P54687 (BCAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 2-oxoglutaric acid + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid. 2-oxoglutaric acid + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamic acid.
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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Traceable author statement. Source: ProtInc branched chain family amino acid biosynthetic process Traceable author statement. Source: ProtInc branched chain family amino acid catabolic process Traceable author statement. Source: Reactome cell proliferation Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	L-isoleucine transaminase activity Inferred from electronic annotation. Source: EC L-leucine transaminase activity Inferred from electronic annotation. Source: EC L-valine transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Branched-chain-amino-acid aminotransferase, cytosolic

PRO_0000103292

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.4

Modified residue

222

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant

59

1

T → M.
Corresponds to variant rs17374285 [ dbSNP | Ensembl ].

VAR_047681

Natural variant

321

1

E → K.
Corresponds to variant rs7313020 [ dbSNP | Ensembl ].

VAR_019614

Natural variant

330

1

G → S. Ref.1
Corresponds to variant rs1057204 [ dbSNP | Ensembl ].

VAR_047682

Experimental info

Sequence conflict

2

1

Missing in AAB08528. Ref.1

Sequence conflict

8

1

Missing in AAB08528. Ref.1

Sequence conflict

165

1

T → A in AAB08528. Ref.1

Sequence conflict

237

1

A → D in AAB08528. Ref.1

Sequence conflict

251

1

E → R in AAB08528. Ref.1

Sequence conflict

317

1

T → S in BAB71129. Ref.2

Secondary structure

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386

Helix Strand Turn

Details...

Helix

27 – 29

3

Helix

44 – 46

3

Turn

49 – 51

3

Beta strand

55 – 63

9

Turn

64 – 66

3

Beta strand

72 – 75

4

Beta strand

79 – 81

3

Helix

86 – 89

4

Beta strand

93 – 95

3

Beta strand

98 – 102

5

Beta strand

108 – 112

5

Helix

113 – 127

15

Helix

134 – 147

14

Helix

149 – 151

3

Beta strand

154 – 157

4

Beta strand

159 – 168

10

Beta strand

179 – 190

12

Beta strand

202 – 205

4

Helix

225 – 228

4

Helix

231 – 239

9

Beta strand

243 – 249

7

Turn

250 – 253

4

Beta strand

254 – 258

5

Beta strand

261 – 268

8

Beta strand

274 – 278

5

Beta strand

282 – 285

4

Helix

289 – 301

13

Beta strand

303 – 308

6

Helix

313 – 321

9

Beta strand

325 – 332

8

Turn

333 – 335

3

Beta strand

336 – 345

10

Beta strand

348 – 351

4

Helix

355 – 357

3

Helix

360 – 373

14

Beta strand

382 – 384

3

Sequences

	Sequence		Length	Mass (Da)
	P54687 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: A43535303A702512	FASTA	386	42,966
	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

References

	« Hide 'large scale' referencesShow '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: 8692959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"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: 16141215] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GABAPENTIN.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U21551 mRNA. Translation: AAB08528.1.
AK056255 mRNA. Translation: BAB71129.1.
AC023796 Genomic DNA. No translation available.
AC026310 Genomic DNA. No translation available.
AC092867 Genomic DNA. No translation available.

IPI

IPI00382412.

RefSeq

NP_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.

UniGene

Hs.438993.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P54687.

SMR

P54687. Positions 24-385.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1180265.

STRING

P54687.

Polymorphism databases

DMDM

215274162.

Proteomic databases

PRIDE

P54687.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261192; ENSP00000261192; ENSG00000060982.

GeneID

586.

KEGG

hsa:586.

Organism-specific databases

CTD

586.

GeneCards

GC12M024868.

H-InvDB

HIX0010492.

HGNC

HGNC:976. BCAT1.

MIM

113520. gene.

neXtProt

NX_P54687.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04227.

HOVERGEN

HBG050678.

InParanoid

P54687.

OMA

DLAHQWG.

OrthoDB

EOG4BZN2N.

PhylomeDB

P54687.

Enzyme and pathway databases

BRENDA

2.6.1.42. 4472.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P54687.

Bgee

P54687.

CleanEx

HS_BCAT1.

Genevestigator

P54687.

GermOnline

ENSG00000060982. Homo sapiens.

Family and domain databases

InterPro

IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]

KO

K00826.

PANTHER

PTHR11825. Aminotrans_IV. 1 hit.
PTHR11825:SF2. B_amino_transII. 1 hit.

Pfam

PF01063. Aminotran_4. 1 hit.
[Graphical view]

PIRSF

PIRSF006468. BCAT1. 1 hit.

SUPFAM

SSF56752. Aminotrans_IV. 1 hit.

TIGRFAMs

TIGR01123. IlvE_II. 1 hit.

PROSITE

PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00996. Gabapentin.
DB00142. L-Glutamic Acid.
DB00167. L-Isoleucine.
DB00149. L-Leucine.
DB00161. L-Valine.
DB00114. Pyridoxal Phosphate.

SOURCE

Search...

Entry information

Entry name

BCAT1_HUMAN

Accession

Primary (citable) accession number: P54687
Secondary accession number(s): Q96MY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.