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Q08491

- SKI7_YEAST

UniProt

Q08491 - SKI7_YEAST

Protein

Superkiller protein 7

Gene

SKI7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Represses the expression of non-poly(A) mRNAs like L-A or M viruses and is therefore involved in antiviral system. Mediates interactions via its N-terminus between the exosome and the SKI complex which operate in the 3'-to-5' mRNA-decay pathway. By interacting with NAM7, is also required for nonsense-mediated 3'-to-5' mRNA-decay (NMD). May recognize a stalled 80S ribosome at the 3'-end of a nonstop mRNA which leads to the recruitment of the exosome and SKI complexes to the mRNAs to be degraded.10 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi274 – 2818GTPBy similarity
    Nucleotide bindingi356 – 3605GTPBy similarity
    Nucleotide bindingi427 – 4304GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein binding, bridging Source: SGD

    GO - Biological processi

    1. nonfunctional rRNA decay Source: SGD
    2. nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
    3. nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' Source: SGD
    4. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
    5. regulation of translation Source: UniProtKB-KW
    6. translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Nonsense-mediated mRNA decay, Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33613-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superkiller protein 7
    Gene namesi
    Name:SKI7
    Ordered Locus Names:YOR076C
    ORF Names:YOR29-27
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR076c.
    SGDiS000005602. SKI7.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747Superkiller protein 7PRO_0000269648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881Phosphoserine1 Publication
    Modified residuei90 – 901Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ08491.
    PaxDbiQ08491.
    PeptideAtlasiQ08491.

    Expressioni

    Gene expression databases

    GenevestigatoriQ08491.

    Interactioni

    Subunit structurei

    Interacts with the exosome and with the SKI complex composed of at least SKI2, SKI3 and SKI8. Interacts directly with SKI3 and SKI8.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSL4P538595EBI-1389,EBI-1731
    SKI3P178832EBI-1389,EBI-1861
    SKI8Q027933EBI-1389,EBI-17260
    UPF1Q929002EBI-1389,EBI-373471From a different organism.

    Protein-protein interaction databases

    BioGridi34475. 104 interactions.
    DIPiDIP-995N.
    IntActiQ08491. 17 interactions.
    MINTiMINT-518978.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08491.
    SMRiQ08491. Positions 249-566.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini265 – 503239tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 2818G1PROSITE-ProRule annotation
    Regioni331 – 3355G2PROSITE-ProRule annotation
    Regioni356 – 3594G3PROSITE-ProRule annotation
    Regioni427 – 4304G4PROSITE-ProRule annotation
    Regioni467 – 4693G5PROSITE-ProRule annotation

    Domaini

    The N-terminal domain (residues 1 to 264) is required and sufficient for interaction with the exosome and SKI complexes and for 3'-to-5' mRNA degradation.1 Publication

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5256.
    GeneTreeiENSGT00600000085333.
    KOiK12595.
    OrthoDBiEOG7V1G03.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00009. GTP_EFTU. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q08491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLLEQLARK RIEKSKGLLS ADQSHSTSKS ASLLERLHKN RETKDNNAET    50
    KRKDLKTLLA KDKVKRSDFT PNQHSVSLSL KLSALKKSNS DLEKQGKSVT 100
    LDSKENELPT KRKSPDDKLN LEESWKAIKE MNHYCFLKND PCINQTDDFA 150
    FTNFIIKDKK NSLSTSIPLS SQNSSFLSLK KHNNELLGIF VPCNLPKTTR 200
    KVAIENFNRP SPDDIIQSAQ LNAFNEKLEN LNIKSVPKAE KKEPINLQTP 250
    PTESIDIHSF IATHPLNLTC LFLGDTNAGK STLLGHLLYD LNEISMSSMR 300
    ELQKKSSNLD PSSSNSFKVI LDNTKTEREN GFSMFKKVIQ VENDLLPPSS 350
    TLTLIDTPGS IKYFNKETLN SILTFDPEVY VLVIDCNYDS WEKSLDGPNN 400
    QIYEILKVIS YLNKNSACKK HLIILLNKAD LISWDKHRLE MIQSELNYVL 450
    KENFQWTDAE FQFIPCSGLL GSNLNKTENI TKSKYKSEFD SINYVPEWYE 500
    GPTFFSQLYL LVEHNMNKIE TTLEEPFVGT ILQSSVLQPI AEINYVSLKV 550
    LINSGYIQSG QTIEIHTQYE DFHYYGIVSR MKNSKQILET NTKNNISVGL 600
    NPDILEVLVK IHNTEDFTKK QFHIRKGDII IHSRKTNTLS PNLPNTLKLL 650
    ALRLIKLSIQ THALSDPVDL GSELLLYHNL THNAVKLVKI LGTNDISINP 700
    NQSLIVEVEI IEPDFALNVI DSKYITNNIV LTSIDHKVIA VGRIACQ 747
    Length:747
    Mass (Da):84,779
    Last modified:November 1, 1996 - v1
    Checksum:iD93B956D02050BFA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70678 Genomic DNA. Translation: CAA94561.1.
    Z74984 Genomic DNA. Translation: CAA99269.1.
    BK006948 Genomic DNA. Translation: DAA10855.1.
    PIRiS66959.
    RefSeqiNP_014719.1. NM_001183495.1.

    Genome annotation databases

    EnsemblFungiiYOR076C; YOR076C; YOR076C.
    GeneIDi854243.
    KEGGisce:YOR076C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70678 Genomic DNA. Translation: CAA94561.1 .
    Z74984 Genomic DNA. Translation: CAA99269.1 .
    BK006948 Genomic DNA. Translation: DAA10855.1 .
    PIRi S66959.
    RefSeqi NP_014719.1. NM_001183495.1.

    3D structure databases

    ProteinModelPortali Q08491.
    SMRi Q08491. Positions 249-566.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34475. 104 interactions.
    DIPi DIP-995N.
    IntActi Q08491. 17 interactions.
    MINTi MINT-518978.

    Proteomic databases

    MaxQBi Q08491.
    PaxDbi Q08491.
    PeptideAtlasi Q08491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR076C ; YOR076C ; YOR076C .
    GeneIDi 854243.
    KEGGi sce:YOR076C.

    Organism-specific databases

    CYGDi YOR076c.
    SGDi S000005602. SKI7.

    Phylogenomic databases

    eggNOGi COG5256.
    GeneTreei ENSGT00600000085333.
    KOi K12595.
    OrthoDBi EOG7V1G03.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33613-MONOMER.

    Miscellaneous databases

    NextBioi 976147.

    Gene expression databases

    Genevestigatori Q08491.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames."
      Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.
      Yeast 13:379-390(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2 double-stranded RNA by L-A-HN and confer cold sensitivity in the presence of M and L-A-HN."
      Ridley S.P., Sommer S.S., Wickner R.B.
      Mol. Cell. Biol. 4:761-770(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "The ski7 antiviral protein is an EF1-alpha homolog that blocks expression of non-Poly(A) mRNA in Saccharomyces cerevisiae."
      Benard L., Carroll K., Valle R.C.P., Masison D.C., Wickner R.B.
      J. Virol. 73:2893-2900(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Function of the ski4p (Csl4p) and Ski7p proteins in 3'-to-5' degradation of mRNA."
      van Hoof A., Staples R.R., Baker R.E., Parker R.
      Mol. Cell. Biol. 20:8230-8243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Ski7p G protein interacts with the exosome and the Ski complex for 3'-to-5' mRNA decay in yeast."
      Araki Y., Takahashi S., Kobayashi T., Kajiho H., Hoshino S., Katada T.
      EMBO J. 20:4684-4693(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH THE EXOSOME AND SKI COMPLEXES.
    8. "The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation."
      He W., Parker R.
      Genetics 158:1445-1455(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Exosome-mediated recognition and degradation of mRNAs lacking a termination codon."
      van Hoof A., Frischmeyer P.A., Dietz H.C., Parker R.
      Science 295:2262-2264(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE EXOSOME COMPLEX.
    10. "Interaction between Ski7p and Upf1p is required for nonsense-mediated 3'-to-5' mRNA decay in yeast."
      Takahashi S., Araki Y., Sakuno T., Katada T.
      EMBO J. 22:3951-3959(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NAM7.
    11. "An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3'-->5' degradation."
      Mitchell P., Tollervey D.
      Mol. Cell 11:1405-1413(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus."
      Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., Ahlquist P.
      Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
      Sheth U., Parker R.
      Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Translation of aberrant mRNAs lacking a termination codon or with a shortened 3'-UTR is repressed after initiation in yeast."
      Inada T., Aiba H.
      EMBO J. 24:1584-1595(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Domain interactions within the Ski2/3/8 complex and between the Ski complex and Ski7p."
      Wang L., Lewis M.S., Johnson A.W.
      RNA 11:1291-1302(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKI3 AND SKI8.
    17. "A single subunit, Dis3, is essentially responsible for yeast exosome core activity."
      Dziembowski A., Lorentzen E., Conti E., Seraphin B.
      Nat. Struct. Mol. Biol. 14:15-22(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE EXOSOME.
    18. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSKI7_YEAST
    AccessioniPrimary (citable) accession number: Q08491
    Secondary accession number(s): D6W2D9, O00032
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 233 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3