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O15382

- BCAT2_HUMAN

UniProt

O15382 - BCAT2_HUMAN

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Protein

Branched-chain-amino-acid aminotransferase, mitochondrial

Gene

BCAT2

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. May also function as a transporter of branched chain alpha-keto acids.

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681Substrate

GO - Molecular functioni

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

GO - Biological processi

  1. branched-chain amino acid biosynthetic process Source: ProtInc
  2. branched-chain amino acid catabolic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. isoleucine catabolic process Source: Ensembl
  5. leucine metabolic process Source: Ensembl
  6. regulation of hormone levels Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. valine metabolic process Source: Ensembl
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. 2681.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKO15382.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase, mitochondrial (EC:2.6.1.42)
Short name:
BCAT(m)
Alternative name(s):
Placental protein 18
Short name:
PP18
Gene namesi
Name:BCAT2
Synonyms:BCATM, BCT2, ECA40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:977. BCAT2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi342 – 3421C → A: Reduces activity about 6-fold. 1 Publication
Mutagenesisi345 – 3451C → A: Slight reduction of activity. 1 Publication

Organism-specific databases

PharmGKBiPA25289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionAdd
BLAST
Chaini28 – 392365Branched-chain-amino-acid aminotransferase, mitochondrialPRO_0000001271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291N6-(pyridoxal phosphate)lysine
Modified residuei321 – 3211N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO15382.
PaxDbiO15382.
PRIDEiO15382.

PTM databases

PhosphoSiteiO15382.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO15382.
CleanExiHS_BCAT2.
ExpressionAtlasiO15382. baseline and differential.
GenevestigatoriO15382.

Organism-specific databases

HPAiHPA054091.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi107062. 8 interactions.
IntActiO15382. 3 interactions.
STRINGi9606.ENSP00000322991.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363Combined sources
Beta strandi51 – 533Combined sources
Turni57 – 593Combined sources
Beta strandi63 – 719Combined sources
Beta strandi72 – 754Combined sources
Beta strandi79 – 835Combined sources
Beta strandi86 – 883Combined sources
Helixi93 – 964Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi115 – 1195Combined sources
Helixi120 – 13314Combined sources
Helixi141 – 15414Combined sources
Helixi156 – 1583Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 17510Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi186 – 19712Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi209 – 2135Combined sources
Helixi231 – 2333Combined sources
Turni234 – 2363Combined sources
Helixi237 – 24610Combined sources
Beta strandi250 – 2567Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi268 – 2758Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi289 – 2924Combined sources
Helixi296 – 30813Combined sources
Beta strandi310 – 3156Combined sources
Helixi320 – 3289Combined sources
Beta strandi332 – 3398Combined sources
Turni340 – 3423Combined sources
Beta strandi343 – 35210Combined sources
Beta strandi355 – 3584Combined sources
Helixi362 – 3643Combined sources
Helixi367 – 38014Combined sources
Beta strandi389 – 3913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO15382.
SMRiO15382. Positions 30-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15382.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0115.
GeneTreeiENSGT00390000009532.
HOGENOMiHOG000276704.
HOVERGENiHBG050678.
InParanoidiO15382.
KOiK00826.
OrthoDBiEOG7NGQB7.
PhylomeDBiO15382.
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 (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: O15382-1) [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

        10         20         30         40         50
MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG
60 70 80 90 100
PGEPLVFGKT FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ
110 120 130 140 150
LFEGMKAFKG KDQQVRLFRP WLNMDRMLRS AMRLCLPSFD KLELLECIRR
160 170 180 190 200
LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL GVSQPTRALL FVILCPVGAY
210 220 230 240 250
FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV QQEALKRGCE
260 270 280 290 300
QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS
310 320 330 340 350
LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI
360 370 380 390
LYKDRNLHIP TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV
Length:392
Mass (Da):44,288
Last modified:May 2, 2002 - v2
Checksum:iEC07047264B190DA
GO
Isoform B (identifier: O15382-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:300
Mass (Da):33,777
Checksum:i656A626FEC867073
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541V → L in AAB53087. (PubMed:8702755)Curated
Sequence conflicti207 – 2071T → N in AAB53087. (PubMed:8702755)Curated
Sequence conflicti214 – 2163DPA → EPT in AAB53087. (PubMed:8702755)Curated
Sequence conflicti253 – 2531L → F in AAB53087. (PubMed:8702755)Curated
Sequence conflicti326 – 3261A → P in AAB53087. (PubMed:8702755)Curated
Sequence conflicti330 – 3301G → A in AAB53087. (PubMed:8702755)Curated
Sequence conflicti349 – 3491R → G in AAB53087. (PubMed:8702755)Curated
Sequence conflicti357 – 3571L → F in AAB53087. (PubMed:8702755)Curated
Sequence conflicti370 – 3701L → F in AAB53087. (PubMed:8702755)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861T → R.2 Publications
Corresponds to variant rs11548193 [ dbSNP | Ensembl ].
VAR_048234

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 10092Missing in isoform B. 1 PublicationVSP_000236Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12735.1. [O15382-1]
CCDS54290.1. [O15382-2]
RefSeqiNP_001158245.1. NM_001164773.1. [O15382-2]
NP_001181.2. NM_001190.3. [O15382-1]
NP_001271254.1. NM_001284325.1.
UniGeneiHs.512670.

Genome annotation databases

EnsembliENST00000316273; ENSP00000322991; ENSG00000105552. [O15382-1]
ENST00000545387; ENSP00000440973; ENSG00000105552. [O15382-2]
GeneIDi587.
KEGGihsa:587.
UCSCiuc002pkq.4. human. [O15382-1]
uc002pkt.3. human. [O15382-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS12735.1. [O15382-1 ]
CCDS54290.1. [O15382-2 ]
RefSeqi NP_001158245.1. NM_001164773.1. [O15382-2 ]
NP_001181.2. NM_001190.3. [O15382-1 ]
NP_001271254.1. NM_001284325.1.
UniGenei Hs.512670.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EKF X-ray 1.95 A/B 28-392 [» ]
1EKP X-ray 2.50 A/B 28-392 [» ]
1EKV X-ray 2.25 A/B 28-392 [» ]
1KT8 X-ray 1.90 A/B 28-392 [» ]
1KTA X-ray 1.90 A/B 28-392 [» ]
2A1H X-ray 1.80 A/B 28-392 [» ]
2HDK X-ray 2.40 A/B 28-392 [» ]
2HG8 X-ray 1.80 A/B 28-392 [» ]
2HGW X-ray 1.98 A/B 28-392 [» ]
2HGX X-ray 1.80 A/B 28-392 [» ]
2HHF X-ray 1.80 A/B 28-392 [» ]
ProteinModelPortali O15382.
SMRi O15382. Positions 30-392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107062. 8 interactions.
IntActi O15382. 3 interactions.
STRINGi 9606.ENSP00000322991.

Chemistry

DrugBanki DB00167. L-Isoleucine.
DB00149. L-Leucine.

PTM databases

PhosphoSitei O15382.

Proteomic databases

MaxQBi O15382.
PaxDbi O15382.
PRIDEi O15382.

Protocols and materials databases

DNASUi 587.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316273 ; ENSP00000322991 ; ENSG00000105552 . [O15382-1 ]
ENST00000545387 ; ENSP00000440973 ; ENSG00000105552 . [O15382-2 ]
GeneIDi 587.
KEGGi hsa:587.
UCSCi uc002pkq.4. human. [O15382-1 ]
uc002pkt.3. human. [O15382-2 ]

Organism-specific databases

CTDi 587.
GeneCardsi GC19M049298.
HGNCi HGNC:977. BCAT2.
HPAi HPA054091.
MIMi 113530. gene.
neXtProti NX_O15382.
PharmGKBi PA25289.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0115.
GeneTreei ENSGT00390000009532.
HOGENOMi HOG000276704.
HOVERGENi HBG050678.
InParanoidi O15382.
KOi K00826.
OrthoDBi EOG7NGQB7.
PhylomeDBi O15382.
TreeFami TF300882.

Enzyme and pathway databases

BRENDAi 2.6.1.42. 2681.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK O15382.

Miscellaneous databases

ChiTaRSi BCAT2. human.
EvolutionaryTracei O15382.
GenomeRNAii 587.
NextBioi 2399.
PROi O15382.
SOURCEi Search...

Gene expression databases

Bgeei O15382.
CleanExi HS_BCAT2.
ExpressionAtlasi O15382. baseline and differential.
Genevestigatori O15382.

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. "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.
    , 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. 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. 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.

Entry informationi

Entry nameiBCAT2_HUMAN
AccessioniPrimary (citable) accession number: O15382
Secondary accession number(s): B2RB87
, O00269, Q96KG1, Q9BTB6, Q9BUU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: November 26, 2014
This is version 148 of the entry and version 2 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 19
    Human chromosome 19: 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