ID   SIR4_YEAST              Reviewed;        1358 AA.
AC   P11978; D6VSK9;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   14-DEC-2011, entry version 111.
DE   RecName: Full=Regulatory protein SIR4;
DE   AltName: Full=Silent information regulator 4;
GN   Name=SIR4; Synonyms=ASD1, STE9, UTH2; OrderedLocusNames=YDR227W;
GN   ORFNames=YD9934.12;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88142836; PubMed=3325825;
RA   Marshall M., Mahoney D., Rose A., Hicks J.B., Broach J.R.;
RT   "Functional domains of SIR4, a gene required for position effect
RT   regulation in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 7:4441-4452(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95192063; PubMed=7885847; DOI=10.1093/nar/23.3.507;
RA   Davies C.J., Hutchison C.A. III;
RT   "Insertion site specificity of the transposon Tn3.";
RL   Nucleic Acids Res. 23:507-514(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH RIS1.
RX   PubMed=9271422;
RA   Zhang Z., Buchman A.R.;
RT   "Identification of a member of a DNA-dependent ATPase family that
RT   causes interference with silencing.";
RL   Mol. Cell. Biol. 17:5461-5472(1997).
RN   [6]
RP   REVIEW.
RX   MEDLINE=21579783; PubMed=11722841; DOI=10.1016/S0378-1119(01)00741-7;
RA   Gasser S.M., Cockell M.M.;
RT   "The molecular biology of the SIR proteins.";
RL   Gene 279:1-16(2001).
RN   [7]
RP   INTERACTION WITH YKU80.
RX   PubMed=14551211; DOI=10.1074/jbc.M306841200;
RA   Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.;
RT   "Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p
RT   interaction involved in telomeric silencing.";
RL   J. Biol. Chem. 279:86-94(2004).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1128, AND MASS SPECTROMETRY.
RX   PubMed=15542864; DOI=10.1074/mcp.M400154-MCP200;
RA   Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA   Gygi S.P.;
RT   "A proteomic strategy for gaining insights into protein sumoylation in
RT   yeast.";
RL   Mol. Cell. Proteomics 4:246-254(2005).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH MPS3.
RX   PubMed=18039933; DOI=10.1083/jcb.200706040;
RA   Bupp J.M., Martin A.E., Stensrud E.S., Jaspersen S.L.;
RT   "Telomere anchoring at the nuclear periphery requires the budding
RT   yeast Sad1-UNC-84 domain protein Mps3.";
RL   J. Cell Biol. 179:845-854(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-342; SER-692;
RP   SER-709; SER-711; SER-788 AND SER-1134, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1271-1346.
RX   MEDLINE=22677440; PubMed=12791253; DOI=10.1016/S0969-2126(03)00093-5;
RA   Chang J.F., Hall B.E., Tanny J.C., Moazed D., Filman D.,
RA   Ellenberger T.;
RT   "Structure of the coiled-coil dimerization motif of Sir4 and its
RT   interaction with Sir3.";
RL   Structure 11:637-649(2003).
CC   -!- FUNCTION: The proteins SIR1 through SIR4 are required for
CC       transcriptional repression of the silent mating type loci, HML and
CC       HMR. The proteins SIR2 through SIR4 repress mulitple loci by
CC       modulating chromatin structure. Involves the compaction of
CC       chromatin fiber into a more condensed form.
CC   -!- SUBUNIT: Homodimer. Interacts with MPS3, RIS1, SIR1, SIR2, SIR3,
CC       YKU80 and RAP1 C-terminus.
CC   -!- INTERACTION:
CC       P11938:RAP1; NbExp=2; IntAct=EBI-17237, EBI-14821;
CC       P06700:SIR2; NbExp=7; IntAct=EBI-17237, EBI-17219;
CC       P06701:SIR3; NbExp=7; IntAct=EBI-17237, EBI-17230;
CC       Q04437:YKU80; NbExp=2; IntAct=EBI-17237, EBI-8224;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; M37249; AAA20881.1; -; Genomic_DNA.
DR   EMBL; U13239; AAC33144.1; -; Genomic_DNA.
DR   EMBL; Z48612; CAA88507.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12069.1; -; Genomic_DNA.
DR   PIR; A29360; A29360.
DR   RefSeq; NP_010513.1; NM_001180535.1.
DR   PDB; 1NYH; X-ray; 3.10 A; A=1198-1358.
DR   PDB; 1PL5; X-ray; 2.50 A; A/S=1217-1358.
DR   PDBsum; 1NYH; -.
DR   PDBsum; 1PL5; -.
DR   ProteinModelPortal; P11978; -.
DR   SMR; P11978; 1271-1346.
DR   DIP; DIP-33N; -.
DR   IntAct; P11978; 11.
DR   MINT; MINT-622754; -.
DR   STRING; P11978; -.
DR   PeptideAtlas; P11978; -.
DR   EnsemblFungi; YDR227W; YDR227W; YDR227W.
DR   GeneID; 851813; -.
DR   KEGG; sce:YDR227W; -.
DR   NMPDR; fig|4932.3.peg.1270; -.
DR   CYGD; YDR227w; -.
DR   SGD; S000002635; SIR4.
DR   eggNOG; fuNOG15539; -.
DR   OMA; TNDICSV; -.
DR   OrthoDB; EOG47WRZJ; -.
DR   NextBio; 969671; -.
DR   ArrayExpress; P11978; -.
DR   Genevestigator; P11978; -.
DR   GermOnline; YDR227W; Saccharomyces cerevisiae.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:SGD.
DR   GO; GO:0000783; C:nuclear telomere cap complex; IDA:SGD.
DR   GO; GO:0005724; C:nuclear telomeric heterochromatin; IDA:SGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR   GO; GO:0042393; F:histone binding; TAS:SGD.
DR   GO; GO:0031491; F:nucleosome binding; IDA:SGD.
DR   GO; GO:0030527; F:structural constituent of chromatin; TAS:SGD.
DR   GO; GO:0006342; P:chromatin silencing; TAS:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:SGD.
DR   GO; GO:0001308; P:negative regulation of chromatin silencing involved in replicative cell aging; IDA:SGD.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   KO; K11123; -.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Complete proteome; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1358       Regulatory protein SIR4.
FT                                /FTId=PRO_0000097769.
FT   COILED     1271   1347
FT   MOD_RES      62     62       Phosphothreonine.
FT   MOD_RES     274    274       Phosphoserine.
FT   MOD_RES     342    342       Phosphoserine.
FT   MOD_RES     692    692       Phosphoserine.
FT   MOD_RES     709    709       Phosphoserine.
FT   MOD_RES     711    711       Phosphoserine.
FT   MOD_RES     788    788       Phosphoserine.
FT   MOD_RES    1134   1134       Phosphoserine.
FT   CROSSLNK   1128   1128       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VARIANT     994    994       P -> L.
FT   HELIX      1273   1343
SQ   SEQUENCE   1358 AA;  152062 MW;  9C698765964F094E CRC64;
     MPNDNKTPNR SSTPKFTKKP VTPNDKIPER EEKSNEVKTP KIPLFTFAKS KNYSRPSTAI
     HTSPHQPSDV KPTSHKQLQQ PKSSPLKKNN YNSFPHSNLE KISNSKLLSL LRSKTSAGRI
     ESNNPSHDAS RSLASFEQTA FSRHAQQQTS TFNSKPVRTI VPISTSQTNN SFLSGVKSLL
     SEEKIRDYSK EILGINLANE QPVLEKPLKK GSADIGASVI SLTKDKSIRK DTVEEKKEEK
     LNIGKNFAHS DSLSVPKVSA GDSGISPEES KARSPGIAKP NAIQTEVYGI NEESTNERLE
     INQEKPVKLD ENSANSTVAS ALDTNGTSAT TETLTSKKIV PSPKKVAIDQ DKITLHDEKT
     LAPSKHQPIT SEQKMKEDAD LKRMEILKSP HLSKSPADRP QGRRNSRNFS TRDEETTKLA
     FLVEYEGQEN NYNSTSRSTE KKNDMNTSAK NKNGENKKIG KRPPEIMSTE AHVNKVTEET
     TKQIQSVRID GRKVLQKVQG ESHIDSRNNT LNVTPSKRPQ LGEIPNPMKK HKPNEGRTPN
     ISNGTINIQK KLEPKEIVRD ILHTKESSNE AKKTIQNPLN KSQNTALPST HKVTQKKDIK
     IGTNDLFQVE SAPKISSEID RENVKSKDEP VSKAVESKSL LNLFSNVLKA PFIKSESKPF
     SSDALSKEKA NFLETIASTE KPENKTDKVS LSQPVSASKH EYSDNFPVSL SQPSKKSFAN
     HTEDEQIEKK KICRGRMNTI ITHPGKMELV YVSDSDDSSS DNDSLTDLES LSSGESNEIK
     VTNDLDTSAE KDQIQAGKWF DPVLDWRKSD RELTKNILWR IADKTTYDKE TITDLIEQGI
     PKHSYLSGNP LTSVTNDICS VENYETSSAF FYQQVHKKDR LQYLPLYAVS TFENTNNTEK
     NDVTNKNINI GKHSQEQNSS SAKPSQIPTV SSPLGFEETK LSTTPTKSNR RVSHSDTNSS
     KPKNTKENLS KSSWRQEWLA NLKLISVSLV DEFPSELSDS DRQIINEKMQ LLKDIFANNL
     KSAISNNFRE SDIIILKGEI EDYPMSSEIK IYYNELQNKP DAKKARFWSF MKTQRFVSNM
     GFDIQKSCEP VSISTSVKPH VVEPEHMADA KIMPKDILQI TKKPLMVKNV KPSSPPDVKS
     LVQLSTMETK TLPEKKQFDS IFNSNKAKII PGNGKHASEN ISLSFSRPAS YGYFSVGKRV
     PIVEDRRVKQ LDDITDSNTT EILTSVDVLG THSQTGTQQS NMYTSTQKTE LEIDNKDSVT
     ECSKDMKEDG LSFVDIVLSK AASALDEKEK QLAVANEIIR SLSDEVMRNE IRITSLQGDL
     TFTKKCLENA RSQISEKDAK INKLMEKDFQ VNKEIKPY
//