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P17174 (AATC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

EC=2.6.1.1
Alternative name(s):
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene names
Name:GOT1
OrganismHomo sapiens (Human)
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

Plays a key role in amino acid metabolism By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. Ref.11

Subcellular location

Cytoplasm Ref.1.

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Sequence similarities

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

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 residue661Phosphoserine By similarity
Modified residue711Phosphotyrosine Ref.9
Modified residue2591N6-(pyridoxal phosphate)lysine By similarity

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: 1974457] [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: 14702039] [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: 15164054] [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: 15489334] [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: 2241899] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-413.
Tissue: Liver.
[9]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-71, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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.
IPIIPI00219029.
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...

Protein-protein interaction databases

IntActP17174. 3 interactions.
MINTMINT-5002473.
STRINGP17174.

PTM databases

PhosphoSiteP17174.

Polymorphism databases

DMDM5902703.

2D gel databases

REPRODUCTION-2DPAGEIPI00219029.
UCD-2DPAGEP17174.

Proteomic databases

PeptideAtlasP17174.
PRIDEP17174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370508; ENSP00000359539; ENSG00000120053.
GeneID2805.
KEGGhsa:2805.
UCSCuc001kpr.1. human.

Organism-specific databases

CTD2805.
GeneCardsGC10M101146.
H-InvDBHIX0009109.
HGNCHGNC:4432. GOT1.
MIM138180. gene.
neXtProtNX_P17174.
PharmGKBPA28817.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05649.
HOGENOMHBG446828.
HOVERGENHBG000951.
InParanoidP17174.
OMARTCASRL.
OrthoDBEOG47D9G5.
PhylomeDBP17174.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13032.
ReactomeREACT_111217. Metabolism.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpressP17174.
BgeeP17174.
CleanExHS_GOT1.
GenevestigatorP17174.
GermOnlineENSG00000120053. Homo sapiens.

Family and domain databases

InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK14454.
PANTHERPTHR11879. Asp_trans. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00128. L-Aspartic Acid.
DB00151. L-Cysteine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.
NextBio11057.
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: January 25, 2012
This is version 126 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

Human chromosome 10

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families