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P45954

- ACDSB_HUMAN

UniProt

P45954 - ACDSB_HUMAN

Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.

    Catalytic activityi

    Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
    2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+.

    Cofactori

    FAD.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei183 – 1831Substrate; via carbonyl oxygen
    Binding sitei283 – 2831Substrate
    Binding sitei319 – 3191FAD; shared with dimeric partner1 Publication
    Binding sitei330 – 3301FAD; shared with dimeric partner1 Publication
    Active sitei414 – 4141Proton acceptorBy similarity
    Binding sitei415 – 4151Substrate; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 18310FAD1 Publication
    Nucleotide bindingi207 – 2093FAD1 Publication
    Nucleotide bindingi387 – 3915FAD; shared with dimeric partner1 Publication
    Nucleotide bindingi416 – 4183FAD1 Publication

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: Reactome
    2. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.5)
    Short name:
    SBCAD
    Alternative name(s):
    2-methyl branched chain acyl-CoA dehydrogenase
    Short name:
    2-MEBCAD
    2-methylbutyryl-coenzyme A dehydrogenase
    Short name:
    2-methylbutyryl-CoA dehydrogenase
    Gene namesi
    Name:ACADSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:91. ACADSB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD) [MIM:610006]: Autosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti255 – 2551L → F in SBCADD. 2 Publications
    VAR_013010

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610006. phenotype.
    Orphaneti79157. 2-methylbutyryl-CoA dehydrogenase deficiency.
    PharmGKBiPA24427.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionAdd
    BLAST
    Chaini34 – 432399Short/branched chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000519Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
    Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
    Modified residuei284 – 2841N6-acetyllysine; alternate1 Publication
    Modified residuei284 – 2841N6-succinyllysine; alternateBy similarity
    Modified residuei426 – 4261N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP45954.
    PaxDbiP45954.
    PeptideAtlasiP45954.
    PRIDEiP45954.

    PTM databases

    PhosphoSiteiP45954.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP45954.
    BgeeiP45954.
    CleanExiHS_ACADSB.
    GenevestigatoriP45954.

    Organism-specific databases

    HPAiHPA041458.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi106554. 3 interactions.
    IntActiP45954. 1 interaction.
    STRINGi9606.ENSP00000357873.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi59 – 7517
    Helixi77 – 793
    Helixi80 – 867
    Helixi91 – 999
    Turni100 – 1034
    Beta strandi104 – 1074
    Helixi109 – 1113
    Helixi118 – 12912
    Helixi133 – 14412
    Helixi146 – 1538
    Helixi156 – 16813
    Beta strandi172 – 1754
    Beta strandi181 – 1844
    Helixi185 – 1873
    Beta strandi191 – 1955
    Beta strandi198 – 20912
    Turni210 – 2134
    Beta strandi215 – 2239
    Helixi225 – 2317
    Beta strandi232 – 2387
    Beta strandi244 – 2463
    Beta strandi252 – 2543
    Beta strandi260 – 27112
    Helixi272 – 2743
    Beta strandi275 – 2784
    Helixi282 – 31837
    Helixi326 – 3283
    Helixi330 – 35829
    Helixi364 – 38926
    Helixi390 – 3945
    Helixi400 – 4078
    Helixi408 – 4114
    Turni412 – 4143
    Helixi417 – 43115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JIFX-ray2.00A/B/C/D52-432[»]
    ProteinModelPortaliP45954.
    SMRiP45954. Positions 52-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45954.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 2302Substrate binding
    Regioni291 – 2944Substrate binding

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiP45954.
    KOiK09478.
    OMAiFLIFANV.
    PhylomeDBiP45954.
    TreeFamiTF105055.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 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 1 (identifier: P45954-1) [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

    MEGLAVRLLR GSRLLRRNFL TCLSSWKIPP HVSKSSQSEA LLNITNNGIH    50
    FAPLQTFTDE EMMIKSSVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ 100
    GLMGIEVDPE YGGTGASFLS TVLVIEELAK VDASVAVFCE IQNTLINTLI 150
    RKHGTEEQKA TYLPQLTTEK VGSFCLSEAG AGSDSFALKT RADKEGDYYV 200
    LNGSKMWISS AEHAGLFLVM ANVDPTIGYK GITSFLVDRD TPGLHIGKPE 250
    NKLGLRASST CPLTFENVKV PEANILGQIG HGYKYAIGSL NEGRIGIAAQ 300
    MLGLAQGCFD YTIPYIKERI QFGKRLFDFQ GLQHQVAHVA TQLEAARLLT 350
    YNAARLLEAG KPFIKEASMA KYYASEIAGQ TTSKCIEWMG GVGYTKDYPV 400
    EKYFRDAKIG TIYEGASNIQ LNTIAKHIDA EY 432
    Length:432
    Mass (Da):47,485
    Last modified:November 1, 1995 - v1
    Checksum:i1EB5F894B1944E99
    GO
    Isoform 2 (identifier: P45954-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-102: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:330
    Mass (Da):36,025
    Checksum:i1BFB4E4C8E0F3615
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131R → K.2 Publications
    Corresponds to variant rs12263012 [ dbSNP | Ensembl ].
    VAR_048177
    Natural varianti209 – 2091S → G.
    Corresponds to variant rs1799823 [ dbSNP | Ensembl ].
    VAR_014749
    Natural varianti255 – 2551L → F in SBCADD. 2 Publications
    VAR_013010
    Natural varianti316 – 3161I → V.1 Publication
    Corresponds to variant rs1131430 [ dbSNP | Ensembl ].
    VAR_048178
    Natural varianti376 – 3761E → G.
    Corresponds to variant rs12357783 [ dbSNP | Ensembl ].
    VAR_048179

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 102102Missing in isoform 2. 1 PublicationVSP_055778Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12778 mRNA. Translation: AAA74424.1.
    AF260678
    , AF260668, AF260669, AF260670, AF260671, AF260672, AF260673, AF260674, AF260675, AF260676, AF260677 Genomic DNA. Translation: AAF97921.1.
    AK298638 mRNA. Translation: BAG60813.1.
    AK314241 mRNA. Translation: BAG36909.1.
    AL731666, AC012391, AC073585 Genomic DNA. Translation: CAI10847.1.
    CH471066 Genomic DNA. Translation: EAW49291.1.
    BC013756 mRNA. Translation: AAH13756.1.
    AL831821 mRNA. Translation: CAD38535.2.
    CCDSiCCDS7634.1.
    PIRiA55680.
    RefSeqiNP_001600.1. NM_001609.3.
    UniGeneiHs.81934.

    Genome annotation databases

    EnsembliENST00000358776; ENSP00000357873; ENSG00000196177. [P45954-1]
    ENST00000368869; ENSP00000357862; ENSG00000196177. [P45954-2]
    GeneIDi36.
    KEGGihsa:36.
    UCSCiuc001lhb.3. human.

    Polymorphism databases

    DMDMi1168283.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12778 mRNA. Translation: AAA74424.1 .
    AF260678
    , AF260668 , AF260669 , AF260670 , AF260671 , AF260672 , AF260673 , AF260674 , AF260675 , AF260676 , AF260677 Genomic DNA. Translation: AAF97921.1 .
    AK298638 mRNA. Translation: BAG60813.1 .
    AK314241 mRNA. Translation: BAG36909.1 .
    AL731666 , AC012391 , AC073585 Genomic DNA. Translation: CAI10847.1 .
    CH471066 Genomic DNA. Translation: EAW49291.1 .
    BC013756 mRNA. Translation: AAH13756.1 .
    AL831821 mRNA. Translation: CAD38535.2 .
    CCDSi CCDS7634.1.
    PIRi A55680.
    RefSeqi NP_001600.1. NM_001609.3.
    UniGenei Hs.81934.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JIF X-ray 2.00 A/B/C/D 52-432 [» ]
    ProteinModelPortali P45954.
    SMRi P45954. Positions 52-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106554. 3 interactions.
    IntActi P45954. 1 interaction.
    STRINGi 9606.ENSP00000357873.

    Chemistry

    DrugBanki DB00167. L-Isoleucine.
    DB00313. Valproic Acid.

    PTM databases

    PhosphoSitei P45954.

    Polymorphism databases

    DMDMi 1168283.

    Proteomic databases

    MaxQBi P45954.
    PaxDbi P45954.
    PeptideAtlasi P45954.
    PRIDEi P45954.

    Protocols and materials databases

    DNASUi 36.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358776 ; ENSP00000357873 ; ENSG00000196177 . [P45954-1 ]
    ENST00000368869 ; ENSP00000357862 ; ENSG00000196177 . [P45954-2 ]
    GeneIDi 36.
    KEGGi hsa:36.
    UCSCi uc001lhb.3. human.

    Organism-specific databases

    CTDi 36.
    GeneCardsi GC10P124758.
    HGNCi HGNC:91. ACADSB.
    HPAi HPA041458.
    MIMi 600301. gene.
    610006. phenotype.
    neXtProti NX_P45954.
    Orphaneti 79157. 2-methylbutyryl-CoA dehydrogenase deficiency.
    PharmGKBi PA24427.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi P45954.
    KOi K09478.
    OMAi FLIFANV.
    PhylomeDBi P45954.
    TreeFami TF105055.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    Reactomei REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    ChiTaRSi ACADSB. human.
    EvolutionaryTracei P45954.
    GenomeRNAii 36.
    NextBioi 139.
    PROi P45954.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45954.
    Bgeei P45954.
    CleanExi HS_ACADSB.
    Genevestigatori P45954.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family."
      Rozen R., Vockley J., Zhou L., Milos R., Willard J., Fu K., Vicanek C., Low-Nang L., Torban E., Fournier B.
      Genomics 24:280-287(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism."
      Andresen B.S., Christensen E., Corydon T.J., Bross P., Pilgaard B., Wanders R.J.A., Ruiter J.P.N., Simonsen H., Winter V., Knudsen I., Schroeder L.D., Gregersen N., Skovby F.
      Am. J. Hum. Genet. 67:1095-1103(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Esophagus and Mammary gland.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1), VARIANT LYS-13.
      Tissue: Mammary gland.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-432 (ISOFORM 1), VARIANTS LYS-13 AND VAL-316.
      Tissue: Skeletal muscle.
    8. "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-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of human short-branched chain acyl-CoA dehydrogenase."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-432 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT.
    11. Cited for: VARIANT SBCADD PHE-255.
    12. "Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping."
      Madsen P.P., Kibaek M., Roca X., Sachidanandam R., Krainer A.R., Christensen E., Steiner R.D., Gibson K.M., Corydon T.J., Knudsen I., Wanders R.J., Ruiter J.P.N., Gregersen N., Andresen B.S.
      Hum. Genet. 118:680-690(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SBCADD PHE-255.

    Entry informationi

    Entry nameiACDSB_HUMAN
    AccessioniPrimary (citable) accession number: P45954
    Secondary accession number(s): B4DQ51, Q5SQN6, Q96CX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 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 10
      Human chromosome 10: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3