CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017670
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phospholipase DDHD1 
Protein Synonyms/Alias
 DDHD domain-containing protein 1; Phosphatidic acid-preferring phospholipase A1 homolog; PA-PLA1 
Gene Name
 DDHD1 
Gene Synonyms/Alias
 KIAA1705 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
177WFYKEDKKTWKPFIGubiquitination[1]
380TQKLGFSKASSSGTRubiquitination[1]
426MDQGRIIKNTAMMREubiquitination[1]
562LYEQLLQKEEELPDEubiquitination[2]
587LDELYITKRRLKEIEubiquitination[1, 2]
755LGAASIGKGLGGMLFubiquitination[1]
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] 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
 Phospholipase that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change the substrate specificity. 
Sequence Annotation
 DOMAIN 611 886 DDHD.
 ACT_SITE 537 537 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Hereditary spastic paraplegia; Hydrolase; Lipid degradation; Lipid metabolism; Neurodegeneration; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 900 AA 
Protein Sequence
MNYPGRGSPR SPEHNGRGGG GGAWELGSDA RPAFGGGVCC FEHLPGGDPD DGDVPLALLR 60
GEPGLHLAPG TDDHNHHLAL DPCLSDENYD FSSAESGSSL RYYSEGESGG GGSSLSLHPP 120
QQPPLVPTNS GGGGATGGSP GERKRTRLGG PAARHRYEVV TELGPEEVRW FYKEDKKTWK 180
PFIGYDSLRI ELAFRTLLQT TGARPQGGDR DGDHVCSPTG PASSSGEDDD EDRACGFCQS 240
TTGHEPEMVE LVNIEPVCVR GGLYEVDVTQ GECYPVYWNQ ADKIPVMRGQ WFIDGTWQPL 300
EEEESNLIEQ EHLNCFRGQQ MQENFDIEVS KSIDGKDAVH SFKLSRNHVD WHSVDEVYLY 360
SDATTSKIAR TVTQKLGFSK ASSSGTRLHR GYVEEATLED KPSQTTHIVF VVHGIGQKMD 420
QGRIIKNTAM MREAARKIEE RHFSNHATHV EFLPVEWRSK LTLDGDTVDS ITPDKVRGLR 480
DMLNSSAMDI MYYTSPLYRD ELVKGLQQEL NRLYSLFCSR NPDFEEKGGK VSIVSHSLGC 540
VITYDIMTGW NPVRLYEQLL QKEEELPDER WMSYEERHLL DELYITKRRL KEIEERLHGL 600
KASSMTQTPA LKFKVENFFC MGSPLAVFLA LRGIRPGNTG SQDHILPREI CNRLLNIFHP 660
TDPVAYRLEP LILKHYSNIS PVQIHWYNTS NPLPYEHMKP SFLNPAKEPT SVSENEGIST 720
IPSPVTSPVL SRRHYGESIT NIGKASILGA ASIGKGLGGM LFSRFGRSST TQSSETSKDS 780
MEDEKKPVAS PSATTVGTQT LPHSSSGFLD SAYFRLQESF FNLPQLLFPE NVMQNKDNAL 840
VELDHRIDFE LREGLVESRY WSAVTSHTAY WSSLDVALFL LTFMYKHEHD DDAKPNLDPI 900 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR004177; DDHD. 
Pfam
 PF02862; DDHD 
SMART
  
PROSITE
 PS51043; DDHD 
PRINTS