Phospholipase C-gamma-1 (PLCG1) is a ubiquitously expressed, cytosolic phosphoinositide-specific phospholipase C that hydrolyses phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) at the inner leaflet of the plasma membrane to generate the second messengers inositol 1,4,5-trisphosphate (IP3), which releases Ca2+ from ER stores, and diacylglycerol (DAG), which activates protein kinase C and RasGRP. Besides the conserved PLC core (PH domain, EF-hands, split X/Y TIM-barrel catalytic domain, C2 domain), PLCG1 carries a gamma-specific regulatory array (split PH, tandem nSH2-cSH2, SH3) inserted between X and Y. In resting cells the cSH2 domain holds the enzyme autoinhibited; the nSH2 domain docks onto phosphotyrosines of activated receptor tyrosine kinases (EGFR, PDGFR, FGFR pY766, VEGFR2, TRK, RET, ALK) or of adaptors such as LAT and SLP-76 in T cells, after which phosphorylation of Tyr783 releases autoinhibition and permits membrane engagement and catalysis. PLCG1 thereby couples growth factor and antigen receptors to Ca2+ and PKC signaling, with downstream roles in cell migration, proliferation, angiogenesis and T cell activation. The SH3 domain also mediates lipase-independent scaffolding interactions. In T cells its SH2 domains also cross-link phospho-LAT into phase-separated signalling clusters and shield LAT from dephosphorylation by CD45. Somatic activating mutations occur in T cell lymphomas and angiosarcoma, and a germline gain-of-function variant causes immune dysregulation with autoimmunity and autoinflammation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001726 ruffle | IDA PMID:17229814 Obligatory role for phospholipase C-gamma(1) in villin-induc... | ACCEPT | Summary: PLCG1 redistributes to ruffles and lamellipodia after EGF stimulation, where PI(4,5)P2 substrate and activated receptor are enriched. Reason: Supported by UniProt-curated localization (PubMed:17229814) and live-cell imaging of EGF-induced PLCG1 translocation to membrane ruffles. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0001726 ruffle | IEA GO_REF:0000044 | ACCEPT | Summary: PLCG1 redistributes to ruffles and lamellipodia after EGF stimulation, where PI(4,5)P2 substrate and activated receptor are enriched. Reason: Supported by UniProt-curated localization (PubMed:17229814) and live-cell imaging of EGF-induced PLCG1 translocation to membrane ruffles. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0002862 negative regulation of inflammatory response to antigenic stimulus | TAS Reactome:R-HSA-9664323 | MARK AS OVER ANNOTATED | Summary: Reactome 'FCGR3A-mediated IL10 synthesis' places PLCG1 in a pathway leading to IL-10 production. Reason: PLCG1's contribution here is generic PIP2 hydrolysis downstream of an Fc receptor; attributing negative regulation of inflammatory response to PLCG1 is a distal pathway-level inference. Human PLCG1 gain-of-function variants in fact cause immune dysregulation with increased proinflammatory signaling. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | IBA GO_REF:0000033 | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function, supported by extensive biochemistry, structural work and human gain-of-function variants that increase IP3 production. The IBA placement at PTN007434641 (PLC family) is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) PMID:23063561 Among families of proteins involved in signal transduction, phospholipase C (PLC) enzymes that generate second messengers from phosphatidylinositol 4,5-bisphosphate (PIP2) incorporate a number of different protein modules. file:human/PLCG1/PLCG1-deep-research-falcon.md This enzymatic reaction produces two critical second messengers that propagate distinct signaling pathways: inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | IDA PMID:2550068 Isolation and characterization of one soluble and two membra... | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function. The cited platelet purification paper is abstract-only in cache and reports PIP2 hydrolysis by cytosolic 'PLC-II' (a recorded synonym of PLCG1); regardless of the precise attribution, the activity is clearly correct for PLCG1 and we defer to the curator. Supporting Evidence: PMID:2550068 mPLC-I, mPLC-II, and PLC-II hydrolyzed both PI and PIP2 PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | IEA GO_REF:0000120 | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function, supported by extensive biochemistry, structural work and human gain-of-function variants that increase IP3 production. The IBA placement at PTN007434641 (PLC family) is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) PMID:23063561 Among families of proteins involved in signal transduction, phospholipase C (PLC) enzymes that generate second messengers from phosphatidylinositol 4,5-bisphosphate (PIP2) incorporate a number of different protein modules. |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | ISS GO_REF:0000024 | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function, supported by extensive biochemistry, structural work and human gain-of-function variants that increase IP3 production. The IBA placement at PTN007434641 (PLC family) is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) PMID:23063561 Among families of proteins involved in signal transduction, phospholipase C (PLC) enzymes that generate second messengers from phosphatidylinositol 4,5-bisphosphate (PIP2) incorporate a number of different protein modules. |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | TAS Reactome:R-HSA-202407 | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function, supported by extensive biochemistry, structural work and human gain-of-function variants that increase IP3 production. The IBA placement at PTN007434641 (PLC family) is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) PMID:23063561 Among families of proteins involved in signal transduction, phospholipase C (PLC) enzymes that generate second messengers from phosphatidylinositol 4,5-bisphosphate (PIP2) incorporate a number of different protein modules. |
| GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity | TAS Reactome:R-HSA-2730847 | ACCEPT | Summary: PLCG1 is a phosphoinositide-specific phospholipase C that hydrolyses PI(4,5)P2 to IP3 and DAG; this is its core catalytic activity. Reason: Core function, supported by extensive biochemistry, structural work and human gain-of-function variants that increase IP3 production. The IBA placement at PTN007434641 (PLC family) is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) PMID:23063561 Among families of proteins involved in signal transduction, phospholipase C (PLC) enzymes that generate second messengers from phosphatidylinositol 4,5-bisphosphate (PIP2) incorporate a number of different protein modules. |
| GO:0004629 C-type glycerophospholipase activity | IDA PMID:20510673 Phospholipase C-gamma1 is required for the epidermal growth ... | MODIFY | Summary: C-type glycerophospholipase activity is the parent of the PI(4,5)P2-specific phospholipase C activity of PLCG1. Reason: Correct but too general. The relevant assays measure IP3 production from PI(4,5)P2, so the more informative GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity should be used. Proposed replacements: phosphatidylinositol-4,5-bisphosphate phospholipase C activity Supporting Evidence: PMID:20510673 PLC-Ξ³1 activity was determined by measuring accumulation of IP3 |
| GO:0004629 C-type glycerophospholipase activity | IMP PMID:37422272 A gain-of-function variation in PLCG1 causes a new immune dy... | MODIFY | Summary: C-type glycerophospholipase activity is the parent of the PI(4,5)P2-specific phospholipase C activity of PLCG1. Reason: Correct but too general. The relevant assays measure IP3 production from PI(4,5)P2, so the more informative GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity should be used. Proposed replacements: phosphatidylinositol-4,5-bisphosphate phospholipase C activity Supporting Evidence: PMID:37422272 The PLCΞ³1 S1021F mutant showed increased production of intracellular IP3 after anti-CD3 stimulation, as measured by IP-one ELISA PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0004629 C-type glycerophospholipase activity | TAS Reactome:R-HSA-1112666 | MODIFY | Summary: C-type glycerophospholipase activity is the parent of the PI(4,5)P2-specific phospholipase C activity of PLCG1. Reason: Correct but too general. The relevant assays measure IP3 production from PI(4,5)P2, so the more informative GO:0004435 phosphatidylinositol-4,5-bisphosphate phospholipase C activity should be used. Proposed replacements: phosphatidylinositol-4,5-bisphosphate phospholipase C activity Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0005085 guanyl-nucleotide exchange factor activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Guanine nucleotide exchange factor activity toward dynamin-1 transferred by ISS from rat Plcg1 (SH3-domain mediated). Reason: Reported for rat PLCG1 SH3 domain acting on DNM1 in endocytosis (UniProt 'By similarity'); a non-catalytic, lipase-independent moonlighting role that has not been widely replicated. Retained as non-core; see suggested_questions. |
| GO:0005168 neurotrophin TRKA receptor binding | IPI PMID:15488758 TrkA alternative splicing: a regulated tumor-promoting switc... | KEEP AS NON CORE | Summary: IPI with NTRK1 (TrkA) from a study of the TrkAIII splice variant in neuroblastoma. Reason: PLCG1 is a well-established SH2-domain effector of Trk receptors (pY785 in TrkA), so the binding is credible; the cached paper is abstract-only and focuses on TrkAIII signaling. As a receptor-binding term it describes recruitment rather than PLCG1's catalytic function; the more informative mechanism is phosphotyrosine binding. Supporting Evidence: PMID:8384556 phosphorylated Y-785 is a major and selective interaction site for PLC gamma |
| GO:0005509 calcium ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Calcium ion binding inferred from the EF-hand domain (InterPro). Reason: PI-PLC enzymes bind Ca2+ in the catalytic site as an essential cofactor and contain an EF-hand region; the annotation is plausible but reflects a cofactor/structural property rather than the core function. |
| GO:0005515 protein binding | IPI PMID:10811803 Association of Grb2, Gads, and phospholipase C-gamma 1 with ... | MODIFY | Summary: IPI 'protein binding' from PMID:10811803. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:10811803 Upon T cell activation, LAT becomes highly phosphorylated on tyrosine residues, and Grb2, Gads, and phospholipase C (PLC)-gamma1 bind LAT via Src homology-2 domains. |
| GO:0005515 protein binding | IPI PMID:10873601 Characterization of the tyrosine kinase Tnk1 and its binding... | REMOVE | Summary: IPI 'protein binding' from PMID:10873601. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:11796522 PLC-gamma1 enzyme activity is required for insulin-induced D... | REMOVE | Summary: IPI 'protein binding' from PMID:11796522. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins... | REMOVE | Summary: IPI 'protein binding' from PMID:11896612. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:1396585 Identification of two C-terminal autophosphorylation sites i... | MODIFY | Summary: IPI 'protein binding' from PMID:1396585. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:1396585 These data show that tyrosine phosphorylation of PLC-gamma is dependent on autophosphorylation of the PDGF beta-receptor at Tyr1009 and Tyr1021. |
| GO:0005515 protein binding | IPI PMID:14568990 Role of the pleckstrin homology domain of PLCgamma1 in its i... | REMOVE | Summary: IPI 'protein binding' from PMID:14568990. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:14568990 Role of the pleckstrin homology domain of PLCgamma1 in its i... | REMOVE | Summary: IPI 'protein binding' from PMID:14568990. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:14570588 Human scavenger receptor class B type II (SR-BII) and cellul... | REMOVE | Summary: IPI 'protein binding' from PMID:14570588. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:14722116 The importance of three membrane-distal tyrosines in the ada... | REMOVE | Summary: IPI 'protein binding' from PMID:14722116. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:15641795 NMR dynamics-derived insights into the binding properties of... | MODIFY | Summary: IPI 'protein binding' from PMID:15641795. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:15641795 The signal transduction protein phospholipase C-gamma1 (PLC-gamma1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor receptor (PDGFR). |
| GO:0005515 protein binding | IPI PMID:15929943 Novel Src homology 3 domain-binding motifs identified from p... | REMOVE | Summary: IPI 'protein binding' from PMID:15929943. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: IPI 'protein binding' from PMID:16273093. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: IPI 'protein binding' from PMID:16273093. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: IPI 'protein binding' from PMID:16273093. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:16525023 Akt binds to and phosphorylates phospholipase C-gamma1 in re... | REMOVE | Summary: IPI 'protein binding' from PMID:16525023. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:1656221 A tyrosine-phosphorylated carboxy-terminal peptide of the fi... | MODIFY | Summary: IPI 'protein binding' from PMID:1656221. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:1656221 A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1. |
| GO:0005515 protein binding | IPI PMID:16921170 Interaction of phospholipase C-gamma1 with villin regulates ... | REMOVE | Summary: IPI 'protein binding' from PMID:16921170. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:16938345 Evidence of LAT as a dual substrate for Lck and Syk in T lym... | REMOVE | Summary: IPI 'protein binding' from PMID:16938345. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17229814 Obligatory role for phospholipase C-gamma(1) in villin-induc... | REMOVE | Summary: IPI 'protein binding' from PMID:17229814. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: IPI 'protein binding' from PMID:17474147. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:17936057 A2 isoform of mammalian translation factor eEF1A displays in... | REMOVE | Summary: IPI 'protein binding' from PMID:17936057. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:19264842 PLC-gamma1 and Rac1 coregulate EGF-induced cytoskeleton remo... | REMOVE | Summary: IPI 'protein binding' from PMID:19264842. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:20808760 Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake b... | REMOVE | Summary: IPI 'protein binding' from PMID:20808760. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:20932831 Grb14 inhibits FGF receptor signaling through the regulation... | REMOVE | Summary: IPI 'protein binding' from PMID:20932831. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: IPI 'protein binding' from PMID:21706016. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:21725281 Sequential phosphorylation of SLP-76 at tyrosine 173 is requ... | REMOVE | Summary: IPI 'protein binding' from PMID:21725281. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:23063561 Structural and functional integration of the PLCΞ³ interactio... | REMOVE | Summary: IPI 'protein binding' from PMID:23063561. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:23063561 Structural and functional integration of the PLCΞ³ interactio... | REMOVE | Summary: IPI 'protein binding' from PMID:23063561. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: IPI 'protein binding' from PMID:23397142. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:23460737 GRB2-mediated recruitment of THEMIS to LAT is essential for ... | REMOVE | Summary: IPI 'protein binding' from PMID:23460737. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:24440983 Competition between Grb2 and PlcΞ³1 for FGFR2 regulates basal... | REMOVE | Summary: IPI 'protein binding' from PMID:24440983. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:24642916 Fine specificity and molecular competition in SLAM family re... | REMOVE | Summary: IPI 'protein binding' from PMID:24642916. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:24642916 Fine specificity and molecular competition in SLAM family re... | REMOVE | Summary: IPI 'protein binding' from PMID:24642916. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:24642916 Fine specificity and molecular competition in SLAM family re... | REMOVE | Summary: IPI 'protein binding' from PMID:24642916. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: IPI 'protein binding' from PMID:24728074. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:24728074 We observed that Tyr(P)-1349 was able to recruit primarily SH2 domains from PLCG1 and SH2D1B with moderate affinity. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: IPI 'protein binding' from PMID:24728074. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:24728074 We observed that Tyr(P)-1349 was able to recruit primarily SH2 domains from PLCG1 and SH2D1B with moderate affinity. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: IPI 'protein binding' from PMID:24728074. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:24728074 We observed that Tyr(P)-1349 was able to recruit primarily SH2 domains from PLCG1 and SH2D1B with moderate affinity. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: IPI 'protein binding' from PMID:24728074. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:24728074 We observed that Tyr(P)-1349 was able to recruit primarily SH2 domains from PLCG1 and SH2D1B with moderate affinity. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: IPI 'protein binding' from PMID:25241761. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: IPI 'protein binding' from PMID:25241761. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:28598420 Tespa1 regulates T cell receptor-induced calcium signals by ... | REMOVE | Summary: IPI 'protein binding' from PMID:28598420. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:31413325 HENA, heterogeneous network-based data set for Alzheimer's d... | REMOVE | Summary: IPI 'protein binding' from PMID:31413325. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: IPI 'protein binding' from PMID:35384245. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: IPI 'protein binding' from PMID:35384245. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: IPI 'protein binding' from PMID:35384245. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:7537096 Formation of signal transfer complexes between stem cell and... | REMOVE | Summary: IPI 'protein binding' from PMID:7537096. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:7537265 Functional interaction between c-Src and its mitotic target,... | REMOVE | Summary: IPI 'protein binding' from PMID:7537265. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:7693694 Sequence specificity in recognition of the epidermal growth ... | REMOVE | Summary: IPI 'protein binding' from PMID:7693694. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:7993895 Identification of amino acids in the N-terminal SH2 domain o... | MODIFY | Summary: IPI 'protein binding' from PMID:7993895. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:7993895 Photoaffinity labeling and site-directed mutagenesis have been used to identify amino acid residues of the phospholipase C gamma 1 (PLC gamma 1) N-terminal SH2 domain involved in recognition of the activated epidermal growth factor receptor (EGFR). |
| GO:0005515 protein binding | IPI PMID:8321198 Control of fibroblast growth factor receptor kinase signal t... | MODIFY | Summary: IPI 'protein binding' from PMID:8321198. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8321198 Although phosphotyrosine 766 is sufficient for interaction of PLC gamma 1 and other SH2 substrates with the FGF-R kinase |
| GO:0005515 protein binding | IPI PMID:8384556 Tyrosine 785 is a major determinant of Trk--substrate intera... | MODIFY | Summary: IPI 'protein binding' from PMID:8384556. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8384556 phosphorylated Y-785 is a major and selective interaction site for PLC gamma |
| GO:0005515 protein binding | IPI PMID:8627166 CD22 associates with protein tyrosine phosphatase 1C, Syk, a... | REMOVE | Summary: IPI 'protein binding' from PMID:8627166. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:8657103 Phospholipase C-gamma1 interacts with conserved phosphotyros... | MODIFY | Summary: IPI 'protein binding' from PMID:8657103. The reported interaction is mediated by a PLCG1 SH2 domain engaging a phosphotyrosine on the partner (activated receptor tyrosine kinase or adaptor), the canonical mechanism by which PLCG1 is recruited to activated signaling complexes. Reason: Generic 'protein binding' is uninformative. The cited study specifically shows phosphotyrosine-dependent SH2-domain binding, which is captured by GO:0001784 phosphotyrosine residue binding. This SH2/pTyr recruitment is how PLCG1 couples to receptor tyrosine kinases (e.g. FGFR1 pY766, PDGFRB pY1021, EGFR) and to LAT/SYK in immune receptor signaling. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: PMID:8657103 Glutathione S-transferase fusion proteins containing the C-terminal Src-homology 2 [SH2(C)] domain of PLC-gamma1 bound to tyrosyl phosphorylated Syk. |
| GO:0005515 protein binding | IPI PMID:8892607 Evidence that the Wiskott-Aldrich syndrome protein may be in... | REMOVE | Summary: IPI 'protein binding' from PMID:8892607. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: IPI 'protein binding' from PMID:9020117. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: IPI 'protein binding' from PMID:9020117. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: IPI 'protein binding' from PMID:9020117. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9045636 Interaction between Sam68 and Src family tyrosine kinases, F... | REMOVE | Summary: IPI 'protein binding' from PMID:9045636. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9489702 LAT: the ZAP-70 tyrosine kinase substrate that links T cell ... | REMOVE | Summary: IPI 'protein binding' from PMID:9489702. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9593725 Association of the insulin receptor with phospholipase C-gam... | REMOVE | Summary: IPI 'protein binding' from PMID:9593725. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005515 protein binding | IPI PMID:9697839 BLNK: a central linker protein in B cell activation. | REMOVE | Summary: IPI 'protein binding' from PMID:9697839. The interaction may well be real (PLCG1 has many partners through its SH2, SH3 and split-PH domains), but the annotation conveys no functional information. Reason: Generic 'protein binding' is uninformative per project and GO guidelines; removal does not dispute the reported interaction. Where the partner recognition is phosphotyrosine/SH2-mediated and demonstrated in the cited study, it is captured elsewhere in this review as GO:0001784 phosphotyrosine residue binding; the core activity is GO:0004435. |
| GO:0005737 cytoplasm | IDA PMID:15702972 Molecular cloning and characterization of a novel phospholip... | ACCEPT | Summary: Cytoplasmic localization reported in a PLC-eta cloning paper (abstract-only in cache), presumably with PLCG1 as a comparator. Reason: Cytoplasm is clearly correct for PLCG1 (cytosolic in resting cells). The cached abstract concerns PLC-eta; per project policy we do not second-guess an experimental annotation whose full text we cannot read, and the location is consistent with all other evidence. |
| GO:0005829 cytosol | IDA PMID:2550068 Isolation and characterization of one soluble and two membra... | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. The cited paper (abstract-only in cache) resolved cytosolic phosphoinositide-specific PLC forms from human platelets; we defer to the curator for attribution of the 'PLC-II' form to PLCG1 (PLC-II is a recorded synonym of PLCG1). Supporting Evidence: PMID:2550068 mPLC-I, mPLC-II, and PLC-II hydrolyzed both PI and PIP2 |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1169406 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-1169406. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1678841 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-1678841. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202212 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-202212. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202248 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-202248. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202331 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-202331. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202354 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-202354. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029268 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2029268. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029270 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2029270. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-210283 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-210283. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-212706 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-212706. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-212710 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-212710. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-213406 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-213406. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-213407 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-213407. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396594 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2396594. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396606 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2396606. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424476 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2424476. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424481 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2424481. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424484 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2424484. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424486 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2424486. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424487 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2424487. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730833 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730833. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730840 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730840. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730841 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730841. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730851 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730851. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730856 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730856. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730858 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730858. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730889 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730889. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730892 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-2730892. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4420121 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-4420121. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4420153 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-4420153. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637795 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-5637795. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637800 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-5637800. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853755 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-8853755. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664270 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9664270. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664278 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9664278. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665032 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665032. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665034 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665034. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665410 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665410. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665411 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665411. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665704 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665704. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665706 | ACCEPT | Summary: PLCG1 is a soluble cytosolic enzyme in resting cells and is recruited to membranes only upon receptor activation. Reactome places PLCG1 in the cytosol for the pre-recruitment or post-release state of the reaction Reactome:R-HSA-9665706. Reason: Cytosol is the resting location of PLCG1, from which it is recruited via SH2 domains to phosphorylated receptors at the plasma membrane; consistent with the biochemical purification of a cytosolic PLC-gamma form and with live-cell translocation studies. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | IDA PMID:20510673 Phospholipase C-gamma1 is required for the epidermal growth ... | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:20510673 In response to the EGFR ligand epidermal growth factor (EGF), PLC-gamma1 was translocated not only to the plasma membrane but also to the nucleus. |
| GO:0005886 plasma membrane | IDA PMID:20510673 Phospholipase C-gamma1 is required for the epidermal growth ... | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:20510673 In response to the EGFR ligand epidermal growth factor (EGF), PLC-gamma1 was translocated not only to the plasma membrane but also to the nucleus. |
| GO:0005886 plasma membrane | IDA PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:22454520 Confocal microscopy analysis indicated that EGF induced a strong colocalisation of the two proteins at the plasma membrane, in particular at the level of cell protrusions |
| GO:0005886 plasma membrane | IDA PMID:2550068 Isolation and characterization of one soluble and two membra... | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. The cited platelet purification paper is abstract-only in cache and describes membrane-associated PLC forms; the location is clearly correct for PLCG1 so we defer to the curator. Supporting Evidence: PMID:2550068 mPLC-I, mPLC-II, and PLC-II hydrolyzed both PI and PIP2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247841 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1247841. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247842 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1247842. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247844 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1247844. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1524182 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1524182. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1524186 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1524186. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1839094 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1839094. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1839098 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1839098. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1839100 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1839100. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1855221 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-1855221. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-186765 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-186765. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202354 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-202354. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202407 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-202407. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2029268 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-2029268. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2029272 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-2029272. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212710 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-212710. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212713 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-212713. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2424485 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-2424485. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2424487 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-2424487. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2730847 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-2730847. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-4420121 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-4420121. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-4420202 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-4420202. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637792 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5637792. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637795 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5637795. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637800 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5637800. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654147 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654147. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654148 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654148. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654149 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654149. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654151 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654151. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654157 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654157. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654159 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654159. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654163 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654163. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654165 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654165. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654167 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654167. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654169 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654169. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654222 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654222. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654224 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654224. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654748 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5654748. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655243 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655243. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655244 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655244. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655247 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655247. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655301 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655301. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655313 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655313. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655336 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655336. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655341 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655341. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655343 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-5655343. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9026894 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9026894. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9034855 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9034855. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664271 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9664271. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664278 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9664278. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665032 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9665032. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665411 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9665411. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665704 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9665704. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700149 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9700149. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700171 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9700171. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9710917 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9710917. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712086 | ACCEPT | Summary: PLCG1 translocates to the plasma membrane upon receptor tyrosine kinase or immune receptor activation, where it hydrolyses its substrate PI(4,5)P2. Reactome places PLCG1 at the plasma membrane in the receptor-bound/active state for Reactome:R-HSA-9712086. Reason: The plasma membrane (inner leaflet) is where PLCG1 acts on PI(4,5)P2; membrane recruitment via SH2 domain binding to activated receptors is well documented. Supporting Evidence: PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: lipid metabolic process: PLCG1 hydrolyses the membrane phosphoinositide PI(4,5)P2. Reason: Correct (if general) metabolic description of the PI(4,5)P2 phospholipase C reaction. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | ACCEPT | Summary: signal transduction from InterPro mapping of the PI-PLC domains. Reason: Correct but general; the informative process is GO:0048015 phosphatidylinositol-mediated signaling. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | ACCEPT | Summary: PLCG1 is a direct SH2-recruited effector of activated EGFR, phosphorylated and activated to hydrolyse PI(4,5)P2. Reason: Classic, well-established effector role in EGFR signaling; PLCG1 performs a signaling step (second messenger generation). Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0007173 epidermal growth factor receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: PLCG1 is a direct SH2-recruited effector of activated EGFR, phosphorylated and activated to hydrolyse PI(4,5)P2. Reason: Classic, well-established effector role in EGFR signaling; PLCG1 performs a signaling step (second messenger generation). Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 PMID:11331309 The translocation of PLC gamma to the plasma membrane required the functional Src homology 2 domains |
| GO:0008081 phosphoric diester hydrolase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Phosphoric diester hydrolase activity is a correct but very general parent of PI(4,5)P2 phospholipase C activity (InterPro mapping). Reason: Correct high-level IEA; the specific activity is GO:0004435. |
| GO:0008180 COP9 signalosome | IDA PMID:22561606 Tespa1 is involved in late thymocyte development through the... | UNDECIDED | Summary: IDA to COP9 signalosome from the Tespa1 paper, which describes Tespa1 as a component of the TCR 'signalosome' associating with PLC-gamma1 and GRB2. Reason: The COP9 signalosome (CSN) is a defined eight-subunit (COPS1-8) cullin-deneddylase complex; PLCG1 is not a CSN subunit and no CSN association is reported for it. The cited abstract refers to the TCR/LAT signalosome, a signaling assembly unrelated to CSN, so the term may be a lexical mis-mapping of 'signalosome'. Only the abstract is cached, so the curator's full-text basis cannot be checked; left UNDECIDED rather than removed. Candidate for REMOVE once the full text confirms that no COP9 signalosome association is reported. Supporting Evidence: PMID:22561606 Tespa1 associated with the TCR signaling components PLC-Ξ³1 and Grb2 |
| GO:0009395 phospholipid catabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: phospholipid catabolic process: PLCG1 hydrolyses the membrane phosphoinositide PI(4,5)P2. Reason: Correct (if general) metabolic description of the PI(4,5)P2 phospholipase C reaction. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0010634 positive regulation of epithelial cell migration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PLCG1 is required for villin-induced and EGF-stimulated epithelial cell migration. Reason: Well-supported downstream cellular role of PLCG1 signaling, but a pleiotropic consequence rather than its core molecular role. Supporting Evidence: PMID:17229814 The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). |
| GO:0010634 positive regulation of epithelial cell migration | IMP PMID:17229814 Obligatory role for phospholipase C-gamma(1) in villin-induc... | KEEP AS NON CORE | Summary: PLCG1 is required for villin-induced and EGF-stimulated epithelial cell migration. Reason: Well-supported downstream cellular role of PLCG1 signaling, but a pleiotropic consequence rather than its core molecular role. Supporting Evidence: PMID:17229814 The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). |
| GO:0016477 cell migration | IMP PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | KEEP AS NON CORE | Summary: PLCG1 knockdown impairs EGF/PDK1-dependent cancer cell invasion/migration. Reason: Downstream cellular outcome of PLCG1 signaling. Supporting Evidence: PMID:22454520 We further show that this novel PDK1-PLCΞ³1 pathway is important for cancer cell invasion. |
| GO:0019722 calcium-mediated signaling | IEA GO_REF:0000117 | ACCEPT | Summary: PLCG1 produces IP3, initiating Ca2+-mediated signaling downstream of RTK and antigen receptors. Reason: PLCG1 performs the step that generates the Ca2+-mobilising messenger. Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 |
| GO:0019722 calcium-mediated signaling | IMP PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | ACCEPT | Summary: PLCG1 produces IP3, initiating Ca2+-mediated signaling downstream of RTK and antigen receptors. Reason: PLCG1 performs the step that generates the Ca2+-mobilising messenger. Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 |
| GO:0019901 protein kinase binding | IPI PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | KEEP AS NON CORE | Summary: IPI with PDK1 (PDPK1), which associates with PLCG1 and regulates its tyrosine phosphorylation after EGF stimulation. Reason: Reported interaction regulates PLCG1 activation; PLCG1 is the regulated partner, so this is not a core function of PLCG1 itself. Supporting Evidence: PMID:22454520 Here we demonstrate that PDK1 regulates PLCΞ³1 activation in a mechanism involving association of the two enzymes and modulation of PLCΞ³1 tyrosine phosphorylation. |
| GO:0030027 lamellipodium | IDA PMID:17229814 Obligatory role for phospholipase C-gamma(1) in villin-induc... | ACCEPT | Summary: PLCG1 redistributes to ruffles and lamellipodia after EGF stimulation, where PI(4,5)P2 substrate and activated receptor are enriched. Reason: Supported by UniProt-curated localization (PubMed:17229814) and live-cell imaging of EGF-induced PLCG1 translocation to membrane ruffles. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0030027 lamellipodium | IEA GO_REF:0000044 | ACCEPT | Summary: PLCG1 redistributes to ruffles and lamellipodia after EGF stimulation, where PI(4,5)P2 substrate and activated receptor are enriched. Reason: Supported by UniProt-curated localization (PubMed:17229814) and live-cell imaging of EGF-induced PLCG1 translocation to membrane ruffles. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0032587 ruffle membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PLCG1 colocalises with activated EGFR and PI(4,5)P2 in membrane ruffles. Reason: Directly observed by real-time imaging; the IBA placement (with PLCG2) is consistent. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0032587 ruffle membrane | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | ACCEPT | Summary: PLCG1 colocalises with activated EGFR and PI(4,5)P2 in membrane ruffles. Reason: Directly observed by real-time imaging; the IBA placement (with PLCG2) is consistent. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0032587 ruffle membrane | IEA GO_REF:0000117 | ACCEPT | Summary: PLCG1 colocalises with activated EGFR and PI(4,5)P2 in membrane ruffles. Reason: Directly observed by real-time imaging; the IBA placement (with PLCG2) is consistent. Supporting Evidence: PMID:11331309 Colocalization with the receptor was observed in the plasma membrane and in membrane ruffles where PI 4,5-P(2) substrate could also be visualized. |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000002 | ACCEPT | Summary: intracellular signal transduction from InterPro mapping of the PI-PLC domains. Reason: Correct but general; the informative process is GO:0048015 phosphatidylinositol-mediated signaling. |
| GO:0038095 Fc-epsilon receptor signaling pathway | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Reactome/ARBA place PLCG1 (with PLCG2) as the PIP2-hydrolysing effector downstream of FcERI/SYK/LAT in mast cells. Reason: PLC-gamma isoforms act downstream of FcERI via LAT/SLP-76; PLCG1 and PLCG2 both contribute in mast cells. A cell-type-specific pathway context of the core activity. |
| GO:0038095 Fc-epsilon receptor signaling pathway | TAS Reactome:R-HSA-2454202 | KEEP AS NON CORE | Summary: Reactome/ARBA place PLCG1 (with PLCG2) as the PIP2-hydrolysing effector downstream of FcERI/SYK/LAT in mast cells. Reason: PLC-gamma isoforms act downstream of FcERI via LAT/SLP-76; PLCG1 and PLCG2 both contribute in mast cells. A cell-type-specific pathway context of the core activity. |
| GO:0043536 positive regulation of blood vessel endothelial cell migration | IDA PMID:20011604 A phosphoinositide 3-kinase/phospholipase Cgamma1 pathway re... | KEEP AS NON CORE | Summary: PI3K-dependent PLCG1 activation contributes to FGF-2-induced endothelial cell migration and capillary tube formation. Reason: Supported by the cited endothelial study; a context-specific downstream outcome of PLCG1 signaling (PLCG1 is also essential for vasculogenesis in mouse). Supporting Evidence: PMID:20011604 PI3K activity is required for FGF-2-induced PLCgamma1 activation and the PI3K/PLCgamma1 pathway is involved in FGF-2-dependent cell migration, determined using Transwell assay, and in FGF-2-induced capillary tube formation (tubulogenesis assays in vitro). |
| GO:0045766 positive regulation of angiogenesis | IDA PMID:20011604 A phosphoinositide 3-kinase/phospholipase Cgamma1 pathway re... | KEEP AS NON CORE | Summary: PI3K-dependent PLCG1 activation contributes to FGF-2-induced endothelial cell migration and capillary tube formation. Reason: Supported by the cited endothelial study; a context-specific downstream outcome of PLCG1 signaling (PLCG1 is also essential for vasculogenesis in mouse). Supporting Evidence: PMID:20011604 PI3K activity is required for FGF-2-induced PLCgamma1 activation and the PI3K/PLCgamma1 pathway is involved in FGF-2-dependent cell migration, determined using Transwell assay, and in FGF-2-induced capillary tube formation (tubulogenesis assays in vitro). |
| GO:0046488 phosphatidylinositol metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: phosphatidylinositol metabolic process: PLCG1 hydrolyses the membrane phosphoinositide PI(4,5)P2. Reason: Correct (if general) metabolic description of the PI(4,5)P2 phospholipase C reaction. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0046488 phosphatidylinositol metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: phosphatidylinositol metabolic process: PLCG1 hydrolyses the membrane phosphoinositide PI(4,5)P2. Reason: Correct (if general) metabolic description of the PI(4,5)P2 phospholipase C reaction. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) |
| GO:0048015 phosphatidylinositol-mediated signaling | IBA GO_REF:0000033 | ACCEPT | Summary: PLCG1 generates the second messengers IP3 and DAG from PI(4,5)P2, which is the defining step of phosphatidylinositol-mediated signaling. Reason: Core process; PLCG1 directly performs the catalytic step. IBA placement is appropriate. Supporting Evidence: PMID:37422272 PLCG1 encodes phospholipase C (PLC) Ξ³1, an enzyme activated by receptor and non-receptor tyrosine kinases and hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce critical second messengers, including diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (IP3) file:human/PLCG1/PLCG1-deep-research-falcon.md This enzymatic reaction produces two critical second messengers that propagate distinct signaling pathways: inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) |
| GO:0050851 antigen receptor-mediated signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: PLCG1 is the PLC-gamma isoform recruited to the LAT/SLP-76 signalosome in T cells (antigen receptor signaling). Reason: Well established; PLCG1 performs the PIP2 hydrolysis step of antigen receptor signaling. Supporting Evidence: PMID:10811803 Upon T cell activation, LAT becomes highly phosphorylated on tyrosine residues, and Grb2, Gads, and phospholipase C (PLC)-gamma1 bind LAT via Src homology-2 domains. PMID:37422272 We observed overproduction of IP3 under stimulation with anti-CD3 |
| GO:0050852 T cell receptor signaling pathway | TAS Reactome:R-HSA-202403 | ACCEPT | Summary: Reactome TCR signaling: PLCG1 is recruited to phosphorylated LAT and SLP-76, phosphorylated by ITK/ZAP70-pathway kinases and hydrolyses PIP2. Reason: PLCG1 is the dominant PLC isoform in T cells and performs a central step of TCR signaling (IP3/DAG generation leading to Ca2+/NFAT and PKC/RasGRP signaling). Supporting Evidence: PMID:10811803 Upon T cell activation, LAT becomes highly phosphorylated on tyrosine residues, and Grb2, Gads, and phospholipase C (PLC)-gamma1 bind LAT via Src homology-2 domains. PMID:37422272 We observed overproduction of IP3 under stimulation with anti-CD3 |
| GO:0051209 release of sequestered calcium ion into cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: PLCG1-generated IP3 triggers release of Ca2+ from ER stores. Reason: PLCG1 supplies the IP3 that gates ER Ca2+ release (the channel itself is the IP3 receptor). Retained consistent with the PAINT placement and with the treatment of PLCG2; the more precise regulatory statement is GO:0051281, also annotated. Supporting Evidence: PMID:37422272 Consistent with the increased IP3 production, the S1021F mutant resulted in an elevated level of calcium flux under anti-CD3 stimulation |
| GO:0051281 positive regulation of release of sequestered calcium ion into cytosol | IMP PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | ACCEPT | Summary: Loss of PLCG1 reduces EGF-induced intracellular Ca2+ rise; gain-of-function PLCG1 increases Ca2+ flux. Reason: Accurately captures PLCG1's role upstream of IP3 receptor-mediated Ca2+ release. Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 PMID:37422272 Consistent with the increased IP3 production, the S1021F mutant resulted in an elevated level of calcium flux under anti-CD3 stimulation |
| GO:0071364 cellular response to epidermal growth factor stimulus | IDA PMID:17229814 Obligatory role for phospholipase C-gamma(1) in villin-induc... | KEEP AS NON CORE | Summary: PLCG1 responds to EGF by translocation, tyrosine phosphorylation and activation. Reason: Correct but largely redundant with GO:0007173 EGFR signaling pathway. Supporting Evidence: PMID:17229814 Basal as well as epidermal growth factor (EGF)-stimulated cell migration was accompanied by tyrosine phosphorylation of villin and its association with PLC-gamma(1). |
| GO:0071364 cellular response to epidermal growth factor stimulus | IMP PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | KEEP AS NON CORE | Summary: PLCG1 responds to EGF by translocation, tyrosine phosphorylation and activation. Reason: Correct but largely redundant with GO:0007173 EGFR signaling pathway. Supporting Evidence: PMID:22454520 Downregulation of PLCΞ³1 also inhibited the EGF-mediated calcium increase in PC3 |
| GO:0120025 plasma membrane bounded cell projection | IDA PMID:22454520 A novel regulatory mechanism links PLCΞ³1 to PDK1. | ACCEPT | Summary: PLCG1 colocalises with PDK1 at EGF-induced cell protrusions. Reason: Directly observed by confocal microscopy in the cited study; consistent with ruffle/lamellipodium localization. Supporting Evidence: PMID:22454520 Confocal microscopy analysis indicated that EGF induced a strong colocalisation of the two proteins at the plasma membrane, in particular at the level of cell protrusions |
| GO:0120548 phosphatidylinositol phospholipase C activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: Hydrolysis of phosphatidylinositol (PI) to inositol 1-phosphate and DAG (RHEA:43484), transferred from rat Plcg1 and Rhea mapping. Reason: PLC-gamma enzymes hydrolyse PI in vitro in addition to PI(4,5)P2, but PI(4,5)P2 is the physiological substrate that generates IP3 and DAG. Retained as a real but secondary activity. Supporting Evidence: PMID:1379697 Stimulation of certain receptor tyrosine kinases results in the tyrosine phosphorylation and activation of phospholipase C gamma (PLC gamma), an enzyme that catalyses the hydrolysis of phosphatidylinositol (PtdIns). PMID:2550068 mPLC-I, mPLC-II, and PLC-II hydrolyzed both PI and PIP2 |
| GO:0120548 phosphatidylinositol phospholipase C activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Hydrolysis of phosphatidylinositol (PI) to inositol 1-phosphate and DAG (RHEA:43484), transferred from rat Plcg1 and Rhea mapping. Reason: PLC-gamma enzymes hydrolyse PI in vitro in addition to PI(4,5)P2, but PI(4,5)P2 is the physiological substrate that generates IP3 and DAG. Retained as a real but secondary activity. Supporting Evidence: PMID:1379697 Stimulation of certain receptor tyrosine kinases results in the tyrosine phosphorylation and activation of phospholipase C gamma (PLC gamma), an enzyme that catalyses the hydrolysis of phosphatidylinositol (PtdIns). PMID:2550068 mPLC-I, mPLC-II, and PLC-II hydrolyzed both PI and PIP2 |
| GO:0140324 lysophospholipase C activity | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Lysophospholipase C activity transferred by ISS from rat Plcg1. Reason: No human evidence and no characterised lysophospholipid substrate for PLCG1 appears in the literature reviewed; the documented substrates are PI(4,5)P2 (physiological) and PI. The transferred term is not well supported as a function of PLCG1. |
| GO:1905564 positive regulation of vascular endothelial cell proliferation | IMP PMID:27464494 MiR-30s Family Inhibit the Proliferation and Apoptosis in Hu... | KEEP AS NON CORE | Summary: miR-30e targeting of PLCG1 3'UTR affects coronary artery endothelial cell proliferation. Reason: Indirect evidence (miRNA targeting, abstract-only). PLCG1 contributes to growth-factor-driven endothelial proliferation, so the direction is plausible, but this is a downstream cellular outcome. Supporting Evidence: PMID:27464494 initially explored the effects of miR-30b and miR-30e on cell cycle and apoptosis through targeting ITGA4 and PLCG1 |
| GO:2000353 positive regulation of endothelial cell apoptotic process | IMP PMID:27464494 MiR-30s Family Inhibit the Proliferation and Apoptosis in Hu... | MARK AS OVER ANNOTATED | Summary: miR-30e targeting of PLCG1 3'UTR reportedly affects endothelial apoptosis. Reason: Evidence is indirect (miRNA targeting in one study, abstract-only) and PLCG1 is more usually described as pro-survival downstream of RTKs; a positive regulation of endothelial apoptosis is not a robust or characteristic role of PLCG1. Supporting Evidence: PMID:27464494 initially explored the effects of miR-30b and miR-30e on cell cycle and apoptosis through targeting ITGA4 and PLCG1 |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:1379697 Point mutation of an FGF receptor abolishes phosphatidylinos... | NEW | Summary: PLCG1 is recruited via its nSH2 domain to FGFR1 pY766 (conserved in FGFR2-4), phosphorylated by the receptor kinase and hydrolyses PIP2; mutation of Y766 abolishes FGF-induced PI turnover and Ca2+ flux. Reason: PLCG1 performs a catalytic step of the FGFR pathway (second-messenger generation), so it passes the participation test; it is not merely a substrate or a requirement. Comparator check: PLCG1 already carries GO:0007173 EGFR signaling pathway for the same effector role, and FRS2, the other direct FGFR-docked effector, carries GO:0008543 (IGI/IBA). Neither human, mouse nor rat PLCG1 currently carries GO:0008543, which appears to be a gap rather than a convention, given that the analogous EGFR term is annotated. Note that FGFR-driven mitogenesis does not require the PLCG1 branch. Evidence code is IGI with FGFR1 (UniProtKB:P11362) as the interacting gene, because the perturbation in PMID:1379697 is the FGFR1 Y766F mutation, not a mutation in PLCG1. Supporting Evidence: PMID:1379697 a fibroblast growth factor (FGF) receptor with a single point mutation at residue 766 replacing tyrosine with phenylalanine fails to associate with PLC gamma in response to FGF PMID:23063561 the requirement of a single phosphorylated tyrosine (pY766 for FGFR1) in the unstructured receptor C-terminal tail has been shown to be necessary and sufficient for the recruitment of PLCΞ³ isoforms PMID:20011604 PI3K activity is required for FGF-2-induced PLCgamma1 activation and the PI3K/PLCgamma1 pathway is involved in FGF-2-dependent cell migration, determined using Transwell assay, and in FGF-2-induced capillary tube formation (tubulogenesis assays in vitro). PMID:23063561 In the context of fibroblast growth-factor receptor signaling, the coordinated involvement of nSH2 and cSH2 domains mediates efficient phosphorylation of PLCΞ³1 |
| GO:0048008 platelet-derived growth factor receptor signaling pathway | IDA PMID:1396585 Identification of two C-terminal autophosphorylation sites i... | NEW | Summary: PLCG1 binds PDGFRB pY1009/pY1021 via its SH2 domains and is tyrosine phosphorylated and activated by the receptor. Reason: PLCG1 is the catalytic PIP2-hydrolysing effector of PDGFR signalling; PDGFR is a core receptor context alongside EGFR, FGFR and VEGFR2. Supporting Evidence: PMID:1396585 tyrosine phosphorylation of PLC-gamma is dependent on autophosphorylation of the PDGF beta-receptor at Tyr1009 and Tyr1021 PMID:15641795 is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor receptor (PDGFR) |
| GO:0048010 vascular endothelial growth factor receptor signaling pathway | IDA PMID:11387210 A single autophosphorylation site on KDR/Flk-1 is essential ... | NEW | Summary: PLC-gamma binds phospho-Y1175 of KDR/VEGFR2 through its C-terminal SH2 domain, is tyrosine phosphorylated in a Y1175-dependent manner and drives the PLC-gamma-PKC-MAPK route to endothelial DNA synthesis. Reason: Lead from the falcon deep research report, checked against the primary paper. PLCG1 performs a step of VEGFR2 signalling (PIP2 hydrolysis generating the DAG that activates PKC and the Raf-MEK-ERK route), so it passes the participation test in the same way as the existing EGFR term and the proposed FGFR/PDGFR terms; the core-function text already names VEGFR2 as a core receptor context. Comparator check: other VEGFR2 effectors (PRKCB, PRKD1/2, PTK2, SRC, FYN, VAV1) carry GO:0048010 in human GOA, so the term is used for signalling effectors. Caveat: the study expressed human KDR in mouse and bovine endothelial cells and detected endogenous PLC-gamma with a pan-PLC-gamma antibody; PLCG1 is the predominant endothelial PLC-gamma isoform, but a human-cell PLCG1-specific experiment would be stronger. Supporting Evidence: PMID:11387210 the C-terminal SH2 domain of PLC-Ξ³ is directly associated with the phosphorylated Y1175 on KDR/Flk-1 PMID:11387210 the PY1175 site is the single major PLC-Ξ³-binding site on KDR |
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Download this section (compressed HTML)Q: Should the rat-derived ISS annotations for guanyl-nucleotide exchange factor activity (dynamin-1) and lysophospholipase C activity be retained for human PLCG1 without human evidence?
Q: How much of PLCG1's contribution to mitogenesis and migration is lipase-independent (SH3/SH2 scaffolding) versus dependent on PIP2 hydrolysis, and should lipase-independent roles be captured with separate MF terms?
Q: Which receptor contexts (EGFR, FGFR, PDGFR, VEGFR2, TCR) should be treated as core pathway annotations for PLCG1, given its broad use as a common RTK/immune receptor effector?
Q: Is the IDA COP9 signalosome annotation from the Tespa1 study (PMID:22561606) a mis-mapping of 'TCR signalosome', and should the source curator be contacted?
Q: Does human PLCG1 have physiologically relevant lysophospholipase C activity, as transferred by ISS from rat?
Q: Should the non-catalytic, SH2/SH3-mediated cross-linking of phospho-LAT and SOS1 that promotes LAT condensate formation and shields LAT from CD45 (PMID:33929486, largely in vitro reconstitution) be captured as a separate scaffold-type molecular function, and how much does it contribute to TCR signalling relative to PIP2 hydrolysis in primary T cells?
Q: Review-level sources summarised in deep research place PLCG1 at focal adhesions (with GIT1, beta-PIX and FAK) and describe a nuclear ~120 kDa PLCG1 fragment. Is there primary human evidence strong enough to support focal adhesion or nucleus localization annotations?
Q: Deep research describes AKT as an SH3-domain binding partner of PLCG1, whereas the cited interaction evidence here was read as PLCG1 being an AKT1 substrate. Is there a direct SH3-dependent PLCG1-AKT interaction?
Experiment: Compare PLCG1 Tyr783 phosphorylation, IP1 accumulation and Ca2+ flux after FGF stimulation in isogenic human cells expressing wild-type or Y766F FGFR1, with and without PLCG1 nSH2/cSH2 point mutants.
Hypothesis: The FGFR pY766 docking site is the sole route for PLCG1 activation downstream of FGFR in human cells.
Type: isogenic mutational signaling assay
Experiment: Test purified human PLCG1 SH3 domain and full-length protein for DNM1 GDP/GTP exchange in vitro, and assess endocytosis in PLCG1-null human cells rescued with lipase-dead versus SH3-mutant PLCG1.
Hypothesis: Human PLCG1 SH3 domain has GEF activity toward dynamin-1.
Type: in vitro GEF assay and rescue
Experiment: Measure basal and receptor-stimulated PIP2 hydrolysis of purified variants on liposomes and relate to HDX-MS/structural changes at the cSH2-C2 interface.
Hypothesis: Disease-associated activating PLCG1 variants (S345F, S1021F) act by weakening cSH2-C2 autoinhibition.
Type: biochemical and structural variant analysis
Experiment: Rescue PLCG1-knockout cells with lipase-dead (e.g. catalytic H335A) versus SH3-mutant PLCG1 to separate lipase-dependent from SH3/GEF-dependent outputs in EGF-induced migration and mitogenesis.
Experiment: Assay recombinant human PLCG1 against lysophosphatidylinositol and other lysophospholipids to test the ISS-transferred lysophospholipase C activity.
Experiment: Reconstitute PLCG1-deficient Jurkat T cells with lipase-dead, nSH2-mutant, cSH2-mutant and SH3-mutant PLCG1 and measure LAT microcluster size, LAT Y132 phosphorylation, Ca2+ flux and ERK activation, to separate the condensate-scaffold role from PIP2 hydrolysis.
Experiment: Knock down PLCG1 in human endothelial cells (HUVEC) and test VEGF-A-induced IP3/Ca2+, PKC and ERK activation and DNA synthesis, with rescue by wild-type versus SH2-mutant PLCG1, to confirm the isoform-specific role downstream of KDR pY1175.
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