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Identification
HMDB Protein ID HMDBP00284
Secondary Accession Numbers
  • 5516
  • HMDBP03635
Name Aspartate aminotransferase, mitochondrial
Synonyms
  1. FABP-1
  2. FABPpm
  3. Fatty acid-binding protein
  4. Glutamate oxaloacetate transaminase 2
  5. Plasma membrane-associated fatty acid-binding protein
  6. Transaminase A
  7. mAspAT
  8. Kynurenine aminotransferase 4
  9. Kynurenine aminotransferase IV
  10. Kynurenine--oxoglutarate transaminase 4
  11. Kynurenine--oxoglutarate transaminase IV
Gene Name GOT2
Protein Type Enzyme
Biological Properties
General Function Involved in transferase activity, transferring nitrogenous groups
Specific Function Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 2-Oxocarboxylic acid metabolism
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Alanine, aspartate and glutamate metabolism
  • Arginine and proline metabolism
  • Argininemia
  • Argininosuccinic Aciduria
  • Carbamoyl Phosphate Synthetase Deficiency
  • Citrullinemia Type I
  • Cysteine and methionine metabolism
  • Fat digestion and absorption
  • Glutamate Metabolism
  • Glutaminolysis and Cancer
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • Malate-Aspartate Shuttle
  • Ornithine Transcarbamylase Deficiency (OTC Deficiency)
  • Phenylalanine metabolism
  • Phenylalanine, tyrosine and tryptophan biosynthesis
  • Succinic semialdehyde dehydrogenase deficiency
  • Tyrosine metabolism
  • Urea Cycle
Reactions
L-Aspartic acid + Oxoglutaric acid → Oxalacetic acid + L-Glutamic acid details
L-Kynurenine + Oxoglutaric acid → 4-(2-Aminophenyl)-2,4-dioxobutanoic acid + L-Glutamic acid details
L-Phenylalanine + Oxoglutaric acid → Phenylpyruvic acid + L-Glutamic acid details
L-Tyrosine + Oxoglutaric acid → 4-Hydroxyphenylpyruvic acid + L-Glutamic acid details
L-Cysteine + Oxoglutaric acid → 3-Mercaptopyruvic acid + DL-Glutamate details
Cysteic acid + Oxoglutaric acid → 3-Sulfopyruvic acid + L-Glutamic acid details
3-Sulfinoalanine + Oxoglutaric acid → 3-Sulfinylpyruvic acid + L-Glutamic acid details
4-Hydroxy-L-glutamic acid + Oxoglutaric acid → D-4-Hydroxy-2-oxoglutarate + L-Glutamic acid details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
response to ethanol
2-oxoglutarate metabolic process
glutamate metabolic process
aspartate biosynthetic process
aspartate catabolic process
gluconeogenesis
glutamate catabolic process to 2-oxoglutarate
glutamate catabolic process to aspartate
oxaloacetate metabolic process
4-hydroxyproline catabolic process
cellular amino acid biosynthetic process
fatty acid transport
Cellular Component
mitochondrial matrix
plasma membrane
mitochondrial inner membrane
Function
binding
catalytic activity
transferase activity
transferase activity, transferring nitrogenous groups
cofactor binding
pyridoxal phosphate binding
transaminase activity
Molecular Function
kynurenine-oxoglutarate transaminase activity
pyridoxal phosphate binding
L-aspartate:2-oxoglutarate aminotransferase activity
L-phenylalanine:2-oxoglutarate aminotransferase activity
Process
metabolic process
cellular metabolic process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Cell membrane
  2. Mitochondrion matrix
Gene Properties
Chromosome Location 16
Locus 16q21
SNPs GOT2
Gene Sequence
>1293 bp
ATGGCCCTGCTGCATTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATACCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGTCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
Protein Properties
Number of Residues 430
Molecular Weight 47517.285
Theoretical pI 9.005
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Aspartate aminotransferase, mitochondrial
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
GenBank ID Protein 62898103
UniProtKB/Swiss-Prot ID P00505
UniProtKB/Swiss-Prot Entry Name AATM_HUMAN
PDB IDs Not Available
GenBank Gene ID AK223271
GeneCard ID GOT2
GenAtlas ID GOT2
HGNC ID HGNC:4433
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
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  5. Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed:3207426 ]
  6. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed:4052435 ]
  7. Zhou SL, Gordon RE, Bradbury M, Stump D, Kiang CL, Berk PD: Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells. Hepatology. 1998 Apr;27(4):1064-74. [PubMed:9537447 ]
  8. Amanchy R, Kalume DE, Iwahori A, Zhong J, Pandey A: Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res. 2005 Sep-Oct;4(5):1661-71. [PubMed:16212419 ]