LMP000865 UniProt Annotations
Gene Name phospholipase C, gamma 1 Protein Entry PLCG1_MOUSE UniProt ID Q62077 Species Mouse
Comment type Description Catalytic Activity 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Cofactor Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Domain The SH3 domain mediates interaction with RALGPS1 (By similarity). The SH3 domain also mediates interaction with CLNK. {ECO:0000250, ECO:0000269|PubMed:11463797}. Enzyme Regulation Activated by phosphorylation on tyrosine residues. Function Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand- mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. {ECO:0000269|PubMed:15308098}. Interaction P14753:Epor; NbExp=4; IntAct=EBI-300133, EBI-617901; Q60631:Grb2; NbExp=2; IntAct=EBI-300133, EBI-1688; O54957:Lat; NbExp=2; IntAct=EBI-300133, EBI-6390034; P48356:Lepr; NbExp=2; IntAct=EBI-300133, EBI-2257257; Ptm Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ (By similarity). {ECO:0000250}. Ptm Ubiquitinated by CBLB in activated T-cells. {ECO:0000269|PubMed:15308098}. Similarity Contains 1 C2 domain. {ECO:0000255|PROSITE- ProRule:PRU00041}. Similarity Contains 1 EF-hand domain. {ECO:0000255|PROSITE- ProRule:PRU00448}. Similarity Contains 1 PI-PLC X-box domain. {ECO:0000255|PROSITE- ProRule:PRU00270}. Similarity Contains 1 PI-PLC Y-box domain. {ECO:0000255|PROSITE- ProRule:PRU00271}. Similarity Contains 1 SH3 domain. {ECO:0000255|PROSITE- ProRule:PRU00192}. Similarity Contains 2 PH domains. {ECO:0000255|PROSITE- ProRule:PRU00145}. Similarity Contains 2 SH2 domains. {ECO:0000255|PROSITE- ProRule:PRU00191}. Subcellular Location Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000250}. Subunit Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. 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 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. Interacts with FLT4 and KIT. Interacts with AXL (By similarity). Interacts with SYK; activates PLCG1 (By similarity). Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with TESPA1 (By similarity). Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1. {ECO:0000250, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10748127, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16000869, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9299537}.
We use Cookies
This site uses cookies and other tracking technologies to assist with navigation and your ability to provide feedback, analyze your use of our products and services, assist with our promotional and marketing efforts, and provide content from third parties.
More Options
Accept