GPAT2
Glycerol-3-phosphate acyltransferase 2, mitochondrial
Also known as: CT123, GPAT2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q6NUI2
- Gene
- GPAT2
- Ensembl
- ENSG00000186281
- Chromosome
- 2
- Canonical length
- 795 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Mitochondria
OverviewNCBI Gene
Enables glycerol-3-phosphate O-acyltransferase activity. Predicted to be involved in glycerol-3-phosphate metabolic process; glycerolipid biosynthetic process; and piRNA processing. Located in mitochondrion. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
795 residues, UniProt reviewed canonical sequence.
>Q6NUI2|GPAT2
1 MATMLEGRCQ TQPRSSPSGR EASLWSSGFG MKLEAVTPFL GKYRPFVGRC CQTCTPKSWE
61 SLFHRSITDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPPCQDV PQKIMESTGV
121 QNLLSGRVPG GTGEGQVPDL VKKEVQRILG HIQAPPRPFL VRLFSWALLR FLNCLFLNVQ
181 LHKGQMKMVQ KAAQAGLPLV LLSTHKTLLD GILLPFMLLS QGLGVLRVAW DSRACSPALR
241 ALLRKLGGLF LPPEASLSLD SSEGLLARAV VQAVIEQLLV SGQPLLIFLE EPPGALGPRL
301 SALGQAWVGF VVQAVQVGIV PDALLVPVAV TYDLVPDAPC DIDHASAPLG LWTGALAVLR
361 SLWSRWGCSH RICSRVHLAQ PFSLQEYIVS ARSCWGGRQT LEQLLQPIVL GQCTAVPDTE
421 KEQEWTPITG PLLALKEEDQ LLVRRLSCHV LSASVGSSAV MSTAIMATLL LFKHQKLLGE
481 FSWLTEEILL RGFDVGFSGQ LRSLLQHSLS LLRAHVALLR IRQGDLLVVP QPGPGLTHLA
541 QLSAELLPVF LSEAVGACAV RGLLAGRVPP QGPWELQGIL LLSQNELYRQ ILLLMHLLPQ
601 DLLLLKPCQS SYCYCQEVLD RLIQCGLLVA EETPGSRPAC DTGRQRLSRK LLWKPSGDFT
661 DSDSDDFGEA DGRYFRLSQQ SHCPDFFLFL CRLLSPLLKA FAQAAAFLRQ GQLPDTELGY
721 TEQLFQFLQA TAQEEGIFEC ADPKLAISAV WTFRDLGVLQ QTPSPAGPRL HLSPTFASLD
781 NQEKLEQFIR QFICSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against GPAT2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 2
- Mean surface accessibility (rSASA)
- 0.28
- Highest tissue expression
- 10 nTPM
Expression across tissuesHPA
Tissue
- testis: 10 nTPM
- heart muscle: 9 nTPM
- adipose tissue: 7.1 nTPM
- choroid plexus: 6.8 nTPM
- epididymis: 5.7 nTPM
- breast: 5.6 nTPM
Single-cell type
- breast lactating cells: 596 nCPM
- early primary spermatocytes: 83 nCPM
- epididymal principal cells: 78 nCPM
- pericytes: 30 nCPM
- cardiomyocytes: 22 nCPM
- lacrimal acinar cells: 21 nCPM
Immune cell
- naive B-cell: 4.1 nTPM
- memory B-cell: 2.1 nTPM
- gdT-cell: 1.4 nTPM
- MAIT T-cell: 1.3 nTPM
- non-classical monocyte: 1.3 nTPM
- naive CD8 T-cell: 1.1 nTPM
Brain region
- choroid plexus: 5.7 nTPM
- thalamus: 3 nTPM
- pons: 2.2 nTPM
- white matter: 1.9 nTPM
- basal ganglia: 1.7 nTPM
- cerebral cortex: 1.7 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about GPAT2.
Disease | GeneticClinVar
3 pathogenic / likely-pathogenic of 129 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.12
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.17
- DepMap mean gene effect
- -0.33
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- CDP-diacylglycerol biosynthetic process
- glycerol-3-phosphate metabolic process
- glycerophospholipid metabolic process
- phosphatidic acid biosynthetic process
- piRNA processing
- triglyceride biosynthetic process
Molecular functions
- 1-acylglycerol-3-phosphate O-acyltransferase activity
- glycerol-3-phosphate O-acyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of GPAT2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads GPAT2 as an antibody target. Whether an autoantibody or antibody against GPAT2 could matter depends on whether native GPAT2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
GPAT2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label GPAT2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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