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P11182

- ODB2_HUMAN

UniProt

P11182 - ODB2_HUMAN

Protein

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Gene

DBT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 3 (01 Jul 1993)
      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). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

    Catalytic activityi

    2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei452 – 4521Sequence Analysis
    Active sitei456 – 4561Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12007.
    BRENDAi2.3.1.168. 2681.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC:2.3.1.168)
    Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase complex component E2
    Short name:
    BCKAD-E2
    Short name:
    BCKADE2
    Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
    Dihydrolipoamide branched chain transacylase
    Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
    Gene namesi
    Name:DBT
    Synonyms:BCATE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2698. DBT.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: ProtInc
    2. mitochondrial matrix Source: Reactome
    3. mitochondrial nucleoid Source: BHF-UCL
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Maple syrup urine disease 2 (MSUD2) [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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981I → M in MSUD2. 1 Publication
    VAR_015099
    Natural varianti276 – 2761F → C in MSUD2. 1 Publication
    VAR_004978
    Natural varianti384 – 3841G → S in MSUD2. 2 Publications
    Corresponds to variant rs12021720 [ dbSNP | Ensembl ].
    VAR_015100

    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.
    PharmGKBiPA27167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6161MitochondrionSequence AnalysisAdd
    BLAST
    Chaini62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialPRO_0000020489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-lipoyllysineBy similarity
    Modified residuei133 – 1331N6-succinyllysineBy similarity
    Modified residuei196 – 1961N6-acetyllysine; alternateBy similarity
    Modified residuei196 – 1961N6-succinyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-acetyllysineBy similarity
    Modified residuei243 – 2431N6-acetyllysineBy similarity
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei261 – 2611N6-succinyllysineBy similarity
    Modified residuei289 – 2891N6-acetyllysine; alternateBy similarity
    Modified residuei289 – 2891N6-succinyllysine; alternateBy similarity
    Modified residuei295 – 2951N6-acetyllysine1 Publication
    Modified residuei304 – 3041N6-acetyllysineBy similarity
    Modified residuei435 – 4351N6-acetyllysineBy similarity
    Modified residuei440 – 4401N6-acetyllysine; alternateBy similarity
    Modified residuei440 – 4401N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP11182.
    PaxDbiP11182.
    PRIDEiP11182.

    PTM databases

    PhosphoSiteiP11182.

    Expressioni

    Gene expression databases

    ArrayExpressiP11182.
    BgeeiP11182.
    CleanExiHS_DBT.
    GenevestigatoriP11182.

    Organism-specific databases

    HPAiHPA026481.
    HPA026485.
    HPA026533.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    BioGridi107997. 10 interactions.
    IntActiP11182. 6 interactions.
    MINTiMINT-1161634.
    STRINGi9606.ENSP00000359151.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi65 – 684
    Beta strandi79 – 846
    Beta strandi94 – 963
    Beta strandi99 – 1024
    Beta strandi107 – 1093
    Beta strandi116 – 1216
    Beta strandi125 – 1295
    Beta strandi133 – 1397
    Helixi175 – 1839
    Helixi188 – 1903
    Helixi196 – 1983
    Helixi202 – 21312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K8MNMR-A62-145[»]
    1K8ONMR-A62-145[»]
    1ZWVNMR-A165-213[»]
    2COONMR-A163-220[»]
    3RNMX-ray2.40E/F165-213[»]
    ProteinModelPortaliP11182.
    SMRiP11182. Positions 62-147, 163-220, 249-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11182.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 13874Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281564.
    HOVERGENiHBG104085.
    InParanoidiP11182.
    KOiK09699.
    OrthoDBiEOG7GFB4W.
    PhylomeDBiP11182.
    TreeFamiTF314182.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR015761. BCKDC_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PANTHERiPTHR23151:SF46. PTHR23151:SF46. 1 hit.
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11182-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP    50
    HHFLKTTAAL RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE 100
    VQSDKASVTI TSRYDGVIKK LYYNLDDIAY VGKPLVDIET EALKDSEEDV 150
    VETPAVSHDE HTHQEIKGRK TLATPAVRRL AMENNIKLSE VVGSGKDGRI 200
    LKEDILNYLE KQTGAILPPS PKVEIMPPPP KPKDMTVPIL VSKPPVFTGK 250
    DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EIDLTELVKL REELKPIAFA 300
    RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT 350
    EQGLIVPNVK NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN 400
    IGSIGGTFAK PVIMPPEVAI GALGSIKAIP RFNQKGEVYK AQIMNVSWSA 450
    DHRVIDGATM SRFSNLWKSY LENPAFMLLD LK 482
    Length:482
    Mass (Da):53,487
    Last modified:July 1, 1993 - v3
    Checksum:iA7CA728C8F33D126
    GO

    Sequence cautioni

    The sequence AAA35589.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAA64512.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti321 – 3211Q → P in AAA64512. (PubMed:2742576)Curated
    Sequence conflicti354 – 3541L → V in AAA64512. (PubMed:2742576)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981I → M in MSUD2. 1 Publication
    VAR_015099
    Natural varianti276 – 2761F → C in MSUD2. 1 Publication
    VAR_004978
    Natural varianti384 – 3841G → S in MSUD2. 2 Publications
    Corresponds to variant rs12021720 [ dbSNP | Ensembl ].
    VAR_015100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66785 mRNA. Translation: CAA47285.1.
    J03208 mRNA. Translation: AAA35589.1. Different initiation.
    M27093 mRNA. Translation: AAA64512.1. Different initiation.
    BT007372 mRNA. Translation: AAP36036.1.
    AL445928 Genomic DNA. Translation: CAH72257.1.
    AK313191 mRNA. Translation: BAG36008.1.
    CH471097 Genomic DNA. Translation: EAW72963.1.
    BC016675 mRNA. Translation: AAH16675.1.
    M19301 mRNA. Translation: AAA59200.1. Sequence problems.
    X68104 Genomic DNA. Translation: CAA48225.1.
    CCDSiCCDS767.1.
    PIRiA32422.
    RefSeqiNP_001909.3. NM_001918.3.
    UniGeneiHs.709187.

    Genome annotation databases

    EnsembliENST00000370132; ENSP00000359151; ENSG00000137992.
    GeneIDi1629.
    KEGGihsa:1629.
    UCSCiuc001dta.3. human.

    Polymorphism databases

    DMDMi400668.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66785 mRNA. Translation: CAA47285.1 .
    J03208 mRNA. Translation: AAA35589.1 . Different initiation.
    M27093 mRNA. Translation: AAA64512.1 . Different initiation.
    BT007372 mRNA. Translation: AAP36036.1 .
    AL445928 Genomic DNA. Translation: CAH72257.1 .
    AK313191 mRNA. Translation: BAG36008.1 .
    CH471097 Genomic DNA. Translation: EAW72963.1 .
    BC016675 mRNA. Translation: AAH16675.1 .
    M19301 mRNA. Translation: AAA59200.1 . Sequence problems.
    X68104 Genomic DNA. Translation: CAA48225.1 .
    CCDSi CCDS767.1.
    PIRi A32422.
    RefSeqi NP_001909.3. NM_001918.3.
    UniGenei Hs.709187.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K8M NMR - A 62-145 [» ]
    1K8O NMR - A 62-145 [» ]
    1ZWV NMR - A 165-213 [» ]
    2COO NMR - A 163-220 [» ]
    3RNM X-ray 2.40 E/F 165-213 [» ]
    ProteinModelPortali P11182.
    SMRi P11182. Positions 62-147, 163-220, 249-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107997. 10 interactions.
    IntActi P11182. 6 interactions.
    MINTi MINT-1161634.
    STRINGi 9606.ENSP00000359151.

    PTM databases

    PhosphoSitei P11182.

    Polymorphism databases

    DMDMi 400668.

    Proteomic databases

    MaxQBi P11182.
    PaxDbi P11182.
    PRIDEi P11182.

    Protocols and materials databases

    DNASUi 1629.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370132 ; ENSP00000359151 ; ENSG00000137992 .
    GeneIDi 1629.
    KEGGi hsa:1629.
    UCSCi uc001dta.3. human.

    Organism-specific databases

    CTDi 1629.
    GeneCardsi GC01M100652.
    GeneReviewsi DBT.
    H-InvDB HIX0000815.
    HGNCi HGNC:2698. DBT.
    HPAi HPA026481.
    HPA026485.
    HPA026533.
    MIMi 248600. phenotype.
    248610. gene.
    neXtProti NX_P11182.
    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 PA27167.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281564.
    HOVERGENi HBG104085.
    InParanoidi P11182.
    KOi K09699.
    OrthoDBi EOG7GFB4W.
    PhylomeDBi P11182.
    TreeFami TF314182.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-12007.
    BRENDAi 2.3.1.168. 2681.
    Reactomei REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    EvolutionaryTracei P11182.
    GeneWikii DBT_(gene).
    GenomeRNAii 1629.
    NextBioi 6684.
    PROi P11182.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11182.
    Bgeei P11182.
    CleanExi HS_DBT.
    Genevestigatori P11182.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR015761. BCKDC_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    PANTHERi PTHR23151:SF46. PTHR23151:SF46. 1 hit.
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex."
      Lau K.S., Chuang J.L., Herring W.J., Danner D.J., Cox R.P., Chuang D.T.
      Biochim. Biophys. Acta 1132:319-321(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure."
      Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., Yeaman S.J.
      J. Biol. Chem. 263:6165-6168(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase."
      Danner D.J., Litwer S., Herring W.J., Pruckler J.
      J. Biol. Chem. 264:7742-7746(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex."
      Nobukuni Y., Mitsubuchi H., Endo F., Matsuda I.
      Biochem. Biophys. Res. Commun. 161:1035-1041(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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].
    6. "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].
      Tissue: Kidney.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-384.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Skin.
    10. "Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs."
      Lau K.S., Griffin T.A., Hu C.-W.C., Chuang D.T.
      Biochemistry 27:1972-1981(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-313.
    11. "Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene."
      Lau K.S., Herring W.J., Chuang J.L., McKean M., Danner D.J., Cox R.P., Chuang D.T.
      J. Biol. Chem. 267:24090-24096(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    12. "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 47-81.
    13. "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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex."
      Chang C.-F., Chou H.-T., Chuang J.L., Chuang D.T., Huang T.-H.
      J. Biol. Chem. 277:15865-15873(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 62-145.
    16. "Solution structure of the E3-binding domain of dihydrolipoamide branched chain transacylase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 163-220.
    17. "A 17-bp insertion and a Phe215-->Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34."
      Fisher C.W., Lau K.S., Fisher C.R., Wynn R.M., Cox R.P., Chuang D.T.
      Biochem. Biophys. Res. Commun. 174:804-809(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MSUD2 CYS-276.
    18. "Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex."
      Tsuruta M., Mitsubuchi H., Mardy S., Miura Y., Hayashida Y., Kinugasa A., Ishitsu T., Matsuda I., Indo Y.
      J. Hum. Genet. 43:91-100(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MSUD2 MET-98 AND SER-384.

    Entry informationi

    Entry nameiODB2_HUMAN
    AccessioniPrimary (citable) accession number: P11182
    Secondary accession number(s): B2R811, Q5VVL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 185 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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