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P54687 (BCAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Branched-chain-amino-acid aminotransferase, cytosolic

Short name=BCAT(c)
EC=2.6.1.42
Alternative name(s):
Protein ECA39
Gene names
Name:BCAT1
Synonyms:BCT1, ECA39
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.

Catalytic activity

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.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

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

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54687-1)

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.
Isoform 2 (identifier: P54687-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MKDCSNGCSAECTGEGGSKEVVGTF → M
     94-130: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P54687-3)

The sequence of this isoform differs from the canonical sequence as follows:
     94-130: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P54687-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → M
Note: No experimental confirmation available.
Isoform 5 (identifier: P54687-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → MASPLRSAAALARQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Branched-chain-amino-acid aminotransferase, cytosolic
PRO_0000103292

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5
Modified residue2221N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence1 – 2525MKDCS…VVGTF → M in isoform 2.
VSP_042651
Alternative sequence1 – 22MK → M in isoform 4.
VSP_043560
Alternative sequence1 – 22MK → MASPLRSAAALARQ in isoform 5.
VSP_046057
Alternative sequence94 – 13037Missing in isoform 2 and isoform 3.
VSP_042652
Natural variant591T → M.
Corresponds to variant rs17374285 [ dbSNP | Ensembl ].
VAR_047681
Natural variant3211E → K.
Corresponds to variant rs7313020 [ dbSNP | Ensembl ].
VAR_019614
Natural variant3301G → S. Ref.1
Corresponds to variant rs1057204 [ dbSNP | Ensembl ].
VAR_047682

Experimental info

Sequence conflict21Missing in AAB08528. Ref.1
Sequence conflict81Missing in AAB08528. Ref.1
Sequence conflict1651T → A in AAB08528. Ref.1
Sequence conflict2371A → D in AAB08528. Ref.1
Sequence conflict2511E → R in AAB08528. Ref.1
Sequence conflict3001Q → P in BAH11911. Ref.2
Sequence conflict3171T → S in BAB71129. Ref.2

Secondary structure

................................................................... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: A43535303A702512

FASTA38642,966
        10         20         30         40         50         60 
MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG TVFTDHMLTV 

        70         80         90        100        110        120 
EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA FRGVDNKIRL FQPNLNMDRM 

       130        140        150        160        170        180 
YRSAVRATLP VFDKEELLEC IQQLVKLDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPTK 

       190        200        210        220        230        240 
ALLFVLLSPV GPYFSSGTFN PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN 

       250        260        270        280        290        300 
GCQQVLWLYG EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ 

       310        320        330        340        350        360 
WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI HIPTMENGPK 

       370        380 
LASRILSKLT DIQYGREESD WTIVLS 

« Hide

Isoform 2 [UniParc].

Checksum: FDC0B4CC0356E91D
Show »

FASTA32536,298
Isoform 3 [UniParc].

Checksum: 1179C4AB4AD1B455
Show »

FASTA34938,645
Isoform 4 [UniParc].

Checksum: 4713DD9AF2134746
Show »

FASTA38542,838
Isoform 5 [UniParc].

Checksum: 39780ADB0CF85D5A
Show »

FASTA39844,131

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases."
Hu L.Y., Boxer P.A., Kesten S.R., Lei H.J., Wustrow D.J., Moreland D.W., Zhang L., Ahn K., Ryder T.R., Liu X., Rubin J.R., Fahnoe K., Carroll R.T., Dutta S., Fahnoe D.C., Probert A.W., Roof R.L., Rafferty M.F. expand/collapse author list , Kostlan C.R., Scholten J.D., Hood M., Ren X.D., Schielke G.P., Su T.Z., Taylor C.P., Mistry A., McConnell P., Hasemann C., Ohren J.
Bioorg. Med. Chem. Lett. 16:2337-2340(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-386 IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001171562.1. NM_001178091.1.
NP_001171563.1. NM_001178092.1.
NP_001171564.1. NM_001178093.1.
NP_001171565.1. NM_001178094.1.
NP_005495.2. NM_005504.6.
UniGeneHs.438993.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP54687.
SMRP54687. Positions 24-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107061. 12 interactions.
IntActP54687. 3 interactions.
MINTMINT-1180265.
STRING9606.ENSP00000261192.

Chemistry

BindingDBP54687.
ChEMBLCHEMBL4679.
DrugBankDB00996. Gabapentin.
DB00142. L-Glutamic Acid.
DB00167. L-Isoleucine.
DB00149. L-Leucine.
DB00161. L-Valine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP54687.

Polymorphism databases

DMDM215274162.

Proteomic databases

PaxDbP54687.
PRIDEP54687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261192; ENSP00000261192; ENSG00000060982. [P54687-1]
ENST00000342945; ENSP00000339805; ENSG00000060982. [P54687-2]
ENST00000538118; ENSP00000440817; ENSG00000060982. [P54687-4]
ENST00000539282; ENSP00000443459; ENSG00000060982. [P54687-5]
ENST00000539780; ENSP00000440827; ENSG00000060982. [P54687-3]
GeneID586.
KEGGhsa:586.
UCSCuc001rgc.3. human. [P54687-4]
uc001rgd.4. human. [P54687-1]
uc001rge.4. human. [P54687-2]
uc010siy.2. human. [P54687-3]

Organism-specific databases

CTD586.
GeneCardsGC12M024868.
HGNCHGNC:976. BCAT1.
HPAHPA048592.
MIM113520. gene.
neXtProtNX_P54687.
PharmGKBPA25288.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0115.
HOGENOMHOG000276704.
HOVERGENHBG050678.
InParanoidP54687.
KOK00826.
OMANFFGITH.
OrthoDBEOG7NGQB7.
PhylomeDBP54687.
TreeFamTF300882.

Enzyme and pathway databases

BRENDA2.6.1.42. 4472.
ReactomeREACT_111217. Metabolism.
SABIO-RKP54687.

Gene expression databases

ArrayExpressP54687.
BgeeP54687.
CleanExHS_BCAT1.
GenevestigatorP54687.

Family and domain databases

InterProIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFPIRSF006468. BCAT1. 1 hit.
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR01123. ilvE_II. 1 hit.
PROSITEPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54687.
GenomeRNAi586.
NextBio2395.
PROP54687.
SOURCESearch...

Entry information

Entry nameBCAT1_HUMAN
AccessionPrimary (citable) accession number: P54687
Secondary accession number(s): B3KY27 expand/collapse secondary AC list , B7Z2M5, B7Z5L0, F5H5E4, Q68DQ7, Q96MY9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 25, 2008
Last modified: March 19, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM