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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Traceable author statement Ref.1. Source: ProtInc branched-chain amino acid biosynthetic process Traceable author statement PubMed 6933702. Source: ProtInc branched-chain amino acid catabolic process Traceable author statement. Source: Reactome cell proliferation Traceable author statement PubMed 6933702. Source: ProtInc cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome
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 branched-chain-amino-acid transaminase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

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 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

222

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence

1 – 25

25

MKDCS…VVGTF → M in isoform 2.

VSP_042651

Alternative sequence

1 – 2

2

MK → M in isoform 4.

VSP_043560

Alternative sequence

1 – 2

2

MK → MASPLRSAAALARQ in isoform 5.

VSP_046057

Alternative sequence

94 – 130

37

Missing in isoform 2 and isoform 3.

VSP_042652

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

300

1

Q → P in BAH11911. Ref.2

Sequence conflict

317

1

T → S in BAB71129. Ref.2

Secondary structure

1

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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 – 126

14

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 – 206

5

Helix

225 – 228

4

Helix

231 – 238

8

Turn

239 – 241

3

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 – 320

8

Turn

321 – 323

3

Beta strand

325 – 332

8

Turn

333 – 335

3

Beta strand

336 – 351

16

Helix

353 – 357

5

Helix

360 – 373

14

Beta strand

382 – 384

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: FDC0B4CC0356E91D	FASTA	325	36,298
	10 20 30 40 50 60 MKAKDLIVTP ATILKEKPDP NNLVFGTVFT DHMLTVEWSS EFGWEKPHIK PLQNLSLHPG 70 80 90 100 110 120 SSALHYAVEV FDKEELLECI QQLVKLDQEW VPYSTSASLY IRPTFIGTEP SLGVKKPTKA 130 140 150 160 170 180 LLFVLLSPVG PYFSSGTFNP VSLWANPKYV RAWKGGTGDC KMGGNYGSSL FAQCEAVDNG 190 200 210 220 230 240 CQQVLWLYGE DHQITEVGTM NLFLYWINED GEEELATPPL DGIILPGVTR RCILDLAHQW 250 260 270 280 290 300 GEFKVSERYL TMDDLTTALE GNRVREMFGS GTACVVCPVS DILYKGETIH IPTMENGPKL 310 320 ASRILSKLTD IQYGREESDW TIVLS
	Isoform 3 [UniParc]. Checksum: 1179C4AB4AD1B455	FASTA	349	38,645
	10 20 30 40 50 60 MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG TVFTDHMLTV 70 80 90 100 110 120 EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVEVFDKEEL LECIQQLVKL DQEWVPYSTS 130 140 150 160 170 180 ASLYIRPTFI GTEPSLGVKK PTKALLFVLL SPVGPYFSSG TFNPVSLWAN PKYVRAWKGG 190 200 210 220 230 240 TGDCKMGGNY GSSLFAQCEA VDNGCQQVLW LYGEDHQITE VGTMNLFLYW INEDGEEELA 250 260 270 280 290 300 TPPLDGIILP GVTRRCILDL AHQWGEFKVS ERYLTMDDLT TALEGNRVRE MFGSGTACVV 310 320 330 340 CPVSDILYKG ETIHIPTMEN GPKLASRILS KLTDIQYGRE ESDWTIVLS
	Isoform 4 [UniParc]. Checksum: 4713DD9AF2134746	FASTA	385	42,838
	10 20 30 40 50 60 MDCSNGCSAE CTGEGGSKEV VGTFKAKDLI VTPATILKEK PDPNNLVFGT VFTDHMLTVE 70 80 90 100 110 120 WSSEFGWEKP HIKPLQNLSL HPGSSALHYA VELFEGLKAF RGVDNKIRLF QPNLNMDRMY 130 140 150 160 170 180 RSAVRATLPV FDKEELLECI QQLVKLDQEW VPYSTSASLY IRPTFIGTEP SLGVKKPTKA 190 200 210 220 230 240 LLFVLLSPVG PYFSSGTFNP VSLWANPKYV RAWKGGTGDC KMGGNYGSSL FAQCEAVDNG 250 260 270 280 290 300 CQQVLWLYGE DHQITEVGTM NLFLYWINED GEEELATPPL DGIILPGVTR RCILDLAHQW 310 320 330 340 350 360 GEFKVSERYL TMDDLTTALE GNRVREMFGS GTACVVCPVS DILYKGETIH IPTMENGPKL 370 380 ASRILSKLTD IQYGREESDW TIVLS
	Isoform 5 [UniParc]. Checksum: 39780ADB0CF85D5A	FASTA	398	44,131
	10 20 30 40 50 60 MASPLRSAAA LARQDCSNGC SAECTGEGGS KEVVGTFKAK DLIVTPATIL KEKPDPNNLV 70 80 90 100 110 120 FGTVFTDHML TVEWSSEFGW EKPHIKPLQN LSLHPGSSAL HYAVELFEGL KAFRGVDNKI 130 140 150 160 170 180 RLFQPNLNMD RMYRSAVRAT LPVFDKEELL ECIQQLVKLD QEWVPYSTSA SLYIRPTFIG 190 200 210 220 230 240 TEPSLGVKKP TKALLFVLLS PVGPYFSSGT FNPVSLWANP KYVRAWKGGT GDCKMGGNYG 250 260 270 280 290 300 SSLFAQCEAV DNGCQQVLWL YGEDHQITEV GTMNLFLYWI NEDGEEELAT PPLDGIILPG 310 320 330 340 350 360 VTRRCILDLA HQWGEFKVSE RYLTMDDLTT ALEGNRVREM FGSGTACVVC PVSDILYKGE 370 380 390 TIHIPTMENG PKLASRILSK LTDIQYGREE SDWTIVLS

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] [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]	"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. , 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]	"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].
[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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GABAPENTIN.
[7]	"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. , 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

GeneReviews

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.

IPI

IPI00382412.
IPI00798272.
IPI00940330.
IPI00976652.
IPI00983406.

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.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1180265.

STRING

9606.ENSP00000261192.

PTM databases

PhosphoSite

P54687.

Polymorphism databases

DMDM

215274162.

Proteomic databases

PaxDb

P54687.

PRIDE

P54687.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261192; ENSP00000261192; ENSG00000060982.
ENST00000342945; ENSP00000339805; ENSG00000060982.
ENST00000538118; ENSP00000440817; ENSG00000060982.
ENST00000539282; ENSP00000443459; ENSG00000060982.
ENST00000539780; ENSP00000440827; ENSG00000060982.

GeneID

586.

KEGG

hsa:586.

UCSC

uc001rgd.4. human.

Organism-specific databases

CTD

586.

GeneCards

GC12M024868.

HGNC

HGNC:976. BCAT1.

HPA

HPA048592.

MIM

113520. gene.

neXtProt

NX_P54687.

PharmGKB

PA25288.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0115.

HOGENOM

HOG000276704.

HOVERGEN

HBG050678.

InParanoid

P54687.

KO

K00826.

OrthoDB

EOG4BZN2N.

PhylomeDB

P54687.

Enzyme and pathway databases

BRENDA

2.6.1.42. 4472.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P54687.

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]

PANTHER

PTHR11825. PTHR11825. 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

BindingDB

P54687.

ChEMBL

CHEMBL4679.

DrugBank

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

EvolutionaryTrace

P54687.

GenomeRNAi

586.

NextBio

2395.

SOURCE

Search...

Entry information

Entry name

BCAT1_HUMAN

Accession

Primary (citable) accession number: P54687
Secondary accession number(s): B3KY27 , B7Z2M5, B7Z5L0, F5H5E4, Q68DQ7, Q96MY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 134 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.