Aspartate aminotransferase, mitochondrial

Details

Name
Aspartate aminotransferase, mitochondrial
Synonyms
  • 2.6.1.1
  • FABP-1
  • FABPpm
  • Fatty acid-binding protein
  • Glutamate oxaloacetate transaminase 2
  • Kynurenine aminotransferase 4
  • Kynurenine aminotransferase IV
  • Kynurenine--oxoglutarate transaminase 4
  • Kynurenine--oxoglutarate transaminase IV
  • mAspAT
  • Plasma membrane-associated fatty acid-binding protein
  • Transaminase A
Gene Name
GOT2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037006|Aspartate aminotransferase, mitochondrial
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
Number of residues
430
Molecular Weight
47517.285
Theoretical pI
9.38
GO Classification
Functions
amino acid binding / identical protein binding / kynurenine-oxoglutarate transaminase activity / L-aspartate / L-phenylalanine / phospholipid binding / poly(A) RNA binding / pyridoxal phosphate binding
Processes
2-oxoglutarate metabolic process / 4-hydroxyproline catabolic process / aspartate biosynthetic process / aspartate catabolic process / aspartate metabolic process / carbohydrate metabolic process / cellular amino acid biosynthetic process / cellular nitrogen compound metabolic process / fatty acid transport / gluconeogenesis / glucose metabolic process / glutamate catabolic process to 2-oxoglutarate / glutamate catabolic process to aspartate / glutamate metabolic process / oxaloacetate metabolic process / response to ethanol / small molecule metabolic process
Components
cell surface / extracellular exosome / mitochondrial inner membrane / mitochondrial matrix / mitochondrion / myelin sheath / perikaryon / plasma membrane / protein complex
General Function
Pyridoxal phosphate binding
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion matrix
Gene sequence
>lcl|BSEQ0010269|Aspartate aminotransferase, mitochondrial (GOT2)
ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATCGGAGCCAGT
TTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCAACCTGGGGA
AACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGGTATTATGAC
CCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAAATACCAGAG
CAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGACCCGCGTCCG
GAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCGTTCTTTGAC
ATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATGCCTGGGCTGTGCGCCAC
TTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAACATGGGCTTA
TATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAAGCCAAAAGG
GTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCCCTCAATGGG
GCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGGCTGCAAGAA
GTGAAAGTCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCCAACCTCAAG
AAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATGTTCTGTTTC
ACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATCTACATGACA
AAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTACCTTGCCCAT
GCCATTCACCAGGTCACCAAGTAA
Chromosome Location
16
Locus
16q21
External Identifiers
ResourceLink
UniProtKB IDP00505
UniProtKB Entry NameAATM_HUMAN
GenBank Protein ID179104
GenBank Gene IDM22632
GenAtlas IDGOT2
HGNC IDHGNC:4433
General References
  1. 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. [Article]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. 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. [Article]
  6. 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. [Article]
  7. 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. [Article]
  8. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  9. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  10. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00128Aspartic acidapproved, nutraceuticalunknownDetails
DB027834'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-PhosphateexperimentalunknownDetails
DB00114Pyridoxal phosphateapproved, investigational, nutraceuticalunknowncofactorDetails
DB00142Glutamic acidapproved, nutraceuticalunknownDetails
DB00151Cysteineapproved, nutraceuticalunknownsubstrateDetails
DB00114Pyridoxal phosphateapproved, investigational, nutraceuticalunknowncofactorDetails
DB00142Glutamic acidapproved, nutraceuticalunknownsubstrateDetails