CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022522
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 
Protein Synonyms/Alias
 Pancreas-enriched phospholipase C; Phosphoinositide phospholipase C-epsilon-1; Phospholipase C-epsilon-1; PLC-epsilon-1 
Gene Name
 PLCE1 
Gene Synonyms/Alias
 KIAA1516; PLCE; PPLC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
576QSSLPCLKASISASIacetylation[1]
1541KVLLKNKKLKAHQTPmethylation[2]
1555PVDILKQKAHQLASMmethylation[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
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. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine- exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation. 
Sequence Annotation
 DOMAIN 531 790 Ras-GEF.
 DOMAIN 1392 1540 PI-PLC X-box.
 DOMAIN 1730 1846 PI-PLC Y-box.
 DOMAIN 1856 1956 C2.
 DOMAIN 2012 2114 Ras-associating 1.
 DOMAIN 2135 2238 Ras-associating 2.
 REGION 1686 1764 Required for activation by RHOA, RHOB,
 ACT_SITE 1407 1407 By similarity.
 ACT_SITE 1452 1452 By similarity.  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Disease mutation; Golgi apparatus; Guanine-nucleotide releasing factor; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Polymorphism; Reference proteome; Repeat; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2302 AA 
Protein Sequence
MTSEEMTASV LIPVTQRKVV SAQSAADESS EKVSDINISK AHTVRRSGET SHTISQLNKL 60
KEEPSGSNLP KILSIAREKI VSDENSNEKC WEKIMPDSAK NLNINCNNIL RNHQHGLPQR 120
QFYEMYNSVA EEDLCLETGI PSPLERKVFP GIQLELDRPS MGISPLGNQS VIIETGRAHP 180
DSRRAVFHFH YEVDRRMSDT FCTLSENLIL DDCGNCVPLP GGEEKQKKNY VAYTCKLMEL 240
AKNCDNKNEQ LQCDHCDTLN DKYFCFEGSC EKVDMVYSGD SFCRKDFTDS QAAKTFLSHF 300
EDFPDNCDDV EEDAFKSKKE RSTLLVRRFC KNDREVKKSV YTGTRAIVRT LPSGHIGLTA 360
WSYIDQKRNG PLLPCGRVME PPSTVEIRQD GSQRLSEAQW YPIYNAVRRE ETENTVGSLL 420
HFLTKLPASE TAHGRISVGP CLKQCVRDTV CEYRATLQRT SISQYITGSL LEATTSLGAR 480
SGLLSTFGGS TGRMMLKERQ PGPSVANSNA LPSSSAGISK ELIDLQPLIQ FPEEVASILM 540
EQEQTIYRRV LPVDYLCFLT RDLGTPECQS SLPCLKASIS ASILTTQNGE HNALEDLVMR 600
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG LRSRKVLKMW 660
QFMDQSDIET MRSLKDAMAQ HESSCEYRKV VTRALHIPGC KVVPFCGVFL KELCEVLDGA 720
SGLMKLCPRY NSQEETLEFV ADYSGQDNFL QRVGQNGLKN SEKESTVNSI FQVIRSCNRS 780
LETDEEDSPS EGNSSRKSSL KDKSRWQFII GDLLDSDNDI FEQSKEYDSH GSEDSQKAFD 840
HGTELIPWYV LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWVKPTTAS 900
PASSKAKLGV LNNTAEPGKF PLLGNAGLSS LTEGVLDLFA VKAVYMGHPG IDIHTVCVQN 960
KLGSMFLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS GLLELTRAVR KMRKFPDQRQ 1020
QWLRKQYVSL YQEDGRYEGP TLAHAVELFG GRRWSARNPS PGTSAKNAEK PNMQRNNTLG 1080
ISTTKKKKKI LMRGESGEVT DDEMATRKAK MHKECRSRSG SDPQDINEQE ESEVNAIANP 1140
PNPLPSRRAH SLTTAGSPNL AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM 1200
KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDVY AVPCNRSGSE SAPLYTNLTI 1260
DENTSDLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD AIAAASIVTN GTGIESTSLG 1320
IFGVGILQLN DFLVNCQGEH CTYDEILSII QKFEPSISMC HQGLMSFEGF ARFLMDKENF 1380
ASKNDESQEN IKELQLPLSY YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC 1440
WDGDDGMPII YHGHTLTTKI PFKEVVEAID RSAFINSDLP IIISIENHCS LPQQRKMAEI 1500
FKTVFGEKLV TKFLFETDFS DDPMLPSPDQ LRKKVLLKNK KLKAHQTPVD ILKQKAHQLA 1560
SMQVQAYNGG NANPRPANNE EEEDEEDEYD YDYESLSDDN ILEDRPENKS CNDKLQFEYN 1620
EEIPKRIKKA DNSACNKGKV YDMELGEEFY LDQNKKESRQ IAPELSDLVI YCQAVKFPGL 1680
STLNASGSSR GKERKSRKSI FGNNPGRMSP GETASFNKTS GKSSCEGIRQ TWEESSSPLN 1740
PTTSLSAIIR TPKCYHISSL NENAAKRLCR RYSQKLTQHT ACQLLRTYPA ATRIDSSNPN 1800
PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC PMYQKFSPLE 1860
RDLDSMDPAV YSLTIVSGQN VCPSNSMGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW 1920
NEQFLFHVHF EDLVFLRFAV VENNSSAVTA QRIIPLKALK RGYRHLQLRN LHNEVLEISS 1980
LFINSRRMEE NSSGNTMSAS SMFNTEERKC LQTHRVTVHG VPGPEPFTVF TINGGTKAKQ 2040
LLQQILTNEQ DIKPVTTDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE 2100
EGYMGRIVLK TQQENLEEKN IVQDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST 2160
AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK KTTTPKSSQR VLLDQECVFQ 2220
AQSKWKGAGK FILKLKEQVQ ASREDKKKGI SFASELKKLT KSTKQPRGLT SPSQLLTSES 2280
IQTKEEKPVG GLSSSDTMDY RQ 2302 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:UniProtKB.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
 GO:0017016; F:Ras GTPase binding; TAS:UniProtKB.
 GO:0005057; F:receptor signaling protein activity; TAS:UniProtKB.
 GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
 GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
 GO:0006651; P:diacylglycerol biosynthetic process; TAS:UniProtKB.
 GO:0007204; P:elevation of cytosolic calcium ion concentration; TAS:UniProtKB.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
 GO:0032835; P:glomerulus development; IMP:HGNC.
 GO:0007507; P:heart development; TAS:UniProtKB.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0048016; P:inositol phosphate-mediated signaling; TAS:UniProtKB.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
 GO:0006644; P:phospholipid metabolic process; IC:UniProtKB.
 GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; NAS:UniProtKB.
 GO:0007265; P:Ras protein signal transduction; TAS:UniProtKB.
 GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
 GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
 GO:0046578; P:regulation of Ras protein signal transduction; IDA:UniProtKB.
 GO:0006940; P:regulation of smooth muscle contraction; TAS:UniProtKB. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR011992; EF-hand-like_dom.
 IPR001192; Pinositol_PLipase_C.
 IPR017946; PLC-like_Pdiesterase_TIM-brl.
 IPR015359; PLipase_C_EF-hand-like.
 IPR000909; PLipase_C_PInositol-sp_X_dom.
 IPR001711; PLipase_C_Pinositol-sp_Y.
 IPR000159; Ras-assoc.
 IPR023578; Ras_GEF_dom.
 IPR001895; RasGRF_CDC25. 
Pfam
 PF00168; C2
 PF09279; efhand_like
 PF00388; PI-PLC-X
 PF00387; PI-PLC-Y
 PF00788; RA
 PF00617; RasGEF 
SMART
 SM00239; C2
 SM00148; PLCXc
 SM00149; PLCYc
 SM00314; RA
 SM00147; RasGEF 
PROSITE
 PS50004; C2
 PS50007; PIPLC_X_DOMAIN
 PS50008; PIPLC_Y_DOMAIN
 PS50200; RA
 PS00720; RASGEF
 PS50009; RASGEF_CAT 
PRINTS
 PR00390; PHPHLIPASEC.