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P51659 (DHB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. (3R)-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.n12
  2. Enoyl-CoA hydratase 2
    EC=4.2.1.107
    EC=4.2.1.119
    Alternative name(s):
    3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Gene names
Name:HSD17B4
Synonyms:EDH17B4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.7

Catalytic activity

(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. Ref.2

(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. Ref.2

(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O. Ref.2

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homodimer. Ref.7

Subcellular location

Peroxisome.

Tissue specificity

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

Involvement in disease

D-bifunctional protein deficiency (DBPD) [MIM:261515]: Disorder of peroxisomal fatty acid beta-oxidation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Miscellaneous

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

Sequence similarities

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

Contains 1 MaoC-like domain.

Contains 1 SCP2 domain.

Biophysicochemical properties

Kinetic parameters:

KM=10 µM for D-3-hydroxy-octanoyl-CoA Ref.2

KM=13 µM for NAD

KM=2.7 µM for 3-ketooctanoyl-CoA

KM=5.4 µM for NADH

Vmax=8.8 µmol/min/mg enzyme

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell development

Inferred from electronic annotation. Source: Ensembl

alpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

androgen metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

bile acid biosynthetic process

Traceable author statement. Source: Reactome

bile acid metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

estrogen metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

fatty acid beta-oxidation

Inferred from direct assay Ref.16. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

medium-chain fatty-acyl-CoA metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

metabolic process

Inferred from direct assay Ref.2. Source: GOC

oxidation-reduction process

Inferred from direct assay Ref.2. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

very long-chain fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

very long-chain fatty-acyl-CoA metabolic process

Inferred from direct assay Ref.15. Source: UniProtKB

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisomal membrane

Inferred from direct assay PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 15599942. Source: UniProtKB

   Molecular_function17-beta-hydroxysteroid dehydrogenase (NAD+) activity

Inferred from direct assay Ref.1. Source: UniProtKB

3-hydroxyacyl-CoA dehydrogenase activity

Inferred from direct assay Ref.2. Source: UniProtKB

3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity

Traceable author statement. Source: Reactome

isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain-enoyl-CoA hydratase activity

Inferred from direct assay Ref.16Ref.2Ref.15. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.14Ref.2. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

sterol binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51659-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P51659-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MGSPLRFDGR...FAERGALVVV → MVILEAPHLL...ISQCRFFVSM
Note: No experimental confirmation available.
Isoform 3 (identifier: P51659-3)

The sequence of this isoform differs from the canonical sequence as follows:
     20-37: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736Peroxisomal multifunctional enzyme type 2
PRO_0000054583
Chain1 – 311311(3R)-hydroxyacyl-CoA dehydrogenase
PRO_0000400082
Chain312 – 736425Enoyl-CoA hydratase 2
PRO_0000400083

Regions

Domain484 – 600117MaoC-like
Domain624 – 736113SCP2
Nucleotide binding13 – 3725NAD By similarity
Nucleotide binding75 – 762NAD
Nucleotide binding164 – 1685NAD
Nucleotide binding196 – 1994NAD
Region1 – 305305(3R)-hydroxyacyl-CoA dehydrogenase
Region322 – 622301Enoyl-CoA hydratase 2
Region406 – 4072(3R)-3-hydroxydecanoyl-CoA binding By similarity
Region510 – 5156(3R)-3-hydroxydecanoyl-CoA binding By similarity
Motif734 – 7363Microbody targeting signal Potential

Sites

Active site1641Proton acceptor By similarity
Binding site211NAD; via amide nitrogen
Binding site401NAD
Binding site991NAD; via carbonyl oxygen
Binding site1511Substrate By similarity
Binding site4351(3R)-3-hydroxydecanoyl-CoA By similarity
Binding site5331(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
Binding site5631(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity
Binding site7061Substrate
Binding site7241Substrate

Amino acid modifications

Modified residue461N6-acetyllysine; alternate By similarity
Modified residue461N6-succinyllysine; alternate By similarity
Modified residue571N6-succinyllysine By similarity
Modified residue681N6-succinyllysine By similarity
Modified residue841N6-succinyllysine By similarity
Modified residue2751N6-succinyllysine By similarity
Modified residue3041Phosphoserine Ref.9
Modified residue3091Phosphoserine Ref.9
Modified residue3561N6-succinyllysine By similarity
Modified residue4241N6-succinyllysine By similarity
Modified residue5651N6-acetyllysine Ref.11
Modified residue5791N6-succinyllysine By similarity
Modified residue6631N6-succinyllysine By similarity
Modified residue6691N6-acetyllysine Ref.11
Modified residue7071N6-acetyllysine Ref.11
Modified residue7251N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 3838MGSPL…ALVVV → MVILEAPHLLRRKEPETPGL SSRIGPSLCPGFCRKRSVSC CFQNLCNNPMEKIISQCRFF VSM in isoform 2.
VSP_046152
Alternative sequence20 – 3718Missing in isoform 3.
VSP_046153
Natural variant161G → S in DBPD. Ref.15
VAR_037576
Natural variant901F → L.
Corresponds to variant rs28943588 [ dbSNP | Ensembl ].
VAR_052309
Natural variant1061R → H. Ref.4
Corresponds to variant rs25640 [ dbSNP | Ensembl ].
VAR_014872
Natural variant1061R → P in DBPD. Ref.17
Corresponds to variant rs25640 [ dbSNP | Ensembl ].
VAR_065906
Natural variant1401K → N.
Corresponds to variant rs28943589 [ dbSNP | Ensembl ].
VAR_052310
Natural variant2171Y → C in PRLTS1. Ref.18
VAR_065907
Natural variant2921T → S.
Corresponds to variant rs1143650 [ dbSNP | Ensembl ].
VAR_024625
Natural variant4271A → V.
Corresponds to variant rs28943590 [ dbSNP | Ensembl ].
VAR_052311
Natural variant4571N → Y in DBPD; the mutation leads to an unstable protein. Ref.16
VAR_065908
Natural variant4911A → T.
Corresponds to variant rs28943591 [ dbSNP | Ensembl ].
VAR_052312
Natural variant5111W → R. Ref.16
Corresponds to variant rs11539471 [ dbSNP | Ensembl ].
VAR_014873
Natural variant5591I → V. Ref.4
Corresponds to variant rs11205 [ dbSNP | Ensembl ].
VAR_014874
Natural variant6061A → S.
Corresponds to variant rs15228 [ dbSNP | Ensembl ].
VAR_052313
Natural variant6871T → I.
Corresponds to variant rs28943592 [ dbSNP | Ensembl ].
VAR_052314
Natural variant7281M → V.
Corresponds to variant rs28943594 [ dbSNP | Ensembl ].
VAR_052315

Experimental info

Mutagenesis161G → S: No dehydrogenase activity. Ref.8
Mutagenesis3471Y → A: No hydratase activity. Ref.8
Mutagenesis3661E → A: No hydratase activity. Ref.8
Mutagenesis3701D → A: No effect. Ref.8
Mutagenesis4061H → A: No effect. Ref.8
Mutagenesis4081E → A: No effect. Ref.8
Mutagenesis4101Y → A: No effect. Ref.8
Mutagenesis4901D → A: No effect. Ref.8
Mutagenesis5051Y → A: Completely inactive. Ref.8
Mutagenesis5101D → A: No hydratase activity. Ref.8
Mutagenesis5151H → A: Completely inactive. Ref.8
Mutagenesis5171D → A: No effect. Ref.8
Mutagenesis5321H → A: No effect. Ref.8
Sequence conflict5871Q → R in BAG60363. Ref.4

Secondary structure

...................................................................................................... 736
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 7B11E02483328BCE

FASTA73679,686
        10         20         30         40         50         60 
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSLAADKVVE 

        70         80         90        100        110        120 
EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA GILRDRSFAR ISDEDWDIIH 

       130        140        150        160        170        180 
RVHLRGSFQV TRAAWEHMKK QKYGRIIMTS SASGIYGNFG QANYSAAKLG LLGLANSLAI 

       190        200        210        220        230        240 
EGRKSNIHCN TIAPNAGSRM TQTVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 

       250        260        270        280        290        300 
AGWIGKLRWE RTLGAIVRQK NHPMTPEAVK ANWKKICDFE NASKPQSIQE STGSIIEVLS 

       310        320        330        340        350        360 
KIDSEGGVSA NHTSRATSTA TSGFAGAIGQ KLPPFSYAYT ELEAIMYALG VGASIKDPKD 

       370        380        390        400        410        420 
LKFIYEGSSD FSCLPTFGVI IGQKSMMGGG LAEIPGLSIN FAKVLHGEQY LELYKPLPRA 

       430        440        450        460        470        480 
GKLKCEAVVA DVLDKGSGVV IIMDVYSYSE KELICHNQFS LFLVGSGGFG GKRTSDKVKV 

       490        500        510        520        530        540 
AVAIPNRPPD AVLTDTTSLN QAALYRLSGD WNPLHIDPNF ASLAGFDKPI LHGLCTFGFS 

       550        560        570        580        590        600 
ARRVLQQFAD NDVSRFKAIK ARFAKPVYPG QTLQTEMWKE GNRIHFQTKV QETGDIVISN 

       610        620        630        640        650        660 
AYVDLAPTSG TSAKTPSEGG KLQSTFVFEE IGRRLKDIGP EVVKKVNAVF EWHITKGGNI 

       670        680        690        700        710        720 
GAKWTIDLKS GSGKVYQGPA KGAADTTIIL SDEDFMEVVL GKLDPQKAFF SGRLKARGNI 

       730 
MLSQKLQMIL KDYAKL 

« Hide

Isoform 2 [UniParc].

Checksum: 246D60646BD2C7A8
Show »

FASTA76183,025
Isoform 3 [UniParc].

Checksum: 79C506BC0D73B5C2
Show »

FASTA71877,870

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87176 mRNA. Translation: CAA60643.1.
AF057740 expand/collapse EMBL AC list , 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.
PIRS59136.
RefSeqNP_000405.1. NM_000414.3.
NP_001186220.1. NM_001199291.1.
NP_001186221.1. NM_001199292.1.
UniGeneHs.406861.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IKTX-ray1.75A618-736[»]
1S9CX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L320-614[»]
1ZBQX-ray2.71A/B/C/D/E/F1-304[»]
ProteinModelPortalP51659.
SMRP51659. Positions 3-304, 323-606, 622-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109528. 24 interactions.
IntActP51659. 16 interactions.
MINTMINT-1135639.
STRING9606.ENSP00000256216.

Chemistry

ChEMBLCHEMBL5814.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP51659.

Polymorphism databases

DMDM1706396.

Proteomic databases

PaxDbP51659.
PeptideAtlasP51659.
PRIDEP51659.

Protocols and materials databases

DNASU3295.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256216; ENSP00000256216; ENSG00000133835. [P51659-1]
ENST00000504811; ENSP00000420914; ENSG00000133835. [P51659-2]
ENST00000515320; ENSP00000424613; ENSG00000133835. [P51659-3]
GeneID3295.
KEGGhsa:3295.
UCSCuc003ksj.3. human. [P51659-1]

Organism-specific databases

CTD3295.
GeneCardsGC05P118816.
H-InvDBHIX0078166.
HGNCHGNC:5213. HSD17B4.
HPAHPA021302.
HPA021311.
HPA021479.
MIM233400. phenotype.
261515. phenotype.
601860. gene.
neXtProtNX_P51659.
Orphanet300. Bifunctional enzyme deficiency.
2855. Perrault syndrome.
PharmGKBPA29481.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOGENOMHOG000170895.
HOVERGENHBG002174.
InParanoidP51659.
KOK12405.
OMACHESCED.
OrthoDBEOG7RBZ7V.
PhylomeDBP51659.
TreeFamTF105656.

Enzyme and pathway databases

BioCycMetaCyc:HS05792-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP51659.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressP51659.
BgeeP51659.
CleanExHS_HSD17B4.
GenevestigatorP51659.

Family and domain databases

Gene3D3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMSSF55718. SSF55718. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSD17B4. human.
EvolutionaryTraceP51659.
GeneWikiHSD17B4.
GenomeRNAi3295.
NextBio13071.
PROP51659.
SOURCESearch...

Entry information

Entry nameDHB4_HUMAN
AccessionPrimary (citable) accession number: P51659
Secondary accession number(s): B4DNV1 expand/collapse secondary AC list , B4DVS5, E9PB82, F5HE57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM