CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014357
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycerol-3-phosphate acyltransferase 1, mitochondrial 
Protein Synonyms/Alias
 GPAT-1; P90 
Gene Name
 Gpam 
Gene Synonyms/Alias
 Gpat1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
40DWVDCGFKPTFFRSAubiquitination[1]
391GVIRMLRKNYGYVRVubiquitination[1]
779SATYCLVKNAVKMFKacetylation[2, 3, 4, 5]
783CLVKNAVKMFKDIGVacetylation[3, 4, 5]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
 Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis (By similarity). 
Sequence Annotation
 MOTIF 230 235 HXXXXD motif.
 MOD_RES 380 380 Phosphoserine (By similarity).
 MOD_RES 694 694 Phosphoserine.  
Keyword
 Acyltransferase; Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase; Transit peptide; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 827 AA 
Protein Sequence
MEESSVTVGT IDVSYLPSSS EYSLGRCKHT SEDWVDCGFK PTFFRSATLK WKESLMSRKR 60
PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YILFVQERDV 120
HKGMFATSVT ENVLSSSRVQ EAIAEVAAEL NPDGSAQQQS KAIQKVKRKA RKILQEMVAT 180
VSPGMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT 240
FILFCHNIKA PYIASGNNLN IPVFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHV 300
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS SNTIPDILVI PVGISYDRII 360
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGYVRVDF AQPFSLKEYL EGQSQKPVSA 420
PLSLEQALLP AILPSRPNDV ADEHQDLSSN ESRNPADEAF RRRLIANLAE HILFTASKSC 480
AIMSTHIVAC LLLYRHRQGI HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL 540
GNCVTITHTS RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVLNKRCSG 600
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE 660
QDDQEDVSPG LAEQQWDKKL PELNWRSDEE DEDSDFGEEQ RDCYLKVSQS KEHQQFITFL 720
QRLLGPLLEA YSSAAIFVHN FSGPVPESEY LQKLHRYLIT RTERNVAVYA ESATYCLVKN 780
AVKMFKDIGV FKETKQKRVS VLELSSTFLP QCNRQKLLEY ILSFVVL 827 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:MGI.
 GO:0006637; P:acyl-CoA metabolic process; IMP:MGI.
 GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0051607; P:defense response to virus; IMP:MGI.
 GO:0055089; P:fatty acid homeostasis; IMP:MGI.
 GO:0006631; P:fatty acid metabolic process; IMP:MGI.
 GO:0006650; P:glycerophospholipid metabolic process; IMP:MGI.
 GO:0070970; P:interleukin-2 secretion; IMP:MGI.
 GO:0070236; P:negative regulation of activation-induced cell death of T cells; IMP:MGI.
 GO:0055091; P:phospholipid homeostasis; IMP:MGI.
 GO:0042104; P:positive regulation of activated T cell proliferation; IMP:MGI.
 GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
 GO:0050707; P:regulation of cytokine secretion; IMP:MGI.
 GO:0009749; P:response to glucose stimulus; IMP:MGI.
 GO:0019432; P:triglyceride biosynthetic process; IEA:Compara.
 GO:0006641; P:triglyceride metabolic process; IMP:MGI. 
Interpro
 IPR022284; G3P_O-AcylTrfase.
 IPR002123; Plipid/glycerol_acylTrfase. 
Pfam
 PF01553; Acyltransferase 
SMART
 SM00563; PlsC 
PROSITE
  
PRINTS