ESC2_YEAST
ID ESC2_YEAST Reviewed; 456 AA.
AC Q06340; D6VSZ1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein ESC2;
DE AltName: Full=Establishes silent chromatin protein 2;
GN Name=ESC2; OrderedLocusNames=YDR363W;
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=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 [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, AND SUBCELLULAR LOCATION.
RX PubMed=11090616; DOI=10.1016/s1097-2765(00)00076-9;
RA Dhillon N., Kamakaka R.T.;
RT "A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate
RT silencing at HMR.";
RL Mol. Cell 6:769-780(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH SIR2.
RX PubMed=12399377; DOI=10.1093/genetics/162.2.633;
RA Cuperus G., Shore D.;
RT "Restoration of silencing in Saccharomyces cerevisiae by tethering of a
RT novel Sir2-interacting protein, Esc8.";
RL Genetics 162:633-645(2002).
RN [5]
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 [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP DOMAIN.
RX PubMed=15698469; DOI=10.1186/1471-2105-6-22;
RA Novatchkova M., Bachmair A., Eisenhaber B., Eisenhaber F.;
RT "Proteins with two SUMO-like domains in chromatin-associated complexes: the
RT RENi (Rad60-Esc2-NIP45) family.";
RL BMC Bioinformatics 6:22-22(2005).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-125 AND SER-126, AND
RP 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 [10]
RP IDENTIFICATION IN A COMPLEX WITH RTT101 AND MMS1.
RX PubMed=20139071; DOI=10.1074/jbc.m109.082107;
RA Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C.,
RA Kamura T.;
RT "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage
RT response and transcriptional silencing.";
RL J. Biol. Chem. 285:9858-9867(2010).
CC -!- FUNCTION: May be a substrate targeting component of a cullin-RING-based
CC E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR
CC and telomere silencing via the recruitment or stabilizing of the SIR
CC (silent information regulators) complex. {ECO:0000269|PubMed:11090616,
CC ECO:0000269|PubMed:12399377}.
CC -!- SUBUNIT: Component of a cullin-RING ligase (CRL)-like complex composed
CC of at least the cullin RTT101, a linker protein MMS1, and the potential
CC substrate receptor ESC2. Interacts with RTT101 and MMS1. Interacts with
CC SIR2. {ECO:0000269|PubMed:12399377, ECO:0000269|PubMed:20139071}.
CC -!- INTERACTION:
CC Q06340; Q06211: MMS1; NbExp=5; IntAct=EBI-33799, EBI-38894;
CC Q06340; P47050: RTT101; NbExp=4; IntAct=EBI-33799, EBI-25861;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The 2 SUMO-like regions, although related to ubiquitin domains
CC lack the conserved acceptor Gly residue in position 456.
CC {ECO:0000269|PubMed:15698469}.
CC -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28372; AAB64797.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12201.1; -; Genomic_DNA.
DR PIR; S61158; S61158.
DR RefSeq; NP_010650.1; NM_001180671.1.
DR AlphaFoldDB; Q06340; -.
DR BioGRID; 32418; 274.
DR ComplexPortal; CPX-1166; CUL8-MMS1-ESC2 E3 ubiquitin ligase complex.
DR DIP; DIP-5219N; -.
DR IntAct; Q06340; 4.
DR STRING; 4932.YDR363W; -.
DR iPTMnet; Q06340; -.
DR MaxQB; Q06340; -.
DR PaxDb; Q06340; -.
DR PRIDE; Q06340; -.
DR EnsemblFungi; YDR363W_mRNA; YDR363W; YDR363W.
DR GeneID; 851965; -.
DR KEGG; sce:YDR363W; -.
DR SGD; S000002771; ESC2.
DR VEuPathDB; FungiDB:YDR363W; -.
DR eggNOG; ENOG502QS09; Eukaryota.
DR HOGENOM; CLU_048318_0_0_1; -.
DR InParanoid; Q06340; -.
DR OMA; FENEVTN; -.
DR BioCyc; YEAST:G3O-29913-MON; -.
DR PRO; PR:Q06340; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06340; protein.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..456
FT /note="Protein ESC2"
FT /id="PRO_0000227693"
FT REPEAT 169..287
FT /note="SUMO-like region 1"
FT REPEAT 380..456
FT /note="SUMO-like region 2"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..360
FT /evidence="ECO:0000255"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 456 AA; 52542 MW; F691FB73ED2FAF15 CRC64;
MTGDSRSISE PSINLDPDNT SFSDENSDDF FMDNSYDIDE IDHSDESNRQ SVIVDSKVTV
PPSKHSTLTL SDSEDSDAKE QHQSLSRSSS KNVNIEDITE PKPDKPSGRT RGRSVMKESV
VEINSSESDL DEDKNFPRSR SRSRSSIRSI SPAGKYKRQK SSLLYTYDEN DDFFKELAKE
AKKSTTISKE STPDQRKRVY NIKFLSKLEG TINKAVQVKV LGKYEFSKIL PAALDGLMKS
YKIPKVMKDI YKVENVTLYW NNAKLLTFMT CNSLHIPQDF ENEVSDIDVT IVSKEYEKNF
EATLESKLKE EEAALLIKER QEMERKLEKK RNEQEESEYR EFESELKNVE ETQEIKENDT
VMNTKLLQEG GSLSGNSSSM EEVMRIALMG QDNKKIYVHV RRSTPFSKIA EYYRIQKQLP
QKTRVKLLFD HDELDMNECI ADQDMEDEDM VDVIID
