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P35207

- SKI2_YEAST

UniProt

P35207 - SKI2_YEAST

Protein

Antiviral helicase SKI2

Gene

SKI2

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 140 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.13 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi351 – 3588ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB-KW
    5. RNA helicase activity Source: SGD

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    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

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Antiviral defense, Translation regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32462-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antiviral helicase SKI2 (EC:3.6.4.13)
    Alternative name(s):
    Superkiller protein 2
    Gene namesi
    Name:SKI2
    Ordered Locus Names:YLR398C
    ORF Names:L8084.17
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR398c.
    SGDiS000004390. SKI2.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. Ski complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12871287Antiviral helicase SKI2PRO_0000102084Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei209 – 2091Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35207.
    PaxDbiP35207.
    PeptideAtlasiP35207.

    Expressioni

    Gene expression databases

    GenevestigatoriP35207.

    Interactioni

    Subunit structurei

    Component of the SKI complex composed of at least SKI2, SKI3 and SKI8. The SKI complex interacts with SKI7, which makes the link between the SKI complex and the exosome in order to perform mRNA degradation.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SKI3P1788310EBI-1851,EBI-1861
    SKI8Q0279310EBI-1851,EBI-17260

    Protein-protein interaction databases

    BioGridi31657. 130 interactions.
    DIPiDIP-5887N.
    IntActiP35207. 14 interactions.
    MINTiMINT-662639.
    STRINGi4932.YLR398C.

    Structurei

    Secondary structure

    1
    1287
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi302 – 3054
    Helixi315 – 3184
    Helixi332 – 34211
    Beta strandi346 – 3505
    Helixi358 – 37013
    Beta strandi374 – 3807
    Helixi382 – 3843
    Helixi385 – 3939
    Beta strandi401 – 4044
    Beta strandi414 – 4207
    Helixi421 – 43010
    Helixi434 – 4374
    Beta strandi438 – 4436
    Helixi458 – 4647
    Beta strandi470 – 4756
    Helixi481 – 49212
    Beta strandi496 – 5005
    Beta strandi508 – 5147
    Beta strandi517 – 5226
    Helixi530 – 54011
    Helixi613 – 62311
    Beta strandi628 – 6325
    Helixi636 – 6449
    Turni645 – 6484
    Helixi654 – 66815
    Helixi673 – 6764
    Helixi679 – 68810
    Turni689 – 6913
    Beta strandi692 – 6954
    Helixi701 – 71212
    Beta strandi717 – 7215
    Helixi724 – 7274
    Beta strandi734 – 7396
    Beta strandi741 – 7455
    Beta strandi748 – 7514
    Helixi754 – 7618
    Helixi762 – 7643
    Turni767 – 7693
    Beta strandi771 – 7788
    Helixi786 – 7949
    Helixi808 – 81710
    Helixi821 – 8277
    Helixi830 – 85425
    Turni862 – 8643
    Beta strandi865 – 8684
    Helixi871 – 88919
    Helixi895 – 8984
    Beta strandi903 – 9086
    Beta strandi914 – 92310
    Turni924 – 9274
    Beta strandi928 – 9336
    Beta strandi943 – 9453
    Helixi955 – 9617
    Beta strandi971 – 9766
    Helixi977 – 9793
    Beta strandi982 – 9876
    Helixi992 – 9976
    Helixi1000 – 101516
    Helixi1031 – 104414
    Helixi1051 – 10533
    Helixi1061 – 107919
    Turni1080 – 10823
    Helixi1088 – 110114
    Helixi1113 – 11186
    Helixi1126 – 11349
    Helixi1137 – 11404
    Helixi1143 – 11508
    Helixi1151 – 11533
    Helixi1169 – 119123
    Helixi1198 – 12025
    Helixi1203 – 12053
    Turni1208 – 12114
    Helixi1212 – 12209
    Helixi1224 – 12296
    Helixi1235 – 125925
    Helixi1262 – 127514
    Helixi1278 – 12814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A4KX-ray3.25A/C/E/G/I835-1085[»]
    4A4ZX-ray2.40A296-1287[»]
    4BUJX-ray3.70A/E1-834[»]
    A/E1086-1287[»]
    ProteinModelPortaliP35207.
    SMRiP35207. Positions 299-549, 600-1287.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini338 – 496159Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini638 – 815178Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni556 – 57722RNA-binding RGG-boxBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi444 – 4474DEVH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi555 – 59743Arg/Gly-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the helicase family. SKI2 subfamily.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4581.
    GeneTreeiENSGT00750000117758.
    HOGENOMiHOG000163048.
    KOiK12599.
    OMAiVIIMLPD.
    OrthoDBiEOG7WT48P.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR012961. DSH_C.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR016438. RNA_helicase_ATP-dep_SK12/DOB1.
    IPR025696. rRNA_proc-arch_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF08148. DSHCT. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF13234. rRNA_proc-arch. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005198. Antiviral_helicase_SKI2. 1 hit.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35207-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEGFSSSSI QELYQSLKEI TNNADVELFE DRITKLDFES TDEPKHANDI     50
    IKDRFLRPSN ALPWSLLDMV QDVPHTSSPE DCSGKLDYKE LLKVPDPINR 100
    TSYQFKRTGL EGKISGYKEE VDLKEVANAN ASNSLSITRS INHNQNSVRG 150
    STAQLPFTPG GIPMKSVKTD SEQNGSSTMA NATKLLHKDG QGLFDIPEGM 200
    NRGIKPMDSP AENEDQNGQF KELKQLNEID NELDIRIEAN EAKLKEEEKS 250
    AKSISEEIME EATEETTADN ADDAEIDELL PIGIDFGRTK PVSKSVPVKK 300
    EWAHVVDLNH KIENFDELIP NPARSWPFEL DTFQKEAVYH LEQGDSVFVA 350
    AHTSAGKTVV AEYAIAMAHR NMTKTIYTSP IKALSNQKFR DFKETFDDVN 400
    IGLITGDVQI NPDANCLIMT TEILRSMLYR GADLIRDVEF VIFDEVHYVN 450
    DQDRGVVWEE VIIMLPQHVK FILLSATVPN TYEFANWIGR TKQKNIYVIS 500
    TPKRPVPLEI NIWAKKELIP VINQNSEFLE ANFRKHKEIL NGESAKGAPS 550
    KTDNGRGGST ARGGRGGSNT RDGRGGRGNS TRGGANRGGS RGAGAIGSNK 600
    RKFFTQDGPS KKTWPEIVNY LRKRELLPMV VFVFSKKRCE EYADWLEGIN 650
    FCNNKEKSQI HMFIEKSITR LKKEDRDLPQ ILKTRSLLER GIAVHHGGLL 700
    PIVKELIEIL FSKGFIKVLF ATETFAMGLN LPTRTVIFSS IRKHDGNGLR 750
    ELTPGEFTQM AGRAGRRGLD STGTVIVMAY NSPLSIATFK EVTMGVPTRL 800
    QSQFRLTYNM ILNLLRIEAL RVEEMIKYSF SENAKETLQP EHEKQIKVLQ 850
    EELQTIEYKS CEICDNDIEK FLELMLAYKE ATVNLMQEMV KSPSILHILK 900
    EGRLVAFRDP NDCLKLGFVF KVSLKDAVCV IMTFTKPYKL PNGEPNHLIY 950
    FPKADGYRRR NFPKFQKTDF YMEEVPVTAI EVITKRKFAA PLGKVIKKDV 1000
    AALNEFNAET NNILDGKTLK EAINIEKQGL KIHQILLDRT NIRDEIFKLK 1050
    SIKCPNLSQH IVPKFKAHVI KKKIEELYHL MSDQNLSLLP DYEKRLAVLK 1100
    DTEFIDQNHN VLLKGRVACE INSGYELVLT ELILDNFLGS FEPEEIVALL 1150
    SVFVYEGKTR EEEPPIVTPR LAKGKQRIEE IYKKMLCVFN THQIPLTQDE 1200
    AEFLDRKRFA MMNVVYEWAR GLSFKEIMEM SPEAEGTVVR VITWLDEICR 1250
    EVKTASIIIG NSTLHMKMSR AQELIKRDIV FAASLYL 1287
    Length:1,287
    Mass (Da):146,059
    Last modified:May 30, 2000 - v2
    Checksum:i7CCD36CFC0DF8C32
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261W → C in AAA35049. (PubMed:8321235)Curated
    Sequence conflicti759 – 7602QM → L in AAA35049. (PubMed:8321235)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13469 mRNA. Translation: AAA35049.1.
    U19729 Genomic DNA. Translation: AAB82356.1.
    Z18944 Genomic DNA. Translation: CAA79378.1.
    BK006945 Genomic DNA. Translation: DAA09699.1.
    PIRiS55954.
    RefSeqiNP_013502.3. NM_001182286.3.

    Genome annotation databases

    EnsemblFungiiYLR398C; YLR398C; YLR398C.
    GeneIDi851114.
    KEGGisce:YLR398C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13469 mRNA. Translation: AAA35049.1 .
    U19729 Genomic DNA. Translation: AAB82356.1 .
    Z18944 Genomic DNA. Translation: CAA79378.1 .
    BK006945 Genomic DNA. Translation: DAA09699.1 .
    PIRi S55954.
    RefSeqi NP_013502.3. NM_001182286.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A4K X-ray 3.25 A/C/E/G/I 835-1085 [» ]
    4A4Z X-ray 2.40 A 296-1287 [» ]
    4BUJ X-ray 3.70 A/E 1-834 [» ]
    A/E 1086-1287 [» ]
    ProteinModelPortali P35207.
    SMRi P35207. Positions 299-549, 600-1287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31657. 130 interactions.
    DIPi DIP-5887N.
    IntActi P35207. 14 interactions.
    MINTi MINT-662639.
    STRINGi 4932.YLR398C.

    Proteomic databases

    MaxQBi P35207.
    PaxDbi P35207.
    PeptideAtlasi P35207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR398C ; YLR398C ; YLR398C .
    GeneIDi 851114.
    KEGGi sce:YLR398C.

    Organism-specific databases

    CYGDi YLR398c.
    SGDi S000004390. SKI2.

    Phylogenomic databases

    eggNOGi COG4581.
    GeneTreei ENSGT00750000117758.
    HOGENOMi HOG000163048.
    KOi K12599.
    OMAi VIIMLPD.
    OrthoDBi EOG7WT48P.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32462-MONOMER.

    Miscellaneous databases

    NextBioi 967830.
    PROi P35207.

    Gene expression databases

    Genevestigatori P35207.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR012961. DSH_C.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR016438. RNA_helicase_ATP-dep_SK12/DOB1.
    IPR025696. rRNA_proc-arch_dom.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF08148. DSHCT. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF13234. rRNA_proc-arch. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005198. Antiviral_helicase_SKI2. 1 hit.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA."
      Widner W.R., Wickner R.B.
      Mol. Cell. Biol. 13:4331-4341(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(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. "The yeast BDF1 gene encodes a transcription factor involved in the expression of a broad class of genes including snRNAs."
      Lygerou Z., Conesa C., Lesage P., Swanson R.N., Ruet A., Carlson M., Sentenac A., Seraphin B.
      Nucleic Acids Res. 22:5332-5340(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162.
      Strain: ATCC 204508 / S288c.
    5. "Chromosomal superkiller mutants of Saccharomyces cerevisiae."
      Toh-e A., Guerry P., Wickner R.B.
      J. Bacteriol. 136:1002-1007(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "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.
    7. "Synthetic lethality of sep1 (xrn1) ski2 and sep1 (xrn1) ski3 mutants of Saccharomyces cerevisiae is independent of killer virus and suggests a general role for these genes in translation control."
      Johnson A.W., Kolodner R.D.
      Mol. Cell. Biol. 15:2719-2727(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system."
      Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.
      Mol. Cell. Biol. 15:2763-2771(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex."
      Anderson J.S.J., Parker R.P.
      EMBO J. 17:1497-1506(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs."
      van Hoof A., Lennertz P., Parker R.
      Mol. Cell. Biol. 20:441-452(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in vivo."
      Brown J.T., Bai X., Johnson A.W.
      RNA 6:449-457(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SKI3 AND SKI8, SUBCELLULAR LOCATION.
    12. Cited for: FUNCTION.
    13. "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 OF THE SKI COMPLEX.
    14. "A cis-acting element known to block 3' mRNA degradation enhances expression of polyA-minus mRNA in wild-type yeast cells and phenocopies a ski mutant."
      Brown J.T., Johnson A.W.
      RNA 7:1566-1577(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SKI COMPLEX.
    15. "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.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    18. "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.
    19. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    20. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: MODELING OF THE SKI COMPLEX 3D-STRUCTURE.

    Entry informationi

    Entry nameiSKI2_YEAST
    AccessioniPrimary (citable) accession number: P35207
    Secondary accession number(s): D6VZ33, Q06047
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 5770 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3