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P17174 (AATC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate aminotransferase, cytoplasmic

Short name=cAspAT
EC=2.6.1.1
EC=2.6.1.3
Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name=cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene names
Name:GOT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. Ref.9

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. Ref.13

Subcellular location

Cytoplasm Ref.1.

Polymorphism

Genetic variations in GOT1 are associated with low serum aspartate aminotransferase and define the aspartate aminotransferase serum level quantitative trait locus 1 (ASTQTL1) [MIM:614419].

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Aspartate aminotransferase activity found to be increased in cerebral spinal fluid (CSF) of patients with Alzheimer disease (Ref.9). Fetal serum levels of the enzyme in the umbilical artery and vein are found to be significantly higher than maternal serum levels (Ref.12).

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

L-methionine salvage from methylthioadenosine

Traceable author statement. Source: Reactome

aspartate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

aspartate catabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from expression pattern PubMed 8396422. Source: UniProtKB

fatty acid homeostasis

Inferred from electronic annotation. Source: Ensembl

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glutamate catabolic process to 2-oxoglutarate

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process to aspartate

Inferred from electronic annotation. Source: Ensembl

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycerol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

oxaloacetate metabolic process

Inferred from electronic annotation. Source: Ensembl

polyamine metabolic process

Traceable author statement. Source: Reactome

response to glucocorticoid

Inferred from expression pattern PubMed 8396422. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon terminus

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 7060339. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

lysosome

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from direct assay PubMed 2182221Ref.8PubMed 2731362PubMed 6391741. Source: UniProtKB

L-cysteine:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

L-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carboxylic acid binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylserine decarboxylase activity

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 413412Aspartate aminotransferase, cytoplasmic
PRO_0000123879

Sites

Binding site391Aspartate; via amide nitrogen
Binding site1411Aspartate
Binding site1951Aspartate
Binding site3871Aspartate

Amino acid modifications

Modified residue2591N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant3891Missing Results in markedly diminished enzymatic activity. Ref.11
VAR_067256

Experimental info

Sequence conflict2151H → R AA sequence Ref.8

Secondary structure

................................................................ 413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17174 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 69FE68BF0C045219

FASTA41346,248
        10         20         30         40         50         60 
MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK 

        70         80         90        100        110        120 
IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL 

       130        140        150        160        170        180 
ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN 

       190        200        210        220        230        240 
APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA 

       250        260        270        280        290        300 
IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP 

       310        320        330        340        350        360 
AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM 

       370        380        390        400        410 
FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ 

« Hide

References

« Hide 'large scale' references
[1]"Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection."
Bousquet-Lemercier B., Pol S., Pave-Preux M., Hanoune J., Barouki R.
Biochemistry 29:5293-5299(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Liver.
[2]"Genomic structure and mutation analysis of GOT1 in the urofacial (Ochoa) syndrome gene critical region on chromosome 10."
Wang C.Y., Huang Y.Q., Shi J.D., Marron M.P., Ruan Q.G., Hawkins-Lee B., Ochoa B., She J.X.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Yu W., Sarginson J., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]"The amino acid sequence of cytosolic aspartate aminotransferase from human liver."
Doyle J.M., Schinina M.E., Bossa F., Doonan S.
Biochem. J. 270:651-657(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-413.
Tissue: Liver.
[9]"Amino acids and transaminases activity in ventricular CSF and in brain of normal and Alzheimer patients."
D'Aniello A., Fisher G., Migliaccio N., Cammisa G., D'Aniello E., Spinelli P.
Neurosci. Lett. 388:49-53(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Genome-wide association study identifies genetic variants in GOT1 determining serum aspartate aminotransferase levels."
Shen H., Damcott C., Shuldiner S.R., Chai S., Yang R., Hu H., Gibson Q., Ryan K.A., Mitchell B.D., Gong D.W.
J. Hum. Genet. 56:801-805(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ASTQTL1, VARIANT ASN-389 DEL, CHARACTERIZATION OF VARIANT ASN-389 DEL.
[12]"Relationship between glutamate, GOT and GPT levels in maternal and fetal blood: a potential mechanism for fetal neuroprotection."
Zlotnik A., Tsesis S., Gruenbaum B.F., Ohayon S., Gruenbaum S.E., Boyko M., Sheiner E., Brotfain E., Shapira Y., Teichberg V.I.
Early Hum. Dev. 88:773-778(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FETAL BLOOD LEVELS.
[13]"Crystal structure of human glutamate oxaloacetate transaminase 1 (GOT1)."
Structural genomics consortium (SGC)
Submitted (AUG-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-412 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND TARTARIC ACID, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-259.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37400 mRNA. Translation: AAA35563.1.
AF080467 expand/collapse EMBL AC list , AF080459, AF080460, AF080461, AF080462, AF080463, AF080464, AF080465, AF080466 Genomic DNA. Translation: AAC32851.1.
AF052153 mRNA. Translation: AAC28622.1.
AK312684 mRNA. Translation: BAG35564.1.
AL391684 Genomic DNA. Translation: CAH73859.1.
CH471066 Genomic DNA. Translation: EAW49869.1.
BC000498 mRNA. Translation: AAH00498.1.
CCDSCCDS7479.1.
PIRS13035.
S29027.
RefSeqNP_002070.1. NM_002079.2.
UniGeneHs.500756.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3II0X-ray2.05A/B/C/D14-412[»]
ProteinModelPortalP17174.
SMRP17174. Positions 14-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109067. 12 interactions.
IntActP17174. 3 interactions.
MINTMINT-5002473.
STRING9606.ENSP00000359539.

Chemistry

ChEMBLCHEMBL2189139.
DrugBankDB00128. L-Aspartic Acid.
DB00151. L-Cysteine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP17174.

Polymorphism databases

DMDM5902703.

2D gel databases

REPRODUCTION-2DPAGEIPI00219029.
UCD-2DPAGEP17174.

Proteomic databases

MaxQBP17174.
PaxDbP17174.
PeptideAtlasP17174.
PRIDEP17174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370508; ENSP00000359539; ENSG00000120053.
GeneID2805.
KEGGhsa:2805.
UCSCuc001kpr.3. human.

Organism-specific databases

CTD2805.
GeneCardsGC10M101146.
HGNCHGNC:4432. GOT1.
MIM138180. gene.
614419. phenotype.
neXtProtNX_P17174.
PharmGKBPA28817.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1448.
HOGENOMHOG000185898.
HOVERGENHBG000951.
InParanoidP17174.
KOK14454.
OMASSRIRQM.
PhylomeDBP17174.
TreeFamTF314089.

Enzyme and pathway databases

BioCycMetaCyc:HS04361-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP17174.

Gene expression databases

ArrayExpressP17174.
BgeeP17174.
CleanExHS_GOT1.
GenevestigatorP17174.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGOT1. human.
EvolutionaryTraceP17174.
GeneWikiGOT1.
GenomeRNAi2805.
NextBio11057.
PROP17174.
SOURCESearch...

Entry information

Entry nameAATC_HUMAN
AccessionPrimary (citable) accession number: P17174
Secondary accession number(s): B2R6R7, Q5VW80
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM