CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008364
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 
Protein Synonyms/Alias
 Phosphoinositide phospholipase C-delta-1; Phospholipase C-III; PLC-III; Phospholipase C-delta-1; PLC-delta-1 
Gene Name
 PLCD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
49YKLQEDCKTIWQESRubiquitination[1]
86HRTEGLEKFARDVPEubiquitination[1]
102RCFSIVFKDQRNTLDubiquitination[1]
163KDNKMSFKELQNFLKubiquitination[1, 2, 3]
712EDYDASSKNDFIGQSubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
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. Essential for trophoblast and placental development. 
Sequence Annotation
 DOMAIN 21 130 PH.
 DOMAIN 140 175 EF-hand 1.
 DOMAIN 176 211 EF-hand 2.
 DOMAIN 296 440 PI-PLC X-box.
 DOMAIN 492 609 PI-PLC Y-box.
 DOMAIN 616 720 C2.
 REGION 30 57 Substrate binding (By similarity).
 ACT_SITE 311 311 By similarity.
 ACT_SITE 356 356 By similarity.
 METAL 312 312 Calcium 1; catalytic (By similarity).
 METAL 341 341 Calcium 1; catalytic (By similarity).
 METAL 343 343 Calcium 1; catalytic (By similarity).
 METAL 390 390 Calcium 1; catalytic (By similarity).
 METAL 651 651 Calcium 2; via carbonyl oxygen (By
 METAL 653 653 Calcium 2 (By similarity).
 METAL 677 677 Calcium 2 (By similarity).
 METAL 706 706 Calcium 3 (By similarity).
 METAL 707 707 Calcium 3; via carbonyl oxygen (By
 METAL 708 708 Calcium 3 (By similarity).
 BINDING 438 438 Substrate (By similarity).
 BINDING 440 440 Substrate (By similarity).
 BINDING 522 522 Substrate (By similarity).
 BINDING 549 549 Substrate (By similarity).  
Keyword
 Alternative splicing; Calcium; Complete proteome; Disease mutation; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Polymorphism; Reference proteome; Repeat; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 756 AA 
Protein Sequence
MDSGRDFLTL HGLQDDEDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR 60
TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPEDRCFSIV FKDQRNTLDL IAPSPADAQH 120
WVLGLHKIIH HSGSMDQRQK LQHWIHSCLR KADKNKDNKM SFKELQNFLK ELNIQVDDSY 180
ARKIFRECDH SQTDSLEDEE IEAFYKMLTQ RVEIDRTFAE AAGSGETLSV DQLVTFLQHQ 240
QREEAAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFSLA HRRVYQDMGQ 300
PLSHYLVSSS HNTYLLEDQL AGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF 360
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCTLEQQRV MARHLHAILG PMLLNRPLDG 420
VTNSLPSPEQ LKGKILLKGK KLGGLLPPGG EGGPEATVVS DEDEAAEMED EAVRSRVQHK 480
PKEDKLRLAQ ELSDMVIYCK SVHFGGFSSP GTPGQAFYEM ASFSENRALR LLQESGNGFV 540
RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYQ GRFQDNGACG 600
YVLKPAFLRD PNGTFNPRAL AQGPWWARKR LNIRVISGQQ LPKVNKNKNS IVDPKVTVEI 660
HGVSRDVASR QTAVITNNGF NPWWDTEFAF EVVVPDLALI RFLVEDYDAS SKNDFIGQST 720
IPLNSLKQGY RHVHLMSKNG DQHPSATLFV KISLQD 756 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
 GO:0001525; P:angiogenesis; IEA:Compara.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0060716; P:labyrinthine layer blood vessel development; IEA:Compara.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara. 
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.
 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. 
Pfam
 PF00168; C2
 PF09279; efhand_like
 PF00388; PI-PLC-X
 PF00387; PI-PLC-Y 
SMART
 SM00239; C2
 SM00054; EFh
 SM00233; PH
 SM00148; PLCXc
 SM00149; PLCYc 
PROSITE
 PS50004; C2
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50003; PH_DOMAIN
 PS50007; PIPLC_X_DOMAIN
 PS50008; PIPLC_Y_DOMAIN 
PRINTS
 PR00390; PHPHLIPASEC.