ID SAS10_YEAST Reviewed; 610 AA. AC Q12136; Q05842; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 66. DE RecName: Full=Something about silencing protein 10; DE AltName: Full=U3 small nucleolar RNA-associated protein 3; DE AltName: Full=U3 snoRNA-associated protein 11; DE AltName: Full=U three protein 3; GN Name=SAS10; Synonyms=UTP3; OrderedLocusNames=YDL153C; ORFNames=D1545; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], OVEREXPRESSION, AND SUBCELLULAR LOCATION. RX PubMed=9611201; RA Kamakaka R.T., Rine J.; RT "Sir- and silencer-independent disruption of silencing in RT Saccharomyces by Sas10p."; RL Genetics 149:903-914(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97127830; PubMed=8972581; RX DOI=10.1002/(SICI)1097-0061(199612)12:15<1587::AID-YEA46>3.0.CO;2-6; RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.; RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV."; RL Yeast 12:1587-1592(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX MEDLINE=22082292; PubMed=12068309; DOI=10.1038/nature00769; RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M., RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., RA Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.; RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA RT biogenesis."; RL Nature 417:967-970(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND MASS RP SPECTROMETRY. RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-339, AND RP MASS 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-336; SER-339 RP AND SER-477, AND MASS 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-316; SER-336; RP SER-339; SER-477 AND SER-483, 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). CC -!- FUNCTION: Primarily required at the G2/M phase. Essential for CC viability: involved in nucleolar processing of pre-18S ribosomal CC RNA as part of the ribosomal small subunit (SSU) processome. CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component CC of the ribosomal small subunit (SSU) processome composed of at CC least 40 protein subunits and snoRNA U3. CC -!- INTERACTION: CC P38149:-; NbExp=1; IntAct=EBI-36084, EBI-21176; CC P32462:ERG24; NbExp=1; IntAct=EBI-36084, EBI-6502; CC P38225:FAT1; NbExp=1; IntAct=EBI-36084, EBI-6819; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. CC -!- MISCELLANEOUS: When overexpressed, has a role in the structure of CC silenced chromatin. Overproduction causes derepression of gene CC expression at both HML and HMR, as well as at the rDNA locus and CC at telomeres. CC -!- SIMILARITY: Belongs to the SAS10 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U63063; AAB05801.1; -; mRNA. DR EMBL; X97751; CAA66339.1; ALT_INIT; Genomic_DNA. DR EMBL; Z74201; CAA98726.1; -; Genomic_DNA. DR EMBL; AY692844; AAT92863.1; -; Genomic_DNA. DR PIR; S67701; S67701. DR RefSeq; NP_010128.1; -. DR DIP; DIP:5047N; -. DR IntAct; Q12136; 35. DR Ensembl; YDL153C; Saccharomyces cerevisiae. DR GeneID; 851403; -. DR GenomeReviews; Z71256_GR; YDL153C. DR KEGG; sce:YDL153C; -. DR NMPDR; fig|4932.3.peg.865; -. DR CYGD; YDL153c; -. DR SGD; S000002312; SAS10. DR HOGENOM; Q12136; -. DR OMA; Q12136; LRQQKKH. DR NextBio; 968573; -. DR GermOnline; YDL153C; Saccharomyces cerevisiae. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0032040; C:small-subunit processome; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of trici...; IMP:SGD. DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separat...; IMP:SGD. DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature...; IMP:SGD. DR GO; GO:0016458; P:gene silencing; IEA:InterPro. DR InterPro; IPR007146; Sas10/Utp3/C1D. DR InterPro; IPR018972; Sas10_C. DR Pfam; PF04000; Sas10_Utp3; 1. DR Pfam; PF09368; Sas10_Utp3_C; 1. PE 1: Evidence at protein level; KW Cell cycle; Complete proteome; Nucleus; Phosphoprotein; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing. FT CHAIN 1 610 Something about silencing protein 10. FT /FTId=PRO_0000114330. FT COMPBIAS 75 86 Poly-Glu. FT COMPBIAS 167 172 Poly-Glu. FT COMPBIAS 360 365 Poly-Glu. FT MOD_RES 314 314 Phosphoserine. FT MOD_RES 316 316 Phosphoserine. FT MOD_RES 336 336 Phosphoserine. FT MOD_RES 339 339 Phosphoserine. FT MOD_RES 477 477 Phosphoserine. FT MOD_RES 483 483 Phosphoserine. SQ SEQUENCE 610 AA; 70259 MW; 9278BF873834FC7E CRC64; MVRKGSNRTK TSEVGDEINP YGLNEVDDFA SKREKVLLGQ STFGDSNKDD DHSLLEDEDE EEVLAMDEDD ESIDEREDEE EEEEEELDGA AAYKKIFGRN LETDQLPEED EENGMLDNEN AWGSTKGEYY GADDLDDDEA AKEIEKEALR QQKKHLEELN MNDYLDEEEE EEWVKSAKEF DMGEFKNSTK QADTKTSITD ILNMDDEARD NYLRTMFPEF APLSKEFTEL APKFDELKKS EENEFNKLKL IALGSYLGTI SCYYSILLHE LHNNEDFTSM KGHPVMEKIL TTKEIWRQAS ELPSSFDVNE GDGSESEETA NIEAFNEKKL NELQNSEDSD AEDGGKQKQE IDEEERESDE EEEEEDVDID DFEEYVAQSR LHSKPKTSSM PEADDFIESE IADVDAQDKK ARRRTLRFYT SKIDQQENKK TDRFKGDDDI PYKERLFERQ QRLLDEARKR GMHDNNGADL DDKDYGSEDE AVSRSINTQG ENDYYQQVQR GKQDKKISRK EAHKNAVIAA REGKLAELAE NVSGDGKRAI NYQILKNKGL TPKRNKDNRN SRVKKRKKYQ KAQKKLKSVR AVYSGGQSGV YEGEKTGIKK GLTRSVKFKN //