HSD17B10

Functionⁱ

Mitochondrial dehydrogenase that catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone (PubMed:9553139, PubMed:23042678, PubMed:12917011, PubMed:18996107, PubMed:25925575, PubMed:28888424). Catalyzes the third step in the beta-oxidation of fatty acids (PubMed:9553139, PubMed:12917011, PubMed:18996107, PubMed:25925575, PubMed:28888424). Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids (PubMed:12917011). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids (PubMed:12917011). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426).9 Publications

In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424). Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N₁-methylguanine and N₁-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705).7 Publications

Catalytic activityⁱ

(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD⁺ = 2-methylacetoacetyl-CoA + NADH.1 Publication

Testosterone + NAD(P)⁺ = androst-4-ene-3,17-dione + NAD(P)H.2 Publications

(S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.5 Publications

Kineticsⁱ

Kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). Kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	155	Substrate1 Publication	1
Active siteⁱ	168	Proton acceptor1 Publication	1
Binding siteⁱ	172	NAD1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	12 – 41	NAD1 PublicationAdd BLAST		30

GO - Molecular functionⁱ

3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
3-hydroxyacyl-CoA dehydrogenase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 25925575
- 28888424
cholate 7-alpha-dehydrogenase activity
Source: ProtInc
Traceable author statementⁱ
- 9338779
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22681889
testosterone dehydrogenase [NAD(P)] activity
Source: UniProtKB
Inferred from direct assayⁱ
- 28888424
tRNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 29040705

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

branched-chain amino acid catabolic process Source: Reactome
lipid metabolic process
Source: ProtInc
Traceable author statementⁱ
- 9338779
mitochondrial tRNA 3'-end processing
Source: UniProtKB
Inferred from direct assayⁱ
- 29040705
mitochondrial tRNA 5'-end processing
Source: UniProtKB
Inferred from direct assayⁱ
mitochondrial tRNA methylation
Source: UniProtKB
Inferred from direct assayⁱ
- 25925575
- 28888424
mitochondrial tRNA processing Source: Reactome
mitochondrion organization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20077426
protein homotetramerization
Source: UniProtKB
Inferred from direct assayⁱ
- 25925575

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	tRNA processing
Ligand	NAD

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS01071-MONOMER
BRENDAⁱ	1.1.1.178 2681 1.1.1.35 2681
Reactomeⁱ	R-HSA-6785470 tRNA processing in the mitochondrion R-HSA-6787450 tRNA modification in the mitochondrion R-HSA-70895 Branched-chain amino acid catabolism R-HSA-8868766 rRNA processing in the mitochondrion
SABIO-RKⁱ	Q99714

Chemistry databases

SwissLipidsⁱ	SLP:000000787

SwissLipidsⁱ

SLP:000000787

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.355 Publications) Alternative name(s): 17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.512 Publications) Short name: 17-beta-HSD 10 2-methyl-3-hydroxybutyryl-CoA dehydrogenase1 Publication Short name: MHBD1 Publication 3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.1781 Publication) 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 dehydrogenase/reductase family 5C member 1 Short-chain type dehydrogenase/reductase XH98G2 Type II HADH
Gene namesⁱ	Name:HSD17B10 Synonyms:ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000072506.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4800 HSD17B10
MIMⁱ	300256 gene
neXtProtⁱ	NX_Q99714

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

HDS10 mitochondrial disease (HSD10MD)12 Publications

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

Disease descriptionAn X-linked multisystemic disorder with highly variable severity. Age at onset ranges from the neonatal period to early childhood. Features include progressive neurodegeneration, psychomotor retardation, loss of mental and motor skills, seizures, cardiomyopathy, and visual and hearing impairment. Some patients manifest lactic acidosis and metabolic acidosis.

Mental retardation, X-linked 17 (MRX17)1 Publication

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.

Disease descriptionA 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.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	20	S → F: Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. 2 Publications		1
Mutagenesisⁱ	172	K → A: Abolishes dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. Does not affect homotetramerization. 2 Publications		1

Keywords - Diseaseⁱ

Disease mutation, Mental retardation, Neurodegeneration

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3028
MalaCards human disease database More...MalaCardsⁱ	HSD17B10
MIMⁱ	300438 phenotype 300705 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000072506
Orphanetⁱ	85295 HSD10 disease, atypical type 391428 HSD10 disease, infantile type 391457 HSD10 disease, neonatal type
PharmGKBⁱ	PA162391638

Chemistry databases

ChEMBLⁱ	CHEMBL4159
Drug and drug target database More...DrugBankⁱ	DB00157 NADH

Polymorphism and mutation databases

BioMutaⁱ	HSD17B10
DMDMⁱ	2492759

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000054810	2 – 261	3-hydroxyacyl-CoA dehydrogenase type-2Add BLAST		260

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources	1
Modified residueⁱ	53	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	53	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	69	N6-acetyllysineBy similarity	1
Modified residueⁱ	99	N6-acetyllysineBy similarity	1
Modified residueⁱ	105	N6-acetyllysineBy similarity	1
Modified residueⁱ	212	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	212	N6-succinyllysine; alternateBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q99714
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q99714
PaxDbⁱ	Q99714
PeptideAtlas More...PeptideAtlasⁱ	Q99714
PRIDEⁱ	Q99714
ProteomicsDBⁱ	78427 78428 [Q99714-2]
TopDownProteomicsⁱ	Q99714-1 [Q99714-1] Q99714-2 [Q99714-2]

2D gel databases

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

PTM databases

iPTMnetⁱ	Q99714
PhosphoSitePlusⁱ	Q99714
SwissPalmⁱ	Q99714

Expressionⁱ

Tissue specificityⁱ

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

Gene expression databases

Bgeeⁱ	ENSG00000072506 Expressed in 104 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_HSD17B10
ExpressionAtlasⁱ	Q99714 baseline and differential
Genevisibleⁱ	Q99714 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA001432

HPAⁱ

HPA001432

Interactionⁱ

Subunit structureⁱ

Homotetramer (PubMed:15342248, PubMed:20077426, PubMed:25925575). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31 (PubMed:18984158, PubMed:25925575, PubMed:26950678, PubMed:28888424). Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex (PubMed:23042678, PubMed:29040705).8 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
APP	P05067	4	EBI-79964,EBI-77613
EEF2	P13639	3	EBI-79964,EBI-352560
TRAP1	Q12931	3	EBI-79964,EBI-1055869
TRMT10C	Q7L0Y3	4	EBI-79964,EBI-2107046

Protein-protein interaction databases

BioGridⁱ	109278, 381 interactors
IntActⁱ	Q99714, 181 interactors
Molecular INTeraction database More...MINTⁱ	Q99714
STRINGⁱ	9606.ENSP00000168216

Chemistry databases

BindingDBⁱ	Q99714

BindingDBⁱ

Q99714

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	12 – 16	Combined sources	5
Turnⁱ	17 – 19	Combined sources	3
Helixⁱ	21 – 32	Combined sources	12
Beta strandⁱ	36 – 41	Combined sources	6
Helixⁱ	47 – 54	Combined sources	8
Beta strandⁱ	58 – 62	Combined sources	5
Helixⁱ	68 – 82	Combined sources	15
Beta strandⁱ	87 – 90	Combined sources	4
Beta strandⁱ	100 – 102	Combined sources	3
Turnⁱ	103 – 106	Combined sources	4
Helixⁱ	111 – 121	Combined sources	11
Helixⁱ	123 – 136	Combined sources	14
Beta strandⁱ	148 – 153	Combined sources	6
Helixⁱ	157 – 160	Combined sources	4
Helixⁱ	166 – 186	Combined sources	21
Helixⁱ	187 – 189	Combined sources	3
Beta strandⁱ	191 – 198	Combined sources	8
Helixⁱ	204 – 208	Combined sources	5
Helixⁱ	216 – 219	Combined sources	4
Beta strandⁱ	222 – 224	Combined sources	3
Helixⁱ	230 – 242	Combined sources	13
Beta strandⁱ	250 – 254	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	Q99714
SMRⁱ	Q99714
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q99714

EvolutionaryTraceⁱ

Q99714

Family & Domainsⁱ

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG1199 Eukaryota ENOG410XNNW LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00920000148965
HOVERGENⁱ	HBG002145
InParanoidⁱ	Q99714
KEGG Orthology (KO) More...KOⁱ	K08683
OMAⁱ	LMGLVNC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0G9O
PhylomeDBⁱ	Q99714
TreeFamⁱ	TF354307

Family and domain databases

InterProⁱ	View protein in InterPro IPR036291 NAD(P)-bd_dom_sf IPR020904 Sc_DH/Rdtase_CS IPR002347 SDR_fam
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00106 adh_short, 1 hit
PRINTSⁱ	PR00081 GDHRDH PR00080 SDRFAMILY
SUPFAMⁱ	SSF51735 SSF51735, 1 hit
PROSITEⁱ	View protein in PROSITE PS00061 ADH_SHORT, 1 hit

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 Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.ⁱShow all

Isoform 1 (identifier: Q99714-1) [UniParc]FASTA Add 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]FASTA Add to basket

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

« 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 LFGTPLLTSL 
       210        220        230        240        250
PEKVCNFLAS QVPFPSRLGD PAEYAHLVQA IIENPFLNGE VIRLDGAIRM 

QP

Note: No experimental confirmation available.

Show »

Length:252

Mass (Da):25,984

Checksum:ⁱF36BB71070CE872D

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation
	Q5H928	Q5H928_HUMAN		3-hydroxyacyl-CoA dehydrogenase typ... 3-hydroxyacyl-CoA dehydrogenase type-2 (Hydroxysteroid (17-beta) dehydrogenase 10)	HSD17B10 RP3-339A18.2-004	169	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_080049	12	V → L in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing. 1 Publication	1
Natural variantⁱVAR_078863	65	V → A in HSD10MD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs104886492EnsemblClinVar.	1
Natural variantⁱVAR_078864	86	D → G in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD+ binding. 1 PublicationCorresponds to variant dbSNP:rs587777651EnsemblClinVar.	1
Natural variantⁱVAR_015987	122	L → V in HSD10MD. 1 PublicationCorresponds to variant dbSNP:rs28935476EnsemblClinVar.	1
Natural variantⁱVAR_015988	130	R → C in HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization. 7 PublicationsCorresponds to variant dbSNP:rs28935475EnsemblClinVar.	1
Natural variantⁱVAR_078865	165	Q → H in HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD+. 2 Publications	1
Natural variantⁱVAR_080050	176	V → M in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing. 1 Publication	1
Natural variantⁱVAR_080051	210	P → S in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization. 2 Publications	1
Natural variantⁱVAR_078866	212	K → E in HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing. 1 PublicationCorresponds to variant dbSNP:rs886041974EnsemblClinVar.	1
Natural variantⁱVAR_080052	226	R → Q in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 2 Publications	1
Natural variantⁱVAR_032093	247	N → S in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 3 PublicationsCorresponds to variant dbSNP:rs122461163Ensembl.	1
Natural variantⁱVAR_078867	249	E → Q in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity. 1 PublicationCorresponds to variant dbSNP:rs62626305Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_007830	191 – 199	Missing in isoform 2. 1 Publication		9

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14354.1 [Q99714-1] CCDS35300.1 [Q99714-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001032900.1, NM_001037811.2 [Q99714-2] NP_004484.1, NM_004493.2 [Q99714-1]
UniGeneⁱ	Hs.171280

Genome annotation databases

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

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q99714	Hydroxysteroid dehydrogenase 10 isoform 1 (Fragment)		HUMAN		261	UniRef100_Q99714
HSD17B10 isoform 1		PANTR		261
Hydroxysteroid 17-beta dehydrogenase 10		PANPA		261
UPI0000E9BBD5		HUMAN		265

Protein	Similar proteins		Species	Score	Length	Source
Q99714	Hydroxysteroid dehydrogenase 10 isoform 1 (Fragment)		HUMAN		261	UniRef90_Q99714
HSD17B10 isoform 1		PANTR		261
Hydroxysteroid 17-beta dehydrogenase 10		PANPA		261
Hydroxysteroid 17-beta dehydrogenase 10		OTOGA		261
Hydroxysteroid 17-beta dehydrogenase 10		NOMLE		261
+44

Protein	Similar proteins		Species	Score	Length	Source
Q99714	3-hydroxyacyl-CoA dehydrogenase type-2		MOUSE		261	UniRef50_Q99714
3-hydroxyacyl-CoA dehydrogenase type-2		DROME		255
3-hydroxyacyl-CoA dehydrogenase type-2	)	RAT		261
Hydroxysteroid dehydrogenase 10 isoform 1 (Fragment)		HUMAN		261
HSD17B10 isoform 1		PANTR		261
+2868

Entry informationⁱ

Entry nameⁱ	HCD2_HUMAN
Accessionⁱ	Q99714Primary (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:	September 12, 2018
	This is version 200 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q99714 (HCD2_HUMAN)

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3-hydroxyacyl-CoA dehydrogenase type-2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ