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Q16836

- HCDH_HUMAN

UniProt

Q16836 - HCDH_HUMAN

Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

HADH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.

    Catalytic activityi

    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571NAD2 Publications
    Binding sitei73 – 731Coenzyme A
    Binding sitei80 – 801Coenzyme A
    Binding sitei122 – 1221NAD2 Publications
    Binding sitei127 – 1271NAD2 Publications
    Binding sitei149 – 1491Coenzyme A
    Binding sitei149 – 1491NAD2 Publications
    Sitei170 – 1701Important for catalytic activityCurated
    Binding sitei173 – 1731NAD2 Publications
    Binding sitei305 – 3051NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 396NAD2 Publications

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: Reactome
    2. NAD+ binding Source: InterPro

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. fatty acid beta-oxidation Source: Reactome
    3. negative regulation of insulin secretion Source: Ensembl
    4. response to activity Source: Ensembl
    5. response to drug Source: Ensembl
    6. response to insulin Source: Ensembl
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06563-MONOMER.
    ReactomeiREACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RKQ16836.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (EC:1.1.1.35)
    Short name:
    HCDH
    Alternative name(s):
    Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
    Short-chain 3-hydroxyacyl-CoA dehydrogenase
    Gene namesi
    Name:HADH
    Synonyms:HAD, HADHSC, SCHAD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4799. HADH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: HPA
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency) [MIM:231530]: A metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401A → T in HADH deficiency. 1 Publication
    VAR_024079
    Natural varianti57 – 571D → E in HADH deficiency. 1 Publication
    VAR_024080
    Familial hyperinsulinemic hypoglycemia 4 (HHF4) [MIM:609975]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. HHF4 should be easily recognizable by analysis of acylcarnitine species and that this disorder responds well to treatment with diazoxide. It provides the first 'experiment of nature' that links impaired fatty acid oxidation to hyperinsulinism and that provides support for the concept that a lipid signaling pathway is implicated in the control of insulin secretion.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti258 – 2581P → L in HHF4; loss of activity. 1 Publication
    VAR_024081

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi231530. phenotype.
    609975. phenotype.
    Orphaneti71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
    PharmGKBiPA29173.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1212MitochondrionAdd
    BLAST
    Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialPRO_0000007406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801N6-succinyllysineBy similarity
    Modified residuei81 – 811N6-acetyllysine; alternateBy similarity
    Modified residuei81 – 811N6-succinyllysine; alternateBy similarity
    Modified residuei87 – 871N6-acetyllysine; alternateBy similarity
    Modified residuei87 – 871N6-succinyllysine; alternateBy similarity
    Modified residuei125 – 1251N6-acetyllysineBy similarity
    Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
    Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-succinyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
    Modified residuei206 – 2061N6-succinyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
    Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
    Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
    Modified residuei241 – 2411N6-succinyllysine; alternateBy similarity
    Modified residuei312 – 3121N6-acetyllysine; alternate1 Publication
    Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16836.
    PaxDbiQ16836.
    PRIDEiQ16836.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00298406.
    UCD-2DPAGEO00324.
    Q16836.

    PTM databases

    PhosphoSiteiQ16836.

    Expressioni

    Tissue specificityi

    Expressed in liver, kidney, pancreas, heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ16836.
    BgeeiQ16836.
    CleanExiHS_HADH.
    GenevestigatoriQ16836.

    Organism-specific databases

    HPAiHPA039588.
    HPA043888.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi109283. 7 interactions.
    IntActiQ16836. 3 interactions.
    MINTiMINT-5004681.
    STRINGi9606.ENSP00000312288.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 335
    Helixi37 – 4812
    Beta strandi52 – 565
    Helixi60 – 7920
    Beta strandi82 – 843
    Helixi86 – 9813
    Beta strandi100 – 1045
    Helixi106 – 1094
    Helixi110 – 1123
    Beta strandi114 – 1185
    Helixi124 – 13411
    Turni135 – 1373
    Beta strandi143 – 1464
    Beta strandi149 – 1513
    Helixi153 – 1575
    Helixi163 – 1653
    Beta strandi166 – 1716
    Turni175 – 1773
    Beta strandi180 – 1845
    Helixi191 – 20313
    Beta strandi207 – 2115
    Turni215 – 2184
    Helixi219 – 23517
    Helixi241 – 25212
    Helixi258 – 2658
    Helixi267 – 27913
    Turni280 – 2834
    Helixi285 – 2873
    Helixi291 – 2988
    Turni304 – 3074
    Beta strandi308 – 3125

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F0YX-ray1.80A/B13-314[»]
    1F12X-ray2.40A/B13-314[»]
    1F14X-ray2.30A/B13-314[»]
    1F17X-ray2.30A/B13-314[»]
    1IL0X-ray2.20A/B13-314[»]
    1LSJX-ray2.50A/B13-314[»]
    1LSOX-ray2.60A/B13-314[»]
    1M75X-ray2.30A/B13-314[»]
    1M76X-ray2.15A/B13-314[»]
    2HDHX-ray2.20A/B24-314[»]
    3HADX-ray2.00A/B13-314[»]
    3RQSX-ray2.00A/B1-314[»]
    ProteinModelPortaliQ16836.
    SMRiQ16836. Positions 1-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16836.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000141498.
    HOVERGENiHBG000832.
    KOiK00022.
    OrthoDBiEOG7K3TMS.
    PhylomeDBiQ16836.
    TreeFamiTF300886.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    PROSITEiPS00067. 3HCDH. 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: Q16836-1) [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

    MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG    50
    HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 100
    ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 150
    LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 200
    SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL 250
    GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN 300
    KFGKKTGEGF YKYK 314
    Length:314
    Mass (Da):34,294
    Last modified:November 2, 2010 - v3
    Checksum:i0C6F7C01BBCE646A
    GO
    Isoform 2 (identifier: Q16836-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGRAGLEAPPPPCGVTGTPGARGLQGRVGPRPQSLAFRGCLPRASSLPGSPRCRRRCHTM
         236-236: R → RDFQTCGDSNSGLGFSLK

    Show »
    Length:390
    Mass (Da):42,140
    Checksum:i3C20D80AAC4EB142
    GO
    Isoform 3 (identifier: Q16836-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         236-236: R → RDFQTCGDSNSGLGFSLK

    Note: No experimental confirmation available.

    Show »
    Length:331
    Mass (Da):36,051
    Checksum:i11B5646AD077A666
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q16836-2)
    Sequence conflicti41 – 411L → P in AAB58153. 1 PublicationCurated
    Sequence conflicti56 – 561R → H in AAB58153. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401A → T in HADH deficiency. 1 Publication
    VAR_024079
    Natural varianti57 – 571D → E in HADH deficiency. 1 Publication
    VAR_024080
    Natural varianti86 – 861L → P.4 Publications
    Corresponds to variant rs4956145 [ dbSNP | Ensembl ].
    VAR_026764
    Natural varianti152 – 1521Q → H.1 Publication
    Corresponds to variant rs1051519 [ dbSNP | Ensembl ].
    VAR_055701
    Natural varianti258 – 2581P → L in HHF4; loss of activity. 1 Publication
    VAR_024081

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGRAGLEAPPPPCGVTGTPG ARGLQGRVGPRPQSLAFRGC LPRASSLPGSPRCRRRCHTM in isoform 2. 1 PublicationVSP_016551
    Alternative sequencei236 – 2361R → RDFQTCGDSNSGLGFSLK in isoform 2 and isoform 3. 1 PublicationVSP_016552

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96752 mRNA. Translation: CAA65528.1.
    AF001902 mRNA. Translation: AAB54008.1.
    AF001903 mRNA. Translation: AAB54009.1.
    AF001904 Genomic DNA. Translation: AAB58153.1.
    AF095703 Genomic DNA. Translation: AAD13581.1.
    AC114733 Genomic DNA. Translation: AAY41050.1.
    AC118062 Genomic DNA. No translation available.
    BC000306 mRNA. Translation: AAH00306.1.
    CCDSiCCDS3678.1. [Q16836-1]
    CCDS54790.1. [Q16836-3]
    PIRiJC4879.
    RefSeqiNP_001171634.2. NM_001184705.2.
    NP_005318.3. NM_005327.4.
    UniGeneiHs.438289.

    Genome annotation databases

    EnsembliENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1]
    ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
    GeneIDi3033.
    KEGGihsa:3033.
    UCSCiuc003hyq.3. human. [Q16836-1]

    Polymorphism databases

    DMDMi311033442.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96752 mRNA. Translation: CAA65528.1 .
    AF001902 mRNA. Translation: AAB54008.1 .
    AF001903 mRNA. Translation: AAB54009.1 .
    AF001904 Genomic DNA. Translation: AAB58153.1 .
    AF095703 Genomic DNA. Translation: AAD13581.1 .
    AC114733 Genomic DNA. Translation: AAY41050.1 .
    AC118062 Genomic DNA. No translation available.
    BC000306 mRNA. Translation: AAH00306.1 .
    CCDSi CCDS3678.1. [Q16836-1 ]
    CCDS54790.1. [Q16836-3 ]
    PIRi JC4879.
    RefSeqi NP_001171634.2. NM_001184705.2.
    NP_005318.3. NM_005327.4.
    UniGenei Hs.438289.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F0Y X-ray 1.80 A/B 13-314 [» ]
    1F12 X-ray 2.40 A/B 13-314 [» ]
    1F14 X-ray 2.30 A/B 13-314 [» ]
    1F17 X-ray 2.30 A/B 13-314 [» ]
    1IL0 X-ray 2.20 A/B 13-314 [» ]
    1LSJ X-ray 2.50 A/B 13-314 [» ]
    1LSO X-ray 2.60 A/B 13-314 [» ]
    1M75 X-ray 2.30 A/B 13-314 [» ]
    1M76 X-ray 2.15 A/B 13-314 [» ]
    2HDH X-ray 2.20 A/B 24-314 [» ]
    3HAD X-ray 2.00 A/B 13-314 [» ]
    3RQS X-ray 2.00 A/B 1-314 [» ]
    ProteinModelPortali Q16836.
    SMRi Q16836. Positions 1-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109283. 7 interactions.
    IntActi Q16836. 3 interactions.
    MINTi MINT-5004681.
    STRINGi 9606.ENSP00000312288.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei Q16836.

    Polymorphism databases

    DMDMi 311033442.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00298406.
    UCD-2DPAGE O00324.
    Q16836.

    Proteomic databases

    MaxQBi Q16836.
    PaxDbi Q16836.
    PRIDEi Q16836.

    Protocols and materials databases

    DNASUi 3033.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309522 ; ENSP00000312288 ; ENSG00000138796 . [Q16836-1 ]
    ENST00000603302 ; ENSP00000474560 ; ENSG00000138796 . [Q16836-3 ]
    GeneIDi 3033.
    KEGGi hsa:3033.
    UCSCi uc003hyq.3. human. [Q16836-1 ]

    Organism-specific databases

    CTDi 3033.
    GeneCardsi GC04P108910.
    GeneReviewsi HADH.
    HGNCi HGNC:4799. HADH.
    HPAi HPA039588.
    HPA043888.
    MIMi 231530. phenotype.
    601609. gene.
    609975. phenotype.
    neXtProti NX_Q16836.
    Orphaneti 71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
    PharmGKBi PA29173.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000141498.
    HOVERGENi HBG000832.
    KOi K00022.
    OrthoDBi EOG7K3TMS.
    PhylomeDBi Q16836.
    TreeFami TF300886.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS06563-MONOMER.
    Reactomei REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RK Q16836.

    Miscellaneous databases

    ChiTaRSi HADH. human.
    EvolutionaryTracei Q16836.
    GeneWikii Hydroxyacyl-Coenzyme_A_dehydrogenase.
    GenomeRNAii 3033.
    NextBioi 12006.
    PROi Q16836.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16836.
    Bgeei Q16836.
    CleanExi HS_HADH.
    Genevestigatori Q16836.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000105. HCDH. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence."
      Vredendaal P.J.C.M., van den Berg I.E.T., Malingre H.E.M., Stroobants A.K., Oldeweghuis D.E.M., Berger R.
      Biochem. Biophys. Res. Commun. 223:718-723(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-86 AND HIS-152.
      Tissue: Liver.
    2. "Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4 glucose transporter cytoplasmic C-terminus: possible crosstalk between glucose transport and fatty acid metabolism."
      Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), VARIANT PRO-86.
      Tissue: Skeletal muscle.
    3. "Human short chain L-3-hydroxyacyl-CoA dehydrogenase."
      O'Brien L.K., Sims H.F., Strauss A.W.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-86.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 PRO-86.
      Tissue: Lung.
    6. "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-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism."
      Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J.
      Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
    9. "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase."
      Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J.
      J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
    10. "3-hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease."
      Yang S.-Y., He X.-Y., Schulz H.
      FEBS J. 272:4874-4883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene."
      O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J., Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W.
      J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000)
      Cited for: VARIANTS HADH DEFICIENCY THR-40 AND GLU-57.
    12. "Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion."
      Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K., Krywawych S., Datta V., Malingre H.E.M., Berger R., van den Berg I.E.T.
      J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HHF4 LEU-258, CHARACTERIZATION OF VARIANT HHF4 LEU-258.

    Entry informationi

    Entry nameiHCDH_HUMAN
    AccessioniPrimary (citable) accession number: Q16836
    Secondary accession number(s): J3KQ17
    , O00324, O00397, O00753, Q4W5B4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 165 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, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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