AATM_HUMAN
ID AATM_HUMAN Reviewed; 430 AA.
AC P00505; B4DJA6; E7ERW2; Q53FL3; Q9BWA3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE Short=mAspAT;
DE EC=2.6.1.1 {ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819};
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:P00507};
DE AltName: Full=Fatty acid-binding protein;
DE Short=FABP-1;
DE AltName: Full=Glutamate oxaloacetate transaminase 2;
DE AltName: Full=Kynurenine aminotransferase 4;
DE AltName: Full=Kynurenine aminotransferase IV;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE Short=FABPpm;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=GOT2 {ECO:0000312|HGNC:HGNC:4433};
GN Synonyms=KYAT4 {ECO:0000312|HGNC:HGNC:4433};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-346.
RX PubMed=3207426; DOI=10.1016/s0006-291x(88)81017-9;
RA Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B.,
RA Berthelot P., Hanoune J., Barouki R.;
RT "Nucleotide sequence and tissue distribution of the human mitochondrial
RT aspartate aminotransferase mRNA.";
RL Biochem. Biophys. Res. Commun. 157:1309-1315(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-346.
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-428.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 30-430, AND VARIANT GLY-346.
RX PubMed=4052435; DOI=10.1016/0167-4838(85)90172-4;
RA Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S.,
RA Bossa F.;
RT "The primary structure of mitochondrial aspartate aminotransferase from
RT human heart.";
RL Biochim. Biophys. Acta 832:46-51(1985).
RN [7]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9537447; DOI=10.1002/hep.510270423;
RA Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.;
RT "Ethanol up-regulates fatty acid uptake and plasma membrane expression and
RT export of mitochondrial aspartate aminotransferase in HepG2 cells.";
RL Hepatology 27:1064-1074(1998).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159; LYS-234;
RP LYS-296; LYS-396 AND LYS-404, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; TYR-96; SER-143 AND
RP THR-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN DEE82, VARIANTS DEE82 LEU-209
RP DEL; GLY-262; GLY-337 AND VAL-366, AND CHARACTERIZATION OF VARIANTS DEE82
RP GLY-262 AND VAL-366.
RX PubMed=31422819; DOI=10.1016/j.ajhg.2019.07.015;
RA van Karnebeek C.D.M., Ramos R.J., Wen X.Y., Tarailo-Graovac M.,
RA Gleeson J.G., Skrypnyk C., Brand-Arzamendi K., Karbassi F., Issa M.Y.,
RA van der Lee R., Droegemoeller B.I., Koster J., Rousseau J., Campeau P.M.,
RA Wang Y., Cao F., Li M., Ruiter J., Ciapaite J., Kluijtmans L.A.J.,
RA Willemsen M.A.A.P., Jans J.J., Ross C.J., Wintjes L.T., Rodenburg R.J.,
RA Huigen M.C.D.G., Jia Z., Waterham H.R., Wasserman W.W., Wanders R.J.A.,
RA Verhoeven-Duif N.M., Zaki M.S., Wevers R.A.;
RT "Bi-allelic GOT2 mutations cause a treatable malate-aspartate shuttle-
RT related encephalopathy.";
RL Am. J. Hum. Genet. 105:534-548(2019).
RN [14] {ECO:0007744|PDB:5AX8}
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 30-430, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=26902786; DOI=10.5582/bst.2015.01150;
RA Jiang X., Wang J., Chang H., Zhou Y.;
RT "Recombinant expression, purification and crystallographic studies of the
RT mature form of human mitochondrial aspartate aminotransferase.";
RL Biosci. Trends 10:79-84(2016).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
CC malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
CC redox balance. Is important for metabolite exchange between
CC mitochondria and cytosol, and for amino acid metabolism. Facilitates
CC cellular uptake of long-chain free fatty acids.
CC {ECO:0000269|PubMed:31422819, ECO:0000269|PubMed:9537447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P00507};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:26902786};
CC Temperature dependence:
CC Optimum temperature is 47.5 degrees Celsius.
CC {ECO:0000269|PubMed:26902786};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:9537447}. Cell membrane
CC {ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes
CC translocation to the cell membrane. {ECO:0000269|PubMed:9537447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00505-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00505-2; Sequence=VSP_054848;
CC -!- INDUCTION: Up-regulated by long-time exposure to alcohol.
CC {ECO:0000269|PubMed:9537447}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 82 (DEE82)
CC [MIM:618721]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE82 is an autosomal recessive metabolic
CC encephalopathy characterized by epilepsy from the first year of life,
CC global developmental delay, hypotonia and feeding difficulties apparent
CC soon after birth, and intellectual and motor disabilities. Other
CC features include poor overall growth, progressive microcephaly and
CC biochemical abnormalities, including increased serum lactate and
CC ammonia. {ECO:0000269|PubMed:31422819}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M22632; AAA35568.1; -; mRNA.
DR EMBL; AK295993; BAG58768.1; -; mRNA.
DR EMBL; AK223271; BAD96991.1; -; mRNA.
DR EMBL; AC012183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000525; AAH00525.1; -; mRNA.
DR CCDS; CCDS10801.1; -. [P00505-1]
DR CCDS; CCDS67045.1; -. [P00505-2]
DR PIR; A31873; XNHUDM.
DR RefSeq; NP_001273149.1; NM_001286220.1. [P00505-2]
DR RefSeq; NP_002071.2; NM_002080.3. [P00505-1]
DR PDB; 5AX8; X-ray; 2.99 A; A/B/C/D=30-430.
DR PDBsum; 5AX8; -.
DR AlphaFoldDB; P00505; -.
DR SMR; P00505; -.
DR BioGRID; 109068; 61.
DR IntAct; P00505; 24.
DR MINT; P00505; -.
DR STRING; 9606.ENSP00000245206; -.
DR ChEMBL; CHEMBL4524033; -.
DR DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugCentral; P00505; -.
DR TCDB; 9.A.70.1.1; the aspartate amino transferase (aat) family.
DR GlyGen; P00505; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P00505; -.
DR MetOSite; P00505; -.
DR PhosphoSitePlus; P00505; -.
DR SwissPalm; P00505; -.
DR BioMuta; GOT2; -.
DR DMDM; 308153643; -.
DR UCD-2DPAGE; P00505; -.
DR CPTAC; CPTAC-518; -.
DR CPTAC; CPTAC-519; -.
DR EPD; P00505; -.
DR jPOST; P00505; -.
DR MassIVE; P00505; -.
DR MaxQB; P00505; -.
DR PaxDb; P00505; -.
DR PeptideAtlas; P00505; -.
DR PRIDE; P00505; -.
DR ProteomicsDB; 17864; -.
DR ProteomicsDB; 51258; -. [P00505-1]
DR TopDownProteomics; P00505-1; -. [P00505-1]
DR Antibodypedia; 15396; 646 antibodies from 40 providers.
DR DNASU; 2806; -.
DR Ensembl; ENST00000245206.10; ENSP00000245206.5; ENSG00000125166.13. [P00505-1]
DR Ensembl; ENST00000434819.2; ENSP00000394100.2; ENSG00000125166.13. [P00505-2]
DR GeneID; 2806; -.
DR KEGG; hsa:2806; -.
DR MANE-Select; ENST00000245206.10; ENSP00000245206.5; NM_002080.4; NP_002071.2.
DR UCSC; uc002eof.2; human. [P00505-1]
DR CTD; 2806; -.
DR DisGeNET; 2806; -.
DR GeneCards; GOT2; -.
DR HGNC; HGNC:4433; GOT2.
DR HPA; ENSG00000125166; Group enriched (heart muscle, liver, skeletal muscle, tongue).
DR MalaCards; GOT2; -.
DR MIM; 138150; gene.
DR MIM; 618721; phenotype.
DR neXtProt; NX_P00505; -.
DR OpenTargets; ENSG00000125166; -.
DR PharmGKB; PA28818; -.
DR VEuPathDB; HostDB:ENSG00000125166; -.
DR eggNOG; KOG1411; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P00505; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P00505; -.
DR TreeFam; TF300641; -.
DR BioCyc; MetaCyc:HS04858-MON; -.
DR BRENDA; 2.6.1.1; 2681.
DR PathwayCommons; P00505; -.
DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SignaLink; P00505; -.
DR SIGNOR; P00505; -.
DR BioGRID-ORCS; 2806; 151 hits in 1080 CRISPR screens.
DR ChiTaRS; GOT2; human.
DR GeneWiki; GOT2; -.
DR GenomeRNAi; 2806; -.
DR Pharos; P00505; Tbio.
DR PRO; PR:P00505; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P00505; protein.
DR Bgee; ENSG00000125166; Expressed in hindlimb stylopod muscle and 203 other tissues.
DR ExpressionAtlas; P00505; baseline and differential.
DR Genevisible; P00505; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
DR GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl.
DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IEP:UniProtKB.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase;
KW Cell membrane; Direct protein sequencing; Disease variant; Epilepsy;
KW Lipid transport; Membrane; Methylation; Mitochondrion; Nitration;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:4052435,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 30..430
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000001215"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 73
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 73
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 96
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 96
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 107
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 107
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 159
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 185
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 185
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 227
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 279
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 296
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 296
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 309
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 309
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12344"
FT MOD_RES 313
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 338
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 338
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 363
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 363
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 396
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 396
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 404
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 404
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT VAR_SEQ 83..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054848"
FT VARIANT 2
FT /note="A -> S (in dbSNP:rs11558171)"
FT /id="VAR_055494"
FT VARIANT 188
FT /note="G -> S (in dbSNP:rs11076256)"
FT /id="VAR_031710"
FT VARIANT 209
FT /note="Missing (in DEE82; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31422819"
FT /id="VAR_083488"
FT VARIANT 262
FT /note="R -> G (in DEE82; decreased glutamate oxaloacetate
FT transferase activity; dbSNP:rs752927520)"
FT /evidence="ECO:0000269|PubMed:31422819"
FT /id="VAR_083489"
FT VARIANT 337
FT /note="R -> G (in DEE82; unknown pathological significance;
FT dbSNP:rs1247507359)"
FT /evidence="ECO:0000269|PubMed:31422819"
FT /id="VAR_083490"
FT VARIANT 346
FT /note="V -> G (in dbSNP:rs30842)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:3207426, ECO:0000269|PubMed:4052435"
FT /id="VAR_031711"
FT VARIANT 366
FT /note="G -> V (in DEE82; unknown pathological significance;
FT decreased glutamate oxaloacetate transferase activity;
FT dbSNP:rs1597696047)"
FT /evidence="ECO:0000269|PubMed:31422819"
FT /id="VAR_083491"
FT VARIANT 428
FT /note="V -> A (in dbSNP:rs17849335)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031712"
FT CONFLICT 110..111
FT /note="AE -> EA (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> T (in Ref. 3; BAD96991)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:5AX8"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5AX8"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5AX8"
FT TURN 247..251
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:5AX8"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:5AX8"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 298..315
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 334..364
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 388..398
FT /evidence="ECO:0007829|PDB:5AX8"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:5AX8"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:5AX8"
SQ SEQUENCE 430 AA; 47518 MW; F559567ABF2DB346 CRC64;
MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV
LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR
YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR IIGMRTQLVS
NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY
LAHAIHQVTK
