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P00505

- AATM_HUMAN

UniProt

P00505 - AATM_HUMAN

Protein

Aspartate aminotransferase, mitochondrial

Gene

GOT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.1 Publication

    Catalytic activityi

    L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
    L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651Substrate; via amide nitrogenBy similarity
    Binding sitei162 – 1621SubstrateBy similarity
    Binding sitei215 – 2151SubstrateBy similarity
    Binding sitei407 – 4071SubstrateBy similarity

    GO - Molecular functioni

    1. kynurenine-oxoglutarate transaminase activity Source: UniProtKB-EC
    2. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
    3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    4. poly(A) RNA binding Source: UniProtKB
    5. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. 4-hydroxyproline catabolic process Source: BHF-UCL
    3. aspartate biosynthetic process Source: Ensembl
    4. aspartate catabolic process Source: UniProtKB
    5. aspartate metabolic process Source: UniProtKB
    6. carbohydrate metabolic process Source: Reactome
    7. cellular amino acid biosynthetic process Source: Reactome
    8. cellular nitrogen compound metabolic process Source: Reactome
    9. fatty acid transport Source: UniProtKB
    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. oxaloacetate metabolic process Source: Ensembl
    16. response to ethanol Source: UniProtKB
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04858-MONOMER.
    ReactomeiREACT_1520. Gluconeogenesis.
    REACT_238. Amino acid synthesis and interconversion (transamination).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate aminotransferase, mitochondrial (EC:2.6.1.1, EC:2.6.1.7)
    Short name:
    mAspAT
    Alternative name(s):
    Fatty acid-binding protein
    Short name:
    FABP-1
    Glutamate oxaloacetate transaminase 2
    Kynurenine aminotransferase 4
    Kynurenine aminotransferase IV
    Kynurenine--oxoglutarate transaminase 4
    Kynurenine--oxoglutarate transaminase IV
    Plasma membrane-associated fatty acid-binding protein
    Short name:
    FABPpm
    Transaminase A
    Gene namesi
    Name:GOT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4433. GOT2.

    Subcellular locationi

    Mitochondrion matrix 1 Publication. Cell membrane 1 Publication
    Note: Exposure to alcohol promotes translocation to the cell membrane.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28818.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929Mitochondrion1 PublicationAdd
    BLAST
    Chaini30 – 430401Aspartate aminotransferase, mitochondrialPRO_0000001215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591N6-acetyllysineBy similarity
    Modified residuei73 – 731N6-acetyllysine; alternate1 Publication
    Modified residuei73 – 731N6-succinyllysine; alternateBy similarity
    Modified residuei82 – 821N6-acetyllysineBy similarity
    Modified residuei90 – 901N6-acetyllysine; alternate1 Publication
    Modified residuei90 – 901N6-succinyllysine; alternateBy similarity
    Modified residuei96 – 961Nitrated tyrosineBy similarity
    Modified residuei107 – 1071N6-acetyllysine; alternateBy similarity
    Modified residuei107 – 1071N6-succinyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
    Modified residuei159 – 1591N6-acetyllysine; alternate1 Publication
    Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity
    Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei227 – 2271N6-succinyllysineBy similarity
    Modified residuei234 – 2341N6-acetyllysine1 Publication
    Modified residuei279 – 2791N6-(pyridoxal phosphate)lysine; alternateBy similarity
    Modified residuei279 – 2791N6-acetyllysine; alternateBy similarity
    Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
    Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
    Modified residuei302 – 3021N6-acetyllysineBy similarity
    Modified residuei309 – 3091N6-acetyllysine; alternateBy similarity
    Modified residuei309 – 3091N6-succinyllysine; alternateBy similarity
    Modified residuei338 – 3381N6-acetyllysine; alternateBy similarity
    Modified residuei338 – 3381N6-succinyllysine; alternateBy similarity
    Modified residuei345 – 3451N6-acetyllysineBy similarity
    Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
    Modified residuei364 – 3641N6-acetyllysineBy similarity
    Modified residuei387 – 3871N6-acetyllysineBy similarity
    Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
    Modified residuei396 – 3961N6-succinyllysine; alternateBy similarity
    Modified residuei404 – 4041N6-acetyllysine; alternate1 Publication
    Modified residuei404 – 4041N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Nitration

    Proteomic databases

    MaxQBiP00505.
    PaxDbiP00505.
    PRIDEiP00505.

    2D gel databases

    UCD-2DPAGEP00505.

    PTM databases

    PhosphoSiteiP00505.

    Expressioni

    Inductioni

    Up-regulated by long-time exposure to alcohol.1 Publication

    Gene expression databases

    ArrayExpressiP00505.
    BgeeiP00505.
    CleanExiHS_GOT2.
    GenevestigatoriP00505.

    Organism-specific databases

    HPAiHPA018139.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi109068. 15 interactions.
    IntActiP00505. 7 interactions.
    MINTiMINT-1406848.
    STRINGi9606.ENSP00000245206.

    Structurei

    3D structure databases

    ProteinModelPortaliP00505.
    SMRiP00505. Positions 30-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1448.
    HOGENOMiHOG000185898.
    HOVERGENiHBG000951.
    InParanoidiP00505.
    KOiK14455.
    OMAiRVGAFTM.
    OrthoDBiEOG74J980.
    PhylomeDBiP00505.
    TreeFamiTF300641.

    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: P00505-1) [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

    MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA    50
    FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG 100
    GLAEFCKASA ELALGENSEV LKSGRFVTVQ TISGTGALRI GASFLQRFFK 150
    FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FTGAVEDISK 200
    IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA FFDMAYQGFA 250
    SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE 300
    AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR 350
    IIGMRTQLVS NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI 400
    YMTKDGRISV AGVTSSNVGY LAHAIHQVTK 430
    Length:430
    Mass (Da):47,518
    Last modified:October 5, 2010 - v3
    Checksum:iF559567ABF2DB346
    GO
    Isoform 2 (identifier: P00505-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         83-125: Missing.

    Show »
    Length:387
    Mass (Da):43,030
    Checksum:iFF09030A2B5C4E62
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1112AE → EA AA sequence (PubMed:4052435)Curated
    Sequence conflicti255 – 2551D → N AA sequence (PubMed:4052435)Curated
    Sequence conflicti258 – 2581A → T in BAD96991. 1 PublicationCurated
    Sequence conflicti305 – 3051E → Q AA sequence (PubMed:4052435)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → S.
    Corresponds to variant rs11558171 [ dbSNP | Ensembl ].
    VAR_055494
    Natural varianti188 – 1881G → S.
    Corresponds to variant rs11076256 [ dbSNP | Ensembl ].
    VAR_031710
    Natural varianti346 – 3461V → G.3 Publications
    Corresponds to variant rs30842 [ dbSNP | Ensembl ].
    VAR_031711
    Natural varianti428 – 4281V → A.1 Publication
    Corresponds to variant rs17849335 [ dbSNP | Ensembl ].
    VAR_031712

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei83 – 12543Missing in isoform 2. 1 PublicationVSP_054848Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22632 mRNA. Translation: AAA35568.1.
    AK295993 mRNA. Translation: BAG58768.1.
    AK223271 mRNA. Translation: BAD96991.1.
    AC012183 Genomic DNA. No translation available.
    BC000525 mRNA. Translation: AAH00525.1.
    CCDSiCCDS10801.1. [P00505-1]
    CCDS67045.1. [P00505-2]
    PIRiA31873. XNHUDM.
    RefSeqiNP_001273149.1. NM_001286220.1. [P00505-2]
    NP_002071.2. NM_002080.3. [P00505-1]
    UniGeneiHs.599470.

    Genome annotation databases

    EnsembliENST00000245206; ENSP00000245206; ENSG00000125166. [P00505-1]
    ENST00000434819; ENSP00000394100; ENSG00000125166. [P00505-2]
    GeneIDi2806.
    KEGGihsa:2806.
    UCSCiuc002eof.1. human. [P00505-1]

    Polymorphism databases

    DMDMi308153643.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22632 mRNA. Translation: AAA35568.1 .
    AK295993 mRNA. Translation: BAG58768.1 .
    AK223271 mRNA. Translation: BAD96991.1 .
    AC012183 Genomic DNA. No translation available.
    BC000525 mRNA. Translation: AAH00525.1 .
    CCDSi CCDS10801.1. [P00505-1 ]
    CCDS67045.1. [P00505-2 ]
    PIRi A31873. XNHUDM.
    RefSeqi NP_001273149.1. NM_001286220.1. [P00505-2 ]
    NP_002071.2. NM_002080.3. [P00505-1 ]
    UniGenei Hs.599470.

    3D structure databases

    ProteinModelPortali P00505.
    SMRi P00505. Positions 30-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109068. 15 interactions.
    IntActi P00505. 7 interactions.
    MINTi MINT-1406848.
    STRINGi 9606.ENSP00000245206.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei P00505.

    Polymorphism databases

    DMDMi 308153643.

    2D gel databases

    UCD-2DPAGE P00505.

    Proteomic databases

    MaxQBi P00505.
    PaxDbi P00505.
    PRIDEi P00505.

    Protocols and materials databases

    DNASUi 2806.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245206 ; ENSP00000245206 ; ENSG00000125166 . [P00505-1 ]
    ENST00000434819 ; ENSP00000394100 ; ENSG00000125166 . [P00505-2 ]
    GeneIDi 2806.
    KEGGi hsa:2806.
    UCSCi uc002eof.1. human. [P00505-1 ]

    Organism-specific databases

    CTDi 2806.
    GeneCardsi GC16M058741.
    H-InvDB HIX0013095.
    HGNCi HGNC:4433. GOT2.
    HPAi HPA018139.
    MIMi 138150. gene.
    neXtProti NX_P00505.
    PharmGKBi PA28818.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1448.
    HOGENOMi HOG000185898.
    HOVERGENi HBG000951.
    InParanoidi P00505.
    KOi K14455.
    OMAi RVGAFTM.
    OrthoDBi EOG74J980.
    PhylomeDBi P00505.
    TreeFami TF300641.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04858-MONOMER.
    Reactomei REACT_1520. Gluconeogenesis.
    REACT_238. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    ChiTaRSi Got2. human.
    GeneWikii GOT2.
    GenomeRNAii 2806.
    NextBioi 11061.
    PROi P00505.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00505.
    Bgeei P00505.
    CleanExi HS_GOT2.
    Genevestigatori P00505.

    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. "Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA."
      Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B., Berthelot P., Hanoune J., Barouki R.
      Biochem. Biophys. Res. Commun. 157:1309-1315(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-346.
    2. "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] (ISOFORM 2), VARIANT GLY-346.
      Tissue: Subthalamic nucleus.
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Gastric mucosa.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT ALA-428.
      Tissue: Muscle.
    6. "The primary structure of mitochondrial aspartate aminotransferase from human heart."
      Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S., Bossa F.
      Biochim. Biophys. Acta 832:46-51(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-430, VARIANT GLY-346.
    7. "Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells."
      Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.
      Hepatology 27:1064-1074(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159; LYS-234; LYS-296; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAATM_HUMAN
    AccessioniPrimary (citable) accession number: P00505
    Secondary accession number(s): B4DJA6
    , E7ERW2, Q53FL3, Q9BWA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 160 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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3