ESC1_YEAST
ID ESC1_YEAST Reviewed; 1658 AA.
AC Q03661; D6W044; Q04988;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Silent chromatin protein ESC1;
DE AltName: Full=Establishes silent chromatin protein 1;
GN Name=ESC1; OrderedLocusNames=YMR219W; ORFNames=YM8261.13, YM9959.01;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH SIR4, AND SUBCELLULAR LOCATION.
RX PubMed=12417731; DOI=10.1128/mcb.22.23.8292-8301.2002;
RA Andrulis E.D., Zappulla D.C., Ansari A., Perrod S., Laiosa C.V.,
RA Gartenberg M.R., Sternglanz R.;
RT "Esc1, a nuclear periphery protein required for Sir4-based plasmid
RT anchoring and partitioning.";
RL Mol. Cell. Biol. 22:8292-8301(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP FUNCTION.
RX PubMed=15620354; DOI=10.1016/j.cell.2004.11.008;
RA Gartenberg M.R., Neumann F.R., Laroche T., Blaszczyk M., Gasser S.M.;
RT "Sir-mediated repression can occur independently of chromosomal and
RT subnuclear contexts.";
RL Cell 119:955-967(2004).
RN [6]
RP FUNCTION, INTERACTION WITH SIR4, AND SUBCELLULAR LOCATION.
RX PubMed=15014445; DOI=10.1038/sj.emboj.7600144;
RA Taddei A., Hediger F., Neumann F.R., Bauer C., Gasser S.M.;
RT "Separation of silencing from perinuclear anchoring functions in yeast
RT Ku80, Sir4 and Esc1 proteins.";
RL EMBO J. 23:1301-1312(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-911 AND SER-1326,
RP AND IDENTIFICATION BY 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-500; SER-532; SER-579;
RP SER-662; SER-865; SER-866; SER-888; SER-1166; SER-1254 AND SER-1326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-579; SER-583;
RP SER-608; SER-865; SER-866; SER-888; SER-911; SER-937; SER-1092; SER-1096;
RP SER-1098; SER-1176; SER-1178; SER-1214; SER-1254; SER-1290; SER-1326;
RP SER-1332; SER-1403; SER-1409; SER-1450; SER-1454; SER-1539; SER-1590 AND
RP SER-1591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in the clustering of telomeres at the nuclear
CC periphery, forming discrete subcompartments that accumulate a complex
CC of histone-binding silencing factors like SIR4. Required for SIR4-
CC mediated anchoring and partitioning of plasmids.
CC {ECO:0000269|PubMed:12417731, ECO:0000269|PubMed:15014445,
CC ECO:0000269|PubMed:15620354}.
CC -!- SUBUNIT: Interacts with SIR4. {ECO:0000269|PubMed:12417731,
CC ECO:0000269|PubMed:15014445}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12417731,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15014445}.
CC Note=Concentrated at the nuclear periphery.
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DR EMBL; Z49809; CAA89934.1; -; Genomic_DNA.
DR EMBL; Z49939; CAA90190.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10118.1; -; Genomic_DNA.
DR PIR; S55101; S55101.
DR RefSeq; NP_013946.1; NM_001182726.1.
DR PDB; 6QSZ; X-ray; 2.50 A; B/D/F/H/J/L/N/P=1443-1458.
DR PDBsum; 6QSZ; -.
DR AlphaFoldDB; Q03661; -.
DR SMR; Q03661; -.
DR BioGRID; 35397; 220.
DR DIP; DIP-7971N; -.
DR IntAct; Q03661; 2.
DR MINT; Q03661; -.
DR STRING; 4932.YMR219W; -.
DR iPTMnet; Q03661; -.
DR MaxQB; Q03661; -.
DR PaxDb; Q03661; -.
DR PRIDE; Q03661; -.
DR EnsemblFungi; YMR219W_mRNA; YMR219W; YMR219W.
DR GeneID; 855259; -.
DR KEGG; sce:YMR219W; -.
DR SGD; S000004832; ESC1.
DR VEuPathDB; FungiDB:YMR219W; -.
DR eggNOG; ENOG502SDFK; Eukaryota.
DR HOGENOM; CLU_003498_0_0_1; -.
DR InParanoid; Q03661; -.
DR OMA; HEDSARA; -.
DR BioCyc; YEAST:G3O-32901-MON; -.
DR PRO; PR:Q03661; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03661; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR InterPro; IPR001611; Leu-rich_rpt.
DR PROSITE; PS51450; LRR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1658
FT /note="Silent chromatin protein ESC1"
FT /id="PRO_0000203333"
FT REGION 36..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..951
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1623
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1658 AA; 187138 MW; 3893F968305A757D CRC64;
MSKKKETFTP RANKLKLTTP RRKLKILSSL LDADEDSKMK DQHGYSRVHN DKYRVAKPTQ
HSTLHESISS RRSSHIHNKS LHEDSARALS WVDSLINRGK SILTTLEKED ALFERSLEEE
RQRFQLHDSL MNKYTGNSKS HQRLIDLRKS QYGTDTSFQN NDEIPLDSFI SSPLPDAEDE
SSSNIDSDKD EDLEGKQSLI KDFDLENDEY ELSEEEKNSD GQSSPSIMIL SDEEYAEEGA
LQDVSNDEYA EEEGQVERKN IGQEQANVEN ATQISSSDSS EGQNYSEGVE MELEDDIDVE
SDAEKDESQG AEGTEHSVDF SKYMQPRTDN TKIPVIEKYE SDEHKVHQRY SEDGAFDFGS
VNISVDDESE DEESQAESYS ANAENVYHHN EHELDDKELI EDIESSDSES QSAQESEQGS
EDDFEYKMKN EKSTSEETEN TSESRDQGFA KDAYTKNKVE QQENDEEPEK DDIIRSSLDK
NFHGNNNKSE YSENVLENET DPAIVERENQ INDVEGYDVT GKSVESDLHE HSPDNLYDLA
ARAMLQFQQS RNSNCPQKEE QVSESYLGHS NGSNLSGRSL DESEEQIPLK DFTGENNNNL
KTDRGDLSSS VEIEVEKVSE KKLDGSTEKE LVPLSTDTTI NNSSLGNEDS IYYSLDDADA
ISENLTDVPL MEIKTTPKYE VVISESVYSS TSYEDNTVAM PPQVEYTSPF MNDPFNSLND
DYEKKHDLLK STLAALAPAF TKKDAEFVEA GVTKSCLTST SGHTNIFHTS KETKQVSDLD
ESTENVTFEN ENTGDENKNQ SKNFPGVANS TDKSTEDNTD EKYFSAINYT NVTGDSSCED
IIETASNVEE NLRYCEKDMN EAEMSSGDEC VKQNDDGSKT QISFSTDSPD NFQESNDNTE
FSSTKYKVRN SDLEDDESLK KELTKAEVVD KLDEEESEDS YEQDYADPEP GNDEGSNENI
VKGTKKDTLG IVEPENEKVN KVHEEETLFE ANVSSSVNVQ NKDMHTDVIN QEAQANYEAG
ERKYYIQNTD TEEAHISIIE RIDENAIGNN MEIPERSCVE KTHNEVLFER RATTIENTKA
LENNTNMHDQ VSQACSDSDR DQDSTAEKNV EGSAKHNLDI RVSSSEIESV EPLKPESDRS
NIFSSPIRVI GAVVKGVGKV VDVAESFVKK IDVMDSESDD NVDIGDYNQD IFNKSNSTDA
SVNMKSVSSK ERDSDEDEAV ILGGVTAEAH NDNGNNSRVI NIDPTTNGAY EEDSEVFRQQ
VKDKENLHKS EEPLVEGLQS EQHFEKKDHS ENEEEFDTIY GDITSANIHS NAPDDIKRQQ
LLKNLSDLEN YSQRLIEDSR RGKNQEESDE VNTSRERDLT FEKSVNEKYA GAIEEDTFSE
LDISIQHPEH EEDLDLSNNQ ERSIEELNSE PEEAELYELE IEGPTETAAS SKMNDDERQR
GNIPSTDLPS DPPSDKEEVT DSYPYSNSEN ITAEKSAPTS PEVYEIFSDT PNEVPMEIND
EIPATTLEKH DKTNVTSVLD DRSEHLSSHD VDNEPHDNSI NIKVNEGEEP EHQAVDIPVK
VEVKEEQEEM PSKSVLEEQK PSMELINDKS SPENNNDEET NREKDKTKAK KKSRKRNYNS
RRRKRKITEG SSAASNTKRR RGHEPKSRGQ NTHPSVDK
