Human Gene PLCG1 (ENST00000244007.7) from GENCODE V44
Description: 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. (from UniProt P19174) RefSeq Summary (NM_002660): The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000244007.7 Gencode Gene: ENSG00000124181.15 Transcript (Including UTRs) Position: hg38 chr20:41,136,960-41,175,721 Size: 38,762 Total Exon Count: 33 Strand: + Coding Region Position: hg38 chr20:41,137,642-41,174,509 Size: 36,868 Coding Exon Count: 32
ID:PLCG1_HUMAN DESCRIPTION: RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1; EC=3.1.4.11; AltName: Full=PLC-148; AltName: Full=Phosphoinositide phospholipase C-gamma-1; AltName: Full=Phospholipase C-II; Short=PLC-II; AltName: Full=Phospholipase C-gamma-1; Short=PLC-gamma-1; 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. CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. COFACTOR: Calcium. ENZYME REGULATION: Activated by phosphorylation on tyrosine residues. SUBUNIT: Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine- phosphorylated) (By similarity). Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). 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 (By similarity). Interacts with AXL, FLT4 and KIT. 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). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C (By similarity). Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By similarity). Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome. INTERACTION: P42684:ABL2; NbExp=4; IntAct=EBI-79387, EBI-1102694; Q9ULH1:ASAP1; NbExp=3; IntAct=EBI-79387, EBI-346622; O43150:ASAP2; NbExp=3; IntAct=EBI-79387, EBI-310968; P20273:CD22; NbExp=2; IntAct=EBI-79387, EBI-78277; Q9H1R2:DUSP15; NbExp=2; IntAct=EBI-79387, EBI-1752795; P31994:FCGR2B; NbExp=2; IntAct=EBI-79387, EBI-724784; Q07666:KHDRBS1; NbExp=2; IntAct=EBI-79387, EBI-1364; O43561:LAT; NbExp=2; IntAct=EBI-79387, EBI-1222766; Q92918:MAP4K1; NbExp=6; IntAct=EBI-79387, EBI-881; Q8TB24:RIN3; NbExp=3; IntAct=EBI-79387, EBI-1570523; Q9UPX8:SHANK2; NbExp=4; IntAct=EBI-79387, EBI-1570571; Q9BYB0:SHANK3; NbExp=2; IntAct=EBI-79387, EBI-1752330; Q15036:SNX17; NbExp=2; IntAct=EBI-79387, EBI-1752620; Q07889:SOS1; NbExp=2; IntAct=EBI-79387, EBI-297487; Q07890:SOS2; NbExp=4; IntAct=EBI-79387, EBI-298181; P09327:VIL1; NbExp=5; IntAct=EBI-79387, EBI-1047253; SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. 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, 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. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK 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/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P19174
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
