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P17174

- AATC_HUMAN

UniProt

P17174 - AATC_HUMAN

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Protein

Aspartate aminotransferase, cytoplasmic

Gene
GOT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Aspartate; via amide nitrogen
Binding sitei141 – 1411Aspartate
Binding sitei195 – 1951Aspartate
Binding sitei387 – 3871Aspartate

GO - Molecular functioni

  1. carboxylic acid binding Source: Ensembl
  2. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
  3. L-cysteine:2-oxoglutarate aminotransferase activity Source: UniProtKB
  4. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  5. phosphatidylserine decarboxylase activity Source: Ensembl
  6. pyridoxal phosphate binding Source: InterPro
  7. transaminase activity Source: Reactome

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. aspartate biosynthetic process Source: Ensembl
  3. aspartate catabolic process Source: UniProtKB
  4. aspartate metabolic process Source: UniProtKB
  5. carbohydrate metabolic process Source: Reactome
  6. cellular amino acid biosynthetic process Source: Reactome
  7. cellular nitrogen compound metabolic process Source: Reactome
  8. cellular response to insulin stimulus Source: UniProtKB
  9. fatty acid homeostasis Source: Ensembl
  10. gluconeogenesis Source: Reactome
  11. glucose metabolic process Source: Reactome
  12. glutamate catabolic process to 2-oxoglutarate Source: Ensembl
  13. glutamate catabolic process to aspartate Source: Ensembl
  14. glutamate metabolic process Source: UniProtKB
  15. glycerol biosynthetic process Source: UniProtKB
  16. L-methionine salvage from methylthioadenosine Source: Reactome
  17. oxaloacetate metabolic process Source: Ensembl
  18. polyamine metabolic process Source: Reactome
  19. response to glucocorticoid Source: UniProtKB
  20. small molecule metabolic process Source: Reactome
  21. sulfur amino acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS04361-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
REACT_238. Amino acid synthesis and interconversion (transamination).
REACT_75881. Methionine salvage pathway.
SABIO-RKP17174.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1, EC:2.6.1.3)
Short name:
cAspAT
Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name:
cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene namesi
Name:GOT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:4432. GOT1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. lysosome Source: Ensembl
  6. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MIMi614419. phenotype.
PharmGKBiPA28817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 413412Aspartate aminotransferase, cytoplasmicPRO_0000123879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

MaxQBiP17174.
PaxDbiP17174.
PeptideAtlasiP17174.
PRIDEiP17174.

2D gel databases

REPRODUCTION-2DPAGEIPI00219029.
UCD-2DPAGEP17174.

PTM databases

PhosphoSiteiP17174.

Expressioni

Gene expression databases

ArrayExpressiP17174.
BgeeiP17174.
CleanExiHS_GOT1.
GenevestigatoriP17174.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109067. 12 interactions.
IntActiP17174. 3 interactions.
MINTiMINT-5002473.
STRINGi9606.ENSP00000359539.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2711
Helixi52 – 6211
Helixi78 – 8912
Helixi94 – 974
Beta strandi101 – 1077
Helixi108 – 12316
Beta strandi124 – 1285
Beta strandi134 – 1396
Helixi143 – 1508
Beta strandi156 – 1605
Turni164 – 1674
Helixi171 – 1799
Beta strandi186 – 1905
Turni195 – 1973
Helixi203 – 21614
Beta strandi219 – 2257
Turni227 – 2315
Helixi234 – 2374
Helixi239 – 2468
Beta strandi251 – 2566
Turni258 – 2614
Helixi264 – 2663
Beta strandi268 – 2747
Helixi278 – 29316
Turni294 – 2963
Helixi302 – 31110
Helixi314 – 34431
Helixi352 – 3565
Beta strandi359 – 3635
Helixi368 – 37811
Beta strandi387 – 3893
Helixi390 – 3923
Turni395 – 3973
Helixi398 – 41114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3II0X-ray2.05A/B/C/D14-412[»]
ProteinModelPortaliP17174.
SMRiP17174. Positions 14-412.

Miscellaneous databases

EvolutionaryTraceiP17174.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1448.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP17174.
KOiK14454.
OMAiSSRIRQM.
PhylomeDBiP17174.
TreeFamiTF314089.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P17174-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV    50
LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR 100
VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA 150
AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID 200
PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE 250
FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP 300
AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT 350
WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY 400
VATSIHEAVT KIQ 413
Length:413
Mass (Da):46,248
Last modified:January 23, 2007 - v3
Checksum:i69FE68BF0C045219
GO
Isoform 2 (identifier: P17174-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVG → MQVWSPWKGAMCPRPHKP

Note: No experimental confirmation available.

Show »
Length:392
Mass (Da):44,147
Checksum:i30D3C8E10522C058
GO

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti389 – 3891Missing Results in markedly diminished enzymatic activity. 1 Publication
VAR_067256

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939MAPPS…NLGVG → MQVWSPWKGAMCPRPHKP in isoform 2. VSP_055799Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151H → R AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37400 mRNA. Translation: AAA35563.1.
AF080467
, AF080459, AF080460, AF080461, AF080462, AF080463, AF080464, AF080465, AF080466 Genomic DNA. Translation: AAC32851.1.
AF052153 mRNA. Translation: AAC28622.1.
AK301916 mRNA. Translation: BAH13585.1.
AK312684 mRNA. Translation: BAG35564.1.
AL391684 Genomic DNA. Translation: CAH73859.1.
CH471066 Genomic DNA. Translation: EAW49869.1.
BC000498 mRNA. Translation: AAH00498.1.
CCDSiCCDS7479.1.
PIRiS13035.
S29027.
RefSeqiNP_002070.1. NM_002079.2.
UniGeneiHs.500756.

Genome annotation databases

EnsembliENST00000370508; ENSP00000359539; ENSG00000120053.
ENST00000543866; ENSP00000445578; ENSG00000120053.
GeneIDi2805.
KEGGihsa:2805.
UCSCiuc001kpr.3. human.

Polymorphism databases

DMDMi5902703.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37400 mRNA. Translation: AAA35563.1 .
AF080467
, AF080459 , AF080460 , AF080461 , AF080462 , AF080463 , AF080464 , AF080465 , AF080466 Genomic DNA. Translation: AAC32851.1 .
AF052153 mRNA. Translation: AAC28622.1 .
AK301916 mRNA. Translation: BAH13585.1 .
AK312684 mRNA. Translation: BAG35564.1 .
AL391684 Genomic DNA. Translation: CAH73859.1 .
CH471066 Genomic DNA. Translation: EAW49869.1 .
BC000498 mRNA. Translation: AAH00498.1 .
CCDSi CCDS7479.1.
PIRi S13035.
S29027.
RefSeqi NP_002070.1. NM_002079.2.
UniGenei Hs.500756.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3II0 X-ray 2.05 A/B/C/D 14-412 [» ]
ProteinModelPortali P17174.
SMRi P17174. Positions 14-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109067. 12 interactions.
IntActi P17174. 3 interactions.
MINTi MINT-5002473.
STRINGi 9606.ENSP00000359539.

Chemistry

ChEMBLi CHEMBL2189139.
DrugBanki DB00128. L-Aspartic Acid.
DB00151. L-Cysteine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei P17174.

Polymorphism databases

DMDMi 5902703.

2D gel databases

REPRODUCTION-2DPAGE IPI00219029.
UCD-2DPAGE P17174.

Proteomic databases

MaxQBi P17174.
PaxDbi P17174.
PeptideAtlasi P17174.
PRIDEi P17174.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370508 ; ENSP00000359539 ; ENSG00000120053 .
ENST00000543866 ; ENSP00000445578 ; ENSG00000120053 .
GeneIDi 2805.
KEGGi hsa:2805.
UCSCi uc001kpr.3. human.

Organism-specific databases

CTDi 2805.
GeneCardsi GC10M101146.
HGNCi HGNC:4432. GOT1.
MIMi 138180. gene.
614419. phenotype.
neXtProti NX_P17174.
PharmGKBi PA28817.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1448.
HOGENOMi HOG000185898.
HOVERGENi HBG000951.
InParanoidi P17174.
KOi K14454.
OMAi SSRIRQM.
PhylomeDBi P17174.
TreeFami TF314089.

Enzyme and pathway databases

BioCyci MetaCyc:HS04361-MONOMER.
Reactomei REACT_1520. Gluconeogenesis.
REACT_238. Amino acid synthesis and interconversion (transamination).
REACT_75881. Methionine salvage pathway.
SABIO-RK P17174.

Miscellaneous databases

ChiTaRSi GOT1. human.
EvolutionaryTracei P17174.
GeneWikii GOT1.
GenomeRNAii 2805.
NextBioi 11057.
PROi P17174.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17174.
Bgeei P17174.
CleanExi HS_GOT1.
Genevestigatori P17174.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] (ISOFORM 1).
    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. 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.

Entry informationi

Entry nameiAATC_HUMAN
AccessioniPrimary (citable) accession number: P17174
Secondary accession number(s): B2R6R7, B7Z7E9, Q5VW80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 (1 Publication). Fetal serum levels of the enzyme in the umbilical artery and vein are found to be significantly higher than maternal serum levels (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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