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Q9BQE4

- SELS_HUMAN

UniProt

Q9BQE4 - SELS_HUMAN

Protein

Selenoprotein S

Gene

VIMP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. receptor activity Source: UniProtKB
    5. 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

    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

    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

    ArrayExpressiQ9BQE4.
    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.
    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

    MERQEESLSA RPALETEGLR FLHTTVGSLL ATYGWYIVFS CILLYVVFQK    50
    LSARLRALRQ RQLDRAAAAV EPDVVVKRQE ALAAARLKMQ EELNAQVEKH 100
    KEKLKQLEEE KRRQKIEMWD SMQEGKSYKG NAKKPQEEDS PGPSTSSVLK 150
    RKSDRKPLRG GGYNPLSGEG GGACSWRPGR RGPSSGGUG 189
    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.
    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

    ArrayExpressi Q9BQE4.
    Genevestigatori Q9BQE4.

    Family and domain databases

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

    Publicationsi

    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 1, 2014
    This is version 115 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