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P26440

- IVD_HUMAN

UniProt

P26440 - IVD_HUMAN

Protein

Isovaleryl-CoA dehydrogenase, mitochondrial

Gene

IVD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei171 – 1711Substrate; via carbonyl oxygen
    Binding sitei274 – 2741Substrate
    Active sitei283 – 2831Proton acceptor1 Publication
    Binding sitei309 – 3091FAD1 Publication
    Binding sitei320 – 3201FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 17110FAD1 Publication
    Nucleotide bindingi195 – 1973FAD1 Publication
    Nucleotide bindingi377 – 3815FAD1 Publication
    Nucleotide bindingi406 – 4083FAD1 Publication

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. isovaleryl-CoA dehydrogenase activity Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKP26440.
    UniPathwayiUPA00363; UER00860.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isovaleryl-CoA dehydrogenase, mitochondrial (EC:1.3.8.4)
    Short name:
    IVD
    Gene namesi
    Name:IVD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6186. IVD.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Isovaleric acidemia (IVA) [MIM:243500]: A metabolic disorder characterized by retarded psychomotor development, a peculiar odor resembling sweaty feet, an aversion to dietary protein, and pernicious vomiting, leading to acidosis and coma. The acute neonatal form leads to massive metabolic acidosis from the first days of life and rapid death.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421L → P in IVA. 1 Publication
    VAR_000423
    Natural varianti50 – 501R → P in IVA. 1 Publication
    VAR_015960
    Natural varianti69 – 691D → N in IVA. 1 Publication
    VAR_015961
    Natural varianti94 – 941A → G in IVA. 1 Publication
    VAR_070061
    Natural varianti120 – 1201G → R in IVA. 2 Publications
    Corresponds to variant rs142761835 [ dbSNP | Ensembl ].
    VAR_070062
    Natural varianti196 – 1961I → M in IVA. 1 Publication
    VAR_070063
    Natural varianti199 – 1991G → V in IVA. 1 Publication
    VAR_000424
    Natural varianti276 – 2761L → P in IVA. 1 Publication
    VAR_070064
    Natural varianti311 – 3111A → V in IVA. 1 Publication
    Corresponds to variant rs28940889 [ dbSNP | Ensembl ].
    VAR_015962
    Natural varianti357 – 3571C → R in IVA. 1 Publication
    VAR_015963
    Natural varianti371 – 3711V → A in IVA. 1 Publication
    VAR_015964
    Natural varianti392 – 3921R → C in IVA. 1 Publication
    VAR_015965
    Natural varianti400 – 4001Y → C in IVA. 1 Publication
    VAR_070065
    Natural varianti411 – 4111R → L in IVA. 1 Publication
    VAR_015966

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi283 – 2831E → D: Residual activity. 1 Publication
    Mutagenesisi283 – 2831E → G or Q: Loss of activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi243500. phenotype.
    Orphaneti33. Isovaleric acidemia.
    PharmGKBiPA29984.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929Mitochondrion2 PublicationsAdd
    BLAST
    Chaini30 – 423394Isovaleryl-CoA dehydrogenase, mitochondrialPRO_0000000531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
    Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
    Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
    Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
    Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
    Modified residuei238 – 2381N6-acetyllysineBy similarity
    Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
    Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
    Modified residuei315 – 3151N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP26440.
    PaxDbiP26440.
    PRIDEiP26440.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00645805.
    UCD-2DPAGEP26440.

    PTM databases

    PhosphoSiteiP26440.

    Expressioni

    Gene expression databases

    ArrayExpressiP26440.
    BgeeiP26440.
    CleanExiHS_IVD.
    GenevestigatoriP26440.

    Organism-specific databases

    HPAiHPA041391.
    HPA044250.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi109916. 4 interactions.
    IntActiP26440. 1 interaction.
    STRINGi9606.ENSP00000249760.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 403
    Helixi44 – 6017
    Turni61 – 644
    Helixi65 – 717
    Helixi77 – 8711
    Turni90 – 934
    Helixi96 – 983
    Helixi105 – 11814
    Helixi120 – 13011
    Turni131 – 1333
    Helixi134 – 1407
    Helixi143 – 15412
    Beta strandi160 – 1634
    Beta strandi169 – 1724
    Helixi173 – 1753
    Beta strandi179 – 1824
    Beta strandi184 – 19714
    Helixi199 – 2013
    Beta strandi203 – 2119
    Helixi218 – 2214
    Beta strandi222 – 2287
    Beta strandi234 – 2363
    Beta strandi242 – 2443
    Beta strandi250 – 26112
    Helixi262 – 2643
    Beta strandi265 – 2673
    Helixi272 – 28716
    Helixi289 – 30618
    Helixi316 – 3183
    Helixi320 – 34829
    Helixi354 – 37926
    Helixi380 – 3845
    Helixi390 – 39910
    Turni400 – 4045
    Helixi407 – 41913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IVHX-ray2.60A/B/C/D30-423[»]
    ProteinModelPortaliP26440.
    SMRiP26440. Positions 35-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26440.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 2202Substrate binding
    Regioni281 – 2844Substrate binding
    Regioni404 – 4052Substrate binding

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiP26440.
    KOiK00253.
    OMAiFPNQLWP.
    OrthoDBiEOG74FF0S.
    PhylomeDBiP26440.
    TreeFamiTF105050.

    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: P26440-1) [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

    MATATRLLGW RVASWRLRPP LAGFVSQRAH SLLPVDDAIN GLSEEQRQLR    50
    QTMAKFLQEH LAPKAQEIDR SNEFKNLREF WKQLGNLGVL GITAPVQYGG 100
    SGLGYLEHVL VMEEISRASG AVGLSYGAHS NLCINQLVRN GNEAQKEKYL 150
    PKLISGEYIG ALAMSEPNAG SDVVSMKLKA EKKGNHYILN GNKFWITNGP 200
    DADVLIVYAK TDLAAVPASR GITAFIVEKG MPGFSTSKKL DKLGMRGSNT 250
    CELIFEDCKI PAANILGHEN KGVYVLMSGL DLERLVLAGG PLGLMQAVLD 300
    HTIPYLHVRE AFGQKIGHFQ LMQGKMADMY TRLMACRQYV YNVAKACDEG 350
    HCTAKDCAGV ILYSAECATQ VALDGIQCFG GNGYINDFPM GRFLRDAKLY 400
    EIGAGTSEVR RLVIGRAFNA DFH 423
    Length:423
    Mass (Da):46,319
    Last modified:August 1, 1992 - v1
    Checksum:i121AF14C7F1FA13D
    GO
    Isoform 2 (identifier: P26440-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-78: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:393
    Mass (Da):42,724
    Checksum:i6C75C436286F2617
    GO

    Sequence cautioni

    The sequence BAG53799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAW92413.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW92414.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW92415.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101W → C in AAP35809. 1 PublicationCurated
    Sequence conflicti10 – 101W → C in AAH17202. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421L → P in IVA. 1 Publication
    VAR_000423
    Natural varianti50 – 501R → P in IVA. 1 Publication
    VAR_015960
    Natural varianti69 – 691D → N in IVA. 1 Publication
    VAR_015961
    Natural varianti94 – 941A → G in IVA. 1 Publication
    VAR_070061
    Natural varianti120 – 1201G → R in IVA. 2 Publications
    Corresponds to variant rs142761835 [ dbSNP | Ensembl ].
    VAR_070062
    Natural varianti196 – 1961I → M in IVA. 1 Publication
    VAR_070063
    Natural varianti199 – 1991G → V in IVA. 1 Publication
    VAR_000424
    Natural varianti276 – 2761L → P in IVA. 1 Publication
    VAR_070064
    Natural varianti311 – 3111A → V in IVA. 1 Publication
    Corresponds to variant rs28940889 [ dbSNP | Ensembl ].
    VAR_015962
    Natural varianti357 – 3571C → R in IVA. 1 Publication
    VAR_015963
    Natural varianti371 – 3711V → A in IVA. 1 Publication
    VAR_015964
    Natural varianti392 – 3921R → C in IVA. 1 Publication
    VAR_015965
    Natural varianti400 – 4001Y → C in IVA. 1 Publication
    VAR_070065
    Natural varianti411 – 4111R → L in IVA. 1 Publication
    VAR_015966

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei49 – 7830Missing in isoform 2. 1 PublicationVSP_045193Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34192 mRNA. Translation: AAA52711.1.
    AF191218
    , AF191214, AF191215, AF191216, AF191217 Genomic DNA. Translation: AAF20182.1.
    BT007145 mRNA. Translation: AAP35809.1.
    AK122922 mRNA. Translation: BAG53799.1. Different initiation.
    AK315296 mRNA. Translation: BAG37702.1.
    AC013356 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92413.1. Sequence problems.
    CH471125 Genomic DNA. Translation: EAW92414.1. Sequence problems.
    CH471125 Genomic DNA. Translation: EAW92415.1. Sequence problems.
    BC017202 mRNA. Translation: AAH17202.1.
    AF038318 Genomic DNA. Translation: AAB92584.1.
    PIRiA37033.
    RefSeqiNP_001152980.1. NM_001159508.1.
    NP_002216.2. NM_002225.3.
    UniGeneiHs.513646.

    Genome annotation databases

    EnsembliENST00000479013; ENSP00000417990; ENSG00000128928.
    GeneIDi3712.
    KEGGihsa:3712.
    UCSCiuc001zlq.2. human.

    Polymorphism databases

    DMDMi125051.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34192 mRNA. Translation: AAA52711.1 .
    AF191218
    , AF191214 , AF191215 , AF191216 , AF191217 Genomic DNA. Translation: AAF20182.1 .
    BT007145 mRNA. Translation: AAP35809.1 .
    AK122922 mRNA. Translation: BAG53799.1 . Different initiation.
    AK315296 mRNA. Translation: BAG37702.1 .
    AC013356 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92413.1 . Sequence problems.
    CH471125 Genomic DNA. Translation: EAW92414.1 . Sequence problems.
    CH471125 Genomic DNA. Translation: EAW92415.1 . Sequence problems.
    BC017202 mRNA. Translation: AAH17202.1 .
    AF038318 Genomic DNA. Translation: AAB92584.1 .
    PIRi A37033.
    RefSeqi NP_001152980.1. NM_001159508.1.
    NP_002216.2. NM_002225.3.
    UniGenei Hs.513646.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IVH X-ray 2.60 A/B/C/D 30-423 [» ]
    ProteinModelPortali P26440.
    SMRi P26440. Positions 35-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109916. 4 interactions.
    IntActi P26440. 1 interaction.
    STRINGi 9606.ENSP00000249760.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei P26440.

    Polymorphism databases

    DMDMi 125051.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00645805.
    UCD-2DPAGE P26440.

    Proteomic databases

    MaxQBi P26440.
    PaxDbi P26440.
    PRIDEi P26440.

    Protocols and materials databases

    DNASUi 3712.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000479013 ; ENSP00000417990 ; ENSG00000128928 .
    GeneIDi 3712.
    KEGGi hsa:3712.
    UCSCi uc001zlq.2. human.

    Organism-specific databases

    CTDi 3712.
    GeneCardsi GC15P040697.
    HGNCi HGNC:6186. IVD.
    HPAi HPA041391.
    HPA044250.
    MIMi 243500. phenotype.
    607036. gene.
    neXtProti NX_P26440.
    Orphaneti 33. Isovaleric acidemia.
    PharmGKBi PA29984.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi P26440.
    KOi K00253.
    OMAi FPNQLWP.
    OrthoDBi EOG74FF0S.
    PhylomeDBi P26440.
    TreeFami TF105050.

    Enzyme and pathway databases

    UniPathwayi UPA00363 ; UER00860 .
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK P26440.

    Miscellaneous databases

    ChiTaRSi IVD. human.
    EvolutionaryTracei P26440.
    GenomeRNAii 3712.
    NextBioi 14547.
    PROi P26440.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26440.
    Bgeei P26440.
    CleanExi HS_IVD.
    Genevestigatori P26440.

    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. "Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts."
      Matsubara Y., Ito M., Glassberg R., Satyabhama S., Ikeda Y., Tanaka K.
      J. Clin. Invest. 85:1058-1064(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Exon skipping in IVD RNA processing in isovaleric acidemia caused by point mutations in the coding region of the IVD gene."
      Vockley J., Rogan P.K., Anderson B.D., Willard J., Seelan R.S., Smith D.I., Liu W.
      Am. J. Hum. Genet. 66:356-367(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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: Pericardium and Testis.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [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] (ISOFORM 1).
      Tissue: Brain.
    8. "Structural organization of the human isovaleryl-CoA dehydrogenase gene."
      Parimoo B., Tanaka K.
      Genomics 15:582-590(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-423.
    9. "The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors."
      Vockley J., Nagao M., Parimoo B., Tanaka K.
      J. Biol. Chem. 267:2494-2501(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
    10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-47.
      Tissue: Platelet.
    11. "Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase."
      Mohsen A.W., Vockley J.
      Biochemistry 34:10146-10152(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, MUTAGENESIS OF GLU-283.
    12. "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-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structure of human isovaleryl-CoA dehydrogenase at 2.6-A resolution: structural basis for substrate specificity."
      Tiffany K.A., Roberts D.L., Wang M., Paschke R., Mohsen A.W., Vockley J., Kim J.-J.P.
      Biochemistry 36:8455-8464(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 30-423 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, COFACTOR.
    15. "Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia."
      Vockley J., Parimoo B., Tanaka K.
      Am. J. Hum. Genet. 49:147-157(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IVA PRO-42 AND VAL-199.
    16. "Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia."
      Mohsen A.-W.A., Anderson B.D., Volchenboum S.L., Battaile K.P., Tiffany K.A., Roberts D.L., Kim J.-J.P., Vockley J.
      Biochemistry 37:10325-10335(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IVA PRO-50; ASN-69; VAL-311; ARG-357; ALA-371; CYS-392 AND LEU-411.
    17. "Phenotypic and mutation spectrums of Thai patients with isovaleric acidemia."
      Vatanavicharn N., Liammongkolkul S., Sakamoto O., Sathienkijkanchai A., Wasant P.
      Pediatr. Int. 53:990-994(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IVA GLY-94; ARG-120; PRO-276 AND CYS-400.
    18. "Clinical variability of isovaleric acidemia in a genetically homogeneous population."
      Dercksen M., Duran M., Ijlst L., Mienie L.J., Reinecke C.J., Ruiter J.P., Waterham H.R., Wanders R.J.
      J. Inherit. Metab. Dis. 35:1021-1029(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IVA ARG-120.
    19. "Two novel isovaleryl-CoA dehydrogenase gene mutations in a Chinese infant."
      Bei F., Sun J.H., Yu Y.G., Jia J., Zheng Z.J., Fu Q.H., Cai W.
      Gene 524:396-400(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IVA MET-196.

    Entry informationi

    Entry nameiIVD_HUMAN
    AccessioniPrimary (citable) accession number: P26440
    Secondary accession number(s): B2RCV5
    , B3KVI7, J3KR54, Q53XZ9, Q96AF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 161 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 15
      Human chromosome 15: 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