CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003830
UniProt Accession
Genbank Protein ID
 M20636 
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 
Protein Synonyms/Alias
 PLC-154; Phosphoinositide phospholipase C-beta-1; Phospholipase C-I; PLC-I; Phospholipase C-beta-1; PLC-beta-1 
Gene Name
 Plcb1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
85AKAPKDPKLRELLDVacetylation[1]
839LEDEEEVKKEADPGEubiquitination[2]
1011KLIDLKDKQQQQLLNubiquitination[2]
1111QEVVQYIKRLEEAQSacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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 316 467 PI-PLC X-box.
 DOMAIN 540 656 PI-PLC Y-box.
 DOMAIN 663 761 C2.
 ACT_SITE 331 331 By similarity.
 ACT_SITE 378 378 By similarity.
 MOD_RES 333 333 Phosphothreonine (By similarity).
 MOD_RES 334 334 Phosphotyrosine (By similarity).
 MOD_RES 336 336 Phosphothreonine (By similarity).
 MOD_RES 887 887 Phosphoserine; by PKC (By similarity).
 MOD_RES 1197 1197 Phosphoserine (By similarity).  
Keyword
 Calcium; Complete proteome; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1216 AA 
Protein Sequence
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 60
TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 120
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 180
DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 240
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS 300
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV 360
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ 420
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 480
KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 540
SNLVNYIQPV KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 600
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 660
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 720
NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 780
NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 840
EADPGETSSE APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 900
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 960
RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR 1020
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI 1080
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP 1140
KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS 1200
EEVQGENAGR EFDTPL 1216 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016020; C:membrane; IDA:RGD.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0016607; C:nuclear speck; ISS:BHF-UCL.
 GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
 GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
 GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
 GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
 GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0007612; P:learning; IEP:RGD.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0007613; P:memory; IEP:RGD.
 GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:BHF-UCL.
 GO:0046488; P:phosphatidylinositol metabolic process; IEP:RGD.
 GO:2000560; P:positive regulation of CD24 biosynthetic process; ISS:BHF-UCL.
 GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
 GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
 GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
 GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:BHF-UCL.
 GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:BHF-UCL.
 GO:0034284; P:response to monosaccharide stimulus; IDA:BHF-UCL.
 GO:0043434; P:response to peptide hormone stimulus; IDA:BHF-UCL. 
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.
 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.