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O15382

- BCAT2_HUMAN

UniProt

O15382 - BCAT2_HUMAN

Protein

Branched-chain-amino-acid aminotransferase, mitochondrial

Gene

BCAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.

    Catalytic activityi

    L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
    L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
    L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei168 – 1681Substrate

    GO - Molecular functioni

    1. branched-chain-amino-acid transaminase activity Source: Reactome
    2. L-isoleucine transaminase activity Source: UniProtKB-EC
    3. L-leucine transaminase activity Source: UniProtKB-EC
    4. L-valine transaminase activity Source: UniProtKB-EC

    GO - Biological processi

    1. branched-chain amino acid biosynthetic process Source: ProtInc
    2. branched-chain amino acid catabolic process Source: Reactome
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. isoleucine catabolic process Source: Ensembl
    5. leucine metabolic process Source: Ensembl
    6. regulation of hormone levels Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. valine metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.6.1.42. 2681.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKO15382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Branched-chain-amino-acid aminotransferase, mitochondrial (EC:2.6.1.42)
    Short name:
    BCAT(m)
    Alternative name(s):
    Placental protein 18
    Short name:
    PP18
    Gene namesi
    Name:BCAT2
    Synonyms:BCATM, BCT2, ECA40
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:977. BCAT2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi342 – 3421C → A: Reduces activity about 6-fold. 1 Publication
    Mutagenesisi345 – 3451C → A: Slight reduction of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA25289.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionAdd
    BLAST
    Chaini28 – 392365Branched-chain-amino-acid aminotransferase, mitochondrialPRO_0000001271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei229 – 2291N6-(pyridoxal phosphate)lysine
    Modified residuei321 – 3211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO15382.
    PaxDbiO15382.
    PRIDEiO15382.

    PTM databases

    PhosphoSiteiO15382.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO15382.
    BgeeiO15382.
    CleanExiHS_BCAT2.
    GenevestigatoriO15382.

    Organism-specific databases

    HPAiHPA054091.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi107062. 7 interactions.
    IntActiO15382. 3 interactions.
    STRINGi9606.ENSP00000322991.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 363
    Beta strandi51 – 533
    Turni57 – 593
    Beta strandi63 – 719
    Beta strandi72 – 754
    Beta strandi79 – 835
    Beta strandi86 – 883
    Helixi93 – 964
    Beta strandi100 – 1023
    Beta strandi105 – 1095
    Beta strandi115 – 1195
    Helixi120 – 13314
    Helixi141 – 15414
    Helixi156 – 1583
    Beta strandi162 – 1643
    Beta strandi166 – 17510
    Beta strandi181 – 1833
    Beta strandi186 – 19712
    Beta strandi200 – 2056
    Beta strandi209 – 2135
    Helixi231 – 2333
    Turni234 – 2363
    Helixi237 – 24610
    Beta strandi250 – 2567
    Turni257 – 2604
    Beta strandi261 – 2655
    Beta strandi268 – 2758
    Beta strandi281 – 2855
    Beta strandi289 – 2924
    Helixi296 – 30813
    Beta strandi310 – 3156
    Helixi320 – 3289
    Beta strandi332 – 3398
    Turni340 – 3423
    Beta strandi343 – 35210
    Beta strandi355 – 3584
    Helixi362 – 3643
    Helixi367 – 38014
    Beta strandi389 – 3913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EKFX-ray1.95A/B28-392[»]
    1EKPX-ray2.50A/B28-392[»]
    1EKVX-ray2.25A/B28-392[»]
    1KT8X-ray1.90A/B28-392[»]
    1KTAX-ray1.90A/B28-392[»]
    2A1HX-ray1.80A/B28-392[»]
    2HDKX-ray2.40A/B28-392[»]
    2HG8X-ray1.80A/B28-392[»]
    2HGWX-ray1.98A/B28-392[»]
    2HGXX-ray1.80A/B28-392[»]
    2HHFX-ray1.80A/B28-392[»]
    ProteinModelPortaliO15382.
    SMRiO15382. Positions 30-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15382.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0115.
    HOGENOMiHOG000276704.
    HOVERGENiHBG050678.
    InParanoidiO15382.
    KOiK00826.
    OrthoDBiEOG7NGQB7.
    PhylomeDBiO15382.
    TreeFamiTF300882.

    Family and domain databases

    InterProiIPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005786. B_amino_transII.
    [Graphical view]
    PANTHERiPTHR11825. PTHR11825. 1 hit.
    PfamiPF01063. Aminotran_4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006468. BCAT1. 1 hit.
    SUPFAMiSSF56752. SSF56752. 1 hit.
    TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
    PROSITEiPS00770. AA_TRANSFER_CLASS_4. 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 A (identifier: O15382-1) [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

    MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG    50
    PGEPLVFGKT FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ 100
    LFEGMKAFKG KDQQVRLFRP WLNMDRMLRS AMRLCLPSFD KLELLECIRR 150
    LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL GVSQPTRALL FVILCPVGAY 200
    FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV QQEALKRGCE 250
    QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS 300
    LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI 350
    LYKDRNLHIP TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV 392
    Length:392
    Mass (Da):44,288
    Last modified:May 2, 2002 - v2
    Checksum:iEC07047264B190DA
    GO
    Isoform B (identifier: O15382-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         9-100: Missing.

    Show »
    Length:300
    Mass (Da):33,777
    Checksum:i656A626FEC867073
    GO

    Sequence cautioni

    The sequence AAB53087.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1541V → L in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti207 – 2071T → N in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti214 – 2163DPA → EPT in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti253 – 2531L → F in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti326 – 3261A → P in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti330 – 3301G → A in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti349 – 3491R → G in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti357 – 3571L → F in AAB53087. (PubMed:8702755)Curated
    Sequence conflicti370 – 3701L → F in AAB53087. (PubMed:8702755)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti186 – 1861T → R.2 Publications
    Corresponds to variant rs11548193 [ dbSNP | Ensembl ].
    VAR_048234

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei9 – 10092Missing in isoform B. 1 PublicationVSP_000236Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U68418 mRNA. Translation: AAB67672.1.
    AF268047 mRNA. Translation: AAK38368.1.
    AF268048 mRNA. Translation: AAK38369.1.
    AK314548 mRNA. Translation: BAG37134.1.
    CH471177 Genomic DNA. Translation: EAW52403.1.
    BC001900 mRNA. Translation: AAH01900.1.
    BC004243 mRNA. Translation: AAH04243.2.
    U62739 mRNA. Translation: AAB53087.1. Different initiation.
    CCDSiCCDS12735.1. [O15382-1]
    CCDS54290.1. [O15382-2]
    RefSeqiNP_001158245.1. NM_001164773.1. [O15382-2]
    NP_001181.2. NM_001190.3. [O15382-1]
    NP_001271254.1. NM_001284325.1.
    UniGeneiHs.512670.

    Genome annotation databases

    EnsembliENST00000316273; ENSP00000322991; ENSG00000105552. [O15382-1]
    ENST00000545387; ENSP00000440973; ENSG00000105552. [O15382-2]
    GeneIDi587.
    KEGGihsa:587.
    UCSCiuc002pkq.4. human. [O15382-1]
    uc002pkt.3. human. [O15382-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U68418 mRNA. Translation: AAB67672.1 .
    AF268047 mRNA. Translation: AAK38368.1 .
    AF268048 mRNA. Translation: AAK38369.1 .
    AK314548 mRNA. Translation: BAG37134.1 .
    CH471177 Genomic DNA. Translation: EAW52403.1 .
    BC001900 mRNA. Translation: AAH01900.1 .
    BC004243 mRNA. Translation: AAH04243.2 .
    U62739 mRNA. Translation: AAB53087.1 . Different initiation.
    CCDSi CCDS12735.1. [O15382-1 ]
    CCDS54290.1. [O15382-2 ]
    RefSeqi NP_001158245.1. NM_001164773.1. [O15382-2 ]
    NP_001181.2. NM_001190.3. [O15382-1 ]
    NP_001271254.1. NM_001284325.1.
    UniGenei Hs.512670.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EKF X-ray 1.95 A/B 28-392 [» ]
    1EKP X-ray 2.50 A/B 28-392 [» ]
    1EKV X-ray 2.25 A/B 28-392 [» ]
    1KT8 X-ray 1.90 A/B 28-392 [» ]
    1KTA X-ray 1.90 A/B 28-392 [» ]
    2A1H X-ray 1.80 A/B 28-392 [» ]
    2HDK X-ray 2.40 A/B 28-392 [» ]
    2HG8 X-ray 1.80 A/B 28-392 [» ]
    2HGW X-ray 1.98 A/B 28-392 [» ]
    2HGX X-ray 1.80 A/B 28-392 [» ]
    2HHF X-ray 1.80 A/B 28-392 [» ]
    ProteinModelPortali O15382.
    SMRi O15382. Positions 30-392.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107062. 7 interactions.
    IntActi O15382. 3 interactions.
    STRINGi 9606.ENSP00000322991.

    Chemistry

    DrugBanki DB00167. L-Isoleucine.
    DB00149. L-Leucine.

    PTM databases

    PhosphoSitei O15382.

    Proteomic databases

    MaxQBi O15382.
    PaxDbi O15382.
    PRIDEi O15382.

    Protocols and materials databases

    DNASUi 587.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316273 ; ENSP00000322991 ; ENSG00000105552 . [O15382-1 ]
    ENST00000545387 ; ENSP00000440973 ; ENSG00000105552 . [O15382-2 ]
    GeneIDi 587.
    KEGGi hsa:587.
    UCSCi uc002pkq.4. human. [O15382-1 ]
    uc002pkt.3. human. [O15382-2 ]

    Organism-specific databases

    CTDi 587.
    GeneCardsi GC19M049298.
    HGNCi HGNC:977. BCAT2.
    HPAi HPA054091.
    MIMi 113530. gene.
    neXtProti NX_O15382.
    PharmGKBi PA25289.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0115.
    HOGENOMi HOG000276704.
    HOVERGENi HBG050678.
    InParanoidi O15382.
    KOi K00826.
    OrthoDBi EOG7NGQB7.
    PhylomeDBi O15382.
    TreeFami TF300882.

    Enzyme and pathway databases

    BRENDAi 2.6.1.42. 2681.
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK O15382.

    Miscellaneous databases

    EvolutionaryTracei O15382.
    GenomeRNAii 587.
    NextBioi 2399.
    PROi O15382.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15382.
    Bgeei O15382.
    CleanExi HS_BCAT2.
    Genevestigatori O15382.

    Family and domain databases

    InterProi IPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005786. B_amino_transII.
    [Graphical view ]
    PANTHERi PTHR11825. PTHR11825. 1 hit.
    Pfami PF01063. Aminotran_4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006468. BCAT1. 1 hit.
    SUPFAMi SSF56752. SSF56752. 1 hit.
    TIGRFAMsi TIGR01123. ilvE_II. 1 hit.
    PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)."
      Bledsoe R.K., Dawson P.A., Hutson S.M.
      Biochim. Biophys. Acta 1339:9-13(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-186.
    2. "Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant."
      Than N.G., Sumegi B., Than G.N., Bellyei S., Bohn H.
      Placenta 22:235-243(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
      Tissue: Placenta.
    3. "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 A).
      Tissue: Heart.
    4. 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 A).
      Tissue: Lung and Skin.
    6. "Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases."
      Eden A., Simchen G., Benvenisty N.
      J. Biol. Chem. 271:20242-20245(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-392 (ISOFORM A), VARIANT ARG-186.
      Tissue: Brain.
    7. "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-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The structure of human mitochondrial branched-chain aminotransferase."
      Yennawar N.H., Dunbar J., Conway M.E., Hutson S.M., Farber G.K.
      Acta Crystallogr. D 57:506-515(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-392 IN COMPLEX WITH COFACTOR, SUBUNIT.
    10. "Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms."
      Yennawar N.H., Conway M.E., Yennawar H.P., Farber G.K., Hutson S.M.
      Biochemistry 41:11592-11601(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATES.
    11. "Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin."
      Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam M.M., Hutson S.M.
      J. Biol. Chem. 280:37246-37256(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATE ANALOGS.
    12. "Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis."
      Yennawar N.H., Islam M.M., Conway M., Wallin R., Hutson S.M.
      J. Biol. Chem. 281:39660-39671(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATE ANALOGS, MUTAGENESIS OF CYS-342 AND CYS-345.

    Entry informationi

    Entry nameiBCAT2_HUMAN
    AccessioniPrimary (citable) accession number: O15382
    Secondary accession number(s): B2RB87
    , O00269, Q96KG1, Q9BTB6, Q9BUU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3