P17174 (AATC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, cytoplasmic
EC=2.6.1.1

Alternative name(s):
Glutamate oxaloacetate transaminase 1
Transaminase A

Gene names

Name:

GOT1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB L-methionine salvage from methylthioadenosine Traceable author statement. Source: Reactome aspartate catabolic process Inferred from direct assay Ref.8. Source: UniProtKB cellular response to insulin stimulus Inferred from expression pattern. Source: UniProtKB gluconeogenesis Traceable author statement. Source: Reactome glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB polyamine metabolic process Traceable author statement. Source: Reactome response to glucocorticoid stimulus Inferred from expression pattern. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.8. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 413

412

Aspartate aminotransferase, cytoplasmic

PRO_0000123879

Sites

Binding site

39

1

Aspartate; via amide nitrogen

Binding site

141

1

Aspartate

Binding site

195

1

Aspartate

Binding site

387

1

Aspartate

Amino acid modifications

Modified residue

66

1

Phosphoserine By similarity

Modified residue

71

1

Phosphotyrosine Ref.9

Modified residue

259

1

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

215

1

H → R AA sequence Ref.8

Secondary structure

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413

Helix Strand Turn

Details...

Helix

17 – 27

11

Helix

52 – 62

11

Helix

78 – 88

11

Helix

94 – 97

4

Helix

118 – 123

6

Beta strand

134 – 139

6

Helix

143 – 150

8

Beta strand

156 – 160

5

Turn

164 – 166

3

Helix

175 – 180

6

Beta strand

186 – 190

5

Helix

203 – 216

14

Beta strand

219 – 225

7

Helix

234 – 237

4

Helix

239 – 246

8

Beta strand

251 – 255

5

Turn

258 – 260

3

Helix

264 – 266

3

Beta strand

271 – 274

4

Helix

278 – 293

16

Turn

294 – 296

3

Helix

305 – 311

7

Helix

314 – 320

7

Helix

324 – 344

21

Helix

352 – 356

5

Helix

368 – 378

11

Turn

395 – 397

3

Helix

398 – 411

14

Sequences

	Sequence		Length	Mass (Da)
	P17174 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 69FE68BF0C045219	FASTA	413	46,248
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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 , 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.

IPI

IPI00219029.

PIR

S13035.
S29027.

RefSeq

NP_002070.1. NM_002079.2.

UniGene

Hs.500756.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3II0	X-ray	2.05	A/B/C/D	14-412	[»]

ProteinModelPortal

P17174.

SMR

P17174. Positions 14-412.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17174. 3 interactions.

MINT

MINT-5002473.

STRING

P17174.

PTM databases

PhosphoSite

P17174.

Polymorphism databases

DMDM

5902703.

2D gel databases

REPRODUCTION-2DPAGE

IPI00219029.

UCD-2DPAGE

P17174.

Proteomic databases

PeptideAtlas

P17174.

PRIDE

P17174.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370508; ENSP00000359539; ENSG00000120053.

GeneID

2805.

KEGG

hsa:2805.

UCSC

uc001kpr.1. human.

Organism-specific databases

CTD

2805.

GeneCards

GC10M101146.

H-InvDB

HIX0009109.

HGNC

HGNC:4432. GOT1.

MIM

138180. gene.

neXtProt

NX_P17174.

PharmGKB

PA28817.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05649.

HOGENOM

HBG446828.

HOVERGEN

HBG000951.

InParanoid

P17174.

OMA

RTCASRL.

OrthoDB

EOG47D9G5.

PhylomeDB

P17174.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13032.

Reactome

REACT_111217. Metabolism.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P17174.

Bgee

P17174.

CleanEx

HS_GOT1.

Genevestigator

P17174.

GermOnline

ENSG00000120053. Homo sapiens.

Family and domain databases

InterPro

IPR004839. 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]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

KO

K14454.

PANTHER

PTHR11879. Asp_trans. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00128. L-Aspartic Acid.
DB00151. L-Cysteine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

NextBio

11057.

SOURCE

Search...

Entry information

Entry name

AATC_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.