Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P35207

- SKI2_YEAST

UniProt

P35207 - SKI2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. RNA binding Source: UniProtKB-KW
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP35207.
KOiK12599.
OMAiVIIMLPD.
OrthoDBiEOG7WT48P.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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

        10         20         30         40         50
MSEGFSSSSI QELYQSLKEI TNNADVELFE DRITKLDFES TDEPKHANDI
60 70 80 90 100
IKDRFLRPSN ALPWSLLDMV QDVPHTSSPE DCSGKLDYKE LLKVPDPINR
110 120 130 140 150
TSYQFKRTGL EGKISGYKEE VDLKEVANAN ASNSLSITRS INHNQNSVRG
160 170 180 190 200
STAQLPFTPG GIPMKSVKTD SEQNGSSTMA NATKLLHKDG QGLFDIPEGM
210 220 230 240 250
NRGIKPMDSP AENEDQNGQF KELKQLNEID NELDIRIEAN EAKLKEEEKS
260 270 280 290 300
AKSISEEIME EATEETTADN ADDAEIDELL PIGIDFGRTK PVSKSVPVKK
310 320 330 340 350
EWAHVVDLNH KIENFDELIP NPARSWPFEL DTFQKEAVYH LEQGDSVFVA
360 370 380 390 400
AHTSAGKTVV AEYAIAMAHR NMTKTIYTSP IKALSNQKFR DFKETFDDVN
410 420 430 440 450
IGLITGDVQI NPDANCLIMT TEILRSMLYR GADLIRDVEF VIFDEVHYVN
460 470 480 490 500
DQDRGVVWEE VIIMLPQHVK FILLSATVPN TYEFANWIGR TKQKNIYVIS
510 520 530 540 550
TPKRPVPLEI NIWAKKELIP VINQNSEFLE ANFRKHKEIL NGESAKGAPS
560 570 580 590 600
KTDNGRGGST ARGGRGGSNT RDGRGGRGNS TRGGANRGGS RGAGAIGSNK
610 620 630 640 650
RKFFTQDGPS KKTWPEIVNY LRKRELLPMV VFVFSKKRCE EYADWLEGIN
660 670 680 690 700
FCNNKEKSQI HMFIEKSITR LKKEDRDLPQ ILKTRSLLER GIAVHHGGLL
710 720 730 740 750
PIVKELIEIL FSKGFIKVLF ATETFAMGLN LPTRTVIFSS IRKHDGNGLR
760 770 780 790 800
ELTPGEFTQM AGRAGRRGLD STGTVIVMAY NSPLSIATFK EVTMGVPTRL
810 820 830 840 850
QSQFRLTYNM ILNLLRIEAL RVEEMIKYSF SENAKETLQP EHEKQIKVLQ
860 870 880 890 900
EELQTIEYKS CEICDNDIEK FLELMLAYKE ATVNLMQEMV KSPSILHILK
910 920 930 940 950
EGRLVAFRDP NDCLKLGFVF KVSLKDAVCV IMTFTKPYKL PNGEPNHLIY
960 970 980 990 1000
FPKADGYRRR NFPKFQKTDF YMEEVPVTAI EVITKRKFAA PLGKVIKKDV
1010 1020 1030 1040 1050
AALNEFNAET NNILDGKTLK EAINIEKQGL KIHQILLDRT NIRDEIFKLK
1060 1070 1080 1090 1100
SIKCPNLSQH IVPKFKAHVI KKKIEELYHL MSDQNLSLLP DYEKRLAVLK
1110 1120 1130 1140 1150
DTEFIDQNHN VLLKGRVACE INSGYELVLT ELILDNFLGS FEPEEIVALL
1160 1170 1180 1190 1200
SVFVYEGKTR EEEPPIVTPR LAKGKQRIEE IYKKMLCVFN THQIPLTQDE
1210 1220 1230 1240 1250
AEFLDRKRFA MMNVVYEWAR GLSFKEIMEM SPEAEGTVVR VITWLDEICR
1260 1270 1280
EVKTASIIIG NSTLHMKMSR AQELIKRDIV FAASLYL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P35207.
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. DEAD/DEAH_box_helicase_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 142 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