CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032446
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 
Protein Synonyms/Alias
 PLCB2 protein 
Gene Name
 PLCB2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
419DSPRQQAKMAEYCRTubiquitination[1]
761AVMEEGNKFLGHRIIubiquitination[2]
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] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1170 AA 
Protein Sequence
MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT YQSKEMEFLD 60
ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE 120
NVGKAWAEDV LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR 180
VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH 240
LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN 300
SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC 360
WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM 420
AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSGP TSSSKDTGGE 480
AEGSSPPSAP AGEGTVWAGE EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV 540
TAYEEMSSLV NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM 600
SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG QSGYLLKHEF 660
MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR TYVEVELFGL PGDPKRRYRT 720
KLSPSTNSIN PVWKEEPFVF EKILMPELAS LRVAVMEEGN KFLGHRIIPI NALNSGYHHL 780
CLHSESNMPL TMPALFIFLE MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL 840
PEKPFPLASP VASQVNGALA PTSNGSPEPR TASLEELREL KGVVKLQRRH EKELRELERR 900
GARRWEELLQ RGAAQLAELG PPGVGGVGAC KLGPGKGSRK KRSLPREESA GAAPGEGPEG 960
VDGRVRELKD RLELELLRQG EEQYECVLKR KEQHVAEQIS KMMELAREKQ AAELKALKET 1020
SENDTKEMKK KLETKRLERI QGMTKVTTDK MAQERLKREI NNSHIQEVVQ VIKQMTENLE 1080
RHQEKLEEKQ AACLEQIREM EKQFQKEALA EYEARMKGLE AEVKESVRAC LRTCFPSEAK 1140
DKPERACECP PELCEQDPLI AKADAQESRL 1170 
Gene Ontology
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
 GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0016042; P:lipid catabolic process; IEA:InterPro. 
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.
 IPR016280; PLC-beta.
 IPR014815; PLC-beta_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. 
Pfam
 PF00168; C2
 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.