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Q99714

- HCD2_HUMAN

UniProt

Q99714 - HCD2_HUMAN

Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

HSD17B10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. Catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD).3 Publications

    Catalytic activityi

    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
    (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.
    Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.

    Kineticsi

    1. KM=25.7 µM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)1 Publication
    2. KM=85.2 µM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    3. KM=41 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    4. KM=5 µM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    5. KM=219 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    6. KM=36.4 µM for chenodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    7. KM=1.7 µM for dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
    8. KM=30.6 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)1 Publication
    9. KM=42.3 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees Celsius, and 7.0 for the reductase reaction at 25 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551Substrate
    Active sitei168 – 1681Proton acceptor
    Binding sitei172 – 1721NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 4130NAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    2. 3-hydroxyacyl-CoA dehydrogenase activity Source: Reactome
    3. cholate 7-alpha-dehydrogenase activity Source: ProtInc
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. lipid metabolic process Source: ProtInc
    4. small molecule metabolic process Source: Reactome
    5. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01071-MONOMER.
    BRENDAi1.1.1.135. 908.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKQ99714.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.35)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.51)
    Short name:
    17-beta-HSD 10
    3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.178)
    3-hydroxyacyl-CoA dehydrogenase type II
    Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
    Mitochondrial ribonuclease P protein 2
    Short name:
    Mitochondrial RNase P protein 2
    Short-chain type dehydrogenase/reductase XH98G2
    Type II HADH
    Gene namesi
    Name:HSD17B10
    Synonyms:ERAB, HADH2, MRPP2, SCHAD, XH98G2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4800. HSD17B10.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. endoplasmic reticulum Source: Ensembl
    3. mitochondrial inner membrane Source: Ensembl
    4. mitochondrial matrix Source: Reactome
    5. mitochondrion Source: UniProtKB
    6. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBD deficiency) [MIM:300438]: A disorder that leads to neurological abnormalities, including psychomotor retardation and, in virtually all patients, loss of mental and motor skills.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221L → V in MHBD deficiency. 1 Publication
    Corresponds to variant rs28935476 [ dbSNP | Ensembl ].
    VAR_015987
    Natural varianti130 – 1301R → C in MHBD deficiency. 2 Publications
    Corresponds to variant rs28935475 [ dbSNP | Ensembl ].
    VAR_015988
    Natural varianti247 – 2471N → S in MHBD deficiency; intermediate enzyme activity. 1 Publication
    VAR_032093
    Mental retardation, X-linked, syndromic, 10 (MRXS10) [MIM:300220]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS10 patients manifest mild mental retardation, choreoathetosis and abnormal behavior.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300220. phenotype.
    300438. phenotype.
    300705. phenotype.
    Orphaneti85295. HSD10 disease, atypical type.
    391428. HSD10 disease, infantile type.
    391457. HSD10 disease, neonatal type.
    PharmGKBiPA162391638.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2PRO_0000054810Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei53 – 531N6-acetyllysine; alternateBy similarity
    Modified residuei53 – 531N6-succinyllysine; alternateBy similarity
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei105 – 1051N6-acetyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
    Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99714.
    PaxDbiQ99714.
    PeptideAtlasiQ99714.
    PRIDEiQ99714.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00017726.
    Q99714.
    UCD-2DPAGEQ99714.

    PTM databases

    PhosphoSiteiQ99714.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in normal tissues but is overexpressed in neurons affected in AD.1 Publication

    Gene expression databases

    ArrayExpressiQ99714.
    BgeeiQ99714.
    CleanExiHS_HSD17B10.
    GenevestigatoriQ99714.

    Organism-specific databases

    HPAiHPA001432.

    Interactioni

    Subunit structurei

    Homotetramer By similarity. Interacts with MRPP1/TRMT10C and MRPP3/KIAA0391.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050674EBI-79964,EBI-77613
    TRMT10CQ7L0Y34EBI-79964,EBI-2107046

    Protein-protein interaction databases

    BioGridi109278. 25 interactions.
    IntActiQ99714. 17 interactions.
    MINTiMINT-3059664.
    STRINGi9606.ENSP00000168216.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 165
    Turni17 – 193
    Helixi21 – 3212
    Beta strandi36 – 416
    Helixi47 – 548
    Beta strandi58 – 625
    Helixi68 – 8215
    Beta strandi87 – 904
    Beta strandi100 – 1023
    Turni103 – 1064
    Helixi111 – 12111
    Helixi123 – 13614
    Beta strandi148 – 1536
    Helixi157 – 1604
    Helixi166 – 18621
    Helixi187 – 1893
    Beta strandi191 – 1988
    Helixi204 – 2085
    Helixi216 – 2194
    Beta strandi222 – 2243
    Helixi230 – 24213
    Beta strandi250 – 2545

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F67model-A1-261[»]
    1SO8X-ray2.30A1-261[»]
    1U7TX-ray2.00A/B/C/D1-261[»]
    2O23X-ray1.20A/B1-261[»]
    ProteinModelPortaliQ99714.
    SMRiQ99714. Positions 7-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99714.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG002145.
    InParanoidiQ99714.
    KOiK08683.
    OMAiLMGANEP.
    PhylomeDBiQ99714.
    TreeFamiTF354307.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 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: Q99714-1) [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

    MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ    50
    AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT 100
    YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI 150
    INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL 200
    FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV 250
    IRLDGAIRMQ P 261
    Length:261
    Mass (Da):26,923
    Last modified:January 23, 2007 - v3
    Checksum:i9E74F242E3E6FEF1
    GO
    Isoform 2 (identifier: Q99714-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-199: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:252
    Mass (Da):25,984
    Checksum:iF36BB71070CE872D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221L → V in MHBD deficiency. 1 Publication
    Corresponds to variant rs28935476 [ dbSNP | Ensembl ].
    VAR_015987
    Natural varianti130 – 1301R → C in MHBD deficiency. 2 Publications
    Corresponds to variant rs28935475 [ dbSNP | Ensembl ].
    VAR_015988
    Natural varianti247 – 2471N → S in MHBD deficiency; intermediate enzyme activity. 1 Publication
    VAR_032093

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei191 – 1999Missing in isoform 2. 1 PublicationVSP_007830

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96132 mRNA. Translation: AAC51812.1.
    U73514 mRNA. Translation: AAB68958.1.
    AF069134 mRNA. Translation: AAC39900.1.
    AF035555 mRNA. Translation: AAC15902.1.
    AF037438 Genomic DNA. Translation: AAC16419.1.
    CR456723 mRNA. Translation: CAG33004.1.
    Z97054 Genomic DNA. Translation: CAI42652.1.
    Z97054 Genomic DNA. Translation: CAI42653.1.
    CH471154 Genomic DNA. Translation: EAW93157.1.
    CH471154 Genomic DNA. Translation: EAW93158.1.
    BC000372 mRNA. Translation: AAH00372.1.
    BC008708 mRNA. Translation: AAH08708.1.
    AY092415 mRNA. Translation: AAM18189.1.
    CCDSiCCDS14354.1. [Q99714-1]
    CCDS35300.1. [Q99714-2]
    RefSeqiNP_001032900.1. NM_001037811.2. [Q99714-2]
    NP_004484.1. NM_004493.2. [Q99714-1]
    UniGeneiHs.171280.

    Genome annotation databases

    EnsembliENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]
    ENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]
    GeneIDi3028.
    KEGGihsa:3028.
    UCSCiuc004dsl.1. human. [Q99714-1]
    uc004dsm.1. human. [Q99714-2]

    Polymorphism databases

    DMDMi2492759.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96132 mRNA. Translation: AAC51812.1 .
    U73514 mRNA. Translation: AAB68958.1 .
    AF069134 mRNA. Translation: AAC39900.1 .
    AF035555 mRNA. Translation: AAC15902.1 .
    AF037438 Genomic DNA. Translation: AAC16419.1 .
    CR456723 mRNA. Translation: CAG33004.1 .
    Z97054 Genomic DNA. Translation: CAI42652.1 .
    Z97054 Genomic DNA. Translation: CAI42653.1 .
    CH471154 Genomic DNA. Translation: EAW93157.1 .
    CH471154 Genomic DNA. Translation: EAW93158.1 .
    BC000372 mRNA. Translation: AAH00372.1 .
    BC008708 mRNA. Translation: AAH08708.1 .
    AY092415 mRNA. Translation: AAM18189.1 .
    CCDSi CCDS14354.1. [Q99714-1 ]
    CCDS35300.1. [Q99714-2 ]
    RefSeqi NP_001032900.1. NM_001037811.2. [Q99714-2 ]
    NP_004484.1. NM_004493.2. [Q99714-1 ]
    UniGenei Hs.171280.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F67 model - A 1-261 [» ]
    1SO8 X-ray 2.30 A 1-261 [» ]
    1U7T X-ray 2.00 A/B/C/D 1-261 [» ]
    2O23 X-ray 1.20 A/B 1-261 [» ]
    ProteinModelPortali Q99714.
    SMRi Q99714. Positions 7-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109278. 25 interactions.
    IntActi Q99714. 17 interactions.
    MINTi MINT-3059664.
    STRINGi 9606.ENSP00000168216.

    Chemistry

    BindingDBi Q99714.
    ChEMBLi CHEMBL4159.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei Q99714.

    Polymorphism databases

    DMDMi 2492759.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00017726.
    Q99714.
    UCD-2DPAGE Q99714.

    Proteomic databases

    MaxQBi Q99714.
    PaxDbi Q99714.
    PeptideAtlasi Q99714.
    PRIDEi Q99714.

    Protocols and materials databases

    DNASUi 3028.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000168216 ; ENSP00000168216 ; ENSG00000072506 . [Q99714-1 ]
    ENST00000375304 ; ENSP00000364453 ; ENSG00000072506 . [Q99714-2 ]
    GeneIDi 3028.
    KEGGi hsa:3028.
    UCSCi uc004dsl.1. human. [Q99714-1 ]
    uc004dsm.1. human. [Q99714-2 ]

    Organism-specific databases

    CTDi 3028.
    GeneCardsi GC0XM053475.
    HGNCi HGNC:4800. HSD17B10.
    HPAi HPA001432.
    MIMi 300220. phenotype.
    300256. gene.
    300438. phenotype.
    300705. phenotype.
    neXtProti NX_Q99714.
    Orphaneti 85295. HSD10 disease, atypical type.
    391428. HSD10 disease, infantile type.
    391457. HSD10 disease, neonatal type.
    PharmGKBi PA162391638.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG002145.
    InParanoidi Q99714.
    KOi K08683.
    OMAi LMGANEP.
    PhylomeDBi Q99714.
    TreeFami TF354307.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01071-MONOMER.
    BRENDAi 1.1.1.135. 908.
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK Q99714.

    Miscellaneous databases

    ChiTaRSi HSD17B10. human.
    EvolutionaryTracei Q99714.
    GeneWikii HSD17B10.
    GenomeRNAii 3028.
    NextBioi 11984.
    PROi Q99714.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99714.
    Bgeei Q99714.
    CleanExi HS_HSD17B10.
    Genevestigatori Q99714.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease."
      Yan S.D., Fu J., Soto C., Chen X., Zhu H., Al-Mohanna F., Collinson K., Zhu A., Stern E., Saido T., Tohyama M., Ogawa S., Roher A., Stern D.
      Nature 389:689-695(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Zhuchenko O.P., Wehnert M., Bailey J., Sun Z.S., Lee C.C.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Chromosomal basis of X chromosome inactivation: identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation."
      Miller A.P., Willard H.F.
      Proc. Natl. Acad. Sci. U.S.A. 95:8709-8714(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease."
      He X.Y., Schulz H., Yang S.Y.
      J. Biol. Chem. 273:10741-10746(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CATALYTIC ACTIVITY.
      Tissue: Brain.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    9. "Expression, release and induction of endoplasmic reticulum-associated amyloid beta-binding protein in brain disease."
      Deininger M.H., Meyermann R., Schluesener H.J.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-246.
    10. "Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD."
      Shafqat N., Marschall H.U., Filling C., Nordling E., Wu X.Q., Bjork L., Thyberg J., Martensson E., Salim S., Jornvall H., Oppermann U.
      Biochem. J. 376:49-60(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    11. "The reduced expression of the HADH2 protein causes X-linked mental retardation, choreoathetosis, and abnormal behavior."
      Lenski C., Kooy R.F., Reyniers E., Loessner D., Wanders R.J.A., Winnepenninckx B., Hellebrand H., Engert S., Schwartz C.E., Meindl A., Ramser J.
      Am. J. Hum. Genet. 80:372-377(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRXS10.
    12. Cited for: INVOLVEMENT IN MRX17.
    13. "RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme."
      Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C., Rossmanith W.
      Cell 135:462-474(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH KIAA0391 AND TRMT10C, SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of human ABAD/HSD10 with a bound inhibitor: implications for design of Alzheimer's disease therapeutics."
      Kissinger C.R., Rejto P.A., Pelletier L.A., Thomson J.A., Showalter R.E., Abreo M.A., Agree C.S., Margosiak S., Meng J.J., Aust R.M., Vanderpool D., Li B., Tempczyk-Russell A., Villafranca J.E.
      J. Mol. Biol. 342:943-952(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    17. "2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene."
      Ofman R., Ruiter J.P.N., Feenstra M., Duran M., Poll-The B.T., Zschocke J., Ensenauer R., Lehnert W., Sass J.O., Sperl W., Wanders R.J.A.
      Am. J. Hum. Genet. 72:1300-1307(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MHBD DEFICIENCY VAL-122 AND CYS-130.
    18. "2-methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease."
      Perez-Cerda C., Garcia-Villoria J., Ofman R., Sala P.R., Merinero B., Ramos J., Garcia-Silva M.T., Beseler B., Dalmau J., Wanders R.J.A., Ugarte M., Ribes A.
      Pediatr. Res. 58:488-491(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MHBD DEFICIENCY CYS-130 AND SER-247, CHARACTERIZATION OF VARIANT MHBD DEFICIENCY SER-247.

    Entry informationi

    Entry nameiHCD2_HUMAN
    AccessioniPrimary (citable) accession number: Q99714
    Secondary accession number(s): Q5H927
    , Q6IBS9, Q8TCV9, Q96HD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 166 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3