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UniProtKB/Swiss-Prot entry P11978


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SIR4_YEAST
Primary accession number P11978
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 85)
Name and origin of the protein
Protein name Regulatory protein SIR4
Synonym Silent information regulator 4
Gene name
Name: SIR4
Synonyms: ASD1, STE9, UTH2
OrderedLocusNames: YDR227W
ORFNames: YD9934.12
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3325825 [NCBI, ExPASy, EBI, Israel, Japan]
Marshall M., Mahoney D., Rose A., Hicks J.B., Broach J.R.;
"Functional domains of SIR4, a gene required for position effect regulation in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 7:4441-4452(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/23.3.507; PubMed=7885847 [NCBI, ExPASy, EBI, Israel, Japan]
Davies C.J., Hutchison C.A. III;
"Insertion site specificity of the transposon Tn3.";
Nucleic Acids Res. 23:507-514(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
INTERACTION WITH RIS1.
PubMed=9271422 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Buchman A.R.;
"Identification of a member of a DNA-dependent ATPase family that causes interference with silencing.";
Mol. Cell. Biol. 17:5461-5472(1997).
[5]
REVIEW.
DOI=10.1016/S0378-1119(01)00741-7; PubMed=11722841 [NCBI, ExPASy, EBI, Israel, Japan]
Gasser S.M., Cockell M.M.;
"The molecular biology of the SIR proteins.";
Gene 279:1-16(2001).
[6]
INTERACTION WITH YKU80.
DOI=10.1074/jbc.M306841200; PubMed=14551211 [NCBI, ExPASy, EBI, Israel, Japan]
Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.;
"Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing.";
J. Biol. Chem. 279:86-94(2004).
[7]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1128, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400154-MCP200; PubMed=15542864 [NCBI, ExPASy, EBI, Israel, Japan]
Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P.;
"A proteomic strategy for gaining insights into protein sumoylation in yeast.";
Mol. Cell. Proteomics 4:246-254(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-342; SER-692; SER-709; SER-711; SER-788 AND SER-1134, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1271-1346.
DOI=10.1016/S0969-2126(03)00093-5; PubMed=12791253 [NCBI, ExPASy, EBI, Israel, Japan]
Chang J.F., Hall B.E., Tanny J.C., Moazed D., Filman D., Ellenberger T.;
"Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3.";
Structure 11:637-649(2003).
Comments
  • FUNCTION: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.
  • SUBUNIT: Homodimer. Interacts with RIS1, SIR1, SIR2, SIR3, YKU80 and RAP1 C-terminus.
  • INTERACTION:
    P06701:SIR3; NbExp=3; IntAct=EBI-17237, EBI-17230;
    Q04437:YKU80; NbExp=1; IntAct=EBI-17237, EBI-8224;
  • SUBCELLULAR LOCATION: Nucleus.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M37249; AAA20881.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13239; AAC33144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48612; CAA88507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29360; A29360.
RefSeq NP_010513.1; -.
3D structure databases
PDB
1NYH; X-ray; 3.10 A; A=1198-1358.[ExPASy / RCSB / EBI]
1PL5; X-ray; 2.50 A; A/S=1217-1358.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NYH; -.
1PL5; -.
ModBase P11978.
Protein-protein interaction databases
DIP DIP:33N; -.
IntAct P11978; 9.
Organism-specific databases
CYGD YDR227w; -.
SGD S000002635; SIR4.
Yeast-GFP YDR227W.
Gene expression databases
ArrayExpress P11978; -.
GermOnline YDR227W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005677; Cellular component: chromatin silencing complex (inferred from direct assay from SGD).
GO:0000783; Cellular component: nuclear telomere cap complex (inferred from direct assay from SGD).
GO:0005724; Cellular component: nuclear telomeric heterochromatin (inferred from direct assay from SGD).
GO:0003690; Molecular function: double-stranded DNA binding (inferred from direct assay from SGD).
GO:0042393; Molecular function: histone binding (traceable author statement from SGD).
GO:0031491; Molecular function: nucleosome binding (inferred from direct assay from SGD).
GO:0030527; Molecular function: structural constituent of chromatin (traceable author statement from SGD).
GO:0006342; Biological process: chromatin silencing (traceable author statement from SGD).
GO:0006303; Biological process: double-strand break repair via nonhomologous end joining (inferred from direct assay from SGD).
GO:0001308; Biological process: loss of chromatin silencing during replicative cell aging (inferred from direct assay from SGD).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Proteomic databases
PeptideAtlas P11978; -.
Genome annotation databases
Ensembl YDR227W; Saccharomyces cerevisiae. [Contig view]
GeneID 851813; -.
GenomeReviews Z71256_GR; YDR227W.
KEGG sce:YDR227W; -.
NMPDR fig|4932.3.peg.1270; -.
Phylogenomic databases
HOGENOM P11978; -.
OMA P11978; TNDICSV.
Other
NextBio 969671; -.
ProtoNet P11978.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Coiled coil; Complete proteome; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Repressor; Transcription; Transcription regulation; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1358  1358     Regulatory protein SIR4. PRO_0000097769
COILED   1271   1347  77      
MOD_RES   62     62        Phosphothreonine. 
MOD_RES   274    274        Phosphoserine. 
MOD_RES   342    342        Phosphoserine. 
MOD_RES   692    692        Phosphoserine. 
MOD_RES   709    709        Phosphoserine. 
MOD_RES   711    711        Phosphoserine. 
MOD_RES   788    788        Phosphoserine. 
MOD_RES   1134   1134        Phosphoserine. 
CROSSLNK   1128   1128        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO). 
VARIANT   994    994  1     P -> L. 
HELIX   1273   1343  71      
Sequence information
Length: 1358 AA [This is the length of the unprocessed precursor] Molecular weight: 152062 Da [This is the MW of the unprocessed precursor] CRC64: 9C698765964F094E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPNDNKTPNR SSTPKFTKKP VTPNDKIPER EEKSNEVKTP KIPLFTFAKS KNYSRPSTAI 

        70         80         90        100        110        120 
HTSPHQPSDV KPTSHKQLQQ PKSSPLKKNN YNSFPHSNLE KISNSKLLSL LRSKTSAGRI 

       130        140        150        160        170        180 
ESNNPSHDAS RSLASFEQTA FSRHAQQQTS TFNSKPVRTI VPISTSQTNN SFLSGVKSLL 

       190        200        210        220        230        240 
SEEKIRDYSK EILGINLANE QPVLEKPLKK GSADIGASVI SLTKDKSIRK DTVEEKKEEK 

       250        260        270        280        290        300 
LNIGKNFAHS DSLSVPKVSA GDSGISPEES KARSPGIAKP NAIQTEVYGI NEESTNERLE 

       310        320        330        340        350        360 
INQEKPVKLD ENSANSTVAS ALDTNGTSAT TETLTSKKIV PSPKKVAIDQ DKITLHDEKT 

       370        380        390        400        410        420 
LAPSKHQPIT SEQKMKEDAD LKRMEILKSP HLSKSPADRP QGRRNSRNFS TRDEETTKLA 

       430        440        450        460        470        480 
FLVEYEGQEN NYNSTSRSTE KKNDMNTSAK NKNGENKKIG KRPPEIMSTE AHVNKVTEET 

       490        500        510        520        530        540 
TKQIQSVRID GRKVLQKVQG ESHIDSRNNT LNVTPSKRPQ LGEIPNPMKK HKPNEGRTPN 

       550        560        570        580        590        600 
ISNGTINIQK KLEPKEIVRD ILHTKESSNE AKKTIQNPLN KSQNTALPST HKVTQKKDIK 

       610        620        630        640        650        660 
IGTNDLFQVE SAPKISSEID RENVKSKDEP VSKAVESKSL LNLFSNVLKA PFIKSESKPF 

       670        680        690        700        710        720 
SSDALSKEKA NFLETIASTE KPENKTDKVS LSQPVSASKH EYSDNFPVSL SQPSKKSFAN 

       730        740        750        760        770        780 
HTEDEQIEKK KICRGRMNTI ITHPGKMELV YVSDSDDSSS DNDSLTDLES LSSGESNEIK 

       790        800        810        820        830        840 
VTNDLDTSAE KDQIQAGKWF DPVLDWRKSD RELTKNILWR IADKTTYDKE TITDLIEQGI 

       850        860        870        880        890        900 
PKHSYLSGNP LTSVTNDICS VENYETSSAF FYQQVHKKDR LQYLPLYAVS TFENTNNTEK 

       910        920        930        940        950        960 
NDVTNKNINI GKHSQEQNSS SAKPSQIPTV SSPLGFEETK LSTTPTKSNR RVSHSDTNSS 

       970        980        990       1000       1010       1020 
KPKNTKENLS KSSWRQEWLA NLKLISVSLV DEFPSELSDS DRQIINEKMQ LLKDIFANNL 

      1030       1040       1050       1060       1070       1080 
KSAISNNFRE SDIIILKGEI EDYPMSSEIK IYYNELQNKP DAKKARFWSF MKTQRFVSNM 

      1090       1100       1110       1120       1130       1140 
GFDIQKSCEP VSISTSVKPH VVEPEHMADA KIMPKDILQI TKKPLMVKNV KPSSPPDVKS 

      1150       1160       1170       1180       1190       1200 
LVQLSTMETK TLPEKKQFDS IFNSNKAKII PGNGKHASEN ISLSFSRPAS YGYFSVGKRV 

      1210       1220       1230       1240       1250       1260 
PIVEDRRVKQ LDDITDSNTT EILTSVDVLG THSQTGTQQS NMYTSTQKTE LEIDNKDSVT 

      1270       1280       1290       1300       1310       1320 
ECSKDMKEDG LSFVDIVLSK AASALDEKEK QLAVANEIIR SLSDEVMRNE IRITSLQGDL 

      1330       1340       1350 
TFTKKCLENA RSQISEKDAK INKLMEKDFQ VNKEIKPY 

P11978 in FASTA format

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