Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51659

- DHB4_HUMAN

UniProt

P51659 - DHB4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Peroxisomal multifunctional enzyme type 2

Gene

HSD17B4

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Vmax=8.8 µmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211NAD; via amide nitrogen
Binding sitei40 – 401NAD
Binding sitei99 – 991NAD; via carbonyl oxygen
Binding sitei151 – 1511SubstrateBy similarity
Active sitei164 – 1641Proton acceptorPROSITE-ProRule annotation
Binding sitei435 – 4351(3R)-3-hydroxydecanoyl-CoABy similarity
Binding sitei533 – 5331(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity
Binding sitei563 – 5631(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity
Binding sitei706 – 7061Substrate
Binding sitei724 – 7241Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 3725NADBy similarityAdd
BLAST
Nucleotide bindingi75 – 762NAD
Nucleotide bindingi164 – 1685NAD
Nucleotide bindingi196 – 1994NAD

GO - Molecular functioni

  1. 17-beta-hydroxysteroid dehydrogenase (NAD+) activity Source: UniProtKB
  2. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Source: Reactome
  3. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
  4. isomerase activity Source: UniProtKB-KW
  5. long-chain-enoyl-CoA hydratase activity Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. receptor binding Source: UniProtKB

GO - Biological processi

  1. alpha-linolenic acid metabolic process Source: Reactome
  2. androgen metabolic process Source: UniProtKB
  3. bile acid biosynthetic process Source: Reactome
  4. bile acid metabolic process Source: Reactome
  5. cellular lipid metabolic process Source: Reactome
  6. estrogen metabolic process Source: UniProtKB
  7. fatty acid beta-oxidation Source: UniProtKB
  8. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  9. medium-chain fatty-acyl-CoA metabolic process Source: UniProtKB
  10. metabolic process Source: GOC
  11. osteoblast differentiation Source: UniProt
  12. oxidation-reduction process Source: GOC
  13. Sertoli cell development Source: Ensembl
  14. small molecule metabolic process Source: Reactome
  15. unsaturated fatty acid metabolic process Source: Reactome
  16. very long-chain fatty acid metabolic process Source: Ensembl
  17. 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.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
REACT_17062. Beta-oxidation of very long chain fatty acids.
SABIO-RKP51659.
UniPathwayiUPA00659.

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
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5213. HSD17B4.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. membrane Source: UniProt
  3. mitochondrion Source: Ensembl
  4. peroxisomal matrix Source: Reactome
  5. peroxisomal membrane Source: UniProtKB
  6. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

D-bifunctional protein deficiency (DBPD) [MIM:261515]: Disorder of peroxisomal fatty acid beta-oxidation.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161G → S in DBPD. 1 Publication
VAR_037576
Natural varianti106 – 1061R → P in DBPD. 1 Publication
Corresponds to variant rs25640 [ dbSNP | Ensembl ].
VAR_065906
Natural varianti457 – 4571N → Y in DBPD; the mutation leads to an unstable protein. 1 Publication
VAR_065908
Perrault syndrome 1 (PRLTS1) [MIM:233400]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171Y → C in PRLTS1. 1 Publication
VAR_065907

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161G → S: No dehydrogenase activity. 1 Publication
Mutagenesisi347 – 3471Y → A: No hydratase activity. 1 Publication
Mutagenesisi366 – 3661E → A: No hydratase activity. 1 Publication
Mutagenesisi370 – 3701D → A: No effect. 1 Publication
Mutagenesisi406 – 4061H → A: No effect. 1 Publication
Mutagenesisi408 – 4081E → A: No effect. 1 Publication
Mutagenesisi410 – 4101Y → A: No effect. 1 Publication
Mutagenesisi490 – 4901D → A: No effect. 1 Publication
Mutagenesisi505 – 5051Y → A: Completely inactive. 1 Publication
Mutagenesisi510 – 5101D → A: No hydratase activity. 1 Publication
Mutagenesisi515 – 5151H → A: Completely inactive. 1 Publication
Mutagenesisi517 – 5171D → A: No effect. 1 Publication
Mutagenesisi532 – 5321H → A: No effect. 1 Publication

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Peroxisomal multifunctional enzyme type 2PRO_0000054583Add
BLAST
Chaini1 – 311311(3R)-hydroxyacyl-CoA dehydrogenasePRO_0000400082Add
BLAST
Chaini312 – 736425Enoyl-CoA hydratase 2PRO_0000400083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine; alternateBy similarity
Modified residuei46 – 461N6-succinyllysine; alternateBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei68 – 681N6-succinyllysineBy similarity
Modified residuei84 – 841N6-succinyllysineBy similarity
Modified residuei275 – 2751N6-succinyllysineBy similarity
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei356 – 3561N6-succinyllysineBy similarity
Modified residuei424 – 4241N6-succinyllysineBy similarity
Modified residuei565 – 5651N6-acetyllysine1 Publication
Modified residuei579 – 5791N6-succinyllysineBy similarity
Modified residuei663 – 6631N6-succinyllysineBy similarity
Modified residuei669 – 6691N6-acetyllysine1 Publication
Modified residuei707 – 7071N6-acetyllysine1 Publication
Modified residuei725 – 7251N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51659.
PaxDbiP51659.
PeptideAtlasiP51659.
PRIDEiP51659.

PTM databases

PhosphoSiteiP51659.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP51659.
CleanExiHS_HSD17B4.
ExpressionAtlasiP51659. baseline and differential.
GenevestigatoriP51659.

Organism-specific databases

HPAiHPA021302.
HPA021311.
HPA021479.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi109528. 27 interactions.
IntActiP51659. 16 interactions.
MINTiMINT-1135639.
STRINGi9606.ENSP00000256216.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144Combined sources
Turni15 – 184Combined sources
Helixi20 – 3112Combined sources
Beta strandi35 – 395Combined sources
Helixi53 – 6412Combined sources
Beta strandi68 – 725Combined sources
Helixi76 – 783Combined sources
Helixi79 – 9012Combined sources
Beta strandi95 – 984Combined sources
Helixi108 – 1103Combined sources
Helixi113 – 14129Combined sources
Beta strandi144 – 1496Combined sources
Helixi152 – 1565Combined sources
Helixi162 – 18221Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1948Combined sources
Turni199 – 2046Combined sources
Helixi207 – 2126Combined sources
Helixi215 – 2173Combined sources
Helixi219 – 2257Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi243 – 2519Combined sources
Helixi266 – 2716Combined sources
Helixi273 – 2775Combined sources
Helixi288 – 30316Combined sources
Beta strandi335 – 3395Combined sources
Helixi341 – 35010Combined sources
Helixi358 – 3603Combined sources
Helixi361 – 3644Combined sources
Helixi375 – 3773Combined sources
Helixi378 – 3814Combined sources
Helixi383 – 3853Combined sources
Beta strandi405 – 41511Combined sources
Beta strandi419 – 43214Combined sources
Beta strandi440 – 46223Combined sources
Beta strandi490 – 4967Combined sources
Helixi501 – 5055Combined sources
Helixi506 – 5083Combined sources
Helixi513 – 5153Combined sources
Helixi518 – 5225Combined sources
Turni523 – 5253Combined sources
Helixi533 – 54816Combined sources
Helixi553 – 5553Combined sources
Beta strandi556 – 5638Combined sources
Beta strandi572 – 5809Combined sources
Beta strandi583 – 5908Combined sources
Turni591 – 5933Combined sources
Beta strandi596 – 60510Combined sources
Helixi624 – 64623Combined sources
Beta strandi648 – 67023Combined sources
Beta strandi674 – 6796Combined sources
Beta strandi685 – 6917Combined sources
Helixi692 – 6998Combined sources
Helixi705 – 7106Combined sources
Beta strandi713 – 7197Combined sources
Helixi720 – 73314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-304, 323-606, 622-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51659.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 600117MaoC-likeAdd
BLAST
Domaini624 – 736113SCP2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305(3R)-hydroxyacyl-CoA dehydrogenaseAdd
BLAST
Regioni322 – 622301Enoyl-CoA hydratase 2Add
BLAST
Regioni406 – 4072(3R)-3-hydroxydecanoyl-CoA bindingBy similarity
Regioni510 – 5156(3R)-3-hydroxydecanoyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi734 – 7363Microbody targeting signalSequence Analysis

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP51659.
KOiK12405.
OMAiCHESCED.
OrthoDBiEOG7RBZ7V.
PhylomeDBiP51659.
TreeFamiTF105656.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF54637. 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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti587 – 5871Q → R in BAG60363. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161G → S in DBPD. 1 Publication
VAR_037576
Natural varianti90 – 901F → L.
Corresponds to variant rs28943588 [ dbSNP | Ensembl ].
VAR_052309
Natural varianti106 – 1061R → H.1 Publication
Corresponds to variant rs25640 [ dbSNP | Ensembl ].
VAR_014872
Natural varianti106 – 1061R → P in DBPD. 1 Publication
Corresponds to variant rs25640 [ dbSNP | Ensembl ].
VAR_065906
Natural varianti140 – 1401K → N.
Corresponds to variant rs28943589 [ dbSNP | Ensembl ].
VAR_052310
Natural varianti217 – 2171Y → C in PRLTS1. 1 Publication
VAR_065907
Natural varianti292 – 2921T → S.
Corresponds to variant rs1143650 [ dbSNP | Ensembl ].
VAR_024625
Natural varianti427 – 4271A → V.
Corresponds to variant rs28943590 [ dbSNP | Ensembl ].
VAR_052311
Natural varianti457 – 4571N → Y in DBPD; the mutation leads to an unstable protein. 1 Publication
VAR_065908
Natural varianti491 – 4911A → T.
Corresponds to variant rs28943591 [ dbSNP | Ensembl ].
VAR_052312
Natural varianti511 – 5111W → R.1 Publication
Corresponds to variant rs11539471 [ dbSNP | Ensembl ].
VAR_014873
Natural varianti559 – 5591I → V.1 Publication
Corresponds to variant rs11205 [ dbSNP | Ensembl ].
VAR_014874
Natural varianti606 – 6061A → S.
Corresponds to variant rs15228 [ dbSNP | Ensembl ].
VAR_052313
Natural varianti687 – 6871T → I.
Corresponds to variant rs28943592 [ dbSNP | Ensembl ].
VAR_052314
Natural varianti728 – 7281M → V.
Corresponds to variant rs28943594 [ dbSNP | Ensembl ].
VAR_052315

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838MGSPL…ALVVV → MVILEAPHLLRRKEPETPGL SSRIGPSLCPGFCRKRSVSC CFQNLCNNPMEKIISQCRFF VSM in isoform 2. 1 PublicationVSP_046152Add
BLAST
Alternative sequencei20 – 3718Missing in isoform 3. 1 PublicationVSP_046153Add
BLAST

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.3. human. [P51659-1]

Polymorphism databases

DMDMi1706396.

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 .
CCDSi CCDS4126.1. [P51659-1 ]
CCDS56378.1. [P51659-3 ]
CCDS56379.1. [P51659-2 ]
PIRi S59136.
RefSeqi NP_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.
UniGenei Hs.406861.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IKT X-ray 1.75 A 618-736 [» ]
1S9C X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L 318-615 [» ]
1ZBQ X-ray 2.71 A/B/C/D/E/F 1-304 [» ]
ProteinModelPortali P51659.
SMRi P51659. Positions 3-304, 323-606, 622-736.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109528. 27 interactions.
IntActi P51659. 16 interactions.
MINTi MINT-1135639.
STRINGi 9606.ENSP00000256216.

Chemistry

ChEMBLi CHEMBL5814.

PTM databases

PhosphoSitei P51659.

Polymorphism databases

DMDMi 1706396.

Proteomic databases

MaxQBi P51659.
PaxDbi P51659.
PeptideAtlasi P51659.
PRIDEi P51659.

Protocols and materials databases

DNASUi 3295.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256216 ; ENSP00000256216 ; ENSG00000133835 . [P51659-1 ]
ENST00000504811 ; ENSP00000420914 ; ENSG00000133835 . [P51659-2 ]
ENST00000515320 ; ENSP00000424613 ; ENSG00000133835 . [P51659-3 ]
GeneIDi 3295.
KEGGi hsa:3295.
UCSCi uc003ksj.3. human. [P51659-1 ]

Organism-specific databases

CTDi 3295.
GeneCardsi GC05P118789.
H-InvDB HIX0078166.
HGNCi HGNC:5213. HSD17B4.
HPAi HPA021302.
HPA021311.
HPA021479.
MIMi 233400. phenotype.
261515. phenotype.
601860. gene.
neXtProti NX_P51659.
Orphaneti 300. Bifunctional enzyme deficiency.
2855. Perrault syndrome.
PharmGKBi PA29481.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00530000062928.
HOGENOMi HOG000170895.
HOVERGENi HBG002174.
InParanoidi P51659.
KOi K12405.
OMAi CHESCED.
OrthoDBi EOG7RBZ7V.
PhylomeDBi P51659.
TreeFami TF105656.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:HS05792-MONOMER.
Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
REACT_17062. Beta-oxidation of very long chain fatty acids.
SABIO-RK P51659.

Miscellaneous databases

ChiTaRSi HSD17B4. human.
EvolutionaryTracei P51659.
GeneWikii HSD17B4.
GenomeRNAii 3295.
NextBioi 13071.
PROi P51659.
SOURCEi Search...

Gene expression databases

Bgeei P51659.
CleanExi HS_HSD17B4.
ExpressionAtlasi P51659. baseline and differential.
Genevestigatori P51659.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMi SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV."
    Adamski J., Normand T., Leenders F., Monte D., Begue A., Stehelin D., Jungblut P.W., de Launoit Y.
    Biochem. J. 311:437-443(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein."
    Jiang L.L., Miyazawa S., Souri M., Hashimoto T.
    J. Biochem. 121:364-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 69-77; 81-90; 261-270; 291-310; 312-339; 413-426; 451-459; 478-488 AND 590-631, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  3. "Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV."
    Leenders F., Dolez V., Begue A., Moller G., Gloeckner J.C., de Launoit Y., Adamski J.
    Mamm. Genome 9:1036-1041(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANTS HIS-106 AND VAL-559.
    Tissue: Lung and Spleen.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase."
    Jiang L.L., Kobayashi A., Matsuura H., Fukushima H., Hashimoto T.
    J. Biochem. 120:624-632(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Human peroxisomal multifunctional enzyme type 2. Site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity."
    Qin Y.M., Haapalainen A.M., Kilpelainen S.H., Marttila M.S., Koski M.K., Glumoff T., Novikov D.K., Hiltunen J.K.
    J. Biol. Chem. 275:4965-4972(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-16; TYR-347; GLU-366; ASP-370; HIS-406; GLU-408; TYR-410; ASP-490; TYR-505; ASP-510; HIS-515; ASP-517 AND HIS-532.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565; LYS-669 AND LYS-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution."
    Haapalainen A.M., van Aalten D.M., Merilaeinen G., Jalonen J.E., Pirilae P., Wierenga R.K., Hiltunen J.K., Glumoff T.
    J. Mol. Biol. 313:1127-1138(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 618-736 IN COMPLEX WITH LIGAND.
  14. "Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2."
    Koski K.M., Haapalainen A.M., Hiltunen J.K., Glumoff T.
    J. Mol. Biol. 345:1157-1169(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 320-614.
  15. "Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency."
    van Grunsven E.G., van Berkel E., Ijlst L., Vreken P., de Klerk J.B.C., Adamski J., Lemonde H., Clayton P.T., Cuebas D.A., Wanders R.J.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:2128-2133(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DBPD SER-16.
  16. "Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency."
    van Grunsven E.G., Mooijer P.A., Aubourg P., Wanders R.J.
    Hum. Mol. Genet. 8:1509-1516(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DBPD TYR-457, VARIANT ARG-511.
  17. "D-bifunctional protein deficiency with fetal ascites, polyhydramnios, and contractures of hands and toes."
    Nakano K., Zhang Z., Shimozawa N., Kondo N., Ishii N., Funatsuka M., Shirakawa S., Itoh M., Takashima S., Une M., Kana-aki R.R., Mukai K., Osawa M., Suzuki Y.
    J. Pediatr. 139:865-867(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DBPD PRO-106.
  18. "Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault Syndrome."
    Pierce S.B., Walsh T., Chisholm K.M., Lee M.K., Thornton A.M., Fiumara A., Opitz J.M., Levy-Lahad E., Klevit R.E., King M.C.
    Am. J. Hum. Genet. 87:282-288(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRLTS1 CYS-217.

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: October 29, 2014
This is version 159 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

External Data

Dasty 3