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P21953

- ODBB_HUMAN

UniProt

P21953 - ODBB_HUMAN

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
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    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
    4. protein binding Source: IntAct

    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

    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

    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

    ArrayExpressiP21953.
    BgeeiP21953.
    CleanExiHS_BCKDHB.
    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. 2 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.
    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

    MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ    50
    VAHFTFQPDP EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF 100
    GGVFRCTVGL RDKYGKDRVF NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA 150
    DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL TIRSPWGCVG HGALYHSQSP 200
    EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP KILYRAAAEE 250
    VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE 300
    VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF 350
    LNLEAPISRV CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY 392
    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.
    PIRiA37157.
    RefSeqiNP_000047.1. NM_000056.3.
    NP_898871.1. NM_183050.2.
    UniGeneiHs.654441.

    Genome annotation databases

    EnsembliENST00000320393; ENSP00000318351; ENSG00000083123.
    ENST00000356489; ENSP00000348880; ENSG00000083123.
    ENST00000369760; ENSP00000358775; ENSG00000083123.
    GeneIDi594.
    KEGGihsa:594.
    UCSCiuc003pjd.2. human.

    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.
    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. 2 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 .
    ENST00000356489 ; ENSP00000348880 ; ENSG00000083123 .
    ENST00000369760 ; ENSP00000358775 ; ENSG00000083123 .
    GeneIDi 594.
    KEGGi hsa:594.
    UCSCi uc003pjd.2. human.

    Organism-specific databases

    CTDi 594.
    GeneCardsi GC06P080873.
    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.
    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

    ArrayExpressi P21953.
    Bgeei P21953.
    CleanExi HS_BCKDHB.
    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

    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 1, 2014
    This is version 160 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