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Q9BQE4

- SELS_HUMAN

UniProt

Q9BQE4 - SELS_HUMAN

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Protein

Selenoprotein S

Gene

VIMP

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

Functioni

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.1 Publication

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. receptor activity Source: UniProtKB
  4. selenium binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: UniProtKB
  2. cellular response to insulin stimulus Source: BHF-UCL
  3. cellular response to lipopolysaccharide Source: BHF-UCL
  4. cellular response to oxidative stress Source: BHF-UCL
  5. endoplasmic reticulum unfolded protein response Source: UniProtKB
  6. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. ER overload response Source: BHF-UCL
  8. establishment of protein localization Source: UniProtKB
  9. negative regulation of acute inflammatory response to antigenic stimulus Source: BHF-UCL
  10. negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  11. negative regulation of glucose import Source: BHF-UCL
  12. negative regulation of glycogen biosynthetic process Source: BHF-UCL
  13. negative regulation of inflammatory response Source: BHF-UCL
  14. negative regulation of interleukin-6 production Source: BHF-UCL
  15. negative regulation of macrophage apoptotic process Source: BHF-UCL
  16. negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  17. negative regulation of tumor necrosis factor production Source: BHF-UCL
  18. regulation of gluconeogenesis Source: BHF-UCL
  19. regulation of nitric oxide metabolic process Source: BHF-UCL
  20. response to glucose Source: UniProtKB
  21. response to redox state Source: UniProtKB
  22. retrograde protein transport, ER to cytosol Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Selenoprotein S
Short name:
SelS
Alternative name(s):
VCP-interacting membrane protein
Gene namesi
Name:VIMP
Synonyms:SELS
ORF Names:AD-015, SBBI8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:30396. VIMP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: UniProtKB
  2. endoplasmic reticulum Source: HPA
  3. integral component of endoplasmic reticulum membrane Source: UniProtKB
  4. low-density lipoprotein particle Source: BHF-UCL
  5. plasma membrane Source: BHF-UCL
  6. very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Selenoprotein SPRO_0000097672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BQE4.
PaxDbiQ9BQE4.
PRIDEiQ9BQE4.

PTM databases

PhosphoSiteiQ9BQE4.

Expressioni

Gene expression databases

ExpressionAtlasiQ9BQE4. baseline and differential.
GenevestigatoriQ9BQE4.

Organism-specific databases

HPAiHPA010025.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VcpQ018534EBI-398970,EBI-80597From a different organism.

Protein-protein interaction databases

BioGridi120934. 17 interactions.
IntActiQ9BQE4. 5 interactions.
STRINGi9606.ENSP00000381282.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 6816
Helixi72 – 12150

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q2FX-ray1.50A52-122[»]
ProteinModelPortaliQ9BQE4.
SMRiQ9BQE4. Positions 52-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BQE4.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei28 – 4821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the selenoprotein S family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG76592.
GeneTreeiENSGT00390000015688.
HOGENOMiHOG000168422.
HOVERGENiHBG044521.
InParanoidiQ9BQE4.
KOiK14025.
OMAiKSYKRNA.
OrthoDBiEOG72VH83.
PhylomeDBiQ9BQE4.
TreeFamiTF329454.

Family and domain databases

InterProiIPR009703. Selenoprotein_S.
[Graphical view]
PfamiPF06936. Selenoprotein_S. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BQE4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERQEESLSA RPALETEGLR FLHTTVGSLL ATYGWYIVFS CILLYVVFQK
60 70 80 90 100
LSARLRALRQ RQLDRAAAAV EPDVVVKRQE ALAAARLKMQ EELNAQVEKH
110 120 130 140 150
KEKLKQLEEE KRRQKIEMWD SMQEGKSYKG NAKKPQEEDS PGPSTSSVLK
160 170 180
RKSDRKPLRG GGYNPLSGEG GGACSWRPGR RGPSSGGUG
Length:189
Mass (Da):21,163
Last modified:February 26, 2008 - v3
Checksum:i720DDCC597A7135A
GO

Sequence cautioni

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.

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei188 – 1881Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53979.1.
RefSeqiNP_060915.2. NM_018445.5.
NP_982298.2. NM_203472.2.
UniGeneiHs.32148.

Genome annotation databases

EnsembliENST00000398226; ENSP00000381282; ENSG00000131871.
ENST00000526049; ENSP00000433541; ENSG00000131871.
GeneIDi55829.
KEGGihsa:55829.
UCSCiuc021sxu.1. human.

Polymorphism databases

DMDMi172045769.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS53979.1.
RefSeqi NP_060915.2. NM_018445.5.
NP_982298.2. NM_203472.2.
UniGenei Hs.32148.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q2F X-ray 1.50 A 52-122 [» ]
ProteinModelPortali Q9BQE4.
SMRi Q9BQE4. Positions 52-122.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120934. 17 interactions.
IntActi Q9BQE4. 5 interactions.
STRINGi 9606.ENSP00000381282.

PTM databases

PhosphoSitei Q9BQE4.

Polymorphism databases

DMDMi 172045769.

Proteomic databases

MaxQBi Q9BQE4.
PaxDbi Q9BQE4.
PRIDEi Q9BQE4.

Protocols and materials databases

DNASUi 55829.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398226 ; ENSP00000381282 ; ENSG00000131871 .
ENST00000526049 ; ENSP00000433541 ; ENSG00000131871 .
GeneIDi 55829.
KEGGi hsa:55829.
UCSCi uc021sxu.1. human.

Organism-specific databases

CTDi 55829.
GeneCardsi GC15M101813.
HGNCi HGNC:30396. VIMP.
HPAi HPA010025.
MIMi 607918. gene.
neXtProti NX_Q9BQE4.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG76592.
GeneTreei ENSGT00390000015688.
HOGENOMi HOG000168422.
HOVERGENi HBG044521.
InParanoidi Q9BQE4.
KOi K14025.
OMAi KSYKRNA.
OrthoDBi EOG72VH83.
PhylomeDBi Q9BQE4.
TreeFami TF329454.

Miscellaneous databases

EvolutionaryTracei Q9BQE4.
GeneWikii SELS_(gene).
GenomeRNAii 55829.
NextBioi 61032.
PROi Q9BQE4.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi Q9BQE4. baseline and differential.
Genevestigatori Q9BQE4.

Family and domain databases

InterProi IPR009703. Selenoprotein_S.
[Graphical view ]
Pfami PF06936. Selenoprotein_S. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. 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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. 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.

Entry informationi

Entry nameiSELS_HUMAN
AccessioniPrimary (citable) accession number: Q9BQE4
Secondary accession number(s): Q3B771, Q9P0I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: February 26, 2008
Last modified: October 29, 2014
This is version 116 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3