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Protein

Peroxisomal multifunctional enzyme type 2

Gene

HSD17B4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids.2 Publications

Catalytic activityi

(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.1 Publication
(24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H2O.1 Publication
(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=10 µM for D-3-hydroxy-octanoyl-CoA1 Publication
  2. KM=13 µM for NAD1 Publication
  3. KM=2.7 µM for 3-ketooctanoyl-CoA1 Publication
  4. KM=5.4 µM for NADH1 Publication
  1. Vmax=8.8 µmol/min/mg enzyme1 Publication

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21NAD; via amide nitrogen1
Binding sitei40NAD1
Binding sitei99NAD; via carbonyl oxygen1
Binding sitei151SubstrateBy similarity1
Active sitei164Proton acceptorPROSITE-ProRule annotation1
Binding sitei435(3R)-3-hydroxydecanoyl-CoABy similarity1
Binding sitei533(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity1
Binding sitei563(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei706Substrate1
Binding sitei724Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 37NADBy similarityAdd BLAST25
Nucleotide bindingi75 – 76NAD2
Nucleotide bindingi164 – 168NAD5
Nucleotide bindingi196 – 199NAD4

GO - Molecular functioni

GO - Biological processi

  • alpha-linolenic acid metabolic process Source: Reactome
  • androgen metabolic process Source: UniProtKB
  • bile acid biosynthetic process Source: Reactome
  • estrogen metabolic process Source: UniProtKB
  • fatty acid beta-oxidation Source: UniProtKB
  • fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  • medium-chain fatty-acyl-CoA metabolic process Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • Sertoli cell development Source: Ensembl
  • very long-chain fatty acid metabolic process Source: Ensembl
  • very long-chain fatty-acyl-CoA metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS05792-MONOMER.
ZFISH:HS05792-MONOMER.
BRENDAi4.2.1.119. 2681.
ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-389887. Beta-oxidation of pristanoyl-CoA.
R-HSA-390247. Beta-oxidation of very long chain fatty acids.
SABIO-RKP51659.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000000540.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal multifunctional enzyme type 2
Short name:
MFE-2
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 4
Short name:
17-beta-HSD 4
D-bifunctional protein
Short name:
DBP
Multifunctional protein 2
Short name:
MPF-2
Short chain dehydrogenase/reductase family 8C member 1
Cleaved into the following 2 chains:
Alternative name(s):
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Gene namesi
Name:HSD17B4
Synonyms:EDH17B4, SDR8C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5213. HSD17B4.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • peroxisomal matrix Source: Reactome
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

D-bifunctional protein deficiency (DBPD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDisorder of peroxisomal fatty acid beta-oxidation.
See also OMIM:261515
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03757616G → S in DBPD; no dehydrogenase activity. 2 PublicationsCorresponds to variant rs137853096dbSNPEnsembl.1
Natural variantiVAR_065906106R → P in DBPD. 1 PublicationCorresponds to variant rs25640dbSNPEnsembl.1
Natural variantiVAR_065908457N → Y in DBPD; the mutation leads to an unstable protein. 1 PublicationCorresponds to variant rs137853097dbSNPEnsembl.1
Perrault syndrome 1 (PRLTS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA sex-influenced disorder characterized by sensorineural deafness in both males and females and ovarian dysgenesis in females. Some patients also have neurologic manifestations, including mild mental retardation and cerebellar and peripheral nervous system involvement.
See also OMIM:233400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065907217Y → C in PRLTS1. 1 PublicationCorresponds to variant rs387906825dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi347Y → A: No hydratase activity. 1 Publication1
Mutagenesisi366E → A: No hydratase activity. 1 Publication1
Mutagenesisi370D → A: No effect. 1 Publication1
Mutagenesisi406H → A: No effect. 1 Publication1
Mutagenesisi408E → A: No effect. 1 Publication1
Mutagenesisi410Y → A: No effect. 1 Publication1
Mutagenesisi490D → A: No effect. 1 Publication1
Mutagenesisi505Y → A: Completely inactive. 1 Publication1
Mutagenesisi510D → A: No hydratase activity. 1 Publication1
Mutagenesisi515H → A: Completely inactive. 1 Publication1
Mutagenesisi517D → A: No effect. 1 Publication1
Mutagenesisi532H → A: No effect. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

DisGeNETi3295.
MalaCardsiHSD17B4.
MIMi233400. phenotype.
261515. phenotype.
OpenTargetsiENSG00000133835.
Orphaneti300. Bifunctional enzyme deficiency.
2855. Perrault syndrome.
PharmGKBiPA29481.

Chemistry databases

ChEMBLiCHEMBL5814.

Polymorphism and mutation databases

BioMutaiHSD17B4.
DMDMi1706396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000545831 – 736Peroxisomal multifunctional enzyme type 2Add BLAST736
ChainiPRO_00004000821 – 311(3R)-hydroxyacyl-CoA dehydrogenaseAdd BLAST311
ChainiPRO_0000400083312 – 736Enoyl-CoA hydratase 2Add BLAST425

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine; alternateBy similarity1
Modified residuei46N6-succinyllysine; alternateBy similarity1
Modified residuei52PhosphoserineCombined sources1
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei84N6-succinyllysineBy similarity1
Modified residuei265PhosphothreonineCombined sources1
Modified residuei275N6-succinyllysineBy similarity1
Modified residuei304PhosphoserineCombined sources1
Modified residuei309PhosphoserineCombined sources1
Modified residuei356N6-succinyllysineBy similarity1
Modified residuei424N6-succinyllysineBy similarity1
Modified residuei565N6-acetyllysineCombined sources1
Modified residuei579N6-succinyllysineBy similarity1
Modified residuei663N6-succinyllysineBy similarity1
Modified residuei669N6-acetyllysineCombined sources1
Modified residuei707N6-acetyllysineCombined sources1
Modified residuei725N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP51659.
MaxQBiP51659.
PaxDbiP51659.
PeptideAtlasiP51659.
PRIDEiP51659.
TopDownProteomicsiP51659-1. [P51659-1]

PTM databases

iPTMnetiP51659.
PhosphoSitePlusiP51659.
SwissPalmiP51659.

Expressioni

Tissue specificityi

Present in many tissues with highest concentrations in liver, heart, prostate and testis.

Gene expression databases

BgeeiENSG00000133835.
CleanExiHS_HSD17B4.
ExpressionAtlasiP51659. baseline and differential.
GenevisibleiP51659. HS.

Organism-specific databases

HPAiHPA021302.
HPA021311.
HPA021479.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109528. 41 interactors.
IntActiP51659. 28 interactors.
MINTiMINT-1135639.
STRINGi9606.ENSP00000420914.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Turni15 – 18Combined sources4
Helixi20 – 31Combined sources12
Beta strandi35 – 39Combined sources5
Helixi53 – 64Combined sources12
Beta strandi68 – 72Combined sources5
Helixi76 – 78Combined sources3
Helixi79 – 90Combined sources12
Beta strandi95 – 98Combined sources4
Helixi108 – 110Combined sources3
Helixi113 – 141Combined sources29
Beta strandi144 – 149Combined sources6
Helixi152 – 156Combined sources5
Helixi162 – 182Combined sources21
Helixi183 – 185Combined sources3
Beta strandi187 – 194Combined sources8
Turni199 – 204Combined sources6
Helixi207 – 212Combined sources6
Helixi215 – 217Combined sources3
Helixi219 – 225Combined sources7
Beta strandi236 – 240Combined sources5
Beta strandi243 – 251Combined sources9
Helixi266 – 271Combined sources6
Helixi273 – 277Combined sources5
Helixi288 – 303Combined sources16
Beta strandi335 – 339Combined sources5
Helixi341 – 350Combined sources10
Helixi358 – 360Combined sources3
Helixi361 – 364Combined sources4
Helixi375 – 377Combined sources3
Helixi378 – 381Combined sources4
Helixi383 – 385Combined sources3
Helixi401 – 403Combined sources3
Beta strandi405 – 415Combined sources11
Beta strandi419 – 432Combined sources14
Beta strandi440 – 462Combined sources23
Beta strandi490 – 496Combined sources7
Helixi501 – 505Combined sources5
Helixi506 – 508Combined sources3
Helixi513 – 515Combined sources3
Helixi518 – 522Combined sources5
Turni523 – 525Combined sources3
Helixi533 – 548Combined sources16
Helixi553 – 555Combined sources3
Beta strandi556 – 563Combined sources8
Beta strandi572 – 580Combined sources9
Beta strandi583 – 590Combined sources8
Turni591 – 593Combined sources3
Beta strandi596 – 605Combined sources10
Helixi624 – 646Combined sources23
Beta strandi648 – 670Combined sources23
Beta strandi674 – 679Combined sources6
Beta strandi685 – 691Combined sources7
Helixi692 – 699Combined sources8
Helixi705 – 710Combined sources6
Beta strandi713 – 719Combined sources7
Helixi720 – 733Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IKTX-ray1.75A618-736[»]
1S9CX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L318-615[»]
1ZBQX-ray2.71A/B/C/D/E/F1-304[»]
ProteinModelPortaliP51659.
SMRiP51659.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51659.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini484 – 600MaoC-likeAdd BLAST117
Domaini624 – 736SCP2Add BLAST113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 305(3R)-hydroxyacyl-CoA dehydrogenaseAdd BLAST305
Regioni322 – 622Enoyl-CoA hydratase 2Add BLAST301
Regioni406 – 407(3R)-3-hydroxydecanoyl-CoA bindingBy similarity2
Regioni510 – 515(3R)-3-hydroxydecanoyl-CoA bindingBy similarity6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi734 – 736Microbody targeting signalSequence analysis3

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated
Contains 1 SCP2 domain.Curated

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP51659.
KOiK12405.
OMAiTVMPEDL.
OrthoDBiEOG091G02S9.
PhylomeDBiP51659.
TreeFamiTF105656.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51659-1) [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
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK
60 70 80 90 100
GSLAADKVVE EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA
110 120 130 140 150
GILRDRSFAR ISDEDWDIIH RVHLRGSFQV TRAAWEHMKK QKYGRIIMTS
160 170 180 190 200
SASGIYGNFG QANYSAAKLG LLGLANSLAI EGRKSNIHCN TIAPNAGSRM
210 220 230 240 250
TQTVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE
260 270 280 290 300
RTLGAIVRQK NHPMTPEAVK ANWKKICDFE NASKPQSIQE STGSIIEVLS
310 320 330 340 350
KIDSEGGVSA NHTSRATSTA TSGFAGAIGQ KLPPFSYAYT ELEAIMYALG
360 370 380 390 400
VGASIKDPKD LKFIYEGSSD FSCLPTFGVI IGQKSMMGGG LAEIPGLSIN
410 420 430 440 450
FAKVLHGEQY LELYKPLPRA GKLKCEAVVA DVLDKGSGVV IIMDVYSYSE
460 470 480 490 500
KELICHNQFS LFLVGSGGFG GKRTSDKVKV AVAIPNRPPD AVLTDTTSLN
510 520 530 540 550
QAALYRLSGD WNPLHIDPNF ASLAGFDKPI LHGLCTFGFS ARRVLQQFAD
560 570 580 590 600
NDVSRFKAIK ARFAKPVYPG QTLQTEMWKE GNRIHFQTKV QETGDIVISN
610 620 630 640 650
AYVDLAPTSG TSAKTPSEGG KLQSTFVFEE IGRRLKDIGP EVVKKVNAVF
660 670 680 690 700
EWHITKGGNI GAKWTIDLKS GSGKVYQGPA KGAADTTIIL SDEDFMEVVL
710 720 730
GKLDPQKAFF SGRLKARGNI MLSQKLQMIL KDYAKL
Length:736
Mass (Da):79,686
Last modified:January 23, 2007 - v3
Checksum:i7B11E02483328BCE
GO
Isoform 2 (identifier: P51659-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MGSPLRFDGR...FAERGALVVV → MVILEAPHLL...ISQCRFFVSM

Note: No experimental confirmation available.
Show »
Length:761
Mass (Da):83,025
Checksum:i246D60646BD2C7A8
GO
Isoform 3 (identifier: P51659-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-37: Missing.

Note: No experimental confirmation available.
Show »
Length:718
Mass (Da):77,870
Checksum:i79C506BC0D73B5C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti587Q → R in BAG60363 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03757616G → S in DBPD; no dehydrogenase activity. 2 PublicationsCorresponds to variant rs137853096dbSNPEnsembl.1
Natural variantiVAR_05230990F → L.Corresponds to variant rs28943588dbSNPEnsembl.1
Natural variantiVAR_014872106R → H.2 PublicationsCorresponds to variant rs25640dbSNPEnsembl.1
Natural variantiVAR_065906106R → P in DBPD. 1 PublicationCorresponds to variant rs25640dbSNPEnsembl.1
Natural variantiVAR_052310140K → N.Corresponds to variant rs28943589dbSNPEnsembl.1
Natural variantiVAR_065907217Y → C in PRLTS1. 1 PublicationCorresponds to variant rs387906825dbSNPEnsembl.1
Natural variantiVAR_024625292T → S.Corresponds to variant rs1143650dbSNPEnsembl.1
Natural variantiVAR_052311427A → V.Corresponds to variant rs28943590dbSNPEnsembl.1
Natural variantiVAR_065908457N → Y in DBPD; the mutation leads to an unstable protein. 1 PublicationCorresponds to variant rs137853097dbSNPEnsembl.1
Natural variantiVAR_052312491A → T.Corresponds to variant rs28943591dbSNPEnsembl.1
Natural variantiVAR_014873511W → R.1 PublicationCorresponds to variant rs11539471dbSNPEnsembl.1
Natural variantiVAR_014874559I → V.2 PublicationsCorresponds to variant rs11205dbSNPEnsembl.1
Natural variantiVAR_052313606A → S.Corresponds to variant rs15228dbSNPEnsembl.1
Natural variantiVAR_052314687T → I.Corresponds to variant rs28943592dbSNPEnsembl.1
Natural variantiVAR_052315728M → V.Corresponds to variant rs28943594dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0461521 – 38MGSPL…ALVVV → MVILEAPHLLRRKEPETPGL SSRIGPSLCPGFCRKRSVSC CFQNLCNNPMEKIISQCRFF VSM in isoform 2. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_04615320 – 37Missing in isoform 3. 1 PublicationAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87176 mRNA. Translation: CAA60643.1.
AF057740
, AF057720, AF057721, AF057722, AF057723, AF057724, AF057725, AF057726, AF057727, AF057728, AF057729, AF057730, AF057731, AF057732, AF057733, AF057734, AF057735, AF057736, AF057737, AF057738, AF057739 Genomic DNA. Translation: AAD08652.1.
AK298075 mRNA. Translation: BAG60363.1.
AK301212 mRNA. Translation: BAG62787.1.
AC024564 Genomic DNA. No translation available.
BC003098 mRNA. Translation: AAH03098.1.
CCDSiCCDS4126.1. [P51659-1]
CCDS56378.1. [P51659-3]
CCDS56379.1. [P51659-2]
PIRiS59136.
RefSeqiNP_000405.1. NM_000414.3. [P51659-1]
NP_001186220.1. NM_001199291.2. [P51659-2]
NP_001186221.1. NM_001199292.1. [P51659-3]
NP_001278956.1. NM_001292027.1.
NP_001278957.1. NM_001292028.1.
UniGeneiHs.406861.

Genome annotation databases

EnsembliENST00000256216; ENSP00000256216; ENSG00000133835. [P51659-1]
ENST00000504811; ENSP00000420914; ENSG00000133835. [P51659-2]
ENST00000515320; ENSP00000424613; ENSG00000133835. [P51659-3]
GeneIDi3295.
KEGGihsa:3295.
UCSCiuc003ksj.4. human. [P51659-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87176 mRNA. Translation: CAA60643.1.
AF057740
, AF057720, AF057721, AF057722, AF057723, AF057724, AF057725, AF057726, AF057727, AF057728, AF057729, AF057730, AF057731, AF057732, AF057733, AF057734, AF057735, AF057736, AF057737, AF057738, AF057739 Genomic DNA. Translation: AAD08652.1.
AK298075 mRNA. Translation: BAG60363.1.
AK301212 mRNA. Translation: BAG62787.1.
AC024564 Genomic DNA. No translation available.
BC003098 mRNA. Translation: AAH03098.1.
CCDSiCCDS4126.1. [P51659-1]
CCDS56378.1. [P51659-3]
CCDS56379.1. [P51659-2]
PIRiS59136.
RefSeqiNP_000405.1. NM_000414.3. [P51659-1]
NP_001186220.1. NM_001199291.2. [P51659-2]
NP_001186221.1. NM_001199292.1. [P51659-3]
NP_001278956.1. NM_001292027.1.
NP_001278957.1. NM_001292028.1.
UniGeneiHs.406861.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IKTX-ray1.75A618-736[»]
1S9CX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L318-615[»]
1ZBQX-ray2.71A/B/C/D/E/F1-304[»]
ProteinModelPortaliP51659.
SMRiP51659.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109528. 41 interactors.
IntActiP51659. 28 interactors.
MINTiMINT-1135639.
STRINGi9606.ENSP00000420914.

Chemistry databases

ChEMBLiCHEMBL5814.
SwissLipidsiSLP:000000540.

PTM databases

iPTMnetiP51659.
PhosphoSitePlusiP51659.
SwissPalmiP51659.

Polymorphism and mutation databases

BioMutaiHSD17B4.
DMDMi1706396.

Proteomic databases

EPDiP51659.
MaxQBiP51659.
PaxDbiP51659.
PeptideAtlasiP51659.
PRIDEiP51659.
TopDownProteomicsiP51659-1. [P51659-1]

Protocols and materials databases

DNASUi3295.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256216; ENSP00000256216; ENSG00000133835. [P51659-1]
ENST00000504811; ENSP00000420914; ENSG00000133835. [P51659-2]
ENST00000515320; ENSP00000424613; ENSG00000133835. [P51659-3]
GeneIDi3295.
KEGGihsa:3295.
UCSCiuc003ksj.4. human. [P51659-1]

Organism-specific databases

CTDi3295.
DisGeNETi3295.
GeneCardsiHSD17B4.
H-InvDBHIX0078166.
HGNCiHGNC:5213. HSD17B4.
HPAiHPA021302.
HPA021311.
HPA021479.
MalaCardsiHSD17B4.
MIMi233400. phenotype.
261515. phenotype.
601860. gene.
neXtProtiNX_P51659.
OpenTargetsiENSG00000133835.
Orphaneti300. Bifunctional enzyme deficiency.
2855. Perrault syndrome.
PharmGKBiPA29481.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP51659.
KOiK12405.
OMAiTVMPEDL.
OrthoDBiEOG091G02S9.
PhylomeDBiP51659.
TreeFamiTF105656.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:HS05792-MONOMER.
ZFISH:HS05792-MONOMER.
BRENDAi4.2.1.119. 2681.
ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-389887. Beta-oxidation of pristanoyl-CoA.
R-HSA-390247. Beta-oxidation of very long chain fatty acids.
SABIO-RKP51659.

Miscellaneous databases

ChiTaRSiHSD17B4. human.
EvolutionaryTraceiP51659.
GeneWikiiHSD17B4.
GenomeRNAii3295.
PROiP51659.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000133835.
CleanExiHS_HSD17B4.
ExpressionAtlasiP51659. baseline and differential.
GenevisibleiP51659. HS.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHB4_HUMAN
AccessioniPrimary (citable) accession number: P51659
Secondary accession number(s): B4DNV1
, B4DVS5, E9PB82, F5HE57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 180 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

Miscellaneous

The protein is found both as a full length peptide and in a cleaved version.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.