CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012078
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phospholipase D1 
Protein Synonyms/Alias
 PLD 1; hPLD1; Choline phosphatase 1; Phosphatidylcholine-hydrolyzing phospholipase D1 
Gene Name
 PLD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
189QLEDYLTKILKMPMYubiquitination[1, 2, 3]
501LTDVGSVKRVTSGPSubiquitination[2]
559GKPRKFSKFSLYKQLubiquitination[2]
688IASAVHGKAARDVARubiquitination[2]
796DDKVVFNKIGDAIAQubiquitination[2]
1000RNATIYDKVFRCLPNubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). 
Sequence Annotation
 DOMAIN 81 212 PX.
 DOMAIN 219 328 PH.
 DOMAIN 459 486 PLD phosphodiesterase 1.
 DOMAIN 891 918 PLD phosphodiesterase 2.
 REGION 463 928 Catalytic.
 MOD_RES 629 629 Phosphoserine.
 LIPID 240 240 S-palmitoyl cysteine (By similarity).
 LIPID 241 241 S-palmitoyl cysteine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1074 AA 
Protein Sequence
MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA 60
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF 120
KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR 180
KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC 240
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID 300
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG 360
YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY 420
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVII DQSVAFVGGI 480
DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS 540
IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL 600
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL 660
DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL 720
PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE 780
NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ 840
AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL 900
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARGLRLQCF 960
RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI 1020
NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT 1074 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005768; C:endosome; IDA:MGI.
 GO:0005794; C:Golgi apparatus; IDA:MGI.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
 GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
 GO:0004630; F:phospholipase D activity; TAS:ProtInc.
 GO:0006935; P:chemotaxis; TAS:ProtInc.
 GO:0050830; P:defense response to Gram-positive bacterium; IEA:Compara.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
 GO:0006655; P:phosphatidylglycerol biosynthetic process; TAS:Reactome.
 GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR011993; PH_like_dom.
 IPR001683; Phox.
 IPR025202; PLD-like_dom.
 IPR001849; Pleckstrin_homology.
 IPR001736; PLipase_D/transphosphatidylase.
 IPR016555; PLipase_D_euk.
 IPR015679; PLipase_D_fam. 
Pfam
 PF00169; PH
 PF00614; PLDc
 PF13091; PLDc_2
 PF00787; PX 
SMART
 SM00233; PH
 SM00155; PLDc
 SM00312; PX 
PROSITE
 PS50003; PH_DOMAIN
 PS50035; PLD
 PS50195; PX 
PRINTS