AADAT
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Also known as: AADAT_HUMAN, KAT2, KATII, KYAT2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q8N5Z0
- Gene
- AADAT
- Ensembl
- ENSG00000109576
- Chromosome
- 4
- Canonical length
- 425 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Vesicles,Plasma membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a protein that is highly similar to mouse and rat kynurenine aminotransferase II. The rat protein is a homodimer with two transaminase activities. One activity is the transamination of alpha-aminoadipic acid, a final step in the saccaropine pathway which is the major pathway for L-lysine catabolism. The other activity involves the transamination of kynurenine to produce kynurenine acid, the precursor of kynurenic acid which has neuroprotective properties. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]
Canonical amino-acid sequenceUniProt
425 residues, UniProt reviewed canonical sequence.
>Q8N5Z0|AADAT
1 MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT
61 IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG
121 LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP
181 EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK
241 FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
301 LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV
361 KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL
421 IKESLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against AADAT 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
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.23
- Highest tissue expression
- 63 nTPM
Expression across tissuesHPA
Tissue
- liver: 63 nTPM
- choroid plexus: 16 nTPM
- prostate: 14 nTPM
- retina: 11 nTPM
- endometrium: 9.9 nTPM
- amygdala: 9.7 nTPM
Single-cell type
- extravillous trophoblasts: 113 nCPM
- hepatocytes: 42 nCPM
- breast lactating cells: 41 nCPM
- early primary spermatocytes: 41 nCPM
- adrenal medulla cells: 32 nCPM
- prostatic glandular cells: 28 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- choroid plexus: 24 nTPM
- white matter: 18 nTPM
- cerebral cortex: 18 nTPM
- hypothalamus: 14 nTPM
- pons: 14 nTPM
- basal ganglia: 14 nTPM
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)
- 0.51
- gnomAD pLI
- 0.15
- gnomAD missense Z
- 2.35
- DepMap mean gene effect
- -0.06
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- 2-oxoglutarate metabolic process
- glutamate metabolic process
- kynurenine metabolic process
- L-lysine catabolic process to acetyl-CoA via saccharopine
- alpha-amino acid metabolic process
Molecular functions
- kynurenine-glyoxylate transaminase activity
- kynurenine-oxoglutarate transaminase activity
- protein homodimerization activity
- pyridoxal phosphate binding
- 2-aminoadipate transaminase activity
- glycine:2-oxoglutarate aminotransferase activity
- methionine-glyoxylate transaminase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Aminotransferase, class I/classII, large domain
- Pyridoxal phosphate-dependent transferase, major domain
- Pyridoxal phosphate-dependent transferase
- Aminotransferase class I and II
- Class-I pyridoxal-phosphate-dependent aminotransferase-like
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads AADAT as an antibody target. Whether an autoantibody or antibody against AADAT could matter depends on whether native AADAT is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
AADAT 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 AADAT as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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