CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022105
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma 
Protein Synonyms/Alias
 1-acylglycerol-3-phosphate O-acyltransferase 3; 1-AGP acyltransferase 3; 1-AGPAT 3; Lysophosphatidic acid acyltransferase gamma; LPAAT-gamma 
Gene Name
 AGPAT3 
Gene Synonyms/Alias
 LPAAT3; UNQ759/PRO1490 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
119FGVLGSSKVLAKKELubiquitination[1, 2]
201AKGLPVLKYHLLPRTubiquitination[1, 2]
236TLNFRGNKNPSLLGIubiquitination[1, 2]
247LLGILYGKKYEADMCubiquitination[1, 2]
281LHKLYQEKDALQEIYubiquitination[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] 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]
 [3] 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
 Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. 
Sequence Annotation
 MOTIF 96 101 HXXXXD motif.  
Keyword
 Acyltransferase; Alternative splicing; Complete proteome; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus; Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 376 AA 
Protein Sequence
MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ 60
LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV 120
LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF 180
TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL 240
LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK 300
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE 360
IEKGSSYGNQ EFKKKE 376 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; NAS:UniProtKB.
 GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome. 
Interpro
 IPR002123; Plipid/glycerol_acylTrfase. 
Pfam
 PF01553; Acyltransferase 
SMART
 SM00563; PlsC 
PROSITE
  
PRINTS