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P54687

- BCAT1_HUMAN

UniProt

P54687 - BCAT1_HUMAN

Protein

Branched-chain-amino-acid aminotransferase, cytosolic

Gene

BCAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      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.

    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.

    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. cell proliferation Source: ProtInc
    4. cellular nitrogen compound metabolic process Source: Reactome
    5. G1/S transition of mitotic cell cycle Source: ProtInc
    6. small molecule metabolic process Source: Reactome

    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. 4472.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKP54687.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Branched-chain-amino-acid aminotransferase, cytosolic (EC:2.6.1.42)
    Short name:
    BCAT(c)
    Alternative name(s):
    Protein ECA39
    Gene namesi
    Name:BCAT1
    Synonyms:BCT1, ECA39
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:976. BCAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25288.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Branched-chain-amino-acid aminotransferase, cytosolicPRO_0000103292Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei222 – 2221N6-(pyridoxal phosphate)lysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54687.
    PaxDbiP54687.
    PRIDEiP54687.

    PTM databases

    PhosphoSiteiP54687.

    Expressioni

    Tissue specificityi

    During embryogenesis, expressed in the brain and kidney. Overexpressed in MYC-induced tumors such as Burkitt's lymphoma.

    Gene expression databases

    ArrayExpressiP54687.
    BgeeiP54687.
    CleanExiHS_BCAT1.
    GenevestigatoriP54687.

    Organism-specific databases

    HPAiHPA048592.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi107061. 12 interactions.
    IntActiP54687. 3 interactions.
    MINTiMINT-1180265.
    STRINGi9606.ENSP00000261192.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 293
    Helixi44 – 463
    Turni49 – 513
    Beta strandi55 – 639
    Turni64 – 663
    Beta strandi72 – 754
    Beta strandi79 – 813
    Helixi86 – 894
    Beta strandi93 – 953
    Beta strandi98 – 1025
    Beta strandi108 – 1125
    Helixi113 – 12614
    Helixi134 – 14714
    Helixi149 – 1513
    Beta strandi154 – 1574
    Beta strandi159 – 16810
    Beta strandi179 – 19012
    Beta strandi202 – 2065
    Helixi225 – 2284
    Helixi231 – 2388
    Turni239 – 2413
    Beta strandi243 – 2497
    Turni250 – 2534
    Beta strandi254 – 2585
    Beta strandi261 – 2688
    Beta strandi274 – 2785
    Beta strandi282 – 2854
    Helixi289 – 30113
    Beta strandi303 – 3086
    Helixi313 – 3208
    Turni321 – 3233
    Beta strandi325 – 3328
    Turni333 – 3353
    Beta strandi336 – 35116
    Helixi353 – 3575
    Helixi360 – 37314
    Beta strandi382 – 3843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ABJX-ray2.20A/D/G/J21-386[»]
    2COGX-ray2.10A/B1-386[»]
    2COIX-ray1.90A/B1-386[»]
    2COJX-ray2.40A/B1-386[»]
    ProteinModelPortaliP54687.
    SMRiP54687. Positions 24-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54687.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0115.
    HOGENOMiHOG000276704.
    HOVERGENiHBG050678.
    InParanoidiP54687.
    KOiK00826.
    OMAiALECFEG.
    OrthoDBiEOG7NGQB7.
    PhylomeDBiP54687.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54687-1) [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

    MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG    50
    TVFTDHMLTV EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA 100
    FRGVDNKIRL FQPNLNMDRM YRSAVRATLP VFDKEELLEC IQQLVKLDQE 150
    WVPYSTSASL YIRPTFIGTE PSLGVKKPTK ALLFVLLSPV GPYFSSGTFN 200
    PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN GCQQVLWLYG 250
    EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ 300
    WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI 350
    HIPTMENGPK LASRILSKLT DIQYGREESD WTIVLS 386
    Length:386
    Mass (Da):42,966
    Last modified:November 25, 2008 - v3
    Checksum:iA43535303A702512
    GO
    Isoform 2 (identifier: P54687-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MKDCSNGCSAECTGEGGSKEVVGTF → M
         94-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:325
    Mass (Da):36,298
    Checksum:iFDC0B4CC0356E91D
    GO
    Isoform 3 (identifier: P54687-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         94-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:349
    Mass (Da):38,645
    Checksum:i1179C4AB4AD1B455
    GO
    Isoform 4 (identifier: P54687-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MK → M

    Note: No experimental confirmation available.

    Show »
    Length:385
    Mass (Da):42,838
    Checksum:i4713DD9AF2134746
    GO
    Isoform 5 (identifier: P54687-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MK → MASPLRSAAALARQ

    Note: No experimental confirmation available.

    Show »
    Length:398
    Mass (Da):44,131
    Checksum:i39780ADB0CF85D5A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21Missing in AAB08528. (PubMed:8692959)Curated
    Sequence conflicti8 – 81Missing in AAB08528. (PubMed:8692959)Curated
    Sequence conflicti165 – 1651T → A in AAB08528. (PubMed:8692959)Curated
    Sequence conflicti237 – 2371A → D in AAB08528. (PubMed:8692959)Curated
    Sequence conflicti251 – 2511E → R in AAB08528. (PubMed:8692959)Curated
    Sequence conflicti300 – 3001Q → P in BAH11911. (PubMed:14702039)Curated
    Sequence conflicti317 – 3171T → S in BAB71129. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591T → M.
    Corresponds to variant rs17374285 [ dbSNP | Ensembl ].
    VAR_047681
    Natural varianti321 – 3211E → K.
    Corresponds to variant rs7313020 [ dbSNP | Ensembl ].
    VAR_019614
    Natural varianti330 – 3301G → S.1 Publication
    Corresponds to variant rs1057204 [ dbSNP | Ensembl ].
    VAR_047682

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MKDCS…VVGTF → M in isoform 2. 1 PublicationVSP_042651Add
    BLAST
    Alternative sequencei1 – 22MK → M in isoform 4. 1 PublicationVSP_043560
    Alternative sequencei1 – 22MK → MASPLRSAAALARQ in isoform 5. 1 PublicationVSP_046057
    Alternative sequencei94 – 13037Missing in isoform 2 and isoform 3. 1 PublicationVSP_042652Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21551 mRNA. Translation: AAB08528.1.
    AK056255 mRNA. Translation: BAB71129.1.
    AK128527 mRNA. Translation: BAG54689.1.
    AK294879 mRNA. Translation: BAH11911.1.
    AK299088 mRNA. Translation: BAH12946.1.
    CR749308 mRNA. Translation: CAH18163.1.
    AC023796 Genomic DNA. No translation available.
    AC026310 Genomic DNA. No translation available.
    AC092867 Genomic DNA. No translation available.
    CCDSiCCDS44845.1. [P54687-1]
    CCDS53760.1. [P54687-4]
    CCDS53761.1. [P54687-5]
    CCDS53762.1. [P54687-2]
    CCDS53763.1. [P54687-3]
    RefSeqiNP_001171562.1. NM_001178091.1. [P54687-3]
    NP_001171563.1. NM_001178092.1. [P54687-2]
    NP_001171564.1. NM_001178093.1. [P54687-5]
    NP_001171565.1. NM_001178094.1. [P54687-4]
    NP_005495.2. NM_005504.6. [P54687-1]
    UniGeneiHs.438993.

    Genome annotation databases

    EnsembliENST00000261192; ENSP00000261192; ENSG00000060982. [P54687-1]
    ENST00000342945; ENSP00000339805; ENSG00000060982. [P54687-2]
    ENST00000538118; ENSP00000440817; ENSG00000060982. [P54687-4]
    ENST00000539282; ENSP00000443459; ENSG00000060982. [P54687-5]
    ENST00000539780; ENSP00000440827; ENSG00000060982. [P54687-3]
    GeneIDi586.
    KEGGihsa:586.
    UCSCiuc001rgc.3. human. [P54687-4]
    uc001rgd.4. human. [P54687-1]
    uc001rge.4. human. [P54687-2]
    uc010siy.2. human. [P54687-3]

    Polymorphism databases

    DMDMi215274162.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21551 mRNA. Translation: AAB08528.1 .
    AK056255 mRNA. Translation: BAB71129.1 .
    AK128527 mRNA. Translation: BAG54689.1 .
    AK294879 mRNA. Translation: BAH11911.1 .
    AK299088 mRNA. Translation: BAH12946.1 .
    CR749308 mRNA. Translation: CAH18163.1 .
    AC023796 Genomic DNA. No translation available.
    AC026310 Genomic DNA. No translation available.
    AC092867 Genomic DNA. No translation available.
    CCDSi CCDS44845.1. [P54687-1 ]
    CCDS53760.1. [P54687-4 ]
    CCDS53761.1. [P54687-5 ]
    CCDS53762.1. [P54687-2 ]
    CCDS53763.1. [P54687-3 ]
    RefSeqi NP_001171562.1. NM_001178091.1. [P54687-3 ]
    NP_001171563.1. NM_001178092.1. [P54687-2 ]
    NP_001171564.1. NM_001178093.1. [P54687-5 ]
    NP_001171565.1. NM_001178094.1. [P54687-4 ]
    NP_005495.2. NM_005504.6. [P54687-1 ]
    UniGenei Hs.438993.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ABJ X-ray 2.20 A/D/G/J 21-386 [» ]
    2COG X-ray 2.10 A/B 1-386 [» ]
    2COI X-ray 1.90 A/B 1-386 [» ]
    2COJ X-ray 2.40 A/B 1-386 [» ]
    ProteinModelPortali P54687.
    SMRi P54687. Positions 24-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107061. 12 interactions.
    IntActi P54687. 3 interactions.
    MINTi MINT-1180265.
    STRINGi 9606.ENSP00000261192.

    Chemistry

    BindingDBi P54687.
    ChEMBLi CHEMBL4679.
    DrugBanki DB00996. Gabapentin.
    DB00167. L-Isoleucine.
    DB00149. L-Leucine.
    DB00161. L-Valine.

    PTM databases

    PhosphoSitei P54687.

    Polymorphism databases

    DMDMi 215274162.

    Proteomic databases

    MaxQBi P54687.
    PaxDbi P54687.
    PRIDEi P54687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261192 ; ENSP00000261192 ; ENSG00000060982 . [P54687-1 ]
    ENST00000342945 ; ENSP00000339805 ; ENSG00000060982 . [P54687-2 ]
    ENST00000538118 ; ENSP00000440817 ; ENSG00000060982 . [P54687-4 ]
    ENST00000539282 ; ENSP00000443459 ; ENSG00000060982 . [P54687-5 ]
    ENST00000539780 ; ENSP00000440827 ; ENSG00000060982 . [P54687-3 ]
    GeneIDi 586.
    KEGGi hsa:586.
    UCSCi uc001rgc.3. human. [P54687-4 ]
    uc001rgd.4. human. [P54687-1 ]
    uc001rge.4. human. [P54687-2 ]
    uc010siy.2. human. [P54687-3 ]

    Organism-specific databases

    CTDi 586.
    GeneCardsi GC12M024868.
    HGNCi HGNC:976. BCAT1.
    HPAi HPA048592.
    MIMi 113520. gene.
    neXtProti NX_P54687.
    PharmGKBi PA25288.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0115.
    HOGENOMi HOG000276704.
    HOVERGENi HBG050678.
    InParanoidi P54687.
    KOi K00826.
    OMAi ALECFEG.
    OrthoDBi EOG7NGQB7.
    PhylomeDBi P54687.
    TreeFami TF300882.

    Enzyme and pathway databases

    BRENDAi 2.6.1.42. 4472.
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK P54687.

    Miscellaneous databases

    EvolutionaryTracei P54687.
    GenomeRNAii 586.
    NextBioi 2395.
    PROi P54687.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54687.
    Bgeei P54687.
    CleanExi HS_BCAT1.
    Genevestigatori P54687.

    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. "ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast."
      Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G., Benvenisty N.
      Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-330.
      Tissue: Fetal brain.
    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] (ISOFORMS 1; 2; 3 AND 5).
      Tissue: Brain and Trachea.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Uterine endothelium.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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 (1.9 ANGSTROMS) IN COMPLEX WITH GABAPENTIN.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-386 IN COMPLEX WITH INHIBITOR.

    Entry informationi

    Entry nameiBCAT1_HUMAN
    AccessioniPrimary (citable) accession number: P54687
    Secondary accession number(s): B3KY27
    , B7Z2M5, B7Z5L0, F5H5E4, Q68DQ7, Q96MY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 148 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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