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Q9BQE4 (SELS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenoprotein S

Short name=SelS
Alternative name(s):
VCP-interacting membrane protein
Gene names
Name:VIMP
Synonyms:SELS
ORF Names:AD-015, SBBI8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination. Ref.6

Subunit structure

Interacts with DERL1 and VCP, suggesting that it forms a membrane complex with DERL1 that serves as a receptor for VCP. Also interacts with DERL2, DERL3 and SELK. The SELK-VIMP complex interacts with VCP. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Ref.6 Ref.7 Ref.8 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm By similarity Ref.1 Ref.6.

Sequence similarities

Belongs to the selenoprotein S family.

Sequence caution

The sequence AAF67483.1 differs from that shown. Reason: Frameshift at position 173.

The sequence AAK15708.1 differs from that shown. Reason: Erroneous termination at position 188. Translated as Sec.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
   Coding sequence diversitySelenocysteine
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from direct assay PubMed 16574427. Source: BHF-UCL

ER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

cell redox homeostasis

Inferred from direct assay PubMed 15063746. Source: UniProtKB

cellular response to insulin stimulus

Traceable author statement PubMed 12663463. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from mutant phenotype PubMed 18675776. Source: BHF-UCL

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 18675776. Source: BHF-UCL

endoplasmic reticulum unfolded protein response

Inferred from direct assay Ref.6. Source: UniProtKB

establishment of protein localization

Traceable author statement Ref.6. Source: UniProtKB

negative regulation of acute inflammatory response to antigenic stimulus

Inferred from mutant phenotype PubMed 18675776. Source: BHF-UCL

negative regulation of glucose import

Traceable author statement PubMed 12663463. Source: BHF-UCL

negative regulation of glycogen biosynthetic process

Traceable author statement PubMed 12663463. Source: BHF-UCL

negative regulation of inflammatory response

Inferred by curator PubMed 16574427. Source: BHF-UCL

negative regulation of interleukin-6 production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 17210132. Source: BHF-UCL

negative regulation of macrophage apoptotic process

Inferred from mutant phenotype PubMed 17210132. Source: BHF-UCL

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from mutant phenotype PubMed 18675776. Source: BHF-UCL

negative regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of gluconeogenesis

Traceable author statement PubMed 12663463. Source: BHF-UCL

regulation of nitric oxide metabolic process

Inferred from mutant phenotype PubMed 18675776. Source: BHF-UCL

response to glucose

Inferred from expression pattern PubMed 15063746. Source: UniProtKB

response to redox state

Inferred from direct assay PubMed 15063746. Source: UniProtKB

retrograde protein transport, ER to cytosol

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcytoplasmic microtubule

Inferred from direct assay PubMed 23264731. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: HPA

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.6. Source: UniProtKB

low-density lipoprotein particle

Inferred from direct assay PubMed 17374524. Source: BHF-UCL

plasma membrane

Traceable author statement PubMed 12663463. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 17374524. Source: BHF-UCL

   Molecular_functionantioxidant activity

Inferred from direct assay PubMed 15063746. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

receptor activity

Non-traceable author statement Ref.6. Source: UniProtKB

selenium binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VcpQ018534EBI-398970,EBI-80597From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Selenoprotein S
PRO_0000097672

Regions

Transmembrane28 – 4821Helical; Potential

Amino acid modifications

Non-standard residue1881Selenocysteine
Modified residue1401Phosphoserine Ref.9

Secondary structure

..... 189
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BQE4 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 720DDCC597A7135A

FASTA18921,163
        10         20         30         40         50         60 
MERQEESLSA RPALETEGLR FLHTTVGSLL ATYGWYIVFS CILLYVVFQK LSARLRALRQ 

        70         80         90        100        110        120 
RQLDRAAAAV EPDVVVKRQE ALAAARLKMQ EELNAQVEKH KEKLKQLEEE KRRQKIEMWD 

       130        140        150        160        170        180 
SMQEGKSYKG NAKKPQEEDS PGPSTSSVLK RKSDRKPLRG GGYNPLSGEG GGACSWRPGR 


RGPSSGGUG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of mammalian selenoproteomes."
Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigo R., Gladyshev V.N.
Science 300:1439-1443(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[3]Li N., Wan T., Zhang W., Cao X.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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].
Tissue: Skin.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol."
Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.
Nature 429:841-847(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VCP AND DERL1.
[7]"Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DERL1.
[8]"Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
Lilley B.N., Ploegh H.L.
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DERL1.
[9]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELK; DERL1; DERL2 AND DERL3, IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN1; RPN2; SELK; STT3A AND VCP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY324824 mRNA. Translation: AAP85541.1.
AF157317 mRNA. Translation: AAF67483.1. Frameshift.
AF328864 mRNA. Translation: AAK15708.1. Sequence problems.
AC023024 Genomic DNA. No translation available.
BC005840 mRNA. Translation: AAH05840.2.
BC107774 mRNA. Translation: AAI07775.1.
CCDSCCDS53979.1.
RefSeqNP_060915.2. NM_018445.5.
NP_982298.2. NM_203472.2.
UniGeneHs.32148.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q2FX-ray1.50A52-122[»]
ProteinModelPortalQ9BQE4.
SMRQ9BQE4. Positions 52-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120934. 17 interactions.
IntActQ9BQE4. 5 interactions.
STRING9606.ENSP00000381282.

PTM databases

PhosphoSiteQ9BQE4.

Polymorphism databases

DMDM172045769.

Proteomic databases

MaxQBQ9BQE4.
PaxDbQ9BQE4.
PRIDEQ9BQE4.

Protocols and materials databases

DNASU55829.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398226; ENSP00000381282; ENSG00000131871.
ENST00000526049; ENSP00000433541; ENSG00000131871.
GeneID55829.
KEGGhsa:55829.
UCSCuc021sxu.1. human.

Organism-specific databases

CTD55829.
GeneCardsGC15M101813.
HGNCHGNC:30396. VIMP.
HPAHPA010025.
MIM607918. gene.
neXtProtNX_Q9BQE4.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76592.
HOGENOMHOG000168422.
HOVERGENHBG044521.
InParanoidQ9BQE4.
KOK14025.
OMAKSYKRNA.
OrthoDBEOG72VH83.
PhylomeDBQ9BQE4.
TreeFamTF329454.

Gene expression databases

ArrayExpressQ9BQE4.
GenevestigatorQ9BQE4.

Family and domain databases

InterProIPR009703. Selenoprotein_S.
[Graphical view]
PfamPF06936. Selenoprotein_S. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BQE4.
GeneWikiSELS_(gene).
GenomeRNAi55829.
NextBio61032.
PROQ9BQE4.
SOURCESearch...

Entry information

Entry nameSELS_HUMAN
AccessionPrimary (citable) accession number: Q9BQE4
Secondary accession number(s): Q3B771, Q9P0I6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: February 26, 2008
Last modified: July 9, 2014
This is version 114 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

MIM cross-references

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

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM