PIK3R1 encodes p85alpha and shorter regulatory isoforms of class IA phosphatidylinositol 3-kinase. Its SH2 domains recognize phosphorylated receptors and adaptor proteins, while its p110-binding region stabilizes catalytic PI3K subunits, restrains basal activity and permits stimulus-dependent activation. These functions link growth-factor, insulin and immune-receptor signaling to phosphoinositide production and AKT responses. P110-free p85alpha also has regulatory roles, including IRS sequestration, PTEN stabilization/activity, and XBP1-dependent unfolded-protein responses. The protein is predominantly cytosolic with recruited membrane and context-dependent intracellular pools. Different isoforms and variants can therefore increase or decrease pathway activity and produce distinct metabolic or immune phenotypes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000209 protein polyubiquitination | IDA PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | MARK AS OVER ANNOTATED | Summary: The cited ubiquitination experiment acts on p85alpha as the substrate. Reason: Full PMID27708159 identifies KBTBD2 as the substrate-recognition subunit of a CUL3 ligase and p85alpha as its polyubiquitinated degradation target. It does not establish p85alpha performing the ubiquitination step. The separate ability of p85alpha to protect PTEN from WWP2-dependent degradation (PMID26222500) is regulation of another protein, not evidence that this substrate-only assay establishes protein polyubiquitination participation. Its insulin/PI3K regulatory work is retained separately. Supporting Evidence: PMID:27708159 KBTBD2 targeted p85Ξ±, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85Ξ± ubiquitination and proteasome-mediated degradation. |
| GO:0001678 intracellular glucose homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Role in intracellular glucose homeostasis via insulin/PI3K signaling. Reason: p85Ξ± contributes to glucose handling as the regulatory subunit coupling the insulin receptor/IRS to PI3K-AKT; this is a downstream physiological role rather than the core biochemical function. Electronic annotation from mouse ortholog is biologically reasonable. |
| GO:0001678 intracellular glucose homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Role in intracellular glucose homeostasis (ISS from mouse ortholog). Reason: p85Ξ± contributes to glucose handling as the regulatory subunit coupling the insulin receptor/IRS to PI3K-AKT; this is a downstream physiological role rather than the core biochemical function. Electronic annotation from mouse ortholog is biologically reasonable. |
| GO:0001784 phosphotyrosine residue binding | IEA GO_REF:0000117 | ACCEPT | Summary: SH2 domains of p85Ξ± bind phosphotyrosine (pYXXM) motifs β a core adaptor activity. Reason: p85Ξ± has two SH2 domains that dock tyrosine-phosphorylated YXXM motifs on activated receptors and adaptor/scaffold proteins; this is a well-established core molecular function and the basis of its receptor-coupling role. |
| GO:0001784 phosphotyrosine residue binding | IPI PMID:20624904 Tarp regulates early Chlamydia-induced host cell survival th... | ACCEPT | Summary: p85Ξ± SH2 phosphotyrosine binding confirmed on an SH2/PTB-domain microarray. Reason: Supports the core phosphotyrosine-binding activity of p85Ξ±'s SH2 domains, assayed here on a comprehensive SH2/PTB-domain protein microarray. Supporting Evidence: PMID:20624904 virtually all human SRC homology 2 (SH2) and phosphotyrosine binding domains |
| GO:0005068 transmembrane receptor protein tyrosine kinase adaptor activity | ISS GO_REF:0000024 | ACCEPT | Summary: Adaptor that couples activated receptor tyrosine kinases to the p110 catalytic subunit. Reason: Captures p85Ξ±'s core adaptor role: its SH2 domains bind phospho-RTKs and its iSH2 recruits p110, bridging receptors to PI3K. ISS from the mouse ortholog is consistent with extensive human data. |
| GO:0005158 insulin receptor binding | IPI PMID:7537849 Phosphotyrosine-dependent interaction of SHC and insulin rec... | KEEP AS NON CORE | Summary: p85Ξ± SH2 domains bind the tyrosine-phosphorylated insulin receptor. Reason: p85Ξ± binds phosphorylated INSR (via its SH2 domains at the YTHM/NPEY region; UniProt SUBUNIT), an instance of its general phosphotyrosine-binding/adaptor activity toward a specific receptor. Retained as a specific, non-core facet of the core SH2 function. |
| GO:0005159 insulin-like growth factor receptor binding | IPI PMID:7541045 Non-SH2 domains within insulin receptor substrate-1 and SHC ... | KEEP AS NON CORE | Summary: p85Ξ± interacts directly and specifically with the IGF-I receptor. Reason: Direct SH2-mediated binding of p85Ξ± to IGF1R, a specific instance of its phosphotyrosine-binding adaptor activity toward a receptor tyrosine kinase. Supporting Evidence: PMID:7541045 phosphatidylinositol 3-kinase interact directly and specifically with the IGFIR. |
| GO:0005168 neurotrophin TRKA receptor binding | IPI PMID:15488758 TrkA alternative splicing: a regulated tumor-promoting switc... | KEEP AS NON CORE | Summary: p85Ξ± links to NTRK1/TrkA signaling (PI3K/Akt) in neuroblastoma. Reason: Specific receptor-binding facet of p85Ξ±'s SH2 adaptor activity toward TrkA; TrkA/TrkAIII signals through PI3K/Akt. Retained as non-core, receptor-specific. |
| GO:0005515 protein binding | IPI PMID:10500481 A fluorescent indicator for tyrosine phosphorylation-based i... | MODIFY | Summary: The reported interaction can be specified as insulin receptor binding. Reason: The original interaction record identifies partner P06213. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor binding |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:10660596 Tyrosine dephosphorylation and deactivation of insulin recep... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:10752619 Alternative modes of binding of proteins with tandem SH2 dom... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:10811803 Association of Grb2, Gads, and phospholipase C-gamma 1 with ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:10820259 GRID: a novel Grb-2-related adapter protein that interacts w... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:10978177 Identification of major tyrosine phosphorylation sites in th... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:11123912 NMR structure of the N-SH2 of the p85 subunit of phosphoinos... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:11403293 Split luciferase as an optical probe for detecting protein-p... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:11416002 Tyr(612) and Tyr(632) in human insulin receptor substrate-1 ... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:11710529 Tyrosine phosphorylation-dependent yeast two-hybrid system f... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:11796522 PLC-gamma1 enzyme activity is required for insulin-induced D... | MODIFY | Summary: The reported interaction can be specified as insulin receptor binding. Reason: The original interaction record identifies partner P06213. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor binding |
| GO:0005515 protein binding | IPI PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:1314164 Phosphorylation sites in the PDGF receptor with different sp... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:1330535 Interaction of the p85 subunit of PI 3-kinase and its N-term... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:1380456 Phosphatidylinositol 3'-kinase is activated by association w... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:1382595 Inhibition of SH2 domain/phosphoprotein association by a non... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:14632132 Locating a protein-protein interaction in living cells via s... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:16043515 The p85 regulatory subunit of phosphoinositide 3-kinase down... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:16230374 Insulin receptor substrate is a mediator of phosphoinositide... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:16638574 Reduced phosphatase activity of SHP-2 in LEOPARD syndrome: c... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16858407 Toll-like receptor 3 associates with c-Src tyrosine kinase o... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16917505 Direct binding of p85 to sst2 somatostatin receptor reveals ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16982329 Constitutive c-jun N-terminal kinase activity in acute myelo... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16982329 Constitutive c-jun N-terminal kinase activity in acute myelo... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16982329 Constitutive c-jun N-terminal kinase activity in acute myelo... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:16982329 Constitutive c-jun N-terminal kinase activity in acute myelo... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:18059340 Interaction with PI3-kinase contributes to the cytotoxic act... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:18079394 The structure of a human p110alpha/p85alpha complex elucidat... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:18412956 Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:18641334 ICOS ligation recruits the p50alpha PI3K regulatory subunit ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:18641334 ICOS ligation recruits the p50alpha PI3K regulatory subunit ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19380743 Charting the molecular network of the drug target Bcr-Abl. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19574958 Mal connects TLR2 to PI3Kinase activation and phagocyte pola... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:19574958 Mal connects TLR2 to PI3Kinase activation and phagocyte pola... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19805105 A frequent kinase domain mutation that changes the interacti... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:19807924 Identification of SH3 domain interaction partners of human F... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19864249 High content screening for inhibitors of protein interaction... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:19903481 Involvement of Src tyrosine kinase in Escherichia coli invas... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20007781 Specific apoptosis induction by the dual PI3K/mTor inhibitor... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:20018188 C-mip interacts with the p85 subunit of PI3 kinase and exert... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:20018188 C-mip interacts with the p85 subunit of PI3 kinase and exert... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20227043 An activated ErbB3/NRG1 autocrine loop supports in vivo prol... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20541701 NSAID sulindac and its analog bind RXRalpha and inhibit RXRa... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20598684 Abi1/Hssh3bp1 pY213 links Abl kinase signaling to p85 regula... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20711237 LAPTM4B: a novel cancer-associated gene motivates multidrug ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:20713702 Cancer-derived mutations in the regulatory subunit p85alpha ... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:20713702 Cancer-derived mutations in the regulatory subunit p85alpha ... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab tre... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab tre... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:21241768 Phosphoinositide 3-kinase as a novel functional target for t... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21241768 Phosphoinositide 3-kinase as a novel functional target for t... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner Q9Y4H2. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21827948 Dynamics of the phosphoinositide 3-kinase p110Ξ΄ interaction ... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner O00329. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21946561 NYAP: a phosphoprotein family that links PI3K to WAVE1 signa... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21946561 NYAP: a phosphoprotein family that links PI3K to WAVE1 signa... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:21954290 Tyrosine phosphorylation of the GΞ±-interacting protein GIV p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:22020336 p37Ξ΄ is a new isoform of PI3K p110Ξ΄ that increases cell prol... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner O00329. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:22402981 Integrin/Fak/Src-mediated regulation of cell survival and an... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:22439932 NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR ... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:22810585 Viral immune modulators perturb the human molecular network ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23065768 Activation of rapid oestrogen signalling in aggressive human... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23246379 FLT3 signals via the adapter protein Grb10 and overexpressio... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23275563 Development and application of a DNA microarray-based yeast ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23604317 FBXL2- and PTPL1-mediated degradation of p110-free p85Ξ² regu... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23617393 Insulin receptor substrate-2 is expressed in kidney epitheli... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner Q9Y4H2. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:23643389 Gain of interaction with IRS1 by p110Ξ±-helical domain mutant... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:23643389 Gain of interaction with IRS1 by p110Ξ±-helical domain mutant... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:23676467 FAM83B-mediated activation of PI3K/AKT and MAPK signaling co... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:23853584 The interactomes of influenza virus NS1 and NS2 proteins ide... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:24165795 Dominant-activating germline mutations in the gene encoding ... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner O00329. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The reported interaction can be specified as ErbB-3 class receptor binding. Reason: The original interaction record identifies partner P21860. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: ErbB-3 class receptor binding |
| GO:0005515 protein binding | IPI PMID:24498420 JMJD6 regulates ERΞ± methylation on arginine. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The reported interaction can be specified as insulin-like growth factor receptor binding. Reason: The original interaction record identifies partner P08069. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin-like growth factor receptor binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25253337 Hijacking Dlg1 for oncogenic phosphatidylinositol 3-kinase a... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:25284480 Naturally occurring neomorphic PIK3R1 mutations activate the... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:26210919 Phosphorylation of serine 523 on 5-lipoxygenase in human B l... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:26210919 Phosphorylation of serine 523 on 5-lipoxygenase in human B l... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner Q9Y4H2. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:27135603 A TRAF-like motif of the inducible costimulator ICOS control... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:27478041 Salt-Inducible Kinase 2 Couples Ovarian Cancer Cell Metaboli... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:28169297 Comparative influenza protein interactomes identify the role... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:31031754 Case Study: Mechanism for Increased Follicular Helper T Cell... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner O00329. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:31820037 Elucidation of protein interactions necessary for the mainte... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:32606397 PI3K activation is enhanced by FOXM1D binding to p110 and p8... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:34606829 Mapping the Phospho-dependent ALK Interactome to Identify No... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner O00329. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42336. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: The reported interaction can be specified as phosphatidylinositol 3-kinase binding. Reason: The original interaction record identifies partner P42338. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: phosphatidylinositol 3-kinase binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: The reported interaction can be specified as insulin receptor binding. Reason: The original interaction record identifies partner P06213. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: The reported interaction can be specified as insulin-like growth factor receptor binding. Reason: The original interaction record identifies partner P08069. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin-like growth factor receptor binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:39572596 Multi-layered proteomics identifies insulin-induced upregula... | MODIFY | Summary: The reported interaction can be specified as insulin receptor binding. Reason: The original interaction record identifies partner P06213. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor binding |
| GO:0005515 protein binding | IPI PMID:7536927 Measurement of the binding of tyrosyl phosphopeptides to SH2... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:7537096 Formation of signal transfer complexes between stem cell and... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7568038 p56Lck and p59Fyn regulate CD28 binding to phosphatidylinosi... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7584133 Selective CD28pYMNM mutations implicate phosphatidylinositol... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7589433 Interaction of p85 subunit of PI 3-kinase with insulin and I... | MODIFY | Summary: The reported interaction can be specified as insulin-like growth factor receptor binding. Reason: The original interaction record identifies partner P08069. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin-like growth factor receptor binding |
| GO:0005515 protein binding | IPI PMID:7642582 Localization of the insulin-like growth factor I receptor bi... | MODIFY | Summary: The reported interaction can be specified as insulin-like growth factor receptor binding. Reason: The original interaction record identifies partner P08069. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin-like growth factor receptor binding |
| GO:0005515 protein binding | IPI PMID:7657594 Interaction of the Flt-1 tyrosine kinase receptor with the p... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7680095 SH2 domains exhibit high-affinity binding to tyrosine-phosph... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:7680644 A photoaffinity scan maps regions of the p85 SH2 domain invo... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:7680644 A photoaffinity scan maps regions of the p85 SH2 domain invo... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:7692233 Two signaling molecules share a phosphotyrosine-containing b... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7782332 Growth hormone, interferon-gamma, and leukemia inhibitory fa... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:7797556 Src phosphorylation of the epidermal growth factor receptor ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7807015 CTLA-4 binding to the lipid kinase phosphatidylinositol 3-ki... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:7807015 CTLA-4 binding to the lipid kinase phosphatidylinositol 3-ki... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:8146197 T-cell antigen CD28 interacts with the lipid kinase phosphat... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:8183372 Binding of phosphatidylinositol-3-OH kinase to CD28 is requi... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:8226808 Identification of Trk binding sites for SHC and phosphatidyl... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:8276809 Direct activation of the phosphatidylinositol 3'-kinase by t... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:8382612 Specific phosphopeptide binding regulates a conformational c... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8382612 Specific phosphopeptide binding regulates a conformational c... | MODIFY | Summary: The reported interaction can be specified as insulin receptor substrate binding. Reason: The original interaction record identifies partner P35568. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor substrate binding |
| GO:0005515 protein binding | IPI PMID:8564419 Structure-activity studies of phosphorylated peptide inhibit... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8603569 Interaction of the molecular weight 85K regulatory subunit o... | MODIFY | Summary: The reported interaction can be specified as insulin-like growth factor receptor binding. Reason: The original interaction record identifies partner P08069. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin-like growth factor receptor binding |
| GO:0005515 protein binding | IPI PMID:8670861 Structure of a specific peptide complex of the carboxy-termi... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8961927 Structural and thermodynamic characterization of the interac... | MODIFY | Summary: The p85 proline-rich site binds the Fyn SH3 domain. Reason: The cited structural/thermodynamic study resolves this domain-specific interaction; the supported function is SH3 domain binding, not a transferred Fyn kinase activity. Proposed replacements: SH3 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9153411 Dual specificity of Src homology 2 domains for phosphotyrosi... | MODIFY | Summary: The p85 SH2 interaction is phosphotyrosine-residue binding. Reason: The original source examines phosphotyrosine-containing peptides or their recognition by p85 SH2 domains. This is the specific chemical recognition underpinning receptor/adaptor docking, rather than undifferentiated protein binding. Independent p85 SH2 structural evidence corroborates that class. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:9160881 Yeast two-hybrid in vivo association of the Src kinase Lyn w... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9178760 Intracellular signaling of the Ufo/Axl receptor tyrosine kin... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9223670 The phosphatidylinositol 3' kinase pathway is required for t... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9398332 Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9417079 Growth factor receptor-bound protein 2 SH2/SH3 domain bindin... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9593725 Association of the insulin receptor with phospholipase C-gam... | MODIFY | Summary: The reported interaction can be specified as insulin receptor binding. Reason: The original interaction record identifies partner P06213. Independent target-specific biochemical, structural or curated evidence supports this named binding class; it is more informative than bare protein binding. The original assay is retained as such, without claiming every co-complex/screen row proves purified direct binding. Binding is not interpreted as the catalytic activity of the partner. Proposed replacements: insulin receptor binding |
| GO:0005515 protein binding | IPI PMID:9658397 Determination of Gab1 (Grb2-associated binder-1) interaction... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9813138 Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM ... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005515 protein binding | IPI PMID:9890970 Fyn associates with Cbl and phosphorylates tyrosine 731 in C... | REMOVE | Summary: Interaction annotation captured only as the generic term 'protein binding' (GO:0005515), which conveys no molecular function. Reason: Per curation policy GO:0005515 is uninformative and is removed. The physical interaction may be genuine, but the generic term adds no functional content and specific interactions are not invented from binding data alone. p85Ξ±'s informative molecular functions are captured by dedicated terms: PI3K regulator activity (GO:0046935), phosphotyrosine residue binding (GO:0001784), RTK adaptor activity (GO:0005068) and class IA PI3K complex membership (GO:0005943). |
| GO:0005634 nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Reported nuclear pool of p85Ξ±. Reason: Retain the mouse-derived nuclear pool in its insulin/ER-stress context. The donor source PMID20348926 follows p85βXBP1 complexes and nuclear translocation; this is distinct from assuming that transporting XBP1 automatically places every p85 molecule in the nucleus. The protein also has well-supported cytosolic and membrane-associated pools. Supporting Evidence: |
| GO:0005634 nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Reported nuclear pool of p85Ξ± (ISS from mouse ortholog). Reason: Retain the mouse-derived nuclear pool in its insulin/ER-stress context. The donor source PMID20348926 follows p85βXBP1 complexes and nuclear translocation; this is distinct from assuming that transporting XBP1 automatically places every p85 molecule in the nucleus. The protein also has well-supported cytosolic and membrane-associated pools. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | ACCEPT | Summary: Cytoplasmic localization of p85Ξ±. Reason: The original UPR study examines p85alpha/XBP1 interactions in cultured cells; its nuclear/cytoplasmic fractionation primarily follows XBP1. Independent human PIK3R1 curated localization and the soluble signaling architecture support the cytoplasmic pool, so the biological location is retained without mislabeling the XBP1 assay as new p85 imaging. Supporting Evidence: file:genes/human/PIK3R1/PIK3R1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32606397}. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasmic localization of p85Ξ± (electronic). Reason: Consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm); p85Ξ±/PI3K is a soluble cytoplasmic protein before membrane recruitment. |
| GO:0005801 cis-Golgi network | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cis-Golgi network localization (electronic, mouse ortholog). Reason: The mouse donor maps to PMID25217619. Its full Results/Fig. 1 compare endogenous and recombinant p85alpha with p85beta in NIH3T3 cells and identify p85alpha in perinuclear internal membranes including cis-Golgi. Retain this specific ortholog-derived pool without transferring p85beta invadopodial localization or relabeling the experiment as human p85alpha imaging. Supporting Evidence: |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109699 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114542 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226012 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226014 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250189 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250346 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250353 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1250370 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1306979 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1433514 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1562641 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1676048 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1676109 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177927 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177931 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-177939 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839078 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839080 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839091 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839102 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839107 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1839114 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-186780 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-186800 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-198266 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-198315 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201510 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201515 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202203 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202365 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029271 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029273 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-204798 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-205262 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424480 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424482 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730842 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730870 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-388830 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-388832 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-389158 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-416358 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-437118 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-437162 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-443402 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-508247 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218819 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5357479 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637765 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637801 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654591 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654592 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654594 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654596 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654612 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654614 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654620 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654622 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654637 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654640 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654641 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654643 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654659 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654662 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654667 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654669 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654690 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654692 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654697 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654701 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654705 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654709 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654714 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5654717 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655235 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655240 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655245 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655248 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655252 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655263 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655285 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655289 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655290 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655315 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655320 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5655323 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6790041 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-74737 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-879917 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8851954 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8852019 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854905 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9012657 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9013145 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9014294 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9018766 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9021627 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9021660 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9027275 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-912627 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-914182 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9606887 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9632412 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9658253 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664646 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664664 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664933 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664940 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665407 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665415 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9670431 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9670433 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672162 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672172 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672177 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9672178 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698170 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698174 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9703434 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9706340 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9706345 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712078 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712083 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712084 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9842649 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9845032 | ACCEPT | Summary: Cytosolic localization of p85Ξ± / the class IA PI3K holoenzyme (Reactome TAS). Reason: The p85Ξ±βp110 complex is largely soluble/cytosolic before stimulation, consistent with UniProt SUBCELLULAR LOCATION (Cytoplasm). Duplicate Reactome pathway-level rows are retained; duplicates across evidence are acceptable. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250189 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250462 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306957 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2045911 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2076220 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2394007 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9606887 | ACCEPT | Summary: Plasma membrane localization of the PI3K complex (Reactome TAS). Reason: Upon receptor activation the p85Ξ±βp110 heterodimer is recruited to the cytoplasmic face of the plasma membrane, where p110 accesses PI(4,5)P2; this is where the complex carries out its signaling function. Duplicate Reactome rows retained. |
| GO:0005911 cell-cell junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell-cell junction localization (electronic, mouse ortholog). Reason: Retain the inherited cell-contact localization. The mouse donor traces to PMID23793062 (immunological-synapse signaling), while PMID14699157 independently reports p85/PI3K recruitment to E-cadherin-mediated contacts in human intestinal epithelial cells. The latter supports the broad cell-cell-junction claim without claiming every junctional pool or assigning structural adhesion-molecule activity to p85. |
| GO:0005942 phosphatidylinositol 3-kinase complex | ISS GO_REF:0000024 | MODIFY | Summary: Specify the class IA phosphatidylinositol 3-kinase complex. Reason: PIK3R1 forms the regulatory component of class IA p85βp110 heterodimers. The specific complex term is already supported by human structures and retained independently. This does not imply that every p85 molecule is p110-bound: free p85 and p85 dimers have additional roles. Proposed replacements: phosphatidylinositol 3-kinase complex, class IA |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | IBA GO_REF:0000033 | ACCEPT | Summary: Subunit of the class IA PI3K complex (phylogenetic/IBD inference). Reason: Core complex membership: p85Ξ± is the regulatory subunit of the class IA PI3K heterodimer. The IBA reflects a well-supported ancestral assignment across the p85 family (PANTHER:PTN008302071), with the target itself among the descendant evidences. |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | IEA GO_REF:0000117 | ACCEPT | Summary: Subunit of the class IA PI3K complex (electronic). Reason: Correct complex membership; consistent with all direct structural evidence. |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | IPI PMID:19805105 A frequent kinase domain mutation that changes the interacti... | ACCEPT | Summary: p85Ξ± forms the class IA PI3K complex with p110 (structural/biochemical). Reason: Direct evidence: p85Ξ± (nSH2/iSH2) assembles with the p110Ξ± catalytic subunit into the class IA PI3K complex; the nSH2 forms a scaffold for the whole enzyme. Supporting Evidence: PMID:19805105 domain of p85alpha is shown to form a scaffold for the entire enzyme complex |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | IPI PMID:20713702 Cancer-derived mutations in the regulatory subunit p85alpha ... | ACCEPT | Summary: p85Ξ± binds p110Ξ±/p110Ξ² within the class IA PI3K complex (cancer-mutant study). Reason: Confirms p85Ξ±βp110 complex formation; even oncogenic p85Ξ± mutants retain binding to the catalytic subunits while weakening inhibition and preserving stabilization. Supporting Evidence: PMID:20713702 preserving the stabilizing interaction between p85Ξ± iSH2 and the adapter-binding domain of p110Ξ±. |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | IPI PMID:28108251 Discovery of 7-(3-(piperazin-1-yl)phenyl)pyrrolo[2,1-f][1,2,... | ACCEPT | Summary: p85Ξ± in the class IA PI3K (p110Ξ΄) complex. Reason: Direct-interaction evidence for class IA PI3K complex membership (p110Ξ΄ context). |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | ISS GO_REF:0000024 | ACCEPT | Summary: Class IA PI3K complex membership (ISS). Reason: Correct complex membership by sequence similarity to an ortholog; consistent with all evidence. |
| GO:0005943 phosphatidylinositol 3-kinase complex, class IA | NAS P27986-3 PMID:20379207 The emerging mechanisms of isoform-specific PI3K signalling. | ACCEPT | Summary: p50Ξ± (isoform 3) as a class IA PI3K regulatory subunit. Reason: Isoform-specific (P27986-3 / p50Ξ±) membership of the class IA PI3K complex; the shorter regulatory isoforms also heterodimerize with p110. Retained. |
| GO:0006955 immune response | NAS PMID:27616589 PI3KΞ΄ and primary immunodeficiencies. | KEEP AS NON CORE | Summary: Involvement in immune response (narrative). Reason: Broad immune-response role reflecting p85Ξ±'s function in lymphocyte PI3K signaling (loss causes agammaglobulinemia/immunodeficiency). Pleiotropic/downstream; retained as non-core. |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: Refine generic signal transduction to the PI3K/AKT pathway. Reason: The gene supplies phosphotyrosine-dependent recruitment and regulation of class IA PI3K, thereby participating in PI3K/AKT signaling. This existing specific pathway term describes its signal-transduction work; independent immune, growth-factor and stress roles remain represented. Proposed replacements: phosphatidylinositol 3-kinase/protein kinase B signal transduction |
| GO:0008286 insulin receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Insulin receptor signaling pathway (phylogenetic inference). Reason: Core signaling role: p85Ξ± couples the tyrosine-phosphorylated insulin receptor/IRS to PI3K activation. Well-supported IBA across the p85 family and orthologs. |
| GO:0008286 insulin receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: Insulin receptor signaling pathway (electronic). Reason: Consistent with the IBA and extensive experimental literature on insulin/IRS/PI3K signaling. |
| GO:0010592 positive regulation of lamellipodium assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of lamellipodium assembly (electronic, mouse). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0010592 positive regulation of lamellipodium assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of lamellipodium assembly (ISS, mouse). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MODIFY | Summary: Specify membrane recruitment to the plasma membrane. Reason: PIK3R1 is a soluble regulatory subunit recruited to activated receptor-bearing plasma membranes, not an integral membrane protein. The NK membrane-proteomics source is consistent with peripheral association; independent curated recruitment and structural signaling evidence support the more precise location already retained. Proposed replacements: plasma membrane |
| GO:0016020 membrane | IEA GO_REF:0000107 | MODIFY | Summary: Specify membrane recruitment to the plasma membrane. Reason: PIK3R1 is a soluble regulatory subunit recruited to activated receptor-bearing plasma membranes, not an integral membrane protein. The NK membrane-proteomics source is consistent with peripheral association; independent curated recruitment and structural signaling evidence support the more precise location already retained. Proposed replacements: plasma membrane |
| GO:0019207 kinase regulator activity | IEA GO_REF:0000117 | MODIFY | Summary: Kinase regulator activity β generalizes to PI3K regulator activity. Reason: The specific and evidence-backed activity is regulation of the PI3-kinase (p110) catalytic subunit; the generic 'kinase regulator activity' should be replaced by the specific PI3K regulator term. Proposed replacements: 1-phosphatidylinositol-3-kinase regulator activity |
| GO:0019209 kinase activator activity | IEA GO_REF:0000107 | MODIFY | Summary: Kinase activator activity β specifically PI3K activation. Reason: p85Ξ± enables receptor-driven activation of PI3K (while also restraining basal activity); the generic 'kinase activator activity' should be the PI3K-specific activator term. Proposed replacements: phosphatidylinositol 3-kinase activator activity |
| GO:0019221 cytokine-mediated signaling pathway | IGI PMID:7782332 Growth hormone, interferon-gamma, and leukemia inhibitory fa... | KEEP AS NON CORE | Summary: Cytokine-mediated signaling (growth hormone) via IRS/PI3K. Reason: GH/cytokine receptors signal through JAK2βIRS-1 tyrosine phosphorylation, recruiting p85Ξ±/PI3K. Downstream pathway role; retained as non-core. Supporting Evidence: PMID:7782332 binding of IRS-1 to the 85-kDa regulatory subunit of PI 3'-kinase. |
| GO:0019903 protein phosphatase binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Protein phosphatase binding (electronic). Reason: Protein-phosphatase binding is independently supported by direct p85alphaβPTEN biochemistry and cellular association (PMID26222500). The cited PMID14699157 focuses on hDlg/E-cadherin/p85 complexes and its accessible abstract does not expose the phosphatase-specific experiment; it should not be described as newly verified direct PTEN binding. The biological claim remains supported independently rather than being removed because of this citation limitation. Supporting Evidence: |
| GO:0019903 protein phosphatase binding | IPI PMID:14699157 Human homolog of disc-large is required for adherens junctio... | KEEP AS NON CORE | Summary: Protein phosphatase binding (direct interaction). Reason: Protein-phosphatase binding is independently supported by direct p85alphaβPTEN biochemistry and cellular association (PMID26222500). The cited PMID14699157 focuses on hDlg/E-cadherin/p85 complexes and its accessible abstract does not expose the phosphatase-specific experiment; it should not be described as newly verified direct PTEN binding. The biological claim remains supported independently rather than being removed because of this citation limitation. Supporting Evidence: |
| GO:0030183 B cell differentiation | NAS PMID:20200404 The catalytic PI3K isoforms p110gamma and p110delta contribu... | KEEP AS NON CORE | Summary: B cell differentiation. Reason: Human biallelic p85alpha loss in PMID22351933 causes an early B-lineage developmental block despite preserved p50alpha/p55alpha expression, directly supporting this physiological role. PMID20200404 principally tests mouse catalytic p110gamma/p110delta deficiency and supplies comparative pathway context, not the human p85alpha deficiency experiment. Supporting Evidence: |
| GO:0030217 T cell differentiation | NAS PMID:17371229 The PI3K p110delta controls T-cell development, differentiat... | KEEP AS NON CORE | Summary: T cell differentiation. Reason: p85Ξ±/PI3K signaling contributes to T-cell development and function (CD28/ICOS costimulation). Developmental/pleiotropic; retained as non-core. |
| GO:0032869 cellular response to insulin stimulus | IDA PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | ACCEPT | Summary: Cellular response to insulin stimulus. Reason: Core physiological context: p85Ξ± mediates the cellular insulin response by coupling INSR/IRS to PI3K. Supported by the KBTBD2 study linking p85Ξ± abundance to insulin signaling. Supporting Evidence: PMID:27708159 KBTBD2 targeted p85Ξ±, the regulatory subunit |
| GO:0032869 cellular response to insulin stimulus | IEA GO_REF:0000120 | ACCEPT | Summary: Cellular response to insulin stimulus (electronic). Reason: Consistent with p85Ξ±'s central role in insulin/IRS/PI3K signaling. |
| GO:0032869 cellular response to insulin stimulus | ISS GO_REF:0000024 | ACCEPT | Summary: Cellular response to insulin stimulus (ISS). Reason: Consistent with p85Ξ±'s central role in insulin/IRS/PI3K signaling. |
| GO:0033120 positive regulation of RNA splicing | IMP PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Positive regulation of RNA splicing via the IRE1/XBP1 UPR arm. Reason: Through its ER-stress-dependent interaction with XBP1 and modulation of IRE1Ξ±, p85Ξ± influences the UPR (which includes XBP1 mRNA splicing). A specialized, context-specific role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0034143 regulation of toll-like receptor 4 signaling pathway | IDA PMID:19289601 TLR4/MyD88/PI3K interactions regulate TLR4 signaling. | KEEP AS NON CORE | Summary: Regulation of TLR4 signaling via MyD88/PI3K. Reason: p85Ξ± co-immunoprecipitates with MyD88 (YXXM motif) and modulates TLR4/PI3K signaling. A specific immune-signaling role; retained as non-core. Supporting Evidence: PMID:19289601 MyD88 and p85 were shown previously to |
| GO:0034446 substrate adhesion-dependent cell spreading | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Substrate adhesion-dependent cell spreading (ISS). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0034976 response to endoplasmic reticulum stress | IDA PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Response to endoplasmic reticulum stress (XBP1/UPR). Reason: p85Ξ± modulates the UPR by interacting with XBP1 in an ER-stress-dependent manner; loss reduces nuclear XBP1 and UPR target-gene induction. A specialized role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0034976 response to endoplasmic reticulum stress | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Response to ER stress (electronic). Reason: p85Ξ± modulates the UPR by interacting with XBP1 in an ER-stress-dependent manner; loss reduces nuclear XBP1 and UPR target-gene induction. A specialized role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0034976 response to endoplasmic reticulum stress | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Response to ER stress (ISS). Reason: p85Ξ± modulates the UPR by interacting with XBP1 in an ER-stress-dependent manner; loss reduces nuclear XBP1 and UPR target-gene induction. A specialized role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0035014 phosphatidylinositol 3-kinase regulator activity | IDA PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | ACCEPT | Summary: Phosphatidylinositol 3-kinase regulator activity β core function. Reason: Core molecular function: p85Ξ± is the regulatory subunit of PI3K, stabilizing p110 and restraining/enabling its activity. Directly supported by the KBTBD2 study. Supporting Evidence: PMID:27708159 causing p85Ξ± ubiquitination |
| GO:0035014 phosphatidylinositol 3-kinase regulator activity | ISS GO_REF:0000024 | ACCEPT | Summary: Phosphatidylinositol 3-kinase regulator activity (ISS). Reason: Core regulator activity, supported by sequence similarity to an ortholog and abundant human data. |
| GO:0035655 interleukin-18-mediated signaling pathway | IMP PMID:21321938 Interleukin-18/WNT1-inducible signaling pathway protein-1 si... | KEEP AS NON CORE | Summary: IL-18-mediated signaling via PI3K/Akt. Reason: IL-18 signaling engages PI3K/Akt (with WISP1) to drive vascular smooth-muscle proliferation; p85Ξ± acts as the PI3K regulatory subunit in this pathway. Specific/context; retained as non-core. Supporting Evidence: PMID:21321938 phosphatidylinositol 3-kinase/Akt-dependent IKK/NF-ΞΊB |
| GO:0036312 phosphatidylinositol 3-kinase regulatory subunit binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Phosphatidylinositol 3-kinase regulatory subunit binding (electronic). Reason: p85Ξ± can associate with regulatory subunits (homo/hetero-association, e.g. with PIK3R2); a specific binding facet. Retained as non-core. |
| GO:0042267 natural killer cell mediated cytotoxicity | IDA PMID:16582911 NKG2D-mediated signaling requires a DAP10-bound Grb2-Vav1 in... | KEEP AS NON CORE | Summary: Natural killer cell mediated cytotoxicity via DAP10/PI3K. Reason: The p85 subunit binds DAP10 and, together with Grb2-Vav1, is required for full NK-cell cytotoxicity downstream of NKG2D. A specific immune role; retained as non-core. Supporting Evidence: PMID:16582911 For full calcium release and cytotoxicity to occur, both Grb2-Vav1 and p85 had |
| GO:0042307 positive regulation of protein import into nucleus | IDA PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Positive regulation of protein import into nucleus (XBP1). Reason: p85Ξ± promotes nuclear accumulation/import of XBP1 during the UPR. Specialized role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0042307 positive regulation of protein import into nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of protein import into nucleus (electronic). Reason: Electronic annotation consistent with the XBP1 nuclear-accumulation role. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0043066 negative regulation of apoptotic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Negative regulation of apoptotic process (electronic). Reason: Consistent with p85Ξ±/PI3K-AKT pro-survival signaling and the UPR study (p85Ξ± loss increases apoptosis). Pleiotropic; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Negative regulation of apoptotic process (XBP1/UPR, IMP). Reason: Cells lacking p85Ξ± show increased apoptosis under ER stress, indicating an anti-apoptotic role via the UPR. Retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0043125 ErbB-3 class receptor binding | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | KEEP AS NON CORE | Summary: ErbB-3 (ERBB3) class receptor binding. Reason: p85Ξ± SH2 domains dock the multiple phospho-YXXM motifs of ERBB3, a specific instance of its phosphotyrosine-binding adaptor activity. Retained as non-core. |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IDA PMID:7782332 Growth hormone, interferon-gamma, and leukemia inhibitory fa... | ACCEPT | Summary: PI3K/AKT signal transduction β downstream pathway p85Ξ± enables. Reason: Core downstream pathway: by recruiting/regulating p110, p85Ξ± enables PIP3 production and AKT activation. Growth hormone/IRS-1 engagement of p85Ξ± exemplifies pathway entry. Supporting Evidence: PMID:7782332 binding of IRS-1 to the 85-kDa regulatory subunit of PI 3'-kinase. |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IEA GO_REF:0000117 | ACCEPT | Summary: PI3K/AKT signal transduction (electronic). Reason: Core downstream pathway of the class IA PI3K complex; consistent with all evidence. |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:21321938 Interleukin-18/WNT1-inducible signaling pathway protein-1 si... | ACCEPT | Summary: PI3K/AKT signal transduction (IMP, IL-18 context). Reason: Functional (IMP) support that p85Ξ±/PI3K drives Akt signaling in an IL-18-stimulated context. Supporting Evidence: PMID:21321938 phosphatidylinositol 3-kinase/Akt-dependent IKK/NF-ΞΊB |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | ISS GO_REF:0000024 | ACCEPT | Summary: PI3K/AKT signal transduction (ISS). Reason: Core downstream pathway; consistent with the IBA and human experimental data. |
| GO:0043548 phosphatidylinositol 3-kinase binding | ISS GO_REF:0000024 | ACCEPT | Summary: Phosphatidylinositol 3-kinase (p110) binding. Reason: Binding p110 is an integral part of the regulatory-subunit mechanism, not peripheral merely because it is a binding activity. Human p110alpha/p85alpha structures and mutational experiments support the interface, stabilization and regulation of the catalytic subunit. |
| GO:0043559 insulin binding | IDA PMID:8440175 Ligand-binding properties of the two isoforms of the human i... | UNDECIDED | Summary: Direct insulin-hormone binding by p85alpha remains unresolved. Reason: The accessible PMID8440175 abstract explicitly examines human insulin-receptor isoforms in CHO/Rat1 systems and does not resolve a p85alpha ligand-binding experiment. Full retrieval and the publisher DOI route failed, so the earlier categorical wrong-gene assertion is withdrawn. Established PIK3R1 binding to phosphorylated INSR/IRS proteins supports its signaling role but neither proves nor disproves direct binding to insulin itself. The original experimental annotation remains unresolved pending its full supporting assay. |
| GO:0043560 insulin receptor substrate binding | IEA GO_REF:0000107 | ACCEPT | Summary: Insulin receptor substrate (IRS) binding. Reason: Core adaptor facet: p85Ξ± SH2 domains bind tyrosine-phosphorylated IRS proteins (IRS1/2/4), the principal route by which the insulin/IGF axis engages PI3K. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of transcription by RNA Pol II (electronic). Reason: Indirect transcriptional effects via XBP1/UPR and PI3K-AKT signaling; not a direct DNA/transcription function of p85Ξ±. Retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Positive regulation of transcription by RNA Pol II (XBP1, IMP). Reason: p85Ξ± promotes XBP1 nuclear accumulation and induction of UPR target genes, an indirect transcriptional effect. Retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0045944 positive regulation of transcription by RNA polymerase II | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of transcription by RNA Pol II (ISS). Reason: Indirect transcriptional effect via UPR/PI3K signaling; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0046326 positive regulation of D-glucose import across plasma membrane | ISS PMID:8052599 1-Phosphatidylinositol 3-kinase activity is required for ins... | KEEP AS NON CORE | Summary: Positive regulation of glucose import (GLUT4) β insulin action. Reason: The original PMID8052599 assay used mutant p85alpha in CHO cells and measured impaired insulin-stimulated GLUT1 translocation and glucose uptake. The prior explanation incorrectly called this experiment GLUT4. Retain the existing orthology-supported transport-regulatory role; p85 organizes PI3K signaling and does not itself transport glucose. Supporting Evidence: |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | ISS GO_REF:0000024 | ACCEPT | Summary: Phosphatidylinositol phosphate biosynthetic process (as PI3K subunit). Reason: The p85 regulatory subunit contributes binding, stabilization and signal-dependent activation to the class IA PI3K complex producing phosphoinositide products. That is mechanistic participation in phosphoinositide biosynthesis, despite catalytic phosphate transfer being performed by p110. It is an integral process role, not merely a distant phenotype or a claim of autonomous p85 lipid-kinase activity. |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | ISS GO_REF:0000024 | ACCEPT | Summary: Phosphatidylinositol phosphate biosynthetic process (as PI3K subunit). Reason: The p85 regulatory subunit contributes binding, stabilization and signal-dependent activation to the class IA PI3K complex producing phosphoinositide products. That is mechanistic participation in phosphoinositide biosynthesis, despite catalytic phosphate transfer being performed by p110. It is an integral process role, not merely a distant phenotype or a claim of autonomous p85 lipid-kinase activity. |
| GO:0046935 1-phosphatidylinositol-3-kinase regulator activity | IBA GO_REF:0000033 | ACCEPT | Summary: 1-phosphatidylinositol-3-kinase regulator activity β core function (IBA). Reason: The precise core molecular function of p85Ξ±. Well-supported ancestral (IBD/IBA) assignment across the p85 regulatory-subunit family (PANTHER:PTN008302071) with mouse/rat experimental descendants. Supporting Evidence: file:human/PIK3R1/PIK3R1-deep-research-falcon.md stabilizes p110Ξ±/Ξ²/Ξ΄ while suppressing basal lipid-kinase activity |
| GO:0046982 protein heterodimerization activity | IEA GO_REF:0000107 | ACCEPT | Summary: Protein heterodimerization activity (p85Ξ±βp110 heterodimer). Reason: Class IA PI3K is an obligate p85βp110 heterodimer; p85Ξ±'s iSH2 mediates this heterodimerization. Correct and relevant. |
| GO:0048009 insulin-like growth factor receptor signaling pathway | IDA PMID:7782332 Growth hormone, interferon-gamma, and leukemia inhibitory fa... | KEEP AS NON CORE | Summary: IGF-I receptor signaling pathway. Reason: p85Ξ± couples the IGF1R/IRS module to PI3K; a specific instance of RTK-driven PI3K signaling. Retained as non-core. Supporting Evidence: PMID:7782332 binding of IRS-1 to the 85-kDa regulatory subunit of PI 3'-kinase. |
| GO:0048009 insulin-like growth factor receptor signaling pathway | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: IGF-I receptor signaling pathway (electronic). Reason: Consistent with p85Ξ±'s SH2-mediated coupling to IGF1R/IRS. Retained as non-core. |
| GO:0048009 insulin-like growth factor receptor signaling pathway | IPI PMID:7541045 Non-SH2 domains within insulin receptor substrate-1 and SHC ... | KEEP AS NON CORE | Summary: IGF-I receptor signaling pathway (direct interaction). Reason: Direct p85Ξ±βIGF1R interaction underlies its role in IGF signaling. Supporting Evidence: PMID:7541045 phosphatidylinositol 3-kinase interact directly and specifically with the IGFIR. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (electronic). Reason: The mouse transfer traces to PMID11038173. Its full Fig. 4D analysis reports cytosolicβperinuclear localization of p85alpha in NIH3T3 cells, with a similar endogenous pattern. This supports a conserved contextual pool; it is not by itself an ER-organelle marker or new native human imaging. |
| GO:0048471 perinuclear region of cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (ISS). Reason: The mouse transfer traces to PMID11038173. Its full Fig. 4D analysis reports cytosolicβperinuclear localization of p85alpha in NIH3T3 cells, with a similar endogenous pattern. This supports a conserved contextual pool; it is not by itself an ER-organelle marker or new native human imaging. |
| GO:0048661 positive regulation of smooth muscle cell proliferation | IMP PMID:21321938 Interleukin-18/WNT1-inducible signaling pathway protein-1 si... | KEEP AS NON CORE | Summary: Positive regulation of smooth muscle cell proliferation (IL-18/PI3K). Reason: PI3K/Akt signaling (with p85Ξ± as regulatory subunit) supports vascular smooth-muscle proliferation downstream of IL-18. Context-specific; retained as non-core. Supporting Evidence: PMID:21321938 phosphatidylinositol 3-kinase/Akt-dependent IKK/NF-ΞΊB |
| GO:0050821 protein stabilization | IDA PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Protein stabilization (p110 stabilization / XBP1). Reason: p85Ξ± stabilizes its binding partners β canonically the otherwise-unstable p110 catalytic subunit, and in the UPR it stabilizes/promotes nuclear XBP1. A facet of its regulator/adaptor role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:0051491 positive regulation of filopodium assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of filopodium assembly (electronic). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0051491 positive regulation of filopodium assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of filopodium assembly (ISS). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0051497 negative regulation of stress fiber assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Negative regulation of stress fiber assembly (electronic). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0051497 negative regulation of stress fiber assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Negative regulation of stress fiber assembly (ISS). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0052742 phosphatidylinositol kinase activity | ISS GO_REF:0000024 | REMOVE | Summary: PIK3R1 is the regulatory protein, not the lipid-phosphorylating PI3K catalytic subunit. Reason: The original ISS donor O18683 is retained in the payload; the reason for rejection is the target-specific separation of catalytic p110 from regulatory p85, not donor count or a family-label guess. PMID1322797 explicitly reports that p85alpha lacks PI3-kinase activity, and human p110alpha/p85alpha structures place the kinase domain in p110. This row does not carry a contributes_to flag; the supported regulatory activity and complex membership remain retained. This does not deny other p85 biochemical activities such as reported Rab regulation. Supporting Evidence: PMID:1322797 The 85 kd subunit (p85 alpha) lacks Pl3-kinase activity |
| GO:0060396 growth hormone receptor signaling pathway | IDA PMID:7782332 Growth hormone, interferon-gamma, and leukemia inhibitory fa... | KEEP AS NON CORE | Summary: Growth hormone receptor signaling pathway. Reason: GH receptor signaling recruits p85Ξ±/PI3K via JAK2/IRS-1 tyrosine phosphorylation. Specific pathway instance; retained as non-core. Supporting Evidence: PMID:7782332 binding of IRS-1 to the 85-kDa regulatory subunit of PI 3'-kinase. |
| GO:0061470 T follicular helper cell differentiation | IDA PMID:30523347 Transmembrane domain-mediated Lck association underlies byst... | KEEP AS NON CORE | Summary: T follicular helper cell differentiation via ICOS/PI3K. Reason: The ICOS study links p85 recruitment and PI3K signaling to T-follicular-helper development through receptor mutants and native mouse physiological experiments. Retain the existing human annotation as a conserved signaling contribution with construct/species limits, not direct demonstration that p85alpha alone specifies the lineage or that calcium costimulation requires the same ICOS cytoplasmic motif. Supporting Evidence: |
| GO:0120183 positive regulation of focal adhesion disassembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of focal adhesion disassembly (electronic). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0120183 positive regulation of focal adhesion disassembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of focal adhesion disassembly (ISS). Reason: The mouse-derived process is supported by receptor-responsive p85alpha cytoskeletal signaling. Full PMID11038173 distinguishes the p85-dependent Cdc42/N-WASP arm (filopodia, stress-fiber and focal-adhesion remodeling) from PI3K catalytic activity and Rac-associated lamellipodia. Retain the specific physiological claim as a conserved, context-dependent process contribution, not as direct actin polymerization catalysis or a universal consequence of p85 overexpression. Supporting Evidence: |
| GO:0140767 enzyme-substrate adaptor activity | ISS PMID:1322797 Phosphatidylinositol 3-kinase: structure and expression of t... | MODIFY | Summary: The cited biochemical work supports receptor-kinase adaptor activity. Reason: PMID1322797 explicitly describes p85alpha coupling p110 to activated protein tyrosine kinases. GO0140767 requires recruiting a substrate to its enzyme with substrate-selection specificity; receptor/membrane recruitment alone should not be redescribed as demonstrated lipid-substrate recognition. Refine the existing adaptor claim to the established RTK-adaptor activity already represented here, without denying membrane positioning or p110 regulation. Proposed replacements: transmembrane receptor protein tyrosine kinase adaptor activity Supporting Evidence: PMID:1322797 The 85 kd subunit (p85 alpha) lacks Pl3-kinase activity and acts as an adaptor, coupling the 110 kd subunit (p110) to activated protein tyrosine kinases. |
| GO:0141038 phosphatidylinositol 3-kinase activator activity | ISS GO_REF:0000024 | ACCEPT | Summary: Phosphatidylinositol 3-kinase activator activity. Reason: Stimulus-dependent activation is an integral facet of p85alpha regulation: phosphotyrosine engagement and altered inhibitory contacts enable p110 activity while p85 maintains its stability. Basal inhibition and activation are compatible context-dependent parts of the same regulatory mechanism, not grounds to demote the activating function. |
| GO:1900103 positive regulation of endoplasmic reticulum unfolded protein response | IMP PMID:20348923 A regulatory subunit of phosphoinositide 3-kinase increases ... | KEEP AS NON CORE | Summary: Positive regulation of the ER unfolded protein response (XBP1). Reason: p85Ξ± promotes the UPR via XBP1 nuclear accumulation and IRE1Ξ±/ATF6 activation; loss attenuates the UPR. Specialized role; retained as non-core. Full PMID20348923 distinguishes transfected human-cell interaction/stabilization from mouse fibroblast and liver physiology: XBP1 splicing changes in cultured cells were not reproduced in acutely challenged liver, whereas reduced nuclear XBP1 accumulation was shared. These are regulatory effects through XBP1/UPR, not direct p85 RNA-splicing or transcription catalysis. Supporting Evidence: |
| GO:1903078 positive regulation of protein localization to plasma membrane | ISS PMID:8052599 1-Phosphatidylinositol 3-kinase activity is required for ins... | KEEP AS NON CORE | Summary: Positive regulation of protein localization to plasma membrane (ISS). Reason: The original PMID8052599 assay used mutant p85alpha in CHO cells and measured impaired insulin-stimulated GLUT1 translocation and glucose uptake. The prior explanation incorrectly called this experiment GLUT4. Retain the existing orthology-supported transport-regulatory role; p85 organizes PI3K signaling and does not itself transport glucose. Supporting Evidence: |
| GO:1990578 perinuclear endoplasmic reticulum membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact perinuclear ER-membrane assignment needs resolution beyond the traced perinuclear/cis-Golgi signal. Reason: The mouse donor is an IDA tied to PMID25217619. Full main Results and Fig. 1 describe perinuclear internal membranes and cis-Golgi localization for p85alpha; they do not, in the inspected passages, resolve ER membrane with an ER-specific marker. Its UPR role is not independent evidence of ER residence. The donor curator may have used finer supplementary image information, so the exact compartment is unresolved rather than rejected. Supported perinuclear and cis-Golgi annotations remain intact. |
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