CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004504
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 
Protein Synonyms/Alias
 Phosphoinositide phospholipase C-gamma-2; Phospholipase C-IV; PLC-IV; Phospholipase C-gamma-2; PLC-gamma-2 
Gene Name
 PLCG2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
167SISLRELKTILPLINubiquitination[1]
432FGDLLLTKPTEASADubiquitination[1, 2]
557YCMETGGKDGTFLVRubiquitination[1]
775SMPQRTVKALYDYKAubiquitination[1]
962IRSFVETKADSIIRQubiquitination[1, 2]
980DLLKYNQKGLTRVYPubiquitination[1]
1047PESMRTEKYDPMPPEubiquitination[1]
1233ANRDALVKEFSVNENubiquitination[2]
1262EKRVSNSKFYS****ubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. It is a crucial enzyme in transmembrane signaling. 
Sequence Annotation
 DOMAIN 20 131 PH.
 DOMAIN 312 456 PI-PLC X-box.
 DOMAIN 532 635 SH2 1.
 DOMAIN 646 735 SH2 2.
 DOMAIN 769 829 SH3.
 DOMAIN 930 1044 PI-PLC Y-box.
 DOMAIN 1059 1152 C2.
 ACT_SITE 327 327 By similarity.
 ACT_SITE 372 372 By similarity.
 MOD_RES 753 753 Phosphotyrosine; by BTK.
 MOD_RES 759 759 Phosphotyrosine; by BTK.
 MOD_RES 1197 1197 Phosphotyrosine; by BTK (By similarity).
 MOD_RES 1217 1217 Phosphotyrosine.
 MOD_RES 1245 1245 Phosphotyrosine.  
Keyword
 3D-structure; Calcium; Complete proteome; Disease mutation; Hydrolase; Lipid degradation; Lipid metabolism; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1265 AA 
Protein Sequence
MSTTVNVDSL AEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR QVAWSKTADK 60
IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY GTQFVLSTLS LAADSKEDAV 120
NWLSGLKILH QEAMNASTPT IIESWLRKQI YSVDQTRRNS ISLRELKTIL PLINFKVSSA 180
KFLKDKFVEI GAHKDELSFE QFHLFYKKLM FEQQKSILDE FKKDSSVFIL GNTDRPDASA 240
VYLHDFQRFL IHEQQEHWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS 300
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES SPEAYIRCLR MGCRCIELDC 360
WDGPDGKPVI YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP VILSIEEHCS VEQQRHMAKA 420
FKEVFGDLLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP RGDVDVNMED KKDEHKQQGE 480
LYMWDSIDQK WTRHYCAIAD AKLSFSDDIE QTMEEEVPQD IPPTELHFGE KWFHKKVEKR 540
TSAEKLLQEY CMETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTLKYY 600
LTDNLTFSSI YALIQHYRET HLRCAEFELR LTDPVPNPNP HESKPWYYDS LSRGEAEDML 660
MRIPRDGAFL IRKREGSDSY AITFRARGKV KHCRINRDGR HFVLGTSAYF ESLVELVSYY 720
EKHSLYRKMR LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY 780
KAKRSDELSF CRGALIHNVS KEPGGWWKGD YGTRIQQYFP SNYVEDISTA DFEELEKQII 840
EDNPLGSLCR GILDLNTYNV VKAPQGKNQK SFVFILEPKQ QGDPPVEFAT DRVEELFEWF 900
QSIREITWKI DTKENNMKYW EKNQSIAIEL SDLVVYCKPT SKTKDNLENP DFREIRSFVE 960
TKADSIIRQK PVDLLKYNQK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTADKY 1020
MQMNHALFSL NGRTGYVLQP ESMRTEKYDP MPPESQRKIL MTLTVKVLGA RHLPKLGRSI 1080
ACPFVEVEIC GAEYDNNKFK TTVVNDNGLS PIWAPTQEKV TFEIYDPNLA FLRFVVYEED 1140
MFSDPNFLAH ATYPIKAVKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC 1200
RQLRRRQEEL NNQLFLYDTH QNLRNANRDA LVKEFSVNEN QLQLYQEKCN KRLREKRVSN 1260
SKFYS 1265 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
 GO:0032237; P:activation of store-operated calcium channel activity; IEA:Compara.
 GO:0030183; P:B cell differentiation; ISS:UniProtKB.
 GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
 GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0002316; P:follicular B cell differentiation; IEA:Compara.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Compara.
 GO:0043069; P:negative regulation of programmed cell death; IEA:Compara.
 GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB.
 GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0010468; P:regulation of gene expression; IEA:Compara.
 GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
 GO:0016055; P:Wnt receptor signaling pathway; TAS:UniProtKB. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR011993; PH_like_dom.
 IPR001192; Pinositol_PLipase_C.
 IPR016279; PLC-gamma.
 IPR017946; PLC-like_Pdiesterase_TIM-brl.
 IPR001849; Pleckstrin_homology.
 IPR015359; PLipase_C_EF-hand-like.
 IPR000909; PLipase_C_PInositol-sp_X_dom.
 IPR001711; PLipase_C_Pinositol-sp_Y.
 IPR000980; SH2.
 IPR001452; SH3_domain. 
Pfam
 PF00168; C2
 PF09279; efhand_like
 PF00388; PI-PLC-X
 PF00387; PI-PLC-Y
 PF00017; SH2
 PF00018; SH3_1 
SMART
 SM00239; C2
 SM00233; PH
 SM00148; PLCXc
 SM00149; PLCYc
 SM00252; SH2
 SM00326; SH3 
PROSITE
 PS50004; C2
 PS50003; PH_DOMAIN
 PS50007; PIPLC_X_DOMAIN
 PS50008; PIPLC_Y_DOMAIN
 PS50001; SH2
 PS50002; SH3 
PRINTS
 PR00390; PHPHLIPASEC.
 PR00401; SH2DOMAIN.
 PR00452; SH3DOMAIN.