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Protein

Retinol dehydrogenase 13

Gene

RDH13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Does not exhibit retinol dehydrogenase (RDH) activity in vitro.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei174 – 1741SubstrateBy similarity
Active sitei200 – 2001Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 517NAD or NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.300. 2681.
ReactomeiR-HSA-5365859. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol dehydrogenase 13 (EC:1.1.1.-)
Alternative name(s):
Short chain dehydrogenase/reductase family 7C member 3
Gene namesi
Name:RDH13
Synonyms:SDR7C3
ORF Names:PSEC0082, UNQ736/PRO1430
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:19978. RDH13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134897935.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRDH13.
DMDMi62298570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 331330Retinol dehydrogenase 13PRO_0000054768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8NBN7.
MaxQBiQ8NBN7.
PaxDbiQ8NBN7.
PRIDEiQ8NBN7.

PTM databases

iPTMnetiQ8NBN7.
PhosphoSiteiQ8NBN7.

Expressioni

Tissue specificityi

Expressed mostly in eye, pancreas, placenta and lung. In the retina, detected in the inner segment of the photoreceptor cells. Weak signals were observed in a small population of inner nuclear neurons and the inner plexiform layer.1 Publication

Gene expression databases

BgeeiQ8NBN7.
CleanExiHS_RDH13.
ExpressionAtlasiQ8NBN7. baseline and differential.
GenevisibleiQ8NBN7. HS.

Organism-specific databases

HPAiHPA042006.

Interactioni

Protein-protein interaction databases

BioGridi125200. 30 interactions.
IntActiQ8NBN7. 6 interactions.
MINTiMINT-3041712.
STRINGi9606.ENSP00000391121.

Structurei

3D structure databases

ProteinModelPortaliQ8NBN7.
SMRiQ8NBN7. Positions 26-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000119068.
HOVERGENiHBG078800.
InParanoidiQ8NBN7.
KOiK11161.
OMAiKLANYHF.
PhylomeDBiQ8NBN7.
TreeFamiTF105429.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
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: Q8NBN7-1) [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
MSRYLLPLSA LGTVAGAAVL LKDYVTGGAC PSKATIPGKT VIVTGANTGI
60 70 80 90 100
GKQTALELAR RGGNIILACR DMEKCEAAAK DIRGETLNHH VNARHLDLAS
110 120 130 140 150
LKSIREFAAK IIEEEERVDI LINNAGVMRC PHWTTEDGFE MQFGVNHLGH
160 170 180 190 200
FLLTNLLLDK LKASAPSRII NLSSLAHVAG HIDFDDLNWQ TRKYNTKAAY
210 220 230 240 250
CQSKLAIVLF TKELSRRLQG SGVTVNALHP GVARTELGRH TGIHGSTFSS
260 270 280 290 300
TTLGPIFWLL VKSPELAAQP STYLAVAEEL ADVSGKYFDG LKQKAPAPEA
310 320 330
EDEEVARRLW AESARLVGLE APSVREQPLP R
Length:331
Mass (Da):35,932
Last modified:March 29, 2005 - v2
Checksum:iDC5C1A6E54F1E6CC
GO
Isoform 2 (identifier: Q8NBN7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Show »
Length:260
Mass (Da):28,794
Checksum:i12C82526B01A3174
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061E → V in BAC11591 (PubMed:16303743).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform 2. 1 PublicationVSP_040383Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358473 mRNA. Translation: AAQ88837.1.
AK075392 mRNA. Translation: BAC11591.1.
AC011476 Genomic DNA. No translation available.
BC009881 mRNA. Translation: AAH09881.1.
CCDSiCCDS42627.1. [Q8NBN7-2]
CCDS54320.1. [Q8NBN7-1]
RefSeqiNP_001139443.1. NM_001145971.1. [Q8NBN7-1]
NP_612421.1. NM_138412.3. [Q8NBN7-2]
XP_005258530.1. XM_005258473.1. [Q8NBN7-1]
XP_005277150.1. XM_005277093.1. [Q8NBN7-1]
XP_005277295.1. XM_005277238.1. [Q8NBN7-1]
XP_005277352.1. XM_005277295.1. [Q8NBN7-1]
XP_006725924.1. XM_006725861.1. [Q8NBN7-1]
XP_006726012.1. XM_006725949.1. [Q8NBN7-1]
XP_006726111.1. XM_006726048.1. [Q8NBN7-1]
XP_006726209.1. XM_006726146.1. [Q8NBN7-1]
XP_006726247.1. XM_006726184.1. [Q8NBN7-1]
XP_011524709.1. XM_011526407.1. [Q8NBN7-1]
XP_011545399.1. XM_011547097.1. [Q8NBN7-1]
XP_011545810.1. XM_011547508.1. [Q8NBN7-1]
XP_011546059.1. XM_011547757.1. [Q8NBN7-1]
XP_011546260.1. XM_011547958.1. [Q8NBN7-1]
XP_011546439.1. XM_011548137.1. [Q8NBN7-1]
XP_011546632.1. XM_011548330.1. [Q8NBN7-1]
XP_011546843.1. XM_011548541.1. [Q8NBN7-1]
XP_011546894.1. XM_011548592.1. [Q8NBN7-1]
XP_011546895.1. XM_011548593.1. [Q8NBN7-1]
XP_011546987.1. XM_011548685.1. [Q8NBN7-1]
UniGeneiHs.327631.
Hs.731615.

Genome annotation databases

EnsembliENST00000396247; ENSP00000379547; ENSG00000160439. [Q8NBN7-2]
ENST00000415061; ENSP00000391121; ENSG00000160439. [Q8NBN7-1]
ENST00000610356; ENSP00000477732; ENSG00000160439. [Q8NBN7-2]
ENST00000613257; ENSP00000479552; ENSG00000276341. [Q8NBN7-2]
ENST00000613935; ENSP00000482809; ENSG00000274504. [Q8NBN7-2]
ENST00000615256; ENSP00000477512; ENSG00000276684. [Q8NBN7-1]
ENST00000615688; ENSP00000482782; ENSG00000275474. [Q8NBN7-2]
ENST00000616348; ENSP00000477884; ENSG00000276826. [Q8NBN7-2]
ENST00000620423; ENSP00000482051; ENSG00000278149. [Q8NBN7-2]
ENST00000621614; ENSP00000484637; ENSG00000276684. [Q8NBN7-2]
ENST00000621849; ENSP00000480095; ENSG00000273944. [Q8NBN7-2]
ENST00000622200; ENSP00000484111; ENSG00000274418. [Q8NBN7-2]
ENST00000622572; ENSP00000484246; ENSG00000278284. [Q8NBN7-2]
GeneIDi112724.
KEGGihsa:112724.
UCSCiuc002qio.4. human. [Q8NBN7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358473 mRNA. Translation: AAQ88837.1.
AK075392 mRNA. Translation: BAC11591.1.
AC011476 Genomic DNA. No translation available.
BC009881 mRNA. Translation: AAH09881.1.
CCDSiCCDS42627.1. [Q8NBN7-2]
CCDS54320.1. [Q8NBN7-1]
RefSeqiNP_001139443.1. NM_001145971.1. [Q8NBN7-1]
NP_612421.1. NM_138412.3. [Q8NBN7-2]
XP_005258530.1. XM_005258473.1. [Q8NBN7-1]
XP_005277150.1. XM_005277093.1. [Q8NBN7-1]
XP_005277295.1. XM_005277238.1. [Q8NBN7-1]
XP_005277352.1. XM_005277295.1. [Q8NBN7-1]
XP_006725924.1. XM_006725861.1. [Q8NBN7-1]
XP_006726012.1. XM_006725949.1. [Q8NBN7-1]
XP_006726111.1. XM_006726048.1. [Q8NBN7-1]
XP_006726209.1. XM_006726146.1. [Q8NBN7-1]
XP_006726247.1. XM_006726184.1. [Q8NBN7-1]
XP_011524709.1. XM_011526407.1. [Q8NBN7-1]
XP_011545399.1. XM_011547097.1. [Q8NBN7-1]
XP_011545810.1. XM_011547508.1. [Q8NBN7-1]
XP_011546059.1. XM_011547757.1. [Q8NBN7-1]
XP_011546260.1. XM_011547958.1. [Q8NBN7-1]
XP_011546439.1. XM_011548137.1. [Q8NBN7-1]
XP_011546632.1. XM_011548330.1. [Q8NBN7-1]
XP_011546843.1. XM_011548541.1. [Q8NBN7-1]
XP_011546894.1. XM_011548592.1. [Q8NBN7-1]
XP_011546895.1. XM_011548593.1. [Q8NBN7-1]
XP_011546987.1. XM_011548685.1. [Q8NBN7-1]
UniGeneiHs.327631.
Hs.731615.

3D structure databases

ProteinModelPortaliQ8NBN7.
SMRiQ8NBN7. Positions 26-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125200. 30 interactions.
IntActiQ8NBN7. 6 interactions.
MINTiMINT-3041712.
STRINGi9606.ENSP00000391121.

Chemistry

DrugBankiDB00162. Vitamin A.

PTM databases

iPTMnetiQ8NBN7.
PhosphoSiteiQ8NBN7.

Polymorphism and mutation databases

BioMutaiRDH13.
DMDMi62298570.

Proteomic databases

EPDiQ8NBN7.
MaxQBiQ8NBN7.
PaxDbiQ8NBN7.
PRIDEiQ8NBN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396247; ENSP00000379547; ENSG00000160439. [Q8NBN7-2]
ENST00000415061; ENSP00000391121; ENSG00000160439. [Q8NBN7-1]
ENST00000610356; ENSP00000477732; ENSG00000160439. [Q8NBN7-2]
ENST00000613257; ENSP00000479552; ENSG00000276341. [Q8NBN7-2]
ENST00000613935; ENSP00000482809; ENSG00000274504. [Q8NBN7-2]
ENST00000615256; ENSP00000477512; ENSG00000276684. [Q8NBN7-1]
ENST00000615688; ENSP00000482782; ENSG00000275474. [Q8NBN7-2]
ENST00000616348; ENSP00000477884; ENSG00000276826. [Q8NBN7-2]
ENST00000620423; ENSP00000482051; ENSG00000278149. [Q8NBN7-2]
ENST00000621614; ENSP00000484637; ENSG00000276684. [Q8NBN7-2]
ENST00000621849; ENSP00000480095; ENSG00000273944. [Q8NBN7-2]
ENST00000622200; ENSP00000484111; ENSG00000274418. [Q8NBN7-2]
ENST00000622572; ENSP00000484246; ENSG00000278284. [Q8NBN7-2]
GeneIDi112724.
KEGGihsa:112724.
UCSCiuc002qio.4. human. [Q8NBN7-1]

Organism-specific databases

CTDi112724.
GeneCardsiRDH13.
H-InvDBHIX0158529.
HGNCiHGNC:19978. RDH13.
HPAiHPA042006.
neXtProtiNX_Q8NBN7.
PharmGKBiPA134897935.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000119068.
HOVERGENiHBG078800.
InParanoidiQ8NBN7.
KOiK11161.
OMAiKLANYHF.
PhylomeDBiQ8NBN7.
TreeFamiTF105429.

Enzyme and pathway databases

BRENDAi1.1.1.300. 2681.
ReactomeiR-HSA-5365859. RA biosynthesis pathway.

Miscellaneous databases

GenomeRNAii112724.
PROiQ8NBN7.

Gene expression databases

BgeeiQ8NBN7.
CleanExiHS_RDH13.
ExpressionAtlasiQ8NBN7. baseline and differential.
GenevisibleiQ8NBN7. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2).
    Tissue: Placenta.
  5. "Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina."
    Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G., Matsumura M., Nelson P.S., Palczewski K.
    J. Biol. Chem. 277:45537-45546(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ENZYME ACTIVITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRDH13_HUMAN
AccessioniPrimary (citable) accession number: Q8NBN7
Secondary accession number(s): Q6UX79, Q96G88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: March 29, 2005
Last modified: June 8, 2016
This is version 124 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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