CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 
Protein Synonyms/Alias
 PLC-148; Phosphoinositide phospholipase C-gamma-1; Phospholipase C-II; PLC-II; Phospholipase C-gamma-1; PLC-gamma-1 
Gene Name
 PLCG1 
Gene Synonyms/Alias
 PLC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
159QIERWLRKQFYSVDRubiquitination[1]
175REDRISAKDLKNMLSubiquitination[1]
178RISAKDLKNMLSQVNubiquitination[1]
226SLMYSAQKTMDLPFLubiquitination[1]
430RNMAQYFKKVLGDTLubiquitination[1]
431NMAQYFKKVLGDTLLubiquitination[1]
440LGDTLLTKPVEISADubiquitination[1]
456LPSPNQLKRKILIKHubiquitination[1]
465KILIKHKKLAEGSAYubiquitination[1]
554NEKWFHGKLGAGRDGubiquitination[1]
666QTNAHESKEWYHASLubiquitination[1]
763INEEALEKIGTAEPDubiquitination[1]
793ANPMPTFKCAVKALFubiquitination[1]
797PTFKCAVKALFDYKAubiquitination[1]
890IAIRPEGKNNRLFVFubiquitination[1]
941DARLTEGKIMERRKKubiquitination[1]
987MSSFPETKAEKYVNKubiquitination[1]
1079EAFDPFDKSSLRGLEubiquitination[1]
1193GYRAVPLKNNYSEDLubiquitination[1]
1215KIDIFPAKQENGDLSubiquitination[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] 
Functional 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. 
Sequence Annotation
 DOMAIN 27 142 PH 1.
 DOMAIN 152 187 EF-hand.
 DOMAIN 320 464 PI-PLC X-box.
 DOMAIN 489 523 PH 2; first part.
 DOMAIN 550 657 SH2 1.
 DOMAIN 668 756 SH2 2.
 DOMAIN 791 851 SH3.
 DOMAIN 895 931 PH 2; second part.
 DOMAIN 953 1070 PI-PLC Y-box.
 DOMAIN 1075 1177 C2.
 ACT_SITE 335 335 By similarity.
 ACT_SITE 380 380 By similarity.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 379 379 Phosphotyrosine (By similarity).
 MOD_RES 481 481 Phosphotyrosine (By similarity).
 MOD_RES 506 506 Phosphotyrosine (By similarity).
 MOD_RES 771 771 Phosphotyrosine; by SYK.
 MOD_RES 775 775 Phosphotyrosine.
 MOD_RES 783 783 Phosphotyrosine; by ITK, SYK and TXK.
 MOD_RES 977 977 Phosphotyrosine (By similarity).
 MOD_RES 1221 1221 Phosphoserine.
 MOD_RES 1248 1248 Phosphoserine.
 MOD_RES 1253 1253 Phosphotyrosine.
 MOD_RES 1263 1263 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Calcium; Cell projection; Complete proteome; Host-virus interaction; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1290 AA 
Protein Sequence
MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 60
TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL 120
SLQATSEDEV NMWIKGLTWL MEDTLQAPTP LQIERWLRKQ FYSVDRNRED RISAKDLKNM 180
LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLEASTLRA 240
GERPELCRVS LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 300
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG 360
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA 420
QQRNMAQYFK KVLGDTLLTK PVEISADGLP SPNQLKRKIL IKHKKLAEGS AYEEVPTSMM 480
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEVSS 540
STELHSNEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 600
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT 660
NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE 720
GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP 780
GFYVEANPMP TFKCAVKALF DYKAQREDEL TFIKSAIIQN VEKQEGGWWR GDYGGKKQLW 840
FPSNYVEEMV NPVALEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 900
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KIMERRKKIA LELSELVVYC 960
RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS 1020
SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMTGRHC GYVLQPSTMR DEAFDPFDKS 1080
SLRGLEPCAI SIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW 1140
PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 1200
ELASLLIKID IFPAKQENGD LSPFSGTSLR ERGSDASGQL FHGRAREGSF ESRYQQPFED 1260
FRISQEHLAD HFDSRERRAP RRTRVNGDNR L 1291 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0008180; C:signalosome; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005057; F:receptor signaling protein activity; NAS:UniProtKB.
 GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
 GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
 GO:0045766; P:positive regulation of angiogenesis; IDA:DFLAT.
 GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:DFLAT.
 GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 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
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50003; PH_DOMAIN
 PS50007; PIPLC_X_DOMAIN
 PS50008; PIPLC_Y_DOMAIN
 PS50001; SH2
 PS50002; SH3 
PRINTS
 PR00390; PHPHLIPASEC.
 PR00401; SH2DOMAIN.