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P17174

- AATC_HUMAN

UniProt

P17174 - AATC_HUMAN

Protein

Aspartate aminotransferase, cytoplasmic

Gene

GOT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. biosynthetic process Source: InterPro
    6. carbohydrate metabolic process Source: Reactome
    7. cellular amino acid biosynthetic process Source: Reactome
    8. cellular amino acid metabolic process Source: InterPro
    9. cellular nitrogen compound metabolic process Source: Reactome
    10. cellular response to insulin stimulus Source: UniProtKB
    11. fatty acid homeostasis Source: Ensembl
    12. gluconeogenesis Source: Reactome
    13. glucose metabolic process Source: Reactome
    14. glutamate catabolic process to 2-oxoglutarate Source: Ensembl
    15. glutamate catabolic process to aspartate Source: Ensembl
    16. glutamate metabolic process Source: UniProtKB
    17. glycerol biosynthetic process Source: UniProtKB
    18. L-methionine biosynthetic process from methylthioadenosine Source: Reactome
    19. oxaloacetate metabolic process Source: Ensembl
    20. polyamine metabolic process Source: Reactome
    21. response to glucocorticoid Source: UniProtKB
    22. small molecule metabolic process Source: Reactome
    23. sulfur amino acid metabolic process Source: Reactome

    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

    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)lysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151H → R AA sequence (PubMed:2241899)Curated

    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. 1 PublicationVSP_055799Add
    BLAST

    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. [P17174-1]
    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.

    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 . [P17174-1 ]
    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

    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: October 1, 2014
    This is version 151 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 (PubMed:16039064). Fetal serum levels of the enzyme in the umbilical artery and vein are found to be significantly higher than maternal serum levels (PubMed:22633534).2 Publications

    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