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P05201

- AATC_MOUSE

UniProt

P05201 - AATC_MOUSE

Protein

Aspartate aminotransferase, cytoplasmic

Gene

Got1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    Enzyme regulationi

    Inhibited by calcium ions.1 Publication

    Sites

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

    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: MGI
    6. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. aspartate biosynthetic process Source: MGI
    3. aspartate catabolic process Source: Ensembl
    4. aspartate metabolic process Source: UniProtKB
    5. cellular response to insulin stimulus Source: Ensembl
    6. fatty acid homeostasis Source: MGI
    7. glutamate catabolic process to 2-oxoglutarate Source: MGI
    8. glutamate catabolic process to aspartate Source: MGI
    9. glutamate metabolic process Source: UniProtKB
    10. glycerol biosynthetic process Source: MGI
    11. oxaloacetate metabolic process Source: MGI
    12. response to glucocorticoid Source: Ensembl

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_199099. Methionine salvage pathway.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:95791. Got1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. cytosol Source: MGI
    3. lysosome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 413412Aspartate aminotransferase, cytoplasmicPRO_0000123880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine
    Modified residuei318 – 3181N6-succinyllysine1 Publication

    Proteomic databases

    MaxQBiP05201.
    PaxDbiP05201.
    PRIDEiP05201.

    2D gel databases

    SWISS-2DPAGEP05201.

    PTM databases

    PhosphoSiteiP05201.

    Expressioni

    Tissue specificityi

    Expressed in neurons of the retina. Localizes to the inner and outer plexiform layers, the inner and outer nuclear layer and the outer segments of photoreceptors.1 Publication

    Gene expression databases

    BgeeiP05201.
    CleanExiMM_GOT1.
    GenevestigatoriP05201.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP05201. 21 interactions.
    MINTiMINT-1869597.
    STRINGi10090.ENSMUSP00000026196.

    Structurei

    3D structure databases

    ProteinModelPortaliP05201.
    SMRiP05201. Positions 15-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1448.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    HOVERGENiHBG000951.
    InParanoidiQ3UJH8.
    KOiK14454.
    OMAiCMAGLNH.
    OrthoDBiEOG74J980.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P05201-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV    50
    LPVVRKVEQK IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR 100
    VGGVQSLGGT GALRIGADFL GRWYNGTDNK NTPIYVSSPT WENHNAVFSA 150
    AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN APEFSIFVLH ACAHNPTGTD 200
    PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA IRYFVSEGFE 250
    LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP 300
    AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT 350
    WSHITEQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY 400
    VATSIHEAVT KIQ 413
    Length:413
    Mass (Da):46,248
    Last modified:June 28, 2011 - v3
    Checksum:i0E37C763155EA6B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941L → P in AAA37263. (PubMed:3782150)Curated
    Sequence conflicti94 – 941L → P in CAA30275. (PubMed:3379636)Curated
    Sequence conflicti94 – 941L → P in AAH02057. (PubMed:15489334)Curated
    Sequence conflicti291 – 2911I → N in CAA30275. (PubMed:3379636)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02623 mRNA. Translation: AAA37263.1.
    X07302
    , X07303, X07304, X07305, X07306, X07307, X07308, X07309 Genomic DNA. Translation: CAA30275.1.
    AK146445 mRNA. Translation: BAE27177.1.
    BC002057 mRNA. Translation: AAH02057.1.
    CCDSiCCDS29832.1.
    PIRiS01076.
    RefSeqiNP_034454.2. NM_010324.2.
    UniGeneiMm.19039.

    Genome annotation databases

    EnsembliENSMUST00000026196; ENSMUSP00000026196; ENSMUSG00000025190.
    GeneIDi14718.
    KEGGimmu:14718.
    UCSCiuc012bmb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02623 mRNA. Translation: AAA37263.1 .
    X07302
    , X07303 , X07304 , X07305 , X07306 , X07307 , X07308 , X07309 Genomic DNA. Translation: CAA30275.1 .
    AK146445 mRNA. Translation: BAE27177.1 .
    BC002057 mRNA. Translation: AAH02057.1 .
    CCDSi CCDS29832.1.
    PIRi S01076.
    RefSeqi NP_034454.2. NM_010324.2.
    UniGenei Mm.19039.

    3D structure databases

    ProteinModelPortali P05201.
    SMRi P05201. Positions 15-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P05201. 21 interactions.
    MINTi MINT-1869597.
    STRINGi 10090.ENSMUSP00000026196.

    PTM databases

    PhosphoSitei P05201.

    2D gel databases

    SWISS-2DPAGE P05201.

    Proteomic databases

    MaxQBi P05201.
    PaxDbi P05201.
    PRIDEi P05201.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026196 ; ENSMUSP00000026196 ; ENSMUSG00000025190 .
    GeneIDi 14718.
    KEGGi mmu:14718.
    UCSCi uc012bmb.1. mouse.

    Organism-specific databases

    CTDi 2805.
    MGIi MGI:95791. Got1.

    Phylogenomic databases

    eggNOGi COG1448.
    GeneTreei ENSGT00390000014081.
    HOGENOMi HOG000185898.
    HOVERGENi HBG000951.
    InParanoidi Q3UJH8.
    KOi K14454.
    OMAi CMAGLNH.
    OrthoDBi EOG74J980.
    TreeFami TF314089.

    Enzyme and pathway databases

    Reactomei REACT_199099. Methionine salvage pathway.

    Miscellaneous databases

    NextBioi 286727.
    PROi P05201.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05201.
    CleanExi MM_GOT1.
    Genevestigatori P05201.

    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. "Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes."
      Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.
      J. Biol. Chem. 261:16976-16983(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural organization of the mouse aspartate aminotransferase isoenzyme genes. Introns antedate the divergence of cytosolic and mitochondrial isoenzyme genes."
      Obaru K., Tsuzuki T., Setoyama C., Shimada K.
      J. Mol. Biol. 200:13-22(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart.
    4. "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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-55; 61-81; 87-97; 101-166; 208-236; 260-276; 306-318 AND 347-411, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx."
      Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H.
      J. Biol. Chem. 286:39379-39386(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, ENZYME REGULATION.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiAATC_MOUSE
    AccessioniPrimary (citable) accession number: P05201
    Secondary accession number(s): Q3UJH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3