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Protein

Superkiller protein 3

Gene

SKI3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.9 Publications

GO - Biological processi

  • defense response to virus Source: UniProtKB-KW
  • nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
  • nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' Source: SGD
  • nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
Complete GO annotation...

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

BioCyciYEAST:G3O-34312-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superkiller protein 3
Gene namesi
Name:SKI3
Ordered Locus Names:YPR189W
ORF Names:P9677.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR189W.
SGDiS000006393. SKI3.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • Ski complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14321432Superkiller protein 3PRO_0000106323Add
BLAST

Proteomic databases

MaxQBiP17883.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SKI2P3520710EBI-1861,EBI-1851
SKI7Q084912EBI-1861,EBI-1389
SKI8Q027937EBI-1861,EBI-17260

Protein-protein interaction databases

BioGridi36361. 128 interactions.
DIPiDIP-6379N.
IntActiP17883. 40 interactions.
MINTiMINT-643301.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BUJX-ray3.70B/F1-1432[»]
ProteinModelPortaliP17883.
SMRiP17883. Positions 1-38, 61-91, 640-798, 1036-1081, 1138-1165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati4 – 3734TPR 1Add
BLAST
Repeati47 – 8034TPR 2Add
BLAST
Repeati425 – 45834TPR 3Add
BLAST
Repeati471 – 50737TPR 4Add
BLAST
Repeati508 – 54134TPR 5Add
BLAST
Repeati627 – 66135TPR 6Add
BLAST
Repeati702 – 73534TPR 7Add
BLAST
Repeati736 – 76934TPR 8Add
BLAST
Repeati945 – 98541TPR 9Add
BLAST
Repeati987 – 101832TPR 10Add
BLAST
Repeati1226 – 125934TPR 11Add
BLAST

Sequence similaritiesi

Contains 11 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00390000016407.
HOGENOMiHOG000247860.
InParanoidiP17883.
KOiK12600.
OMAiFIKATAL.
OrthoDBiEOG747PS9.

Family and domain databases

Gene3Di1.25.40.10. 6 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDIKQLLKE AKQELTNRDY EETIEISEKV LKLDPDNYFA HIFLGKALSS
60 70 80 90 100
LPASNNVSSN RNLERATNHY VSAAKLVPDN LLAWKGLFLL FRTTEVVPDI
110 120 130 140 150
LSYDEYFDLC GQYADALLKQ EQSQVELIND IKLLKKTHPD CQKAFYQHLK
160 170 180 190 200
PGSLMAETIG RHLSTPQDAL LNLIKILSNI ETTEIGKTLS QNRLKLKASD
210 220 230 240 250
PDYQIKLNSF SWEIIKNSEI DQLYNQLVNI LADDQKRSEI ENQWLEYRIK
260 270 280 290 300
VLKSMPLDVK KDFFTKVKEM VEDMVLVNHQ SLLAWQKYFE WTDYEDLDNM
310 320 330 340 350
DAPLIIKYFK KFPKDPLAMI LYSWLSSKLS KYDIKSLESA NKPPEGHKKT
360 370 380 390 400
EKETDIKDVD ETNEDEVKDR VEDEVKDRVE DEVKDQDEEA KEDEEEDLDD
410 420 430 440 450
IEIGLLEEEV VTVLTENIVK CKNNILAHRI LCQYYLLTKE YEAALPYIKN
460 470 480 490 500
GISLIAYNIK DLGVHLPLTK REFSLDLATV YTYVDAPKDH NAALKLYDNI
510 520 530 540 550
LSGDFSNIQA KMGKGIIFIE RKNWKDAMTL LTQVHEQSPN NLEVLSELSW
560 570 580 590 600
SKAHMGYMDE ALAGLDTVIK GIKGMDLRSI DFRALNLWRQ AKVYIMKHAS
610 620 630 640 650
INDAKQENVK CAFKLLIQSI KILDTFAPGF STLGDIYCHY YKDHLRAFKC
660 670 680 690 700
YFKAFDLDAG DYTAAKYITE TYASKPNWQA ASSIASRLIK GEKAKAELRS
710 720 730 740 750
NNWPFRVVGI AHLEKQEESD SIEWFQSALR VDPNDVESWV GLGQAYHACG
760 770 780 790 800
RIEASIKVFD KAIQLRPSHT FAQYFKAISL CDVGEYLESL DILEKVCQEA
810 820 830 840 850
ATEESFQIGL VEVLMRCSLD LYSQGFLLKS VSIAKDTIER IKIIISELKC
860 870 880 890 900
ENQQVWIYLS QVLRLFIWIE SKVDTLPVES LVSIFENSQF SGSEEIDSVD
910 920 930 940 950
NIKIDTLLDS TTDDNVSIAC KFLILASKYS VSDQKFTDIA GTVRASYWYN
960 970 980 990 1000
IGISELTAFI TLKEPQYRDA AIFAFKKSIQ LQSNTSETWI GLGIATMDIN
1010 1020 1030 1040 1050
FRVSQHCFIK ATALEPKATN TWFNLAMLGL KKKDTEFAQQ VLNKLQSLAP
1060 1070 1080 1090 1100
QDSSPWLGMA LILEEQGDII GSSKLFAHSF ILSNGRSKAA QFMYAKNVLE
1110 1120 1130 1140 1150
NHINNGDDER DIETVEKLTT ASIALEQFFK KSPDSQFALQ CALLTLERLH
1160 1170 1180 1190 1200
HYENANELAN RLIGILEKKF EKTQDERELF NFAIIKGQFA RIHLGLGNFE
1210 1220 1230 1240 1250
LSIENADLSQ GIISESSDEK SMKTKISNHI CLGLSYFFLN DFDQTLNQFQ
1260 1270 1280 1290 1300
ELLSISKDSK HLVVLIAKVL YDVGESDTKE IALQELTEYI ATSGADLLVT
1310 1320 1330 1340 1350
LTIAAMSILD DKREDLSIIL EELKALPLSK QIIDKHKDAP YLIEEITKRL
1360 1370 1380 1390 1400
YRNDTGKQVW QRSAYFFPNN LKVWERLDKN IQRRIASNGQ NKVTAEEMSK
1410 1420 1430
LYCESKNLRS IQRGMFLCPW NVTAVKALNE CF
Length:1,432
Mass (Da):163,726
Last modified:May 15, 2002 - v2
Checksum:i18FFF78D7CA5A6E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti985 – 9851T → I in AAA50573 (PubMed:2660461).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36940 Genomic DNA. Translation: AAA50573.1.
U25841 Genomic DNA. Translation: AAB64618.1.
BK006949 Genomic DNA. Translation: DAA11605.1.
PIRiS58819.
RefSeqiNP_015515.1. NM_001184286.1.

Genome annotation databases

EnsemblFungiiYPR189W; YPR189W; YPR189W.
GeneIDi856319.
KEGGisce:YPR189W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36940 Genomic DNA. Translation: AAA50573.1.
U25841 Genomic DNA. Translation: AAB64618.1.
BK006949 Genomic DNA. Translation: DAA11605.1.
PIRiS58819.
RefSeqiNP_015515.1. NM_001184286.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BUJX-ray3.70B/F1-1432[»]
ProteinModelPortaliP17883.
SMRiP17883. Positions 1-38, 61-91, 640-798, 1036-1081, 1138-1165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36361. 128 interactions.
DIPiDIP-6379N.
IntActiP17883. 40 interactions.
MINTiMINT-643301.

Proteomic databases

MaxQBiP17883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR189W; YPR189W; YPR189W.
GeneIDi856319.
KEGGisce:YPR189W.

Organism-specific databases

EuPathDBiFungiDB:YPR189W.
SGDiS000006393. SKI3.

Phylogenomic databases

GeneTreeiENSGT00390000016407.
HOGENOMiHOG000247860.
InParanoidiP17883.
KOiK12600.
OMAiFIKATAL.
OrthoDBiEOG747PS9.

Enzyme and pathway databases

BioCyciYEAST:G3O-34312-MONOMER.

Miscellaneous databases

PROiP17883.

Family and domain databases

Gene3Di1.25.40.10. 6 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and nuclear localization signal of the SKI3 antiviral protein of Saccharomyces cerevisiae."
    Rhee S.-K., Icho T., Wickner R.B.
    Yeast 5:149-158(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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. "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.
  5. "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.
  6. "A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
    Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
    Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS TPR REPEATS.
  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. "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, IDENTIFICATION IN THE SKI COMPLEX, SUBCELLULAR LOCATION.
  11. "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: INTERACTION WITH SKI7, FUNCTION OF THE SKI COMPLEX.
  12. "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.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "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.
  16. Cited for: MODELING OF THE SKI COMPLEX 3D-STRUCTURE.

Entry informationi

Entry nameiSKI3_YEAST
AccessioniPrimary (citable) accession number: P17883
Secondary accession number(s): Q06585
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 15, 2002
Last modified: July 6, 2016
This is version 160 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 11900 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.