CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010904
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 
Protein Synonyms/Alias
 Phosphoinositide phospholipase C-beta-3; Phospholipase C-beta-3; PLC-beta-3 
Gene Name
 PLCB3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30RRGSKFIKWDEETSSubiquitination[1]
196ALESCGLKFNRSESIubiquitination[2]
424DSAKQQAKMAEYCRSubiquitination[1]
804AAFEEGGKFVGHRILubiquitination[3, 4, 5]
1029KEGEDEAKRYQEFQNubiquitination[6]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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. 
Sequence Annotation
 DOMAIN 318 468 PI-PLC X-box.
 DOMAIN 590 706 PI-PLC Y-box.
 DOMAIN 713 810 C2.
 REGION 1231 1234 Interaction with SHANK2 (By similarity).
 ACT_SITE 332 332 By similarity.
 ACT_SITE 379 379 By similarity.
 MOD_RES 474 474 Phosphoserine.
 MOD_RES 537 537 Phosphoserine.
 MOD_RES 1105 1105 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Calcium; Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1234 AA 
Protein Sequence
MAGAQPGVHA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME 60
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDARLE EKLMTVVSGP DPVNTVFLNF 120
MAVQDDTAKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS 180
ADKKRVETAL ESCGLKFNRS ESIRPDEFSL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY 240
LTLEQLMDFI NQKQRDPRLN EVLYPPLRPS QARLLIEKYE PNQQFLERDQ MSMEGFSRYL 300
GGEENGILPL EALDLSTDMT QPLSAYFINS SHNTYLTAGQ LAGTSSVEMY RQALLWGCRC 360
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAETA FKTSPYPVIL SFENHVDSAK 420
QQAKMAEYCR SIFGDALLIE PLDKYPLAPG VPLPSPQDLM GRILVKNKKR HRPSAGGPDS 480
AGRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKP SLEPQKSLGD 540
EGLNRGPYVL GPADREDEEE DEEEEEQTDP KKPTTDEGTA SSEVNATEEM STLVNYIEPV 600
KFKSFEAARK RNKCFEMSSF VETKAMEQLT KSPMEFVEYN KQQLSRIYPK GTRVDSSNYM 660
PQLFWNVGCQ LVALNFQTLD VAMQLNAGVF EYNGRSGYLL KPEFMRRPDK SFDPFTEVIV 720
DGIVANALRV KVISGQFLSD RKVGIYVEVD MFGLPVDTRR KYRTRTSQGN SFNPVWDEEP 780
FDFPKVVLPT LASLRIAAFE EGGKFVGHRI LPVSAIRSGY HYVCLRNEAN QPLCLPALLI 840
YTEASDYIPD DHQDYAEALI NPIKHVSLMD QRARQLAALI GESEAQAGQE TCQDTQSQQL 900
GSQPSSNPTP SPLDASPRRP PGPTTSPAST SLSSPGQRDD LIASILSEVA PTPLDELRGH 960
KALVKLRSRQ ERDLRELRKK HQRKAVTLTR RLLDGLAQAQ AEGRCRLRPG ALGGAADVED 1020
TKEGEDEAKR YQEFQNRQVQ SLLELREAQV DAEAQRRLEH LRQALQRLRE VVLDANTTQF 1080
KRLKEMNERE KKELQKILDR KRHNSISEAK MRDKHKKEAE LTEINRRHIT ESVNSIRRLE 1140
EAQKQRHDRL VAGQQQVLQQ LAEEEPKLLA QLAQECQEQR ARLPQEIRRS LLGEMPEGLG 1200
DGPLVACASN GHAPGSSGHL SGADSESQEE NTQL 1234 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
 GO:0004629; F:phospholipase C activity; TAS:ProtInc.
 GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0003073; P:regulation of systemic arterial blood pressure; IDA:MGI.
 GO:0007268; P:synaptic transmission; TAS:Reactome. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR011992; EF-hand-like_dom.
 IPR011993; PH_like_dom.
 IPR001192; Pinositol_PLipase_C.
 IPR016280; PLC-beta.
 IPR014815; PLC-beta_C.
 IPR009535; PLC-beta_CS.
 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. 
Pfam
 PF00168; C2
 PF06631; DUF1154
 PF09279; efhand_like
 PF00388; PI-PLC-X
 PF00387; PI-PLC-Y
 PF08703; PLC-beta_C 
SMART
 SM00239; C2
 SM00148; PLCXc
 SM00149; PLCYc 
PROSITE
 PS50004; C2
 PS50007; PIPLC_X_DOMAIN
 PS50008; PIPLC_Y_DOMAIN 
PRINTS
 PR00390; PHPHLIPASEC.