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Q9BTZ2 (DHRS4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dehydrogenase/reductase SDR family member 4

EC=1.1.1.184
Alternative name(s):
NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase
Short name=CR
Short name=PHCR
NADPH-dependent retinol dehydrogenase/reductase
Short name=NRDR
Short name=humNRDR
Peroxisomal short-chain alcohol dehydrogenase
Short name=PSCD
SCAD-SRL
Short-chain dehydrogenase/reductase family member 4
Gene names
Name:DHRS4
ORF Names:UNQ851/PRO1800
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones By similarity.

Catalytic activity

R-CHOH-R' + NADP+ = R-CO-R' + NADPH.

Subunit structure

Homotetramer By similarity.

Subcellular location

Peroxisome. Note: Isoform 1 is peroxisomal, while isoform 4 is not. Ref.1 Ref.7 Ref.15

Isoform 7: Nucleus Ref.1 Ref.7 Ref.15.

Tissue specificity

Isoform 1 is predominantly expressed in normal cervix (at protein level). Isoform 4 is expressed in some neoplastic cervical tissues, but not in normal cervix (at protein level). Isoform 5 and isoform 6 are expressed in a few neoplastic cervical tissues. Ref.7

Miscellaneous

Inhibited by kaempferol, quercetin, genistein and myristic acid By similarity.

Sequence similarities

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

Sequence caution

The sequence AAD02292.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAL61824.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB18775.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG37057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentNucleus
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalcohol metabolic process

Inferred from direct assay PubMed 18571493. Source: UniProtKB

cellular ketone metabolic process

Inferred from direct assay PubMed 18571493. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 19442656. Source: UniProtKB

protein tetramerization

Inferred from direct assay PubMed 18571493. Source: UniProtKB

steroid metabolic process

Inferred from direct assay PubMed 18571493. Source: UniProtKB

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay Ref.1PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_function3-keto sterol reductase activity

Inferred from direct assay PubMed 18571493PubMed 19056333. Source: UniProtKB

alcohol dehydrogenase [NAD(P)+] activity

Inferred from direct assay PubMed 18571493. Source: UniProtKB

carbonyl reductase (NADPH) activity

Inferred from direct assay PubMed 18571493. Source: UniProtKB

oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Inferred from direct assay PubMed 19442656. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BTZ2-1)

Also known as: SDR-SRL3;

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: Q9BTZ2-2)

Also known as: SDR-SRL1;

The sequence of this isoform differs from the canonical sequence as follows:
     137-222: Missing.
Isoform 3 (identifier: Q9BTZ2-3)

Also known as: SDR-SRL2;

The sequence of this isoform differs from the canonical sequence as follows:
     103-222: Missing.
Isoform 4 (identifier: Q9BTZ2-4)

Also known as: NRDRB1;

The sequence of this isoform differs from the canonical sequence as follows:
     103-136: Missing.
Isoform 5 (identifier: Q9BTZ2-5)

Also known as: NRDRB2;

The sequence of this isoform differs from the canonical sequence as follows:
     103-136: Missing.
     178-222: Missing.
Note: Contains a phosphoserine at position 140.
Isoform 6 (identifier: Q9BTZ2-6)

Also known as: DHRS4L2; NRDRA1;

The sequence of this isoform differs from the canonical sequence as follows:
     19-221: Missing.
Isoform 7 (identifier: Q9BTZ2-7)

Also known as: NRDRA2;

The sequence of this isoform differs from the canonical sequence as follows:
     137-188: TLDINVKAPA...FSPYNVSKTA → RRLSGDRVFH...LCWHRVFPVL
     189-278: Missing.
Note: Mainly localized in the nucleus.
Isoform 8 (identifier: Q9BTZ2-8)

Also known as: NRDRB1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     103-136: Missing.
Note: Enhanced dicarbonyl reductase activity. high expression in liver.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Dehydrogenase/reductase SDR family member 4
PRO_0000054647

Regions

Nucleotide binding36 – 6025NADP By similarity
Motif276 – 2783Microbody targeting signal

Sites

Active site1821Proton acceptor By similarity
Binding site1691Substrate By similarity

Amino acid modifications

Modified residue921N6-acetyllysine; alternate By similarity
Modified residue921N6-succinyllysine; alternate By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue2161N6-acetyllysine; alternate By similarity
Modified residue2161N6-succinyllysine; alternate By similarity
Modified residue2271N6-succinyllysine By similarity
Modified residue2341N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 1818Missing in isoform 8.
VSP_044947
Alternative sequence19 – 221203Missing in isoform 6.
VSP_031435
Alternative sequence103 – 222120Missing in isoform 3.
VSP_008585
Alternative sequence103 – 13634Missing in isoform 4, isoform 5 and isoform 8.
VSP_031436
Alternative sequence137 – 22286Missing in isoform 2.
VSP_008586
Alternative sequence137 – 18852TLDIN…VSKTA → RRLSGDRVFHSSLQSISSLD GQGKRGKHERNPADKKVRRA RGLCWHRVFPVL in isoform 7.
VSP_031437
Alternative sequence178 – 22245Missing in isoform 5.
VSP_031438
Alternative sequence189 – 27890Missing in isoform 7.
VSP_031439
Natural variant311A → T.
Corresponds to variant rs1043442 [ dbSNP | Ensembl ].
VAR_057272
Natural variant2021P → S.
Corresponds to variant rs1043650 [ dbSNP | Ensembl ].
VAR_061846

Experimental info

Sequence conflict371V → A in BAA91953. Ref.8
Sequence conflict501R → W in ABC61321. Ref.7
Sequence conflict891H → M in AAQ13444. Ref.4
Sequence conflict1021T → M in AAD02292. Ref.1
Sequence conflict1261I → L in AAD02292. Ref.1

Secondary structure

........................................... 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SDR-SRL3) [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 3B06A229E1BBE47B

FASTA27829,537
        10         20         30         40         50         60 
MHKAGLLGLC ARAWNSVRMA SSGMTRRDPL ANKVALVTAS TDGIGFAIAR RLAQDGAHVV 

        70         80         90        100        110        120 
VSSRKQQNVD QAVATLQGEG LSVTGTVCHV GKAEDRERLV ATAVKLHGGI DILVSNAAVN 

       130        140        150        160        170        180 
PFFGSIMDVT EEVWDKTLDI NVKAPALMTK AVVPEMEKRG GGSVVIVSSI AAFSPSPGFS 

       190        200        210        220        230        240 
PYNVSKTALL GLTKTLAIEL APRNIRVNCL APGLIKTSFS RMLWMDKEKE ESMKETLRIR 

       250        260        270 
RLGEPEDCAG IVSFLCSEDA SYITGETVVV GGGTPSRL 

« Hide

Isoform 2 (SDR-SRL1) [UniParc].

Checksum: 8DA10FF50043F472
Show »

FASTA19220,540
Isoform 3 (SDR-SRL2) [UniParc].

Checksum: DBE966DBD30D0A3E
Show »

FASTA15816,885
Isoform 4 (NRDRB1) [UniParc].

Checksum: 25DC4A701E3B76FF
Show »

FASTA24425,882
Isoform 5 (NRDRB2) [UniParc].

Checksum: E6015FD7DA879EA4
Show »

FASTA19921,036
Isoform 6 (DHRS4L2) (NRDRA1) [UniParc].

Checksum: A3C9C3CF43B80FA0
Show »

FASTA758,288
Isoform 7 (NRDRA2) [UniParc].

Checksum: 23BD8B69B345AEE8
Show »

FASTA18820,345
Isoform 8 (NRDRB1) [UniParc].

Checksum: ED701E06FA126565
Show »

FASTA22623,917

References

« Hide 'large scale' references
[1]"Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase."
Fransen M., Van Veldhoven P.P., Subramani S.
Biochem. J. 340:561-568(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION.
[2]"cDNA cloning and characterization of peroxisomal short-chain dehydrogenase / reductase that reduces all-trans retinal to retinol."
Furukawa A., Ohnishi T., Huang D., Araki N., Ichikawa Y.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"cDNA cloning of a short isoform of human liver NADP (H) -dependent retinol dehydrogenase/reductase and analysis of its characteristics."
Du J., Huang D.-Y., Liu G.-F., Wang G.-L., Xu X.-L., Wang B., Zhu L.
Yi Chuan Xue Bao 31:661-667(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[4]"Molecular cloning and expression analysis of a novel human cDNA encoding a protein homologous to human Hep27 protein."
Tu Q., Yu L., Bi A., Li N., He W., Zhao S.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"A minor misassignment error inside segmental duplication (MMEISD) of DHRS4 gene in human genome sequence."
Li Y.F., Liu G.-F., Song X.-H., Yang Y.M., Zhong J.C., Du K., Zhu W., Huang D.-Y.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
[6]"cDNA cloning of a short isoform of human neuroblastoma NADP(H)-dependent retinol dehydrogenase/reductase and analysis of its characteristics."
Li Y.F., Liu G.-F., Song X.-H., Du K., Huang D.-Y.
Ai Bian Ji Bian Tu Bian 17:321-326(2005)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"Expression of a novel alternatively spliced variant of NADP(H)-dependent retinol dehydrogenase/reductase with deletion of exon 3 in cervical squamous carcinoma."
Song X.-H., Liang B., Liu G.-F., Li R., Xie J.-P., Du K., Huang D.-Y.
Int. J. Cancer 120:1618-1626(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF 40-278 (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 4), TISSUE SPECIFICITY (ISOFORM 4).
Tissue: Cervix carcinoma and Neuroblastoma.
[8]"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] (ISOFORM 1).
Tissue: Placenta and Skeletal muscle.
[9]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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: Lung.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"Human NRDRB1, an alternatively spliced isoform of NADP(H)-dependent retinol dehydrogenase/reductase enhanced enzymatic activity of Benzil."
Yan Y., Song X., Liu G., Su Z., Du Y., Sui X., Chang X., Huang D.
Cell. Physiol. Biochem. 30:1371-1382(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 8).
[15]"Identification of a novel isoform of DHRS4 protein with a nuclear localization signal."
Su Z., Li R., Song X., Liu G., Li Y., Chang X., Li C., Huang D.
Gene 494:161-167(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORM 7).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF044127 mRNA. Translation: AAD02292.1. Different initiation.
AB045131 mRNA. Translation: BAB18775.1. Different initiation.
AY071856 mRNA. Translation: AAL61824.2. Different initiation.
AF064256 mRNA. Translation: AAQ13444.1.
AY616182 mRNA. Translation: AAT70757.1.
DQ344810 mRNA. Translation: ABD75823.1.
AY943857 mRNA. Translation: AAX49568.1.
DQ325464 mRNA. Translation: ABC61320.1.
DQ338571 mRNA. Translation: ABC61321.1.
AK001870 mRNA. Translation: BAA91953.1.
AK314448 mRNA. Translation: BAG37057.1. Different initiation.
AY358638 mRNA. Translation: AAQ89001.1.
AL136419 Genomic DNA. No translation available.
BC003019 mRNA. Translation: AAH03019.1.
CCDSCCDS61408.1. [Q9BTZ2-7]
CCDS61409.1. [Q9BTZ2-2]
CCDS61410.1. [Q9BTZ2-4]
CCDS61411.1. [Q9BTZ2-5]
CCDS61412.1. [Q9BTZ2-3]
CCDS9605.1. [Q9BTZ2-1]
RefSeqNP_001269916.1. NM_001282987.1. [Q9BTZ2-7]
NP_001269917.1. NM_001282988.1. [Q9BTZ2-4]
NP_001269918.1. NM_001282989.1. [Q9BTZ2-2]
NP_001269919.1. NM_001282990.1. [Q9BTZ2-5]
NP_001269920.1. NM_001282991.1. [Q9BTZ2-3]
NP_066284.2. NM_021004.3. [Q9BTZ2-1]
UniGeneHs.528385.
Hs.743442.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4RX-ray1.70A/B/C/D19-278[»]
ProteinModelPortalQ9BTZ2.
SMRQ9BTZ2. Positions 25-278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116107. 4 interactions.
IntActQ9BTZ2. 2 interactions.

Chemistry

DrugBankDB00162. Vitamin A.

PTM databases

PhosphoSiteQ9BTZ2.

Polymorphism databases

DMDM308153604.

Proteomic databases

MaxQBQ9BTZ2.
PaxDbQ9BTZ2.
PRIDEQ9BTZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313250; ENSP00000326219; ENSG00000157326. [Q9BTZ2-1]
ENST00000397074; ENSP00000380264; ENSG00000157326. [Q9BTZ2-3]
ENST00000397075; ENSP00000380265; ENSG00000157326. [Q9BTZ2-2]
ENST00000421831; ENSP00000404147; ENSG00000157326. [Q9BTZ2-8]
ENST00000558263; ENSP00000453367; ENSG00000157326. [Q9BTZ2-7]
ENST00000558581; ENSP00000452645; ENSG00000157326. [Q9BTZ2-4]
ENST00000559632; ENSP00000453983; ENSG00000157326. [Q9BTZ2-5]
GeneID10901.
KEGGhsa:10901.
UCSCuc001wla.3. human. [Q9BTZ2-1]
uc001wlb.3. human. [Q9BTZ2-4]
uc001wld.4. human. [Q9BTZ2-7]
uc001wle.4. human. [Q9BTZ2-2]
uc010akz.3. human. [Q9BTZ2-5]

Organism-specific databases

CTD10901.
GeneCardsGC14P024422.
HGNCHGNC:16985. DHRS4.
HPAHPA023972.
MIM611596. gene.
neXtProtNX_Q9BTZ2.
PharmGKBPA128395792.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG105779.
InParanoidQ9BTZ2.
KOK11147.
OMAIMDVTEE.
OrthoDBEOG73Z2VD.
PhylomeDBQ9BTZ2.
TreeFamTF315405.

Gene expression databases

BgeeQ9BTZ2.
GenevestigatorQ9BTZ2.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR029511. DHRS4-like.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PANTHERPTHR24322:SF198. PTHR24322:SF198. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BTZ2.
GeneWikiDHRS4.
GenomeRNAi10901.
NextBio35497048.
PROQ9BTZ2.
SOURCESearch...

Entry information

Entry nameDHRS4_HUMAN
AccessionPrimary (citable) accession number: Q9BTZ2
Secondary accession number(s): B2RB10 expand/collapse secondary AC list , B7WNS9, D3YTB8, E2QRL8, O95162, Q20CR0, Q2LC19, Q2LE81, Q58IU4, Q6E0Y1, Q6UWU3, Q71UQ6, Q8TD03, Q9H3N5, Q9NV08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 125 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.

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