AATC_HUMAN
ID AATC_HUMAN Reviewed; 413 AA.
AC P17174; B2R6R7; B7Z7E9; Q5VW80;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000305};
DE Short=cAspAT;
DE EC=2.6.1.1 {ECO:0000269|PubMed:21900944};
DE EC=2.6.1.3 {ECO:0000250|UniProtKB:P13221};
DE AltName: Full=Cysteine aminotransferase, cytoplasmic;
DE AltName: Full=Cysteine transaminase, cytoplasmic;
DE Short=cCAT;
DE AltName: Full=Glutamate oxaloacetate transaminase 1;
DE AltName: Full=Transaminase A;
GN Name=GOT1 {ECO:0000312|HGNC:HGNC:4432};
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 SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=1974457; DOI=10.1021/bi00474a011;
RA Bousquet-Lemercier B., Pol S., Pave-Preux M., Hanoune J., Barouki R.;
RT "Properties of human liver cytosolic aspartate aminotransferase mRNAs
RT generated by alternative polyadenylation site selection.";
RL Biochemistry 29:5293-5299(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wang C.Y., Huang Y.Q., Shi J.D., Marron M.P., Ruan Q.G., Hawkins-Lee B.,
RA Ochoa B., She J.X.;
RT "Genomic structure and mutation analysis of GOT1 in the urofacial (Ochoa)
RT syndrome gene critical region on chromosome 10.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 2-413.
RC TISSUE=Liver;
RX PubMed=2241899; DOI=10.1042/bj2700651;
RA Doyle J.M., Schinina M.E., Bossa F., Doonan S.;
RT "The amino acid sequence of cytosolic aspartate aminotransferase from human
RT liver.";
RL Biochem. J. 270:651-657(1990).
RN [9]
RP FUNCTION.
RX PubMed=16039064; DOI=10.1016/j.neulet.2005.06.030;
RA D'Aniello A., Fisher G., Migliaccio N., Cammisa G., D'Aniello E.,
RA Spinelli P.;
RT "Amino acids and transaminases activity in ventricular CSF and in brain of
RT normal and Alzheimer patients.";
RL Neurosci. Lett. 388:49-53(2005).
RN [10]
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 [11]
RP INVOLVEMENT IN ASTQTL1, VARIANT ASN-389 DEL, FUNCTION, CATALYTIC ACTIVITY,
RP CHARACTERIZATION OF VARIANT ASN-389 DEL, AND POLYMORPHISM.
RX PubMed=21900944; DOI=10.1038/jhg.2011.105;
RA Shen H., Damcott C., Shuldiner S.R., Chai S., Yang R., Hu H., Gibson Q.,
RA Ryan K.A., Mitchell B.D., Gong D.W.;
RT "Genome-wide association study identifies genetic variants in GOT1
RT determining serum aspartate aminotransferase levels.";
RL J. Hum. Genet. 56:801-805(2011).
RN [12]
RP FETAL BLOOD LEVELS.
RX PubMed=22633534; DOI=10.1016/j.earlhumdev.2012.05.001;
RA Zlotnik A., Tsesis S., Gruenbaum B.F., Ohayon S., Gruenbaum S.E., Boyko M.,
RA Sheiner E., Brotfain E., Shapira Y., Teichberg V.I.;
RT "Relationship between glutamate, GOT and GPT levels in maternal and fetal
RT blood: a potential mechanism for fetal neuroprotection.";
RL Early Hum. Dev. 88:773-778(2012).
RN [13]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
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 [15]
RP 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 [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27827456; DOI=10.1038/srep36749;
RA Irino Y., Toh R., Nagao M., Mori T., Honjo T., Shinohara M., Tsuda S.,
RA Nakajima H., Satomi-Kobayashi S., Shinke T., Tanaka H., Ishida T.,
RA Miyata O., Hirata K.I.;
RT "2-Aminobutyric acid modulates glutathione homeostasis in the myocardium.";
RL Sci. Rep. 6:36749-36749(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-412 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE AND TARTARIC ACID, SUBUNIT, AND PYRIDOXAL PHOSPHATE AT LYS-259.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human glutamate oxaloacetate transaminase 1 (GOT1).";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine
CC (PubMed:21900944). Important regulator of levels of glutamate, the
CC major excitatory neurotransmitter of the vertebrate central nervous
CC system. Acts as a scavenger of glutamate in brain neuroprotection. The
CC aspartate aminotransferase activity is involved in hepatic glucose
CC synthesis during development and in adipocyte glyceroneogenesis. Using
CC L-cysteine as substrate, regulates levels of mercaptopyruvate, an
CC important source of hydrogen sulfide. Mercaptopyruvate is converted
CC into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase
CC (3MST). Hydrogen sulfide is an important synaptic modulator and
CC neuroprotectant in the brain. In addition, catalyzes (2S)-2-
CC aminobutanoate, a by-product in the cysteine biosynthesis pathway
CC (PubMed:27827456). {ECO:0000269|PubMed:16039064,
CC ECO:0000269|PubMed:21900944, ECO:0000269|PubMed:27827456}.
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:21900944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-
CC glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:27827456};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225;
CC Evidence={ECO:0000269|PubMed:27827456};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-
CC glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.17}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1974457}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17174-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17174-2; Sequence=VSP_055799;
CC -!- POLYMORPHISM: Genetic variations in GOT1 are associated with low serum
CC aspartate aminotransferase and define the aspartate aminotransferase
CC serum level quantitative trait locus 1 (ASTQTL1) [MIM:614419].
CC {ECO:0000269|PubMed:21900944}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- MISCELLANEOUS: Aspartate aminotransferase activity found to be
CC increased in cerebral spinal fluid (CSF) of patients with Alzheimer
CC disease (PubMed:16039064). Fetal serum levels of the enzyme in the
CC umbilical artery and vein are found to be significantly higher than
CC maternal serum levels (PubMed:22633534). {ECO:0000305|PubMed:16039064,
CC ECO:0000305|PubMed:22633534}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M37400; AAA35563.1; -; mRNA.
DR EMBL; AF080467; AAC32851.1; -; Genomic_DNA.
DR EMBL; AF080459; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080460; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080461; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080462; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080463; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080464; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080465; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF080466; AAC32851.1; JOINED; Genomic_DNA.
DR EMBL; AF052153; AAC28622.1; -; mRNA.
DR EMBL; AK301916; BAH13585.1; -; mRNA.
DR EMBL; AK312684; BAG35564.1; -; mRNA.
DR EMBL; AL391684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49869.1; -; Genomic_DNA.
DR EMBL; BC000498; AAH00498.1; -; mRNA.
DR CCDS; CCDS7479.1; -. [P17174-1]
DR PIR; S13035; S13035.
DR PIR; S29027; S29027.
DR RefSeq; NP_002070.1; NM_002079.2. [P17174-1]
DR PDB; 3II0; X-ray; 2.05 A; A/B/C/D=14-412.
DR PDB; 3WZF; X-ray; 2.99 A; A=2-413.
DR PDB; 6DNA; X-ray; 3.00 A; A/B/C/D/E/F=6-410.
DR PDB; 6DNB; X-ray; 1.70 A; A=3-413.
DR PDB; 6DND; X-ray; 2.10 A; A/B=3-413.
DR PDB; 6LIG; X-ray; 2.62 A; A/B=3-413.
DR PDBsum; 3II0; -.
DR PDBsum; 3WZF; -.
DR PDBsum; 6DNA; -.
DR PDBsum; 6DNB; -.
DR PDBsum; 6DND; -.
DR PDBsum; 6LIG; -.
DR AlphaFoldDB; P17174; -.
DR SMR; P17174; -.
DR BioGRID; 109067; 256.
DR IntAct; P17174; 11.
DR MINT; P17174; -.
DR STRING; 9606.ENSP00000359539; -.
DR BindingDB; P17174; -.
DR ChEMBL; CHEMBL2189139; -.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB04299; Maleic acid.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugCentral; P17174; -.
DR iPTMnet; P17174; -.
DR PhosphoSitePlus; P17174; -.
DR SwissPalm; P17174; -.
DR BioMuta; GOT1; -.
DR DMDM; 5902703; -.
DR REPRODUCTION-2DPAGE; IPI00219029; -.
DR UCD-2DPAGE; P17174; -.
DR EPD; P17174; -.
DR jPOST; P17174; -.
DR MassIVE; P17174; -.
DR MaxQB; P17174; -.
DR PaxDb; P17174; -.
DR PeptideAtlas; P17174; -.
DR PRIDE; P17174; -.
DR ProteomicsDB; 53459; -. [P17174-1]
DR ProteomicsDB; 6862; -.
DR Antibodypedia; 31077; 563 antibodies from 38 providers.
DR DNASU; 2805; -.
DR Ensembl; ENST00000370508.7; ENSP00000359539.5; ENSG00000120053.12. [P17174-1]
DR GeneID; 2805; -.
DR KEGG; hsa:2805; -.
DR MANE-Select; ENST00000370508.7; ENSP00000359539.5; NM_002079.3; NP_002070.1.
DR UCSC; uc001kpr.4; human. [P17174-1]
DR CTD; 2805; -.
DR DisGeNET; 2805; -.
DR GeneCards; GOT1; -.
DR HGNC; HGNC:4432; GOT1.
DR HPA; ENSG00000120053; Group enriched (heart muscle, liver, skeletal muscle, tongue).
DR MalaCards; GOT1; -.
DR MIM; 138180; gene.
DR MIM; 614419; phenotype.
DR neXtProt; NX_P17174; -.
DR OpenTargets; ENSG00000120053; -.
DR PharmGKB; PA28817; -.
DR VEuPathDB; HostDB:ENSG00000120053; -.
DR eggNOG; KOG1412; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P17174; -.
DR OMA; WDQNKRQ; -.
DR PhylomeDB; P17174; -.
DR TreeFam; TF314089; -.
DR BioCyc; MetaCyc:HS04361-MON; -.
DR BRENDA; 2.6.1.1; 2681.
DR BRENDA; 2.6.1.64; 2681.
DR PathwayCommons; P17174; -.
DR Reactome; R-HSA-1237112; Methionine salvage pathway.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
DR SABIO-RK; P17174; -.
DR SignaLink; P17174; -.
DR SIGNOR; P17174; -.
DR BioGRID-ORCS; 2805; 23 hits in 1078 CRISPR screens.
DR ChiTaRS; GOT1; human.
DR EvolutionaryTrace; P17174; -.
DR GeneWiki; GOT1; -.
DR GenomeRNAi; 2805; -.
DR Pharos; P17174; Tbio.
DR PRO; PR:P17174; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P17174; protein.
DR Bgee; ENSG00000120053; Expressed in heart right ventricle and 203 other tissues.
DR ExpressionAtlas; P17174; baseline and differential.
DR Genevisible; P17174; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0047801; F:L-cysteine transaminase activity; ISS:UniProtKB.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
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:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEP: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; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2241899,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..413
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /id="PRO_0000123879"
FT BINDING 39
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 141
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 195
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 387
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13221"
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..39
FT /note="MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVG -> MQVWSPWKG
FT AMCPRPHKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055799"
FT VARIANT 389
FT /note="Missing (results in markedly diminished enzymatic
FT activity; dbSNP:rs749913156)"
FT /evidence="ECO:0000269|PubMed:21900944"
FT /id="VAR_067256"
FT CONFLICT 215
FT /note="H -> R (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6DNA"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 227..231
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6LIG"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 314..344
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6DNB"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:3WZF"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6DNB"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6DNB"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:6DNB"
SQ SEQUENCE 413 AA; 46248 MW; 69FE68BF0C045219 CRC64;
MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK
IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL
ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN
APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA
IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP
AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM
FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ
