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Q99714 (HCD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyacyl-CoA dehydrogenase type-2

EC=1.1.1.35
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 10
Short name=17-beta-HSD 10
EC=1.1.1.51
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 names
Name:HSD17B10
Synonyms:ERAB, HADH2, MRPP2, SCHAD, XH98G2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.10 Ref.13

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. Ref.4 Ref.10

(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH. Ref.4 Ref.10

Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H. Ref.4 Ref.10

Subunit structure

Homotetramer By similarity. Interacts with MRPP1/TRMT10C and MRPP3/KIAA0391. Ref.13

Subcellular location

Mitochondrion Ref.10 Ref.13.

Tissue specificity

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

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.
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. Ref.12

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

KM=25.7 µM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius) Ref.10

KM=85.2 µM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

KM=41 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

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)

KM=219 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

KM=36.4 µM for chenodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

KM=1.7 µM for dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

KM=30.6 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)

KM=42.3 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)

pH dependence:

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

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseDisease mutation
Mental retardation
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranched-chain amino acid catabolic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

lipid metabolic process

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_function3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-hydroxyacyl-CoA dehydrogenase activity

Inferred from experiment. Source: Reactome

cholate 7-alpha-dehydrogenase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.1. Source: IntAct

testosterone dehydrogenase [NAD(P)] activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050674EBI-79964,EBI-77613
TRMT10CQ7L0Y34EBI-79964,EBI-2107046

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99714-1)

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.
Isoform 2 (identifier: Q99714-2)

The sequence of this isoform differs from the canonical sequence as follows:
     191-199: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2
PRO_0000054810

Regions

Nucleotide binding12 – 4130NAD

Sites

Active site1681Proton acceptor
Binding site1551Substrate
Binding site1721NAD

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue531N6-acetyllysine; alternate By similarity
Modified residue531N6-succinyllysine; alternate By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue991N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence191 – 1999Missing in isoform 2.
VSP_007830
Natural variant1221L → V in MHBD deficiency. Ref.17
Corresponds to variant rs28935476 [ dbSNP | Ensembl ].
VAR_015987
Natural variant1301R → C in MHBD deficiency. Ref.17 Ref.18
Corresponds to variant rs28935475 [ dbSNP | Ensembl ].
VAR_015988
Natural variant2471N → S in MHBD deficiency; intermediate enzyme activity. Ref.18
VAR_032093

Secondary structure

.......................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9E74F242E3E6FEF1

FASTA26126,923
        10         20         30         40         50         60 
MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF 

        70         80         90        100        110        120 
APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV 

       130        140        150        160        170        180 
NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL 

       190        200        210        220        230        240 
PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI 

       250        260 
IENPFLNGEV IRLDGAIRMQ P 

« Hide

Isoform 2 [UniParc].

Checksum: F36BB71070CE872D
Show »

FASTA25225,984

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation."
Froyen G., Corbett M., Vandewalle J., Jarvela I., Lawrence O., Meldrum C., Bauters M., Govaerts K., Vandeleur L., Van Esch H., Chelly J., Sanlaville D., van Bokhoven H., Ropers H.-H., Laumonnier F., Ranieri E., Schwartz C.E., Abidi F. expand/collapse author list , Tarpey P.S., Futreal P.A., Whibley A., Raymond F.L., Stratton M.R., Fryns J.-P., Scott R., Peippo M., Sipponen M., Partington M., Mowat D., Field M., Hackett A., Marynen P., Turner G., Gecz J.
Am. J. Hum. Genet. 82:432-443(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease."
Lustbader J.W., Cirilli M., Lin C., Xu H.W., Takuma K., Wang N., Caspersen C., Chen X., Pollak S., Chaney M., Trinchese F., Liu S., Gunn-Moore F., Lue L.-F., Walker D.G., Kuppusamy P., Zewier Z.L., Arancio O. expand/collapse author list , Stern D., Yan S.-S., Wu H.
Science 304:448-452(2004) [PubMed] [Europe PMC] [Abstract]
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.
[19]Erratum
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., Ugarte M., Ribes A.
Pediatr. Res. 59:162-162(2006)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14354.1. [Q99714-1]
CCDS35300.1. [Q99714-2]
RefSeqNP_001032900.1. NM_001037811.2. [Q99714-2]
NP_004484.1. NM_004493.2. [Q99714-1]
UniGeneHs.171280.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F67model-A1-261[»]
1SO8X-ray2.30A1-261[»]
1U7TX-ray2.00A/B/C/D1-261[»]
2O23X-ray1.20A/B1-261[»]
ProteinModelPortalQ99714.
SMRQ99714. Positions 7-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109278. 24 interactions.
IntActQ99714. 18 interactions.
MINTMINT-3059664.
STRING9606.ENSP00000168216.

Chemistry

BindingDBQ99714.
ChEMBLCHEMBL4159.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ99714.

Polymorphism databases

DMDM2492759.

2D gel databases

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

Proteomic databases

MaxQBQ99714.
PaxDbQ99714.
PeptideAtlasQ99714.
PRIDEQ99714.

Protocols and materials databases

DNASU3028.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]
ENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]
ENST00000595128; ENSP00000471470; ENSG00000268188. [Q99714-2]
ENST00000601615; ENSP00000472168; ENSG00000268188. [Q99714-1]
GeneID3028.
KEGGhsa:3028.
UCSCuc004dsl.1. human. [Q99714-1]
uc004dsm.1. human. [Q99714-2]

Organism-specific databases

CTD3028.
GeneCardsGC0XM053475.
HGNCHGNC:4800. HSD17B10.
HPAHPA001432.
MIM300220. phenotype.
300256. gene.
300438. phenotype.
300705. phenotype.
neXtProtNX_Q99714.
Orphanet85295. HSD10 disease, atypical type.
391428. HSD10 disease, infantile type.
391457. HSD10 disease, neonatal type.
PharmGKBPA162391638.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG002145.
InParanoidQ99714.
KOK08683.
OMALMGANEP.
PhylomeDBQ99714.
TreeFamTF354307.

Enzyme and pathway databases

BioCycMetaCyc:HS01071-MONOMER.
BRENDA1.1.1.135. 908.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ99714.

Gene expression databases

ArrayExpressQ99714.
BgeeQ99714.
CleanExHS_HSD17B10.
GenevestigatorQ99714.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSD17B10. human.
EvolutionaryTraceQ99714.
GeneWikiHSD17B10.
GenomeRNAi3028.
NextBio11984.
PROQ99714.
SOURCESearch...

Entry information

Entry nameHCD2_HUMAN
AccessionPrimary (citable) accession number: Q99714
Secondary accession number(s): Q5H927 expand/collapse secondary AC list , Q6IBS9, Q8TCV9, Q96HD5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM