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Q9UKU7

- ACAD8_HUMAN

UniProt

Q9UKU7 - ACAD8_HUMAN

Protein

Isobutyryl-CoA dehydrogenase, mitochondrial

Gene

ACAD8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex.1 Publication

    Catalytic activityi

    Isobutyryl-CoA + ETF = methylacrylyl-CoA + reduced ETF.

    Cofactori

    FAD.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671Substrate; via carbonyl oxygen
    Binding sitei302 – 3021FAD; shared with dimeric partner1 Publication
    Active sitei398 – 3981Proton acceptor
    Binding sitei399 – 3991Substrate; via amide nitrogen
    Binding sitei410 – 4101Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 16710FAD1 Publication
    Nucleotide bindingi191 – 1933FAD1 Publication
    Nucleotide bindingi312 – 3132FAD; shared with dimeric partner1 Publication
    Nucleotide bindingi371 – 3755FAD; shared with dimeric partner1 Publication
    Nucleotide bindingi400 – 4023FAD1 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. lipid metabolic process Source: ProtInc
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. small molecule metabolic process Source: Reactome
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. valine catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Activator, Oxidoreductase

    Keywords - Biological processi

    Branched-chain amino acid catabolism, Transcription, Transcription regulation

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    UniPathwayiUPA00362.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isobutyryl-CoA dehydrogenase, mitochondrial (EC:1.3.99.-)
    Alternative name(s):
    Activator-recruited cofactor 42 kDa component
    Short name:
    ARC42
    Acyl-CoA dehydrogenase family member 8
    Short name:
    ACAD-8
    Gene namesi
    Name:ACAD8
    Synonyms:ARC42, IBD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:87. ACAD8.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Isobutyryl-CoA dehydrogenase deficiency (IBDD) [MIM:611283]: The symptoms of IBDD generally appear until late in infancy or in childhood and can include poor feeding and growth (failure to thrive), a weakened and enlarged heart (dilated cardiomyopathy), seizures, and low numbers of red blood cells (anemia).3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281M → I in IBDD. 1 Publication
    VAR_035071
    Natural varianti134 – 1341D → Y in IBDD. 1 Publication
    VAR_035072
    Natural varianti137 – 1371G → R in IBDD; complete loss of activity. 1 Publication
    VAR_035073
    Natural varianti152 – 1521M → T in IBDD. 1 Publication
    VAR_035074
    Natural varianti203 – 2031V → I in IBDD. 1 Publication
    VAR_035075
    Natural varianti302 – 3021R → Q in IBDD; complete loss of activity. 2 Publications
    VAR_035076
    Natural varianti320 – 3201A → T in IBDD; <20% of wild-type activity. 1 Publication
    VAR_035077
    Natural varianti334 – 3341R → C in IBDD. 1 Publication
    VAR_035078
    Natural varianti385 – 3851Q → R in IBDD. 1 Publication
    VAR_035079

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi611283. phenotype.
    Orphaneti79159. Isobutyryl-CoA dehydrogenase deficiency.
    PharmGKBiPA24423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222MitochondrionSequence AnalysisAdd
    BLAST
    Chaini23 – 415393Isobutyryl-CoA dehydrogenase, mitochondrialPRO_0000000522Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501N6-acetyllysine; alternateBy similarity
    Modified residuei50 – 501N6-succinyllysine; alternateBy similarity
    Modified residuei213 – 2131N6-succinyllysineBy similarity
    Modified residuei231 – 2311N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UKU7.
    PaxDbiQ9UKU7.
    PRIDEiQ9UKU7.

    2D gel databases

    UCD-2DPAGEQ9UKU7.

    PTM databases

    PhosphoSiteiQ9UKU7.

    Expressioni

    Tissue specificityi

    Detected at comparable levels in all tissues examined (heart, lung, brain, skeletal muscle, pancreas and placenta). Weakly expressed in liver and kidney.

    Gene expression databases

    ArrayExpressiQ9UKU7.
    BgeeiQ9UKU7.
    CleanExiHS_ACAD8.
    GenevestigatoriQ9UKU7.

    Organism-specific databases

    HPAiHPA040689.
    HPA043903.

    Interactioni

    Subunit structurei

    Homotetramer, formed by a dimer of dimers. Subunit of the large multiprotein complex ARC/DRIP.3 Publications

    Protein-protein interaction databases

    BioGridi117965. 2 interactions.
    IntActiQ9UKU7. 3 interactions.
    STRINGi9606.ENSP00000281182.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni37 – 404
    Helixi43 – 5917
    Turni60 – 634
    Helixi64 – 707
    Helixi75 – 839
    Helixi93 – 953
    Helixi102 – 11312
    Helixi117 – 13620
    Helixi139 – 15012
    Beta strandi156 – 1594
    Beta strandi165 – 1684
    Helixi169 – 1713
    Beta strandi175 – 1795
    Beta strandi182 – 19312
    Turni194 – 1974
    Beta strandi199 – 21113
    Helixi212 – 2143
    Beta strandi215 – 2217
    Beta strandi227 – 2293
    Beta strandi235 – 2373
    Beta strandi243 – 25412
    Helixi255 – 2573
    Beta strandi258 – 2614
    Helixi265 – 30137
    Helixi309 – 3113
    Helixi313 – 34129
    Helixi347 – 37226
    Helixi373 – 3786
    Helixi384 – 39310
    Turni394 – 3963
    Beta strandi397 – 3993
    Helixi401 – 41414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RX0X-ray1.77A/B/C/D24-415[»]
    ProteinModelPortaliQ9UKU7.
    SMRiQ9UKU7. Positions 32-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKU7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 2774Substrate binding

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiQ9UKU7.
    KOiK11538.
    OMAiWRAQETR.
    OrthoDBiEOG74FF0S.
    PhylomeDBiQ9UKU7.
    TreeFamiTF105052.

    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.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKU7-1) [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

    MLWSGCRRFG ARLGCLPGGL RVLVQTGHRS LTSCIDPSMG LNEEQKEFQK    50
    VAFDFAAREM APNMAEWDQK ELFPVDVMRK AAQLGFGGVY IQTDVGGSGL 100
    SRLDTSVIFE ALATGCTSTT AYISIHNMCA WMIDSFGNEE QRHKFCPPLC 150
    TMEKFASYCL TEPGSGSDAA SLLTSAKKQG DHYILNGSKA FISGAGESDI 200
    YVVMCRTGGP GPKGISCIVV EKGTPGLSFG KKEKKVGWNS QPTRAVIFED 250
    CAVPVANRIG SEGQGFLIAV RGLNGGRINI ASCSLGAAHA SVILTRDHLN 300
    VRKQFGEPLA SNQYLQFTLA DMATRLVAAR LMVRNAAVAL QEERKDAVAL 350
    CSMAKLFATD ECFAICNQAL QMHGGYGYLK DYAVQQYVRD SRVHQILEGS 400
    NEVMRILISR SLLQE 415
    Length:415
    Mass (Da):45,070
    Last modified:May 1, 2000 - v1
    Checksum:iCAFFE91B74E2362D
    GO
    Isoform 2 (identifier: Q9UKU7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         37-37: P → R
         38-164: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:288
    Mass (Da):31,024
    Checksum:i731C090A54E4BCAB
    GO
    Isoform 3 (identifier: Q9UKU7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: Missing.
         399-415: GSNEVMRILISRSLLQE → ELFWQGPGVQSRSFVPFGGPQIALLLPFSSGDLREG

    Note: No experimental confirmation available.

    Show »
    Length:357
    Mass (Da):38,359
    Checksum:iFFFBC112FA06E2FB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101P → L in AAH01964. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281M → I in IBDD. 1 Publication
    VAR_035071
    Natural varianti134 – 1341D → Y in IBDD. 1 Publication
    VAR_035072
    Natural varianti137 – 1371G → R in IBDD; complete loss of activity. 1 Publication
    VAR_035073
    Natural varianti152 – 1521M → T in IBDD. 1 Publication
    VAR_035074
    Natural varianti203 – 2031V → I in IBDD. 1 Publication
    VAR_035075
    Natural varianti302 – 3021R → Q in IBDD; complete loss of activity. 2 Publications
    VAR_035076
    Natural varianti320 – 3201A → T in IBDD; <20% of wild-type activity. 1 Publication
    VAR_035077
    Natural varianti334 – 3341R → C in IBDD. 1 Publication
    VAR_035078
    Natural varianti385 – 3851Q → R in IBDD. 1 Publication
    VAR_035079

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7777Missing in isoform 3. 1 PublicationVSP_055779Add
    BLAST
    Alternative sequencei37 – 371P → R in isoform 2. 1 PublicationVSP_055780
    Alternative sequencei38 – 164127Missing in isoform 2. 1 PublicationVSP_055781Add
    BLAST
    Alternative sequencei399 – 41517GSNEV…SLLQE → ELFWQGPGVQSRSFVPFGGP QIALLLPFSSGDLREG in isoform 3. 1 PublicationVSP_055782Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126245 mRNA. Translation: AAF12736.1.
    AF260689
    , AF260679, AF260680, AF260681, AF260682, AF260683, AF260684, AF260685, AF260686, AF260687, AF260688 Genomic DNA. Translation: AAF97922.1.
    AK000359 mRNA. Translation: BAA91109.1.
    AK074640 mRNA. Translation: BAC11107.1.
    AK299492 mRNA. Translation: BAH13050.1.
    AP000859 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67833.1.
    BC001964 mRNA. Translation: AAH01964.1.
    CCDSiCCDS8498.1.
    RefSeqiNP_055199.1. NM_014384.2.
    UniGeneiHs.14791.

    Genome annotation databases

    EnsembliENST00000281182; ENSP00000281182; ENSG00000151498. [Q9UKU7-1]
    ENST00000374752; ENSP00000363884; ENSG00000151498. [Q9UKU7-2]
    GeneIDi27034.
    KEGGihsa:27034.
    UCSCiuc001qhk.3. human.

    Polymorphism databases

    DMDMi26006699.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126245 mRNA. Translation: AAF12736.1 .
    AF260689
    , AF260679 , AF260680 , AF260681 , AF260682 , AF260683 , AF260684 , AF260685 , AF260686 , AF260687 , AF260688 Genomic DNA. Translation: AAF97922.1 .
    AK000359 mRNA. Translation: BAA91109.1 .
    AK074640 mRNA. Translation: BAC11107.1 .
    AK299492 mRNA. Translation: BAH13050.1 .
    AP000859 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67833.1 .
    BC001964 mRNA. Translation: AAH01964.1 .
    CCDSi CCDS8498.1.
    RefSeqi NP_055199.1. NM_014384.2.
    UniGenei Hs.14791.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RX0 X-ray 1.77 A/B/C/D 24-415 [» ]
    ProteinModelPortali Q9UKU7.
    SMRi Q9UKU7. Positions 32-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117965. 2 interactions.
    IntActi Q9UKU7. 3 interactions.
    STRINGi 9606.ENSP00000281182.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei Q9UKU7.

    Polymorphism databases

    DMDMi 26006699.

    2D gel databases

    UCD-2DPAGE Q9UKU7.

    Proteomic databases

    MaxQBi Q9UKU7.
    PaxDbi Q9UKU7.
    PRIDEi Q9UKU7.

    Protocols and materials databases

    DNASUi 27034.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000281182 ; ENSP00000281182 ; ENSG00000151498 . [Q9UKU7-1 ]
    ENST00000374752 ; ENSP00000363884 ; ENSG00000151498 . [Q9UKU7-2 ]
    GeneIDi 27034.
    KEGGi hsa:27034.
    UCSCi uc001qhk.3. human.

    Organism-specific databases

    CTDi 27034.
    GeneCardsi GC11P134123.
    HGNCi HGNC:87. ACAD8.
    HPAi HPA040689.
    HPA043903.
    MIMi 604773. gene.
    611283. phenotype.
    neXtProti NX_Q9UKU7.
    Orphaneti 79159. Isobutyryl-CoA dehydrogenase deficiency.
    PharmGKBi PA24423.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi Q9UKU7.
    KOi K11538.
    OMAi WRAQETR.
    OrthoDBi EOG74FF0S.
    PhylomeDBi Q9UKU7.
    TreeFami TF105052.

    Enzyme and pathway databases

    UniPathwayi UPA00362 .
    Reactomei REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    EvolutionaryTracei Q9UKU7.
    GeneWikii ACAD8.
    GenomeRNAii 27034.
    NextBioi 49582.
    PROi Q9UKU7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKU7.
    Bgeei Q9UKU7.
    CleanExi HS_ACAD8.
    Genevestigatori Q9UKU7.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family."
      Telford E.A.R., Moynihan L.M., Markham A.F., Lench N.J.
      Biochim. Biophys. Acta 1446:371-376(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Skin fibroblast.
    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], PROBABLE FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    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; 2 AND 3).
      Tissue: Brain and Embryo.
    4. 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).
      Tissue: Cervix.
    7. "Composite co-activator ARC mediates chromatin-directed transcriptional activation."
      Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
      Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 50-61; 70-80 AND 345-355.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases."
      Battaile K.P., Nguyen T.V., Vockley J., Kim J.-J.P.
      J. Biol. Chem. 279:16526-16534(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 24-415 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT.
    10. Cited for: VARIANT IBDD GLN-302, FUNCTION.
    11. "Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants."
      Sass J.O., Sander S., Zschocke J.
      J. Inherit. Metab. Dis. 27:741-745(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IBDD ILE-128 AND ILE-203.
    12. Cited for: VARIANTS IBDD TYR-134; ARG-137; THR-152; GLN-302; THR-320; CYS-334 AND ARG-385, CHARACTERIZATION OF VARIANTS IBDD ARG-137; GLN-302 AND THR-320.

    Entry informationi

    Entry nameiACAD8_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKU7
    Secondary accession number(s): B7Z5W4, Q6ZWP6, Q9BUS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 138 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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