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   09-APR-2025, entry version 226.
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=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate;
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=L-cysteine + 2-oxoglutarate = 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=3-sulfino-L-alanine + 2-oxoglutarate = 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_002079.3. [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; 272.
DR   IntAct; P17174; 191.
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   GlyGen; P17174; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P17174; -.
DR   PhosphoSitePlus; P17174; -.
DR   SwissPalm; P17174; -.
DR   BioMuta; GOT1; -.
DR   DMDM; 5902703; -.
DR   REPRODUCTION-2DPAGE; IPI00219029; -.
DR   jPOST; P17174; -.
DR   MassIVE; P17174; -.
DR   PaxDb; 9606-ENSP00000359539; -.
DR   PeptideAtlas; P17174; -.
DR   PRIDE; P17174; -.
DR   ProteomicsDB; 53459; -. [P17174-1]
DR   ProteomicsDB; 6862; -.
DR   Pumba; P17174; -.
DR   Antibodypedia; 31077; 654 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   AGR; HGNC:4432; -.
DR   CTD; 2805; -.
DR   DisGeNET; 2805; -.
DR   GeneCards; GOT1; -.
DR   HGNC; HGNC:4432; GOT1.
DR   HPA; ENSG00000120053; Tissue enhanced (heart muscle, 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; GTWTHIT; -.
DR   OrthoDB; 6752799at2759; -.
DR   PhylomeDB; P17174; -.
DR   TreeFam; TF314089; -.
DR   BioCyc; MetaCyc:HS04361-MONOMER; -.
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-8963693; Aspartate and asparagine metabolism.
DR   Reactome; R-HSA-9856872; Malate-aspartate shuttle.
DR   SABIO-RK; P17174; -.
DR   SignaLink; P17174; -.
DR   SIGNOR; P17174; -.
DR   BioGRID-ORCS; 2805; 25 hits in 1159 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 205 other cell types or tissues.
DR   ExpressionAtlas; P17174; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0006094; P:gluconeogenesis; 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:0043490; P:malate-aspartate shuttle; IMP:FlyBase.
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   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000044; Aspartate aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000001; Aspartate aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
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; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF3; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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   Proteomics identification; Pyridoxal phosphate; Reference proteome;
KW   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
//