CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031058
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydroxyacetone phosphate acyltransferase 
Protein Synonyms/Alias
 cDNA FLJ53146, highly similar to Dihydroxyacetone phosphate acyltransferase(EC 2.3.1.42) 
Gene Name
 GNPAT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52ILDEMSHKLRLGAIRubiquitination[1, 2]
85VNEEGIQKLQRAIQEubiquitination[2]
251ESTTGLLKARKILSEubiquitination[2, 3]
582VRLGVVEKKKINNNCacetylation[3, 4]
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] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
  
Sequence Annotation
  
Keyword
 Acyltransferase; Complete proteome; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 619 AA 
Protein Sequence
MESSSSSNSY FSVGPTSPSA VVLLYSLSKE SLQSVDVLRE EVSEILDEMS HKLRLGAIRF 60
CAFTLSKVFK QIFSKVCVNE EGIQKLQRAI QEHPVVLLPS HRSYIDFLML SFLLYNYDLP 120
VPVIAAGMDF LGMKMVGELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RNGYAPVEFF 180
LEGTRSRSAK TLTPKFGLLN IVMEPFFKRE VFDTYLVPIS ISYDKILEET LYVYELLGVP 240
KPKESTTGLL KARKILSENF GSIHVYFGDP VSLRSLAAGR MSRSSYNLVP RYIPQKQSED 300
MHAFVTEVAY KMELLQIENM VLSPWTLIVA VLLQNRPSMD FDALVEKTLW LKGLTQAFGG 360
FLIWPDNKPA EEVVPASILL HSNIASLVKD QVILKVDSGD SEVVDGLMLQ HITLLMCSAY 420
RNQLLNIFVR PSLVAVALQM TPGFRKEDVY SCFRFLRDVF ADEFIFLPGN TLKDFEEGCY 480
LLCKSEAIQV TTKDILVTEK GNTVLEFLVG LFKPFVESYQ IICKYLLSEE EDHFSEEQYL 540
AAVRKFTSQL LDQGTSQCYD VLSSDVQKNA LAACVRLGVV EKKKINNNCI FNVNEPATTK 600
LEEMLGCKTP IGKPATAKL 619 
Gene Ontology
 GO:0016020; C:membrane; IEA:InterPro.
 GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:InterPro.
 GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. 
Interpro
 IPR022284; G3P_O-AcylTrfase.
 IPR002123; Plipid/glycerol_acylTrfase. 
Pfam
 PF01553; Acyltransferase 
SMART
 SM00563; PlsC 
PROSITE
  
PRINTS