SAS10_YEAST
ID SAS10_YEAST Reviewed; 610 AA.
AC Q12136; D6VRJ7; Q05842;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Something about silencing protein 10;
DE AltName: Full=U three protein 3;
DE AltName: Full=U3 small nucleolar RNA-associated protein 3;
DE AltName: Full=U3 snoRNA-associated protein 11;
GN Name=SAS10; Synonyms=UTP3; OrderedLocusNames=YDL153C; ORFNames=D1545;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], OVEREXPRESSION, AND SUBCELLULAR LOCATION.
RX PubMed=9611201; DOI=10.1093/genetics/149.2.903;
RA Kamakaka R.T., Rine J.;
RT "Sir- and silencer-independent disruption of silencing in Saccharomyces by
RT Sas10p.";
RL Genetics 149:903-914(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.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 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX 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., Shabanowitz J.,
RA 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-316; SER-336;
RP SER-339 AND SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-316; SER-336; SER-339
RP AND SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Primarily required at the G2/M phase. Essential for
CC viability: involved in nucleolar processing of pre-18S ribosomal RNA as
CC part of the ribosomal small subunit (SSU) processome.
CC {ECO:0000269|PubMed:12068309}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC the ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3. {ECO:0000269|PubMed:12068309}.
CC -!- INTERACTION:
CC Q12136; Q03532: HAS1; NbExp=2; IntAct=EBI-36084, EBI-8170;
CC Q12136; P20448: HCA4; NbExp=3; IntAct=EBI-36084, EBI-5612;
CC Q12136; P32899: IMP3; NbExp=2; IntAct=EBI-36084, EBI-9237;
CC Q12136; P25586: KRR1; NbExp=3; IntAct=EBI-36084, EBI-21773;
CC Q12136; P47083: MPP10; NbExp=10; IntAct=EBI-36084, EBI-11168;
CC Q12136; Q99207: NOP14; NbExp=3; IntAct=EBI-36084, EBI-35157;
CC Q12136; P53317: NOP19; NbExp=3; IntAct=EBI-36084, EBI-23590;
CC Q12136; Q12481: RRP36; NbExp=2; IntAct=EBI-36084, EBI-31770;
CC Q12136; Q12136: SAS10; NbExp=3; IntAct=EBI-36084, EBI-36084;
CC Q12136; P40498: UTP25; NbExp=7; IntAct=EBI-36084, EBI-25113;
CC Q12136; Q02354: UTP6; NbExp=5; IntAct=EBI-36084, EBI-22119;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:9611201}.
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 at
CC telomeres.
CC -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 EMBL; BK006938; DAA11707.1; -; Genomic_DNA.
DR PIR; S67701; S67701.
DR RefSeq; NP_010128.1; NM_001180213.1.
DR PDB; 5WLC; EM; 3.80 A; NB=1-610.
DR PDB; 6KE6; EM; 3.40 A; 5H=1-610.
DR PDB; 6LQP; EM; 3.20 A; 5H=1-610.
DR PDB; 6LQQ; EM; 4.10 A; 5H=1-610.
DR PDB; 6LQR; EM; 8.60 A; 5H=1-610.
DR PDB; 6LQS; EM; 3.80 A; 5H=1-610.
DR PDB; 6LQT; EM; 4.90 A; 5H=1-610.
DR PDB; 6LQU; EM; 3.70 A; 5H=1-610.
DR PDB; 6LQV; EM; 4.80 A; 5H=1-610.
DR PDB; 6ZQA; EM; 4.40 A; UC=1-610.
DR PDB; 6ZQB; EM; 3.90 A; UC=1-610.
DR PDB; 6ZQC; EM; 3.80 A; UC=1-610.
DR PDB; 6ZQD; EM; 3.80 A; UC=1-610.
DR PDB; 6ZQE; EM; 7.10 A; UC=1-610.
DR PDB; 6ZQF; EM; 4.90 A; UC=1-610.
DR PDB; 6ZQG; EM; 3.50 A; UC=1-610.
DR PDB; 7AJT; EM; 4.60 A; UC=1-610.
DR PDB; 7AJU; EM; 3.80 A; UC=1-610.
DR PDB; 7D4I; EM; 4.00 A; 5H=1-610.
DR PDB; 7D5S; EM; 4.60 A; 5H=1-610.
DR PDB; 7D5T; EM; 6.00 A; 5H=1-610.
DR PDB; 7D63; EM; 12.30 A; 5H=1-610.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q12136; -.
DR SMR; Q12136; -.
DR BioGRID; 31910; 189.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-5047N; -.
DR IntAct; Q12136; 69.
DR MINT; Q12136; -.
DR STRING; 4932.YDL153C; -.
DR iPTMnet; Q12136; -.
DR MaxQB; Q12136; -.
DR PaxDb; Q12136; -.
DR PRIDE; Q12136; -.
DR EnsemblFungi; YDL153C_mRNA; YDL153C; YDL153C.
DR GeneID; 851403; -.
DR KEGG; sce:YDL153C; -.
DR SGD; S000002312; SAS10.
DR VEuPathDB; FungiDB:YDL153C; -.
DR eggNOG; KOG3118; Eukaryota.
DR GeneTree; ENSGT00500000044947; -.
DR HOGENOM; CLU_019106_1_0_1; -.
DR InParanoid; Q12136; -.
DR OMA; AQKANKR; -.
DR BioCyc; YEAST:G3O-29548-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q12136; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12136; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0042802; F:identical 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 tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR InterPro; IPR018972; Sas10_C_dom.
DR PANTHER; PTHR13237; PTHR13237; 1.
DR Pfam; PF09368; Sas10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..610
FT /note="Something about silencing protein 10"
FT /id="PRO_0000114330"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..575
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
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
