| Tag | Content |
|---|
| CPLM ID | CPLM-015076 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glycerol-3-phosphate acyltransferase 2, mitochondrial |
Protein Synonyms/Alias | GPAT-2; xGPAT1 |
Gene Name | GPAT2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 42 | AVTPFLGKYRPFVGR | ubiquitination | [1] | | 142 | GQVPDLVKKEVQRIL | ubiquitination | [1] | | 191 | GQMKMVQKAAQAGLP | ubiquitination | [1] | | 656 | GRQRLSRKLLWKPSG | ubiquitination | [1] | | 660 | LSRKLLWKPSGDFTD | ubiquitination | [1] | | 790 | ASLDNQEKLEQFIRQ | ubiquitination | [1] |
|
Reference | [1] 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] |
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 | REGION 180 331 Acyltransferase.
MOTIF 205 210 HXXXXD motif. |
Keyword | Acyltransferase; Alternative splicing; Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 795 AA |
Protein Sequence | MATMLEGRCQ TQPRSSPSGR EASLWSSGFG MKLEAVTPFL GKYRPFVGRC CQTCTPKSWE 60
SLFHRSITDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPPCQDV PQKIMESTGV 120
QNLLSGRVPG GTGEGQVPDL VKKEVQRILG HIQAPPRPFL VRLFSWALLR FLNCLFLNVQ 180
LHKGQMKMVQ KAAQAGLPLV LLSTHKTLLD GILLPFMLLS QGLGVLRVAW DSRACSPALR 240
ALLRKLGGLF LPPEASLSLD SSEGLLARAV VQAVIEQLLV SGQPLLIFLE EPPGALGPRL 300
SALGQAWVGF VVQAVQVGIV PDALLVPVAV TYDLVPDAPC DIDHASAPLG LWTGALAVLR 360
SLWSRWGCSH RICSRVHLAQ PFSLQEYIVS ARSCWGGRQT LEQLLQPIVL GQCTAVPDTE 420
KEQEWTPITG PLLALKEEDQ LLVRRLSCHV LSASVGSSAV MSTAIMATLL LFKHQKGVFL 480
SQLLGEFSWL TEEILLRGFD VGFSGQLRSL LQHSLSLLRA HVALLRIRQG DLLVVPQPGP 540
GLTHLAQLSA ELLPVFLSEA VGACAVRGLL AGRVPPQGPW ELQGILLLSQ NELYRQILLL 600
MHLLPQDLLL LKPCQSSYCY CQEVLDRLIQ CGLLVAEETP GSRPACDTGR QRLSRKLLWK 660
PSGDFTDSDS DDFGEADGRY FRLSQQSHCP DFFLFLCRLL SPLLKAFAQA AAFLRQGQLP 720
DTELGYTEQL FQFLQATAQE EGIFECADPK LAISAVWTFR DLGVLQQTPS PAGPRLHLSP 780
TFASLDNQEK LEQFIRQFIC S 801 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005741; C:mitochondrial outer membrane; TAS:Reactome. GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB. GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:UniProtKB. GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome. GO:0044281; P:small molecule metabolic process; TAS:Reactome. GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB. |
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PROSITE | |
PRINTS | |