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Q99714

- HCD2_HUMAN

UniProt

Q99714 - HCD2_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ99714.
CleanExiHS_HSD17B10.
ExpressionAtlasiQ99714. baseline and differential.
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. 28 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 – 165Combined sources
Turni17 – 193Combined sources
Helixi21 – 3212Combined sources
Beta strandi36 – 416Combined sources
Helixi47 – 548Combined sources
Beta strandi58 – 625Combined sources
Helixi68 – 8215Combined sources
Beta strandi87 – 904Combined sources
Beta strandi100 – 1023Combined sources
Turni103 – 1064Combined sources
Helixi111 – 12111Combined sources
Helixi123 – 13614Combined sources
Beta strandi148 – 1536Combined sources
Helixi157 – 1604Combined sources
Helixi166 – 18621Combined sources
Helixi187 – 1893Combined sources
Beta strandi191 – 1988Combined sources
Helixi204 – 2085Combined sources
Helixi216 – 2194Combined sources
Beta strandi222 – 2243Combined sources
Helixi230 – 24213Combined sources
Beta strandi250 – 2545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118868.
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

        10         20         30         40         50
MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ
60 70 80 90 100
AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT
110 120 130 140 150
YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI
160 170 180 190 200
INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL
210 220 230 240 250
FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV
260
IRLDGAIRMQ P
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 28 interactions.
IntActi Q99714. 17 interactions.
MINTi MINT-3059664.
STRINGi 9606.ENSP00000168216.

Chemistry

ChEMBLi CHEMBL4159.

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.
GeneTreei ENSGT00760000118868.
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

Bgeei Q99714.
CleanExi HS_HSD17B10.
ExpressionAtlasi Q99714. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 168 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