| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-236587,
cpath:CPATH-LOCAL-236587,
cpath:CPATH-LOCAL-236587,
cpath:CPATH-LOCAL-236588,
cpath:CPATH-LOCAL-236588,
cpath:CPATH-LOCAL-236588,
cpath:CPATH-LOCAL-236589,
cpath:CPATH-LOCAL-236589,
cpath:CPATH-LOCAL-236589,
cpath:CPATH-LOCAL-236590,
cpath:CPATH-LOCAL-236590,
cpath:CPATH-LOCAL-236590,
cpath:CPATH-LOCAL-236591,
cpath:CPATH-LOCAL-236591,
cpath:CPATH-LOCAL-236591,
cpath:CPATH-LOCAL-236592,
cpath:CPATH-LOCAL-236592,
cpath:CPATH-LOCAL-236592,
cpath:CPATH-LOCAL-236593,
cpath:CPATH-LOCAL-236593,
cpath:CPATH-LOCAL-236593,
cpath:CPATH-LOCAL-236594,
cpath:CPATH-LOCAL-236594,
cpath:CPATH-LOCAL-236594,
cpath:CPATH-LOCAL-236595,
cpath:CPATH-LOCAL-236595,
cpath:CPATH-LOCAL-236595,
cpath:CPATH-LOCAL-242169,
cpath:CPATH-LOCAL-242169,
cpath:CPATH-LOCAL-242169
|
| http://www.biopax.org/relea... |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
|
| http://www.biopax.org/relea... |
PLCG1_HUMAN,
PLCG1_HUMAN,
PLCG1_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
3.1.4.11,
3.1.4.11,
3.1.4.11,
PLC-148,
PLC-148,
PLC-148,
PLC-II,
PLC-II,
PLC-II,
PLC-gamma-1,
PLC-gamma-1,
PLC-gamma-1,
Phosphoinositide phospholipase C-gamma-1,
Phosphoinositide phospholipase C-gamma-1,
Phosphoinositide phospholipase C-gamma-1,
Phospholipase C-II,
Phospholipase C-II,
Phospholipase C-II,
Phospholipase C-gamma-1,
Phospholipase C-gamma-1,
Phospholipase C-gamma-1
|
| http://www.biopax.org/relea... |
FUNCTION: Plays a role in actin reorganization and cell migration. The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. COFACTOR: Calcium. SUBUNIT: Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET (By similarity). Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro- rich domain of TNK1 via its SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK (By similarity). Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P19174-1; Sequence=Displayed; Name=2; IsoId=P19174-2; Sequence=VSP_038692; DOMAIN: The SH3 domain mediates interaction with CLNK (By similarity). The SH3 domain also mediates interaction with RALGPS1. PTM: Tyrosine phosphorylated in response to signaling via activated FLT3 (By similarity). The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. May be dephosphorylated by PTPRJ. Phosphorylated by ITK on Tyr-783 upon TCR activation in T-cells. PTM: Ubiquitinated by CBLB in activated T-cells (By similarity). SIMILARITY: Contains 1 C2 domain. SIMILARITY: Contains 1 EF-hand domain. SIMILARITY: Contains 2 PH domains. SIMILARITY: Contains 1 PI-PLC X-box domain. SIMILARITY: Contains 1 PI-PLC Y-box domain. SIMILARITY: Contains 2 SH2 domains. SIMILARITY: Contains 1 SH3 domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/plcg1/"; GENE SYNONYMS: PLC1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Plays a role in actin reorganization and cell migration. The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. COFACTOR: Calcium. SUBUNIT: Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET (By similarity). Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro- rich domain of TNK1 via its SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK (By similarity). Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P19174-1; Sequence=Displayed; Name=2; IsoId=P19174-2; Sequence=VSP_038692; DOMAIN: The SH3 domain mediates interaction with CLNK (By similarity). The SH3 domain also mediates interaction with RALGPS1. PTM: Tyrosine phosphorylated in response to signaling via activated FLT3 (By similarity). The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. May be dephosphorylated by PTPRJ. Phosphorylated by ITK on Tyr-783 upon TCR activation in T-cells. PTM: Ubiquitinated by CBLB in activated T-cells (By similarity). SIMILARITY: Contains 1 C2 domain. SIMILARITY: Contains 1 EF-hand domain. SIMILARITY: Contains 2 PH domains. SIMILARITY: Contains 1 PI-PLC X-box domain. SIMILARITY: Contains 1 PI-PLC Y-box domain. SIMILARITY: Contains 2 SH2 domains. SIMILARITY: Contains 1 SH3 domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/plcg1/"; GENE SYNONYMS: PLC1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Plays a role in actin reorganization and cell migration. The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. COFACTOR: Calcium. SUBUNIT: Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET (By similarity). Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro- rich domain of TNK1 via its SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK (By similarity). Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P19174-1; Sequence=Displayed; Name=2; IsoId=P19174-2; Sequence=VSP_038692; DOMAIN: The SH3 domain mediates interaction with CLNK (By similarity). The SH3 domain also mediates interaction with RALGPS1. PTM: Tyrosine phosphorylated in response to signaling via activated FLT3 (By similarity). The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. May be dephosphorylated by PTPRJ. Phosphorylated by ITK on Tyr-783 upon TCR activation in T-cells. PTM: Ubiquitinated by CBLB in activated T-cells (By similarity). SIMILARITY: Contains 1 C2 domain. SIMILARITY: Contains 1 EF-hand domain. SIMILARITY: Contains 2 PH domains. SIMILARITY: Contains 1 PI-PLC X-box domain. SIMILARITY: Contains 1 PI-PLC Y-box domain. SIMILARITY: Contains 2 SH2 domains. SIMILARITY: Contains 1 SH3 domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/plcg1/"; GENE SYNONYMS: PLC1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch |