CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon 
Protein Synonyms/Alias
 1-acylglycerol-3-phosphate O-acyltransferase 5; 1-AGP acyltransferase 5; 1-AGPAT 5; Lysophosphatidic acid acyltransferase epsilon; LPAAT-epsilon 
Gene Name
 AGPAT5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
120GHVRYVLKEGLKWLPubiquitination[1, 2]
150RSAKFNEKEMRNKLQubiquitination[3, 4]
155NEKEMRNKLQSYVDAubiquitination[3, 4, 5]
183RYNPEQTKVLSASQAubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
201QRGLAVLKHVLTPRIubiquitination[4, 5, 6]
209HVLTPRIKATHVAFDubiquitination[4]
253TMTEFLCKECPKIHIubiquitination[4]
290ERFEIKDKMLIEFYEubiquitination[5]
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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] 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
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 C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable. 
Sequence Annotation
 MOTIF 93 98 HXXXXD motif.  
Keyword
 Acyltransferase; Complete proteome; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; Nucleus; Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 364 AA 
Protein Sequence
MLLSLVLHTY SMRYLLPSVV LLGTAPTYVL AWGVWRLLSA FLPARFYQAL DDRLYCVYQS 60
MVLFFFENYT GVQILLYGDL PKNKENIIYL ANHQSTVDWI VADILAIRQN ALGHVRYVLK 120
EGLKWLPLYG CYFAQHGGIY VKRSAKFNEK EMRNKLQSYV DAGTPMYLVI FPEGTRYNPE 180
QTKVLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDCMKN YLDAIYDVTV VYEGKDDGGQ 240
RRESPTMTEF LCKECPKIHI HIDRIDKKDV PEEQEHMRRW LHERFEIKDK MLIEFYESPD 300
PERRKRFPGK SVNSKLSIKK TLPSMLILSG LTAGMLMTDA GRKLYVNTWI YGTLLGCLWV 360
TIKA 364 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
 GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
 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