BCAT1_HUMAN
ID BCAT1_HUMAN Reviewed; 386 AA.
AC P54687; B3KY27; B7Z2M5; B7Z5L0; F5H5E4; Q68DQ7; Q96MY9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE Short=BCAT(c);
DE EC=2.6.1.42;
DE AltName: Full=Protein ECA39;
GN Name=BCAT1; Synonyms=BCT1, ECA39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-330.
RC TISSUE=Fetal brain;
RX PubMed=8692959; DOI=10.1073/pnas.93.14.7143;
RA Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G., Benvenisty N.;
RT "ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S
RT cell cycle regulation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GABAPENTIN.
RX PubMed=16141215; DOI=10.1074/jbc.m506486200;
RA Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam M.M.,
RA Hutson S.M.;
RT "Structural determinants for branched-chain aminotransferase isozyme-
RT specific inhibition by the anticonvulsant drug gabapentin.";
RL J. Biol. Chem. 280:37246-37256(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-386 IN COMPLEX WITH INHIBITOR.
RX PubMed=16143519; DOI=10.1016/j.bmcl.2005.07.058;
RA Hu L.Y., Boxer P.A., Kesten S.R., Lei H.J., Wustrow D.J., Moreland D.W.,
RA Zhang L., Ahn K., Ryder T.R., Liu X., Rubin J.R., Fahnoe K., Carroll R.T.,
RA Dutta S., Fahnoe D.C., Probert A.W., Roof R.L., Rafferty M.F.,
RA Kostlan C.R., Scholten J.D., Hood M., Ren X.D., Schielke G.P., Su T.Z.,
RA Taylor C.P., Mistry A., McConnell P., Hasemann C., Ohren J.;
RT "The design and synthesis of human branched-chain amino acid
RT aminotransferase inhibitors for treatment of neurodegenerative diseases.";
RL Bioorg. Med. Chem. Lett. 16:2337-2340(2006).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P54687-4; P55212: CASP6; NbExp=3; IntAct=EBI-25834445, EBI-718729;
CC P54687-4; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-25834445, EBI-12593112;
CC P54687-4; O14645: DNALI1; NbExp=3; IntAct=EBI-25834445, EBI-395638;
CC P54687-4; P22607: FGFR3; NbExp=3; IntAct=EBI-25834445, EBI-348399;
CC P54687-4; P06396: GSN; NbExp=3; IntAct=EBI-25834445, EBI-351506;
CC P54687-4; O14901: KLF11; NbExp=3; IntAct=EBI-25834445, EBI-948266;
CC P54687-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25834445, EBI-21591415;
CC P54687-4; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25834445, EBI-5280197;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P54687-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54687-2; Sequence=VSP_042651, VSP_042652;
CC Name=3;
CC IsoId=P54687-3; Sequence=VSP_042652;
CC Name=4;
CC IsoId=P54687-4; Sequence=VSP_043560;
CC Name=5;
CC IsoId=P54687-5; Sequence=VSP_046057;
CC -!- TISSUE SPECIFICITY: During embryogenesis, expressed in the brain and
CC kidney. Overexpressed in MYC-induced tumors such as Burkitt's lymphoma.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U21551; AAB08528.1; -; mRNA.
DR EMBL; AK056255; BAB71129.1; -; mRNA.
DR EMBL; AK128527; BAG54689.1; -; mRNA.
DR EMBL; AK294879; BAH11911.1; -; mRNA.
DR EMBL; AK299088; BAH12946.1; -; mRNA.
DR EMBL; CR749308; CAH18163.1; -; mRNA.
DR EMBL; AC023796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44845.1; -. [P54687-1]
DR CCDS; CCDS53760.1; -. [P54687-4]
DR CCDS; CCDS53761.1; -. [P54687-5]
DR CCDS; CCDS53762.1; -. [P54687-2]
DR CCDS; CCDS53763.1; -. [P54687-3]
DR RefSeq; NP_001171562.1; NM_001178091.1. [P54687-3]
DR RefSeq; NP_001171563.1; NM_001178092.1. [P54687-2]
DR RefSeq; NP_001171564.1; NM_001178093.1. [P54687-5]
DR RefSeq; NP_001171565.1; NM_001178094.1. [P54687-4]
DR RefSeq; NP_005495.2; NM_005504.6. [P54687-1]
DR PDB; 2ABJ; X-ray; 2.20 A; A/D/G/J=21-386.
DR PDB; 2COG; X-ray; 2.10 A; A/B=1-386.
DR PDB; 2COI; X-ray; 1.90 A; A/B=1-386.
DR PDB; 2COJ; X-ray; 2.40 A; A/B=1-386.
DR PDBsum; 2ABJ; -.
DR PDBsum; 2COG; -.
DR PDBsum; 2COI; -.
DR PDBsum; 2COJ; -.
DR AlphaFoldDB; P54687; -.
DR SMR; P54687; -.
DR BioGRID; 107061; 60.
DR IntAct; P54687; 31.
DR MINT; P54687; -.
DR STRING; 9606.ENSP00000443459; -.
DR BindingDB; P54687; -.
DR ChEMBL; CHEMBL4679; -.
DR DrugBank; DB00996; Gabapentin.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00167; Isoleucine.
DR DrugBank; DB00149; Leucine.
DR DrugBank; DB07544; N'-(5-CHLOROBENZOFURAN-2-CARBONYL)-2-(TRIFLUOROMETHYL)BENZENESULFONOHYDRAZIDE.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00161; Valine.
DR GlyGen; P54687; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54687; -.
DR MetOSite; P54687; -.
DR PhosphoSitePlus; P54687; -.
DR SwissPalm; P54687; -.
DR BioMuta; BCAT1; -.
DR DMDM; 215274162; -.
DR EPD; P54687; -.
DR jPOST; P54687; -.
DR MassIVE; P54687; -.
DR MaxQB; P54687; -.
DR PaxDb; P54687; -.
DR PeptideAtlas; P54687; -.
DR PRIDE; P54687; -.
DR ProteomicsDB; 26852; -.
DR ProteomicsDB; 56691; -. [P54687-1]
DR ProteomicsDB; 56692; -. [P54687-2]
DR ProteomicsDB; 56693; -. [P54687-3]
DR ProteomicsDB; 56694; -. [P54687-4]
DR Antibodypedia; 24197; 382 antibodies from 32 providers.
DR DNASU; 586; -.
DR Ensembl; ENST00000261192.12; ENSP00000261192.7; ENSG00000060982.15. [P54687-1]
DR Ensembl; ENST00000342945.9; ENSP00000339805.5; ENSG00000060982.15. [P54687-2]
DR Ensembl; ENST00000538118.5; ENSP00000440817.1; ENSG00000060982.15. [P54687-4]
DR Ensembl; ENST00000539282.5; ENSP00000443459.1; ENSG00000060982.15. [P54687-5]
DR Ensembl; ENST00000539780.5; ENSP00000440827.1; ENSG00000060982.15. [P54687-3]
DR GeneID; 586; -.
DR KEGG; hsa:586; -.
DR MANE-Select; ENST00000261192.12; ENSP00000261192.7; NM_005504.7; NP_005495.2.
DR UCSC; uc001rgc.4; human. [P54687-1]
DR CTD; 586; -.
DR DisGeNET; 586; -.
DR GeneCards; BCAT1; -.
DR HGNC; HGNC:976; BCAT1.
DR HPA; ENSG00000060982; Tissue enhanced (pancreas).
DR MIM; 113520; gene.
DR neXtProt; NX_P54687; -.
DR OpenTargets; ENSG00000060982; -.
DR PharmGKB; PA25288; -.
DR VEuPathDB; HostDB:ENSG00000060982; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_3_1; -.
DR InParanoid; P54687; -.
DR OMA; LTEVFAC; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; P54687; -.
DR TreeFam; TF300882; -.
DR BRENDA; 2.6.1.42; 2681.
DR PathwayCommons; P54687; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P54687; -.
DR SignaLink; P54687; -.
DR BioGRID-ORCS; 586; 23 hits in 1081 CRISPR screens.
DR ChiTaRS; BCAT1; human.
DR EvolutionaryTrace; P54687; -.
DR GenomeRNAi; 586; -.
DR Pharos; P54687; Tchem.
DR PRO; PR:P54687; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P54687; protein.
DR Bgee; ENSG00000060982; Expressed in tibia and 179 other tissues.
DR ExpressionAtlas; P54687; baseline and differential.
DR Genevisible; P54687; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; TAS:ProtInc.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd01557; BCAT_beta_family; 1.
DR DisProt; DP02698; -.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Lipid metabolism; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="Branched-chain-amino-acid aminotransferase,
FT cytosolic"
FT /id="PRO_0000103292"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..25
FT /note="MKDCSNGCSAECTGEGGSKEVVGTF -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042651"
FT VAR_SEQ 1..2
FT /note="MK -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_043560"
FT VAR_SEQ 1..2
FT /note="MK -> MASPLRSAAALARQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046057"
FT VAR_SEQ 94..130
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042652"
FT VARIANT 59
FT /note="T -> M (in dbSNP:rs17374285)"
FT /id="VAR_047681"
FT VARIANT 321
FT /note="E -> K (in dbSNP:rs7313020)"
FT /id="VAR_019614"
FT VARIANT 330
FT /note="G -> S (in dbSNP:rs1057204)"
FT /evidence="ECO:0000269|PubMed:8692959"
FT /id="VAR_047682"
FT CONFLICT 2
FT /note="Missing (in Ref. 1; AAB08528)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="Missing (in Ref. 1; AAB08528)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="T -> A (in Ref. 1; AAB08528)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="A -> D (in Ref. 1; AAB08528)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="E -> R (in Ref. 1; AAB08528)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Q -> P (in Ref. 2; BAH11911)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="T -> S (in Ref. 2; BAB71129)"
FT /evidence="ECO:0000305"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2ABJ"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2COG"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2COI"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 179..190
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:2COI"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:2COI"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:2COI"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:2COI"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 336..351
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:2COI"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:2COI"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2COI"
SQ SEQUENCE 386 AA; 42966 MW; A43535303A702512 CRC64;
MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG TVFTDHMLTV
EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA FRGVDNKIRL FQPNLNMDRM
YRSAVRATLP VFDKEELLEC IQQLVKLDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPTK
ALLFVLLSPV GPYFSSGTFN PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN
GCQQVLWLYG EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ
WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI HIPTMENGPK
LASRILSKLT DIQYGREESD WTIVLS
