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P54687

- BCAT1_HUMAN

UniProt

P54687 - BCAT1_HUMAN

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Protein
Branched-chain-amino-acid aminotransferase, cytosolic
Gene
BCAT1, BCT1, ECA39
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. L-isoleucine transaminase activity Source: UniProtKB-EC
  2. L-leucine transaminase activity Source: UniProtKB-EC
  3. L-valine transaminase activity Source: UniProtKB-EC
  4. branched-chain-amino-acid transaminase activity Source: Reactome
Complete GO annotation...

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: ProtInc
  2. branched-chain amino acid biosynthetic process Source: ProtInc
  3. branched-chain amino acid catabolic process Source: Reactome
  4. cell proliferation Source: ProtInc
  5. cellular nitrogen compound metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.42. 4472.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKP54687.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase, cytosolic (EC:2.6.1.42)
Short name:
BCAT(c)
Alternative name(s):
Protein ECA39
Gene namesi
Name:BCAT1
Synonyms:BCT1, ECA39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:976. BCAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Branched-chain-amino-acid aminotransferase, cytosolic
PRO_0000103292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei222 – 2221N6-(pyridoxal phosphate)lysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54687.
PaxDbiP54687.
PRIDEiP54687.

PTM databases

PhosphoSiteiP54687.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP54687.
BgeeiP54687.
CleanExiHS_BCAT1.
GenevestigatoriP54687.

Organism-specific databases

HPAiHPA048592.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi107061. 12 interactions.
IntActiP54687. 3 interactions.
MINTiMINT-1180265.
STRINGi9606.ENSP00000261192.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293
Helixi44 – 463
Turni49 – 513
Beta strandi55 – 639
Turni64 – 663
Beta strandi72 – 754
Beta strandi79 – 813
Helixi86 – 894
Beta strandi93 – 953
Beta strandi98 – 1025
Beta strandi108 – 1125
Helixi113 – 12614
Helixi134 – 14714
Helixi149 – 1513
Beta strandi154 – 1574
Beta strandi159 – 16810
Beta strandi179 – 19012
Beta strandi202 – 2065
Helixi225 – 2284
Helixi231 – 2388
Turni239 – 2413
Beta strandi243 – 2497
Turni250 – 2534
Beta strandi254 – 2585
Beta strandi261 – 2688
Beta strandi274 – 2785
Beta strandi282 – 2854
Helixi289 – 30113
Beta strandi303 – 3086
Helixi313 – 3208
Turni321 – 3233
Beta strandi325 – 3328
Turni333 – 3353
Beta strandi336 – 35116
Helixi353 – 3575
Helixi360 – 37314
Beta strandi382 – 3843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP54687.
SMRiP54687. Positions 24-385.

Miscellaneous databases

EvolutionaryTraceiP54687.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276704.
HOVERGENiHBG050678.
InParanoidiP54687.
KOiK00826.
OMAiALECFEG.
OrthoDBiEOG7NGQB7.
PhylomeDBiP54687.
TreeFamiTF300882.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54687-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG    50
TVFTDHMLTV EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA 100
FRGVDNKIRL FQPNLNMDRM YRSAVRATLP VFDKEELLEC IQQLVKLDQE 150
WVPYSTSASL YIRPTFIGTE PSLGVKKPTK ALLFVLLSPV GPYFSSGTFN 200
PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN GCQQVLWLYG 250
EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ 300
WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI 350
HIPTMENGPK LASRILSKLT DIQYGREESD WTIVLS 386
Length:386
Mass (Da):42,966
Last modified:November 25, 2008 - v3
Checksum:iA43535303A702512
GO
Isoform 2 (identifier: P54687-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MKDCSNGCSAECTGEGGSKEVVGTF → M
     94-130: Missing.

Note: No experimental confirmation available.

Show »
Length:325
Mass (Da):36,298
Checksum:iFDC0B4CC0356E91D
GO
Isoform 3 (identifier: P54687-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     94-130: Missing.

Note: No experimental confirmation available.

Show »
Length:349
Mass (Da):38,645
Checksum:i1179C4AB4AD1B455
GO
Isoform 4 (identifier: P54687-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → M

Note: No experimental confirmation available.

Show »
Length:385
Mass (Da):42,838
Checksum:i4713DD9AF2134746
GO
Isoform 5 (identifier: P54687-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → MASPLRSAAALARQ

Note: No experimental confirmation available.

Show »
Length:398
Mass (Da):44,131
Checksum:i39780ADB0CF85D5A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591T → M.
Corresponds to variant rs17374285 [ dbSNP | Ensembl ].
VAR_047681
Natural varianti321 – 3211E → K.
Corresponds to variant rs7313020 [ dbSNP | Ensembl ].
VAR_019614
Natural varianti330 – 3301G → S.1 Publication
Corresponds to variant rs1057204 [ dbSNP | Ensembl ].
VAR_047682

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MKDCS…VVGTF → M in isoform 2.
VSP_042651Add
BLAST
Alternative sequencei1 – 22MK → M in isoform 4.
VSP_043560
Alternative sequencei1 – 22MK → MASPLRSAAALARQ in isoform 5.
VSP_046057
Alternative sequencei94 – 13037Missing in isoform 2 and isoform 3.
VSP_042652Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing in AAB08528. 1 Publication
Sequence conflicti8 – 81Missing in AAB08528. 1 Publication
Sequence conflicti165 – 1651T → A in AAB08528. 1 Publication
Sequence conflicti237 – 2371A → D in AAB08528. 1 Publication
Sequence conflicti251 – 2511E → R in AAB08528. 1 Publication
Sequence conflicti300 – 3001Q → P in BAH11911. 1 Publication
Sequence conflicti317 – 3171T → S in BAB71129. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44845.1. [P54687-1]
CCDS53760.1. [P54687-4]
CCDS53761.1. [P54687-5]
CCDS53762.1. [P54687-2]
CCDS53763.1. [P54687-3]
RefSeqiNP_001171562.1. NM_001178091.1. [P54687-3]
NP_001171563.1. NM_001178092.1. [P54687-2]
NP_001171564.1. NM_001178093.1. [P54687-5]
NP_001171565.1. NM_001178094.1. [P54687-4]
NP_005495.2. NM_005504.6. [P54687-1]
UniGeneiHs.438993.

Genome annotation databases

EnsembliENST00000261192; ENSP00000261192; ENSG00000060982. [P54687-1]
ENST00000342945; ENSP00000339805; ENSG00000060982. [P54687-2]
ENST00000538118; ENSP00000440817; ENSG00000060982. [P54687-4]
ENST00000539282; ENSP00000443459; ENSG00000060982. [P54687-5]
ENST00000539780; ENSP00000440827; ENSG00000060982. [P54687-3]
GeneIDi586.
KEGGihsa:586.
UCSCiuc001rgc.3. human. [P54687-4]
uc001rgd.4. human. [P54687-1]
uc001rge.4. human. [P54687-2]
uc010siy.2. human. [P54687-3]

Polymorphism databases

DMDMi215274162.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS44845.1. [P54687-1 ]
CCDS53760.1. [P54687-4 ]
CCDS53761.1. [P54687-5 ]
CCDS53762.1. [P54687-2 ]
CCDS53763.1. [P54687-3 ]
RefSeqi NP_001171562.1. NM_001178091.1. [P54687-3 ]
NP_001171563.1. NM_001178092.1. [P54687-2 ]
NP_001171564.1. NM_001178093.1. [P54687-5 ]
NP_001171565.1. NM_001178094.1. [P54687-4 ]
NP_005495.2. NM_005504.6. [P54687-1 ]
UniGenei Hs.438993.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P54687.
SMRi P54687. Positions 24-385.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107061. 12 interactions.
IntActi P54687. 3 interactions.
MINTi MINT-1180265.
STRINGi 9606.ENSP00000261192.

Chemistry

BindingDBi P54687.
ChEMBLi CHEMBL4679.
DrugBanki DB00996. Gabapentin.
DB00142. L-Glutamic Acid.
DB00167. L-Isoleucine.
DB00149. L-Leucine.
DB00161. L-Valine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei P54687.

Polymorphism databases

DMDMi 215274162.

Proteomic databases

MaxQBi P54687.
PaxDbi P54687.
PRIDEi P54687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261192 ; ENSP00000261192 ; ENSG00000060982 . [P54687-1 ]
ENST00000342945 ; ENSP00000339805 ; ENSG00000060982 . [P54687-2 ]
ENST00000538118 ; ENSP00000440817 ; ENSG00000060982 . [P54687-4 ]
ENST00000539282 ; ENSP00000443459 ; ENSG00000060982 . [P54687-5 ]
ENST00000539780 ; ENSP00000440827 ; ENSG00000060982 . [P54687-3 ]
GeneIDi 586.
KEGGi hsa:586.
UCSCi uc001rgc.3. human. [P54687-4 ]
uc001rgd.4. human. [P54687-1 ]
uc001rge.4. human. [P54687-2 ]
uc010siy.2. human. [P54687-3 ]

Organism-specific databases

CTDi 586.
GeneCardsi GC12M024868.
HGNCi HGNC:976. BCAT1.
HPAi HPA048592.
MIMi 113520. gene.
neXtProti NX_P54687.
PharmGKBi PA25288.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0115.
HOGENOMi HOG000276704.
HOVERGENi HBG050678.
InParanoidi P54687.
KOi K00826.
OMAi ALECFEG.
OrthoDBi EOG7NGQB7.
PhylomeDBi P54687.
TreeFami TF300882.

Enzyme and pathway databases

BRENDAi 2.6.1.42. 4472.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK P54687.

Miscellaneous databases

EvolutionaryTracei P54687.
GenomeRNAii 586.
NextBioi 2395.
PROi P54687.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54687.
Bgeei P54687.
CleanExi HS_BCAT1.
Genevestigatori P54687.

Family and domain databases

InterProi IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view ]
PANTHERi PTHR11825. PTHR11825. 1 hit.
Pfami PF01063. Aminotran_4. 1 hit.
[Graphical view ]
PIRSFi PIRSF006468. BCAT1. 1 hit.
SUPFAMi SSF56752. SSF56752. 1 hit.
TIGRFAMsi TIGR01123. ilvE_II. 1 hit.
PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-386 IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiBCAT1_HUMAN
AccessioniPrimary (citable) accession number: P54687
Secondary accession number(s): B3KY27
, B7Z2M5, B7Z5L0, F5H5E4, Q68DQ7, Q96MY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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