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Protein

Dehydrogenase/reductase SDR family member 7

Gene

DHRS7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei190 – 1901SubstrateBy similarity
Active sitei203 – 2031Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi54 – 7825NADBy similarityAdd
BLAST

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrogenase/reductase SDR family member 7 (EC:1.1.-.-)
Alternative name(s):
Retinal short-chain dehydrogenase/reductase 4
Short name:
retSDR4
Gene namesi
Name:DHRS7
Synonyms:DHRS7A, RETSDR4
ORF Names:CGI-86, UNQ285/PRO3448
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:21524. DHRS7.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134974539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 339311Dehydrogenase/reductase SDR family member 7PRO_0000031968Add
BLAST

Proteomic databases

MaxQBiQ9Y394.
PaxDbiQ9Y394.
PRIDEiQ9Y394.

PTM databases

PhosphoSiteiQ9Y394.

Expressioni

Gene expression databases

BgeeiQ9Y394.
CleanExiHS_DHRS7.
ExpressionAtlasiQ9Y394. baseline and differential.
GenevestigatoriQ9Y394.

Organism-specific databases

HPAiHPA031121.

Interactioni

Protein-protein interaction databases

BioGridi119649. 16 interactions.
IntActiQ9Y394. 5 interactions.
STRINGi9606.ENSP00000216500.

Structurei

3D structure databases

ProteinModelPortaliQ9Y394.
SMRiQ9Y394. Positions 19-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0300.
GeneTreeiENSGT00770000120481.
HOVERGENiHBG054346.
InParanoidiQ9Y394.
KOiK11165.
OrthoDBiEOG7W6WM5.
PhylomeDBiQ9Y394.
TreeFamiTF354276.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y394-1) [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
MNWELLLWLL VLCALLLLLV QLLRFLRADG DLTLLWAEWQ GRRPEWELTD
60 70 80 90 100
MVVWVTGASS GIGEELAYQL SKLGVSLVLS ARRVHELERV KRRCLENGNL
110 120 130 140 150
KEKDILVLPL DLTDTGSHEA ATKAVLQEFG RIDILVNNGG MSQRSLCMDT
160 170 180 190 200
SLDVYRKLIE LNYLGTVSLT KCVLPHMIER KQGKIVTVNS ILGIISVPLS
210 220 230 240 250
IGYCASKHAL RGFFNGLRTE LATYPGIIVS NICPGPVQSN IVENSLAGEV
260 270 280 290 300
TKTIGNNGDQ SHKMTTSRCV RLMLISMAND LKEVWISEQP FLLVTYLWQY
310 320 330
MPTWAWWITN KMGKKRIENF KSGVDADSSY FKIFKTKHD
Length:339
Mass (Da):38,299
Last modified:November 1, 1999 - v1
Checksum:i7B251CE5894ED70C
GO
Isoform 2 (identifier: Q9Y394-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Note: No experimental confirmation available.

Show »
Length:289
Mass (Da):32,268
Checksum:i051AF9154FB0DEDF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti218 – 2181R → Q.
Corresponds to variant rs34583017 [ dbSNP | Ensembl ].
VAR_052319

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050Missing in isoform 2. 1 PublicationVSP_008103Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151844 mRNA. Translation: AAD34081.1.
AF126782 mRNA. Translation: AAF06941.1.
AY359031 mRNA. Translation: AAQ89390.1.
AK313285 mRNA. Translation: BAG36093.1.
AL163853 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80770.1.
BC000637 mRNA. Translation: AAH00637.1.
BC007337 mRNA. Translation: AAH07337.1.
CCDSiCCDS9743.1. [Q9Y394-1]
RefSeqiNP_057113.1. NM_016029.2. [Q9Y394-1]
UniGeneiHs.59719.

Genome annotation databases

EnsembliENST00000216500; ENSP00000216500; ENSG00000100612. [Q9Y394-1]
ENST00000536410; ENSP00000442993; ENSG00000100612. [Q9Y394-2]
ENST00000557185; ENSP00000451882; ENSG00000100612. [Q9Y394-1]
GeneIDi51635.
KEGGihsa:51635.
UCSCiuc001xes.3. human. [Q9Y394-1]

Polymorphism databases

DMDMi34395856.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151844 mRNA. Translation: AAD34081.1.
AF126782 mRNA. Translation: AAF06941.1.
AY359031 mRNA. Translation: AAQ89390.1.
AK313285 mRNA. Translation: BAG36093.1.
AL163853 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80770.1.
BC000637 mRNA. Translation: AAH00637.1.
BC007337 mRNA. Translation: AAH07337.1.
CCDSiCCDS9743.1. [Q9Y394-1]
RefSeqiNP_057113.1. NM_016029.2. [Q9Y394-1]
UniGeneiHs.59719.

3D structure databases

ProteinModelPortaliQ9Y394.
SMRiQ9Y394. Positions 19-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119649. 16 interactions.
IntActiQ9Y394. 5 interactions.
STRINGi9606.ENSP00000216500.

PTM databases

PhosphoSiteiQ9Y394.

Polymorphism databases

DMDMi34395856.

Proteomic databases

MaxQBiQ9Y394.
PaxDbiQ9Y394.
PRIDEiQ9Y394.

Protocols and materials databases

DNASUi51635.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216500; ENSP00000216500; ENSG00000100612. [Q9Y394-1]
ENST00000536410; ENSP00000442993; ENSG00000100612. [Q9Y394-2]
ENST00000557185; ENSP00000451882; ENSG00000100612. [Q9Y394-1]
GeneIDi51635.
KEGGihsa:51635.
UCSCiuc001xes.3. human. [Q9Y394-1]

Organism-specific databases

CTDi51635.
GeneCardsiGC14M060610.
H-InvDBHIX0011708.
HGNCiHGNC:21524. DHRS7.
HPAiHPA031121.
MIMi612833. gene.
neXtProtiNX_Q9Y394.
PharmGKBiPA134974539.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0300.
GeneTreeiENSGT00770000120481.
HOVERGENiHBG054346.
InParanoidiQ9Y394.
KOiK11165.
OrthoDBiEOG7W6WM5.
PhylomeDBiQ9Y394.
TreeFamiTF354276.

Miscellaneous databases

GenomeRNAii51635.
NextBioi55569.
PROiQ9Y394.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y394.
CleanExiHS_DHRS7.
ExpressionAtlasiQ9Y394. baseline and differential.
GenevestigatoriQ9Y394.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "Short-chain dehydrogenases/reductases in retina."
    Haeseleer F., Palczewski K.
    Methods Enzymol. 316:372-383(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    Tissue: Retina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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] (ISOFORM 1).
    Tissue: Skeletal muscle.
  5. "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.
    , 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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Eye and Skin.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHRS7_HUMAN
AccessioniPrimary (citable) accession number: Q9Y394
Secondary accession number(s): B2R896, Q9UKU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 115 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.