH3 to effectors). Core adaptor activity. Supporting Evidence: PMID:25870599 Our data demonstrate that the ability of GRB2 to facilitate protein clusters is equally important in regulating TCR-mediated functions as its capacity to recruit effector proteins |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:7539782 Tyrosine phosphorylation of the proto-oncogene product Vav a... | ACCEPT | Summary: Vav is constitutively associated with GRB2 in UT-7 cells; cytokines induce Vav tyrosine phosphorylation. Reason: Consistent with GRB2's established adaptor function linking tyrosine kinases to exchange factors; the abstract shows association rather than bridging, but the MF is well supported for GRB2 overall and the curator's full-text reading is deferred to. Supporting Evidence: PMID:7539782 These data suggest that tyrosine kinases, the adapter Grb2/Ash, and the guanine nucleotide exchange factor Vav are members of a signaling pathway leading to Ras activation in hematopoietic cells file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0030674 protein-macromolecule adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer from mouse Grb2 of protein-macromolecule adaptor activity. Reason: Correct general adaptor MF for GRB2; core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. |
| GO:0031623 receptor internalization | IMP PMID:14985334 Analysis of clathrin-mediated endocytosis of epidermal growt... | KEEP AS NON CORE | Summary: siRNA screen of endocytic proteins identified GRB2 as specifically required for EGFR (not transferrin receptor) internalization. Reason: GRB2 does part of this work by recruiting Cbl to EGFR (and linking EGFR to Tom1L1/clathrin), so the involvement is genuine; it is a receptor-downregulation role secondary to signal propagation. Non-core (consistent with mouse review). Supporting Evidence: PMID:14985334 Thus, CALM is the second protein besides Grb2 that appears to play a specific role in EGFR endocytosis file:human/GRB2/GRB2-deep-research-falcon.md GRB2 can bind phosphorylated EGFR through SH2 while an SH3 domain engages proline-rich Cbl. |
| GO:0035022 positive regulation of Rac protein signal transduction | IC PMID:16475793 Binding of laminin alpha1-chain LG4-5 domain to alpha-dystro... | KEEP AS NON CORE | Summary: Curator inference from laminin/alpha-dystroglycan signalling: GRB2 binds syntrophin and laminin induces Sos1/2 recruitment and Rac1 activation. Reason: GRB2 recruits SOS, whose Rac-GEF activity drives Rac1 activation in this context; plausible and contextual. Non-core. Supporting Evidence: PMID:16475793 E3 or laminin-1 increase Grb2-binding and Rac1 activation |
| GO:0042110 T cell activation | IDA PMID:7568038 p56Lck and p59Fyn regulate CD28 binding to phosphatidylinosi... | KEEP AS NON CORE | Summary: Lck/Fyn phosphorylation of CD28 Tyr191 (YMNM) induces GRB2 SH2 binding to CD28. Reason: Supports GRB2 recruitment to the CD28 costimulatory receptor; T cell activation is a broad cellular outcome of GRB2's adaptor role in TCR/CD28 signalling. Non-core. Supporting Evidence: PMID:7568038 p56Lck and p59Fyn phosphorylate CD28 primarily at Tyr-191 of the Tyr-Met-Asn-Met motif, inducing a 3- to 8-fold increase in p85 (subunit of PI 3-kinase) and GRB-2 SH2 binding to CD28 |
| GO:0042267 natural killer cell mediated cytotoxicity | IDA PMID:16582911 NKG2D-mediated signaling requires a DAP10-bound Grb2-Vav1 in... | KEEP AS NON CORE | Summary: In human NK cells, a GRB2-Vav1 intermediate binding DAP10 is required with p85 for NKG2D-DAP10-mediated calcium release and cytotoxicity. Reason: GRB2 acts as the adaptor linking DAP10 to Vav1 in NKG2D signalling; genuine but cell-type-specific. Non-core. Supporting Evidence: PMID:16582911 For full calcium release and cytotoxicity to occur, both Grb2-Vav1 and p85 had to bind to DAP10 |
| GO:0042552 myelination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of myelination. Reason: Developmental consequence of GRB2-dependent receptor signalling in mouse Schwann cells; pleiotropic, non-core. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. |
| GO:0042770 signal transduction in response to DNA damage | IMP PMID:20160708 Feedback between p21 and reactive oxygen production is neces... | KEEP AS NON CORE | Summary: GRB2 is one node of a p21-GADD45-p38-GRB2-TGFBR2 feedback loop that maintains DNA damage signalling in senescent cells. Reason: The study combines in-silico interactome analysis with target inhibition to describe a senescence-maintaining DDR-p21-GADD45-p38-GRB2-TGFBR2-ROS loop; GRB2 knockdown affected the loop. The role is context-specific and GRB2's precise activity in the loop is not defined; kept as non-core (consistent with mouse review). Supporting Evidence: PMID:20160708 serial signalling through GADD45-MAPK14(p38MAPK)-GRB2-TGFBR2-TGFbeta |
| GO:0042802 identical protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | MARK AS OVER ANNOTATED | Summary: Endogenous GRB2 recovered in SILAC affinity purification over the GRB2 SH2 domain. Reason: Co-purification with a GRB2 SH2 bait does not by itself establish a defined GRB2 self-association; GRB2 dimerization is better supported by the biophysical studies (PMID:22536782, PMID:22726438), for which GO:0042803 protein homodimerization activity is proposed. Supporting Evidence: PMID:12577067 We identified 228 proteins, of which 28 were selectively enriched upon stimulation |
| GO:0042802 identical protein binding | IPI PMID:22536782 Bivalent binding drives the formation of the Grb2-Gab1 signa... | MODIFY | Summary: Biophysical analysis shows GRB2 exists in a monomer-dimer equilibrium and binds GAB1 as a homodimer (1:2 stoichiometry). Reason: The self-interaction is homodimerization; GO:0042803 protein homodimerization activity is the more precise child of identical protein binding. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:22536782 whereas Grb2 exists in a monomer-dimer equilibrium, the proline-rich (PR) domain of Gab1 is a monomer in solution |
| GO:0042802 identical protein binding | IPI PMID:22726438 Inhibition of basal FGF receptor signaling by dimeric Grb2. | MODIFY | Summary: Dimeric GRB2 binds the C-termini of two FGFR2 molecules, restraining basal receptor activation. Reason: The self-interaction is homodimerization with functional consequence for FGFR2 regulation; GO:0042803 protein homodimerization activity is more precise. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:22726438 Dimeric Grb2 binds to the C termini of two FGFR2 molecules |
| GO:0043408 regulation of MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: GRB2-clade adaptors regulate the MAPK cascade by coupling receptors to Ras-Raf-MEK-ERK via SOS. Reason: Sound phylogenetic transfer at PANTHER:PTN005273574 (GRB2 clade of PTHR46037) (fly drk, mouse Grb2 seeds); GRB2's recruitment of SOS drives Ras-ERK activation. Accepted, consistent with the mouse review. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md RAS-GTP activates the RAFβMEKβERK cascade file:human/GRB2/GRB2-deep-research-falcon.md GRB2 SH3 domains engage proline-rich sequences in SOS1/2, recruiting this RAS guanine-nucleotide exchange factor from cytosolic complexes to the inner plasma membrane. |
| GO:0043560 insulin receptor substrate binding | IPI PMID:8388384 Insulin stimulates association of insulin receptor substrate... | KEEP AS NON CORE | Summary: GRB2/ASH fusion protein binds tyrosine-phosphorylated IRS-1 directly (WITH/FROM P35568). Reason: Correct, direct binding; a partner-specific instance of GRB2 SH2 phosphotyrosine binding (GO:0001784). Kept as non-core, consistent with the mouse review. Supporting Evidence: PMID:8388384 suggesting that ASH is able to bind tyrosine-phosphorylated IRS-1 directly |
| GO:0045953 negative regulation of natural killer cell mediated cytotoxicity | IDA PMID:25870599 GRB2 Nucleates T Cell Receptor-Mediated LAT Clusters That Co... | REMOVE | Summary: Negative regulation of natural killer cell mediated cytotoxicity attributed to PMID:25870599. Reason: PMID:25870599 (full text available in the cache) studies GRB2 knockdown in human CD4+ T cells and LAT microclusters; it contains no NK-cell or cytotoxicity experiments, and its findings are that GRB2 is positively required for TCR-induced LAT clustering, calcium flux and cytokine output. The annotation is therefore not supported by the cited paper (likely a curation slip). GRB2 is positively involved in NKG2D-DAP10 cytotoxicity (PMID:16582911). Supporting Evidence: PMID:25870599 GRB2 deficient T cells had substantially reduced production of IL-2 and IFN-Ξ³ PMID:16582911 For full calcium release and cytotoxicity to occur, both Grb2-Vav1 and p85 had to bind to DAP10 |
| GO:0046875 ephrin receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of ephrin receptor binding. Reason: GRB2 binds activated EphB1 via its SH2 domain; a receptor-specific instance of RTK phosphotyrosine binding. Non-core. Supporting Evidence: PMID:8798570 These findings define ligand-activated interaction between ELK and the SH2 domains of Grb2 |
| GO:0046875 ephrin receptor binding | IPI PMID:12925710 EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and pro... | KEEP AS NON CORE | Summary: Activated EphB1 recruits GRB2 and p52Shc (WITH/FROM P54762). Reason: Correct receptor-specific binding; non-core instance of GRB2 RTK docking. Supporting Evidence: PMID:12925710 we demonstrate that activated EphB1 recruits the adaptor proteins Grb2 and p52Shc |
| GO:0048009 insulin-like growth factor receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of insulin-like growth factor receptor signaling pathway. Reason: Receptor-specific instance of GRB2's RTK adaptor function (via IRS/Shc); non-core. Supporting Evidence: PMID:8491186 mediated by the binding of the SH2 domain of GRB2 to phosphotyrosines on both IRS-1 and Shc |
| GO:0050853 B cell receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer from mouse Grb2 of B cell receptor signaling pathway. Reason: GRB2 is recruited to phosphorylated BLNK/SLP-65 downstream of the BCR; a genuine but receptor-specific role. Non-core. Supporting Evidence: PMID:9697839 Tyrosine phosphorylation of BLNK by Syk provides docking sites for these SH2-containing effector molecules |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | MARK AS OVER ANNOTATED | Summary: GRB2 detected in a proteomic survey of extracellular vesicles/exosomes (PMID:19056867). Reason: GRB2 is an abundant cytosolic adaptor; its presence in exosome proteomes most likely reflects passive cytosolic cargo and has no known functional significance. Kept as over-annotation rather than removed because it is experimental HDA evidence. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | MARK AS OVER ANNOTATED | Summary: GRB2 detected in a proteomic survey of extracellular vesicles/exosomes (PMID:20458337). Reason: GRB2 is an abundant cytosolic adaptor; its presence in exosome proteomes most likely reflects passive cytosolic cargo and has no known functional significance. Kept as over-annotation rather than removed because it is experimental HDA evidence. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | MARK AS OVER ANNOTATED | Summary: GRB2 detected in a proteomic survey of extracellular vesicles/exosomes (PMID:23533145). Reason: GRB2 is an abundant cytosolic adaptor; its presence in exosome proteomes most likely reflects passive cytosolic cargo and has no known functional significance. Kept as over-annotation rather than removed because it is experimental HDA evidence. Supporting Evidence: file:human/GRB2/GRB2-deep-research-falcon.md GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. |
| GO:0070436 Grb2-EGFR complex | IDA PMID:20086093 HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regul... | ACCEPT | Summary: Grb2-EGFR complex (IDA) from the ACK1/Nedd4-1 EGFR degradation study. Reason: The GRB2-EGFR complex is one of the best-established GRB2 complexes (GRB2 SH2 binding EGFR pY1068/pY1086); the specific experiment is not described in the cached abstract, but the complex is well supported and the curator's full-text reading is deferred to. Core. Supporting Evidence: PMID:7518560 Grb2 binds directly to the EGFR at Y-1068, to a lesser extent at Y-1086, and indirectly at Y-1173 |
| GO:0071479 cellular response to ionizing radiation | IMP PMID:20160708 Feedback between p21 and reactive oxygen production is neces... | KEEP AS NON CORE | Summary: GRB2 knockdown affected the ROS-DDR feedback loop that stabilises irradiation-induced senescence. Reason: The study combines in-silico interactome analysis with target inhibition to describe a senescence-maintaining DDR-p21-GADD45-p38-GRB2-TGFBR2-ROS loop; GRB2 knockdown affected the loop. Pleiotropic cellular response; non-core. Supporting Evidence: PMID:20160708 These ROS in turn replenish short-lived DNA damage foci and maintain an ongoing DDR |
| GO:2000379 positive regulation of reactive oxygen species metabolic process | IMP PMID:20160708 Feedback between p21 and reactive oxygen production is neces... | KEEP AS NON CORE | Summary: GRB2 is required in the p21-p38-GRB2-TGFBR2 loop that drives mitochondrial ROS production in senescent cells. Reason: The study combines in-silico interactome analysis with target inhibition to describe a senescence-maintaining DDR-p21-GADD45-p38-GRB2-TGFBR2-ROS loop; GRB2 knockdown affected the loop. Indirect, context-specific; non-core. Supporting Evidence: PMID:20160708 long-term activation of the checkpoint gene CDKN1A (p21) induces mitochondrial dysfunction and production of reactive oxygen species (ROS) |
| GO:0050852 T cell receptor signaling pathway | IDA PMID:25870599 GRB2 Nucleates T Cell Receptor-Mediated LAT Clusters That Co... | NEW | Summary: GRB2 performs an adaptor step of TCR signalling: bound to phosphorylated LAT through its SH2 domain, it uses its SH3 domains to cross-link effectors and nucleate LAT microclusters required for PLC-gamma1 recruitment, calcium flux, MAPK activation and cytokine production in human CD4+ T cells. Reason: Participation test: GRB2 does part of the work of the pathway (it is the adaptor that bridges pLAT to SOS1, THEMIS-SHP1 and other effectors and cross-links LAT clusters), rather than being merely required; rescue depends on its own N-SH3 domain. Comparator check: other TCR-proximal adaptors in the same role, LAT (IDA, IBA) and LCP2/SLP-76 (IDA), carry GO:0050852 in GOA, while GRB2 currently has only the broader GO:0042110 T cell activation. Supporting Evidence: PMID:25870599 Add back of wild-type GRB2, but not a novel N-terminal SH3 domain mutant, rescued LAT microcluster formation, calcium mobilization, and cytokine release PMID:23460737 This association is indispensable for THEMIS recruitment to the immunological synapse via the transmembrane adapter linker for activation of T cells (LAT) file:human/GRB2/GRB2-uniprot.txt engagement of the TCR leads to phosphorylation of the adapter protein LAT, which serves as docking site for GRB2 |
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Download this section (compressed HTML)Q: Does GRB2 homodimerization (monomer-dimer equilibrium, Tyr160/Tyr209 phosphorylation-controlled) regulate receptor signalling generally, or is the FGFR2-restraint mechanism specific to FGFR2 and EGFR condensates?
Q: Which of the ~90 GRB2-associated proteins identified by AP-SRM (PMID:21706016) bind GRB2 directly, and through which domain (SH2 versus N-SH3 versus C-SH3)? Domain-resolved data would allow the many generic protein binding rows to be converted to informative phosphotyrosine or proline-rich region binding annotations.
Q: Is the nuclear pool of GRB2 (AGO2-DICER1 complex, stalled-fork protection) regulated independently of its receptor-proximal pool, and does it use the same SH3-mediated interactions?
Q: Is the COP9 signalosome (GO:0008180) annotation to GRB2 supportable in any organism, or is it a family-wide over-propagation (raised independently in the PR
Q: Does GRB2 RNA binding detected by interactome capture reflect a functionally relevant activity, for example connected to its reported nuclear AGO2-DICER1 pool (raised independently in the PR
Experiment: Systematic pull-down or split-luciferase assays with isolated GRB2 N-SH3, SH2 (wild type and R86K) and C-SH3 domains against the proteome-scale GRB2 partner set, with and without phosphatase treatment, to classify each partner as phosphotyrosine-dependent or proline-rich-motif-dependent.
Hypothesis: GRB2 partners detected in proteome-scale screens bind through specific GRB2 domains and phosphorylation states.
Type: binding assay
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