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P21953

- ODBB_HUMAN

UniProt

P21953 - ODBB_HUMAN

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Protein

2-oxoisovalerate dehydrogenase subunit beta, mitochondrial

Gene

BCKDHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.

GO - Molecular functioni

  1. 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Source: ProtInc
  2. alpha-ketoacid dehydrogenase activity Source: Ensembl
  3. carboxy-lyase activity Source: HGNC

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: HGNC
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. response to cAMP Source: Ensembl
  4. response to glucocorticoid Source: Ensembl
  5. response to nutrient Source: Ensembl
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12006.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKP21953.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC:1.2.4.4)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name:
BCKDE1B
Short name:
BCKDH E1-beta
Gene namesi
Name:BCKDHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:987. BCKDHB.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Maple syrup urine disease 1B (MSUD1B) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701R → H in MSUD1B. 1 Publication
VAR_068348
Natural varianti183 – 1831R → P in MSUD1B. 1 Publication
Corresponds to variant rs28934895 [ dbSNP | Ensembl ].
VAR_024851
Natural varianti206 – 2061H → R in MSUD1B. 1 Publication
VAR_004974
Natural varianti278 – 2781G → S in MSUD1B. 1 Publication
VAR_024852
Natural varianti346 – 3461Q → R in MSUD1B. 1 Publication
VAR_068349

Keywords - Diseasei

Disease mutation, Maple syrup urine disease

Organism-specific databases

MIMi248600. phenotype.
Orphaneti268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBiPA25298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionAdd
BLAST
Chaini51 – 3923422-oxoisovalerate dehydrogenase subunit beta, mitochondrialPRO_0000020470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21953.
PaxDbiP21953.
PeptideAtlasiP21953.
PRIDEiP21953.

2D gel databases

REPRODUCTION-2DPAGEIPI00011276.

PTM databases

PhosphoSiteiP21953.

Expressioni

Gene expression databases

BgeeiP21953.
CleanExiHS_BCKDHB.
ExpressionAtlasiP21953. baseline and differential.
GenevestigatoriP21953.

Organism-specific databases

HPAiHPA031580.

Interactioni

Subunit structurei

Heterotetramer of 2 alpha and 2 beta chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
BCKDHAP1269414EBI-1029067,EBI-1029053

Protein-protein interaction databases

BioGridi107066. 4 interactions.
DIPiDIP-6147N.
IntActiP21953. 1 interaction.
MINTiMINT-271857.
STRINGi9606.ENSP00000318351.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi68 – 714
Helixi73 – 8715
Beta strandi92 – 954
Turni96 – 1016
Turni106 – 1094
Helixi110 – 1145
Turni116 – 1183
Beta strandi119 – 1213
Helixi126 – 13813
Beta strandi143 – 1464
Helixi150 – 1523
Helixi154 – 1563
Helixi157 – 1615
Helixi164 – 1663
Helixi167 – 1704
Turni171 – 1733
Beta strandi180 – 1878
Helixi193 – 1953
Helixi201 – 2055
Beta strandi211 – 2133
Helixi218 – 23013
Beta strandi231 – 2333
Beta strandi235 – 2406
Helixi241 – 2433
Turni244 – 2463
Beta strandi249 – 2546
Beta strandi264 – 2674
Beta strandi270 – 2767
Helixi280 – 29516
Beta strandi299 – 3035
Beta strandi306 – 3094
Helixi312 – 32211
Beta strandi325 – 3339
Helixi337 – 34913
Helixi350 – 3523
Beta strandi358 – 3625
Helixi372 – 3754
Helixi379 – 39012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTWX-ray2.70B51-392[»]
1OLSX-ray1.85B51-392[»]
1OLUX-ray1.90B51-392[»]
1OLXX-ray2.25B51-392[»]
1U5BX-ray1.83B51-392[»]
1V11X-ray1.95B51-392[»]
1V16X-ray1.90B51-392[»]
1V1MX-ray2.00B51-392[»]
1V1RX-ray1.80B51-392[»]
1WCIX-ray1.84B51-392[»]
1X7WX-ray1.73B51-392[»]
1X7XX-ray2.10B51-392[»]
1X7YX-ray1.57B51-392[»]
1X7ZX-ray1.72B51-392[»]
1X80X-ray2.00B51-392[»]
2BEUX-ray1.89B51-392[»]
2BEVX-ray1.80B51-392[»]
2BEWX-ray1.79B51-392[»]
2BFBX-ray1.77B51-392[»]
2BFCX-ray1.64B51-392[»]
2BFDX-ray1.39B51-392[»]
2BFEX-ray1.69B51-392[»]
2BFFX-ray1.46B51-392[»]
2J9FX-ray1.88B/D51-392[»]
ProteinModelPortaliP21953.
SMRiP21953. Positions 64-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21953.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281451.
HOVERGENiHBG108210.
InParanoidiP21953.
KOiK00167.
OMAiDKHRCLA.
OrthoDBiEOG79SDXF.
PhylomeDBiP21953.
TreeFamiTF105947.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

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 1 (identifier: P21953-1) [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
MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ
60 70 80 90 100
VAHFTFQPDP EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF
110 120 130 140 150
GGVFRCTVGL RDKYGKDRVF NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA
160 170 180 190 200
DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL TIRSPWGCVG HGALYHSQSP
210 220 230 240 250
EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP KILYRAAAEE
260 270 280 290 300
VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE
310 320 330 340 350
VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF
360 370 380 390
LNLEAPISRV CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY
Length:392
Mass (Da):43,122
Last modified:August 1, 1992 - v2
Checksum:iD78097834D063BB7
GO
Isoform 2 (identifier: P21953-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-218: VVIPRSP → IKVISLS
     219-392: Missing.

Note: No experimental confirmation available.

Show »
Length:218
Mass (Da):23,550
Checksum:iFF30CBDA08FEF0F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 234EGHW → RLPP(PubMed:2335211)Curated
Sequence conflicti322 – 3221T → S in CAA36685. (PubMed:2335211)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411T → I.
Corresponds to variant rs35470366 [ dbSNP | Ensembl ].
VAR_050437
Natural varianti170 – 1701R → H in MSUD1B. 1 Publication
VAR_068348
Natural varianti183 – 1831R → P in MSUD1B. 1 Publication
Corresponds to variant rs28934895 [ dbSNP | Ensembl ].
VAR_024851
Natural varianti206 – 2061H → R in MSUD1B. 1 Publication
VAR_004974
Natural varianti278 – 2781G → S in MSUD1B. 1 Publication
VAR_024852
Natural varianti346 – 3461Q → R in MSUD1B. 1 Publication
VAR_068349

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 2187VVIPRSP → IKVISLS in isoform 2. 1 PublicationVSP_056370
Alternative sequencei219 – 392174Missing in isoform 2. 1 PublicationVSP_056371Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55575 mRNA. Translation: AAA51812.1.
D90391 Genomic DNA. Translation: BAA14389.1.
AK289977 mRNA. Translation: BAF82666.1.
BT020063 mRNA. Translation: AAV38866.1.
AL049696, AL391595 Genomic DNA. Translation: CAC36881.2.
AL391595, AL049696 Genomic DNA. Translation: CAI15049.1.
CH471051 Genomic DNA. Translation: EAW48696.1.
CH471051 Genomic DNA. Translation: EAW48697.1.
CH471051 Genomic DNA. Translation: EAW48698.1.
BC034481 mRNA. Translation: AAH34481.1.
BC040139 mRNA. Translation: AAH40139.1.
U50708 mRNA. Translation: AAB16763.1.
X52446 mRNA. Translation: CAA36685.1.
CCDSiCCDS4994.1. [P21953-1]
PIRiA37157.
RefSeqiNP_000047.1. NM_000056.3.
NP_898871.1. NM_183050.2.
UniGeneiHs.654441.

Genome annotation databases

EnsembliENST00000320393; ENSP00000318351; ENSG00000083123. [P21953-1]
ENST00000356489; ENSP00000348880; ENSG00000083123. [P21953-1]
ENST00000369760; ENSP00000358775; ENSG00000083123. [P21953-2]
ENST00000545529; ENSP00000443564; ENSG00000083123. [P21953-2]
GeneIDi594.
KEGGihsa:594.
UCSCiuc003pjd.2. human. [P21953-1]

Polymorphism databases

DMDMi129034.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55575 mRNA. Translation: AAA51812.1 .
D90391 Genomic DNA. Translation: BAA14389.1 .
AK289977 mRNA. Translation: BAF82666.1 .
BT020063 mRNA. Translation: AAV38866.1 .
AL049696 , AL391595 Genomic DNA. Translation: CAC36881.2 .
AL391595 , AL049696 Genomic DNA. Translation: CAI15049.1 .
CH471051 Genomic DNA. Translation: EAW48696.1 .
CH471051 Genomic DNA. Translation: EAW48697.1 .
CH471051 Genomic DNA. Translation: EAW48698.1 .
BC034481 mRNA. Translation: AAH34481.1 .
BC040139 mRNA. Translation: AAH40139.1 .
U50708 mRNA. Translation: AAB16763.1 .
X52446 mRNA. Translation: CAA36685.1 .
CCDSi CCDS4994.1. [P21953-1 ]
PIRi A37157.
RefSeqi NP_000047.1. NM_000056.3.
NP_898871.1. NM_183050.2.
UniGenei Hs.654441.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DTW X-ray 2.70 B 51-392 [» ]
1OLS X-ray 1.85 B 51-392 [» ]
1OLU X-ray 1.90 B 51-392 [» ]
1OLX X-ray 2.25 B 51-392 [» ]
1U5B X-ray 1.83 B 51-392 [» ]
1V11 X-ray 1.95 B 51-392 [» ]
1V16 X-ray 1.90 B 51-392 [» ]
1V1M X-ray 2.00 B 51-392 [» ]
1V1R X-ray 1.80 B 51-392 [» ]
1WCI X-ray 1.84 B 51-392 [» ]
1X7W X-ray 1.73 B 51-392 [» ]
1X7X X-ray 2.10 B 51-392 [» ]
1X7Y X-ray 1.57 B 51-392 [» ]
1X7Z X-ray 1.72 B 51-392 [» ]
1X80 X-ray 2.00 B 51-392 [» ]
2BEU X-ray 1.89 B 51-392 [» ]
2BEV X-ray 1.80 B 51-392 [» ]
2BEW X-ray 1.79 B 51-392 [» ]
2BFB X-ray 1.77 B 51-392 [» ]
2BFC X-ray 1.64 B 51-392 [» ]
2BFD X-ray 1.39 B 51-392 [» ]
2BFE X-ray 1.69 B 51-392 [» ]
2BFF X-ray 1.46 B 51-392 [» ]
2J9F X-ray 1.88 B/D 51-392 [» ]
ProteinModelPortali P21953.
SMRi P21953. Positions 64-392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107066. 4 interactions.
DIPi DIP-6147N.
IntActi P21953. 1 interaction.
MINTi MINT-271857.
STRINGi 9606.ENSP00000318351.

PTM databases

PhosphoSitei P21953.

Polymorphism databases

DMDMi 129034.

2D gel databases

REPRODUCTION-2DPAGE IPI00011276.

Proteomic databases

MaxQBi P21953.
PaxDbi P21953.
PeptideAtlasi P21953.
PRIDEi P21953.

Protocols and materials databases

DNASUi 594.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320393 ; ENSP00000318351 ; ENSG00000083123 . [P21953-1 ]
ENST00000356489 ; ENSP00000348880 ; ENSG00000083123 . [P21953-1 ]
ENST00000369760 ; ENSP00000358775 ; ENSG00000083123 . [P21953-2 ]
ENST00000545529 ; ENSP00000443564 ; ENSG00000083123 . [P21953-2 ]
GeneIDi 594.
KEGGi hsa:594.
UCSCi uc003pjd.2. human. [P21953-1 ]

Organism-specific databases

CTDi 594.
GeneCardsi GC06P080816.
GeneReviewsi BCKDHB.
HGNCi HGNC:987. BCKDHB.
HPAi HPA031580.
MIMi 248600. phenotype.
248611. gene.
neXtProti NX_P21953.
Orphaneti 268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBi PA25298.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0022.
GeneTreei ENSGT00530000063423.
HOGENOMi HOG000281451.
HOVERGENi HBG108210.
InParanoidi P21953.
KOi K00167.
OMAi DKHRCLA.
OrthoDBi EOG79SDXF.
PhylomeDBi P21953.
TreeFami TF105947.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-12006.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK P21953.

Miscellaneous databases

ChiTaRSi BCKDHB. human.
EvolutionaryTracei P21953.
GeneWikii BCKDHB.
GenomeRNAii 594.
NextBioi 2413.
PROi P21953.
SOURCEi Search...

Gene expression databases

Bgeei P21953.
CleanExi HS_BCKDHB.
ExpressionAtlasi P21953. baseline and differential.
Genevestigatori P21953.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease."
    Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H., Nobukuni Y.
    J. Clin. Invest. 86:242-247(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences."
    Chuang J.L., Cox R.P., Chuang D.T.
    Am. J. Hum. Genet. 58:1373-1377(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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 1).
    Tissue: Hippocampus.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye and Testis.
  8. "Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex."
    Chuang J.L., Cox R.P., Chuang D.T.
    FEBS Lett. 262:305-309(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-392 (ISOFORM 1).
  9. "Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."
    Wynn R.M., Kochi H., Cox R.P., Chuang D.T.
    Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 36-62.
  10. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex."
    Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y., Endo F., Matsuda I.
    Biochim. Biophys. Acta 1225:64-70(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1B ARG-206.
  13. "Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population."
    Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E., Diaz G.A.
    Am. J. Hum. Genet. 69:863-868(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD1B PRO-183 AND SER-278.
  14. "Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic form of maple syrup urine disease (MSUD)."
    Wang Y.P., Qi M.L., Li T.T., Zhao Y.J.
    Gene 498:112-115(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD1B HIS-170 AND ARG-346.

Entry informationi

Entry nameiODBB_HUMAN
AccessioniPrimary (citable) accession number: P21953
Secondary accession number(s): Q5T2J3, Q9BQL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 161 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

External Data

Dasty 3