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P05202

- AATM_MOUSE

UniProt

P05202 - AATM_MOUSE

Protein

Aspartate aminotransferase, mitochondrial

Gene

Got2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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.2 Publications

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.1 Publication

    Sites

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

    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. 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. fatty acid transport Source: Ensembl
    6. glutamate catabolic process to 2-oxoglutarate Source: MGI
    7. glutamate catabolic process to aspartate Source: MGI
    8. glutamate metabolic process Source: UniProtKB
    9. oxaloacetate metabolic process Source: MGI
    10. response to ethanol Source: Ensembl

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Pyridoxal phosphate

    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
    Synonyms:Got-2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:95792. Got2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: UniProtKB
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionAdd
    BLAST
    Chaini30 – 430401Aspartate aminotransferase, mitochondrialPRO_0000001216Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591N6-acetyllysine1 Publication
    Modified residuei73 – 731N6-acetyllysine; alternate2 Publications
    Modified residuei73 – 731N6-succinyllysine; alternate1 Publication
    Modified residuei82 – 821N6-acetyllysine1 Publication
    Modified residuei90 – 901N6-acetyllysine; alternate1 Publication
    Modified residuei90 – 901N6-succinyllysine; alternate1 Publication
    Modified residuei96 – 961Nitrated tyrosine1 Publication
    Modified residuei107 – 1071N6-acetyllysine; alternate1 Publication
    Modified residuei107 – 1071N6-succinyllysine; alternate1 Publication
    Modified residuei122 – 1221N6-acetyllysine; alternate1 Publication
    Modified residuei122 – 1221N6-succinyllysine; alternate1 Publication
    Modified residuei159 – 1591N6-acetyllysine; alternate2 Publications
    Modified residuei159 – 1591N6-succinyllysine; alternate1 Publication
    Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
    Modified residuei185 – 1851N6-succinyllysine; alternate1 Publication
    Modified residuei227 – 2271N6-succinyllysine1 Publication
    Modified residuei234 – 2341N6-acetyllysine1 Publication
    Modified residuei279 – 2791N6-(pyridoxal phosphate)lysine; alternateBy similarity
    Modified residuei279 – 2791N6-acetyllysine; alternate1 Publication
    Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
    Modified residuei296 – 2961N6-succinyllysine; alternate1 Publication
    Modified residuei302 – 3021N6-acetyllysine1 Publication
    Modified residuei309 – 3091N6-acetyllysine; alternate1 Publication
    Modified residuei309 – 3091N6-succinyllysine; alternate1 Publication
    Modified residuei338 – 3381N6-acetyllysine; alternate1 Publication
    Modified residuei338 – 3381N6-succinyllysine; alternate1 Publication
    Modified residuei345 – 3451N6-acetyllysine1 Publication
    Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
    Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
    Modified residuei364 – 3641N6-acetyllysine1 Publication
    Modified residuei387 – 3871N6-acetyllysine1 Publication
    Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
    Modified residuei396 – 3961N6-succinyllysine; alternate1 Publication
    Modified residuei404 – 4041N6-acetyllysine; alternate2 Publications
    Modified residuei404 – 4041N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications

    Keywords - PTMi

    Acetylation, Nitration

    Proteomic databases

    MaxQBiP05202.
    PaxDbiP05202.
    PRIDEiP05202.

    PTM databases

    PhosphoSiteiP05202.

    Expressioni

    Tissue specificityi

    Detected in brain (at protein level).1 Publication

    Gene expression databases

    BgeeiP05202.
    GenevestigatoriP05202.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    IntActiP05202. 5 interactions.
    MINTiMINT-1859771.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni32 – 354
    Helixi43 – 5311
    Helixi78 – 8912
    Helixi103 – 11412
    Helixi119 – 1235
    Beta strandi126 – 1327
    Helixi133 – 14816
    Beta strandi153 – 1608
    Helixi165 – 1728
    Beta strandi175 – 1806
    Turni184 – 1863
    Beta strandi187 – 1893
    Helixi191 – 1999
    Beta strandi206 – 2105
    Turni215 – 2173
    Helixi223 – 23513
    Beta strandi239 – 2457
    Turni247 – 2515
    Helixi254 – 2574
    Helixi259 – 2668
    Beta strandi272 – 2765
    Turni278 – 2803
    Helixi284 – 2863
    Beta strandi288 – 2947
    Helixi298 – 31619
    Helixi322 – 33211
    Helixi334 – 36431
    Helixi373 – 3764
    Beta strandi379 – 3835
    Helixi388 – 39811
    Beta strandi406 – 4094
    Helixi410 – 4123
    Turni415 – 4173
    Helixi418 – 42912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HLMX-ray2.50A/B/C/D30-430[»]
    3PD6X-ray2.40A/B/C/D30-430[»]
    3PDBX-ray2.40A/B/C/D30-430[»]
    ProteinModelPortaliP05202.
    SMRiP05202. Positions 30-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05202.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1448.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    HOVERGENiHBG000951.
    InParanoidiP05202.
    KOiK14455.
    OMAiRVGAFTM.
    OrthoDBiEOG74J980.
    PhylomeDBiP05202.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P05202-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA    50
    FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG 100
    GLAEFCKASA ELALGENNEV LKSGRFVTVQ TISGTGALRV GASFLQRFFK 150
    FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FSGALEDISK 200
    IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA FFDMAYQGFA 250
    SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE 300
    AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR 350
    IISMRTQLVS NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV 400
    YMTKDGRISV AGVTSGNVGY LAHAIHQVTK 430
    Length:430
    Mass (Da):47,411
    Last modified:August 13, 1987 - v1
    Checksum:iD590524CA7FFB885
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681R → G in BAE39800. (PubMed:16141072)Curated
    Sequence conflicti146 – 1461Q → E in AAB91426. (PubMed:10642497)Curated
    Sequence conflicti153 – 1531R → G in BAE39800. (PubMed:16141072)Curated
    Sequence conflicti377 – 3771Q → K in BAE39800. (PubMed:16141072)Curated
    Sequence conflicti421 – 4211L → I in BAE39800. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02622 mRNA. Translation: AAA37264.1.
    X06917
    , X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1.
    M37259
    , M37250, M37251, M37252, M37253, M37254, M37255, M37256, M37258 Genomic DNA. Translation: AAA37265.1. Sequence problems.
    U82470 mRNA. Translation: AAB91426.1.
    AK136556 mRNA. Translation: BAE23042.1.
    AK147953 mRNA. Translation: BAE28248.1.
    AK149886 mRNA. Translation: BAE29146.1.
    AK149926 mRNA. Translation: BAE29171.1.
    AK150194 mRNA. Translation: BAE29370.1.
    AK152921 mRNA. Translation: BAE31596.1.
    AK155075 mRNA. Translation: BAE33029.1.
    AK167767 mRNA. Translation: BAE39800.1.
    BC089015 mRNA. Translation: AAH89015.1.
    BC089341 mRNA. Translation: AAH89341.1.
    CCDSiCCDS22568.1.
    PIRiS01174.
    RefSeqiNP_034455.1. NM_010325.2.
    UniGeneiMm.230169.

    Genome annotation databases

    EnsembliENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
    GeneIDi14719.
    KEGGimmu:14719.
    UCSCiuc009mzi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02622 mRNA. Translation: AAA37264.1 .
    X06917
    , X06918 , X06919 , X06920 , X06921 , X06922 , X06923 , X06924 , X06925 , X06926 Genomic DNA. Translation: CAA30015.1 .
    M37259
    , M37250 , M37251 , M37252 , M37253 , M37254 , M37255 , M37256 , M37258 Genomic DNA. Translation: AAA37265.1 . Sequence problems.
    U82470 mRNA. Translation: AAB91426.1 .
    AK136556 mRNA. Translation: BAE23042.1 .
    AK147953 mRNA. Translation: BAE28248.1 .
    AK149886 mRNA. Translation: BAE29146.1 .
    AK149926 mRNA. Translation: BAE29171.1 .
    AK150194 mRNA. Translation: BAE29370.1 .
    AK152921 mRNA. Translation: BAE31596.1 .
    AK155075 mRNA. Translation: BAE33029.1 .
    AK167767 mRNA. Translation: BAE39800.1 .
    BC089015 mRNA. Translation: AAH89015.1 .
    BC089341 mRNA. Translation: AAH89341.1 .
    CCDSi CCDS22568.1.
    PIRi S01174.
    RefSeqi NP_034455.1. NM_010325.2.
    UniGenei Mm.230169.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HLM X-ray 2.50 A/B/C/D 30-430 [» ]
    3PD6 X-ray 2.40 A/B/C/D 30-430 [» ]
    3PDB X-ray 2.40 A/B/C/D 30-430 [» ]
    ProteinModelPortali P05202.
    SMRi P05202. Positions 30-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P05202. 5 interactions.
    MINTi MINT-1859771.

    Chemistry

    ChEMBLi CHEMBL3647.

    PTM databases

    PhosphoSitei P05202.

    Proteomic databases

    MaxQBi P05202.
    PaxDbi P05202.
    PRIDEi P05202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034097 ; ENSMUSP00000034097 ; ENSMUSG00000031672 .
    GeneIDi 14719.
    KEGGi mmu:14719.
    UCSCi uc009mzi.1. mouse.

    Organism-specific databases

    CTDi 2806.
    MGIi MGI:95792. Got2.

    Phylogenomic databases

    eggNOGi COG1448.
    GeneTreei ENSGT00390000014081.
    HOGENOMi HOG000185898.
    HOVERGENi HBG000951.
    InParanoidi P05202.
    KOi K14455.
    OMAi RVGAFTM.
    OrthoDBi EOG74J980.
    PhylomeDBi P05202.
    TreeFami TF300641.

    Miscellaneous databases

    EvolutionaryTracei P05202.
    NextBioi 286731.
    PROi P05202.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05202.
    Genevestigatori P05202.

    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].
    2. "Structural organization of the mouse mitochondrial aspartate aminotransferase gene."
      Tsuzuki T., Obaru K., Setoyama C., Shimada K.
      J. Mol. Biol. 198:21-31(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/He.
      Tissue: Liver.
    3. "Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA."
      Bradbury M.W., Berk P.D.
      Biochem. J. 345:423-427(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Strain: FVB.
      Tissue: Liver.
    4. "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: BALB/c, C57BL/6J and NOD.
      Tissue: Bone marrow macrophage, Cecum, Dendritic cell and Melanocyte.
    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].
      Strain: C57BL/6.
      Tissue: Brain and Eye.
    6. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296; 310-345; 356-363 AND 397-404, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake."
      Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D.
      Proc. Soc. Exp. Biol. Med. 208:263-270(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
      Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
      J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-159 AND LYS-404, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-107; LYS-122; LYS-159; LYS-185; LYS-227; LYS-296; LYS-309; LYS-338; LYS-363; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    11. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-73; LYS-82; LYS-90; LYS-107; LYS-122; LYS-159; LYS-185; LYS-234; LYS-279; LYS-296; LYS-302; LYS-309; LYS-338; LYS-345; LYS-363; LYS-364; LYS-387; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Structure, expression, and function of kynurenine aminotransferases in human and rodent brains."
      Han Q., Cai T., Tagle D.A., Li J.
      Cell. Mol. Life Sci. 67:353-368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 30-430 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT.
    13. "Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV."
      Han Q., Robinson H., Cai T., Tagle D.A., Li J.
      Biosci. Rep. 31:323-332(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-430 IN COMPLEX WITH L-KYNURENINE; OXALOACETATE AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiAATM_MOUSE
    AccessioniPrimary (citable) accession number: P05202
    Secondary accession number(s): O09188
    , Q3TIP6, Q3UD91, Q5HZH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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

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

    Documents

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

    External Data

    Dasty 3