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O15382 (BCAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=BCAT(m)
EC=2.6.1.42
Alternative name(s):
Placental protein 18
Short name=PP18
Gene names
Name:BCAT2
Synonyms:BCATM, BCT2, ECA40
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. May also function as a transporter of branched chain alpha-keto acids.

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. Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Homodimer. Ref.9

Subcellular location

Isoform A: Mitochondrion.

Isoform B: Cytoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

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

Sequence caution

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Branched-chain amino acid biosynthesis
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranched-chain amino acid biosynthetic process

Traceable author statement Ref.6. Source: ProtInc

branched-chain amino acid catabolic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

isoleucine catabolic process

Inferred from electronic annotation. Source: Ensembl

leucine metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of hormone levels

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

valine metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionL-isoleucine transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-leucine transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-valine transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

branched-chain-amino-acid transaminase activity

Inferred from experiment. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O15382-1)

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 B (identifier: O15382-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion
Chain28 – 392365Branched-chain-amino-acid aminotransferase, mitochondrial
PRO_0000001271

Sites

Binding site1681Substrate

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine
Modified residue3211N6-acetyllysine Ref.7

Natural variations

Alternative sequence9 – 10092Missing in isoform B.
VSP_000236
Natural variant1861T → R. Ref.1 Ref.6
Corresponds to variant rs11548193 [ dbSNP | Ensembl ].
VAR_048234

Experimental info

Mutagenesis3421C → A: Reduces activity about 6-fold. Ref.12
Mutagenesis3451C → A: Slight reduction of activity. Ref.12
Sequence conflict1541V → L in AAB53087. Ref.6
Sequence conflict2071T → N in AAB53087. Ref.6
Sequence conflict214 – 2163DPA → EPT in AAB53087. Ref.6
Sequence conflict2531L → F in AAB53087. Ref.6
Sequence conflict3261A → P in AAB53087. Ref.6
Sequence conflict3301G → A in AAB53087. Ref.6
Sequence conflict3491R → G in AAB53087. Ref.6
Sequence conflict3571L → F in AAB53087. Ref.6
Sequence conflict3701L → F in AAB53087. Ref.6

Secondary structure

....................................................................... 392
Helix Strand Turn

Details...

Sequences

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

Last modified May 2, 2002. Version 2.
Checksum: EC07047264B190DA

FASTA39244,288
        10         20         30         40         50         60 
MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG PGEPLVFGKT 

        70         80         90        100        110        120 
FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ LFEGMKAFKG KDQQVRLFRP 

       130        140        150        160        170        180 
WLNMDRMLRS AMRLCLPSFD KLELLECIRR LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL 

       190        200        210        220        230        240 
GVSQPTRALL FVILCPVGAY FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV 

       250        260        270        280        290        300 
QQEALKRGCE QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS 

       310        320        330        340        350        360 
LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI LYKDRNLHIP 

       370        380        390 
TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV 

« Hide

Isoform B [UniParc].

Checksum: 656A626FEC867073
Show »

FASTA30033,777

References

« Hide 'large scale' references
[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. 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] (ISOFORM A).
Tissue: Heart.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12735.1. [O15382-1]
CCDS54290.1. [O15382-2]
RefSeqNP_001158245.1. NM_001164773.1. [O15382-2]
NP_001181.2. NM_001190.3. [O15382-1]
NP_001271254.1. NM_001284325.1.
UniGeneHs.512670.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO15382.
SMRO15382. Positions 30-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107062. 7 interactions.
IntActO15382. 3 interactions.
STRING9606.ENSP00000322991.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00167. L-Isoleucine.
DB00149. L-Leucine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteO15382.

Proteomic databases

MaxQBO15382.
PaxDbO15382.
PRIDEO15382.

Protocols and materials databases

DNASU587.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316273; ENSP00000322991; ENSG00000105552. [O15382-1]
ENST00000545387; ENSP00000440973; ENSG00000105552. [O15382-2]
GeneID587.
KEGGhsa:587.
UCSCuc002pkq.4. human. [O15382-1]
uc002pkt.3. human. [O15382-2]

Organism-specific databases

CTD587.
GeneCardsGC19M049298.
HGNCHGNC:977. BCAT2.
HPAHPA054091.
MIM113530. gene.
neXtProtNX_O15382.
PharmGKBPA25289.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0115.
HOGENOMHOG000276704.
HOVERGENHBG050678.
InParanoidO15382.
KOK00826.
OrthoDBEOG7NGQB7.
PhylomeDBO15382.
TreeFamTF300882.

Enzyme and pathway databases

BRENDA2.6.1.42. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKO15382.

Gene expression databases

ArrayExpressO15382.
BgeeO15382.
CleanExHS_BCAT2.
GenevestigatorO15382.

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

EvolutionaryTraceO15382.
GenomeRNAi587.
NextBio2399.
PROO15382.
SOURCESearch...

Entry information

Entry nameBCAT2_HUMAN
AccessionPrimary (citable) accession number: O15382
Secondary accession number(s): B2RB87 expand/collapse secondary AC list , O00269, Q96KG1, Q9BTB6, Q9BUU6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 144 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM