SUM1_YEAST
ID SUM1_YEAST Reviewed; 1062 AA.
AC P46676; D6VST9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Suppressor of mar1-1 protein;
DE Short=SUM1-1 protein;
GN Name=SUM1; OrderedLocusNames=YDR310C; ORFNames=D9740.19;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-988.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8754829; DOI=10.1128/mcb.16.8.4281;
RA Chi M.-H., Shore D.;
RT "SUM1-1, a dominant suppressor of SIR mutations in Saccharomyces
RT cerevisiae, increases transcriptional silencing at telomeres and HM mating-
RT type loci and decreases chromosome stability.";
RL Mol. Cell. Biol. 16:4281-4294(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=10562556; DOI=10.1093/emboj/18.22.6448;
RA Xie J., Pierce M., Gailus-Durner V., Wagner M., Winter E., Vershon A.K.;
RT "Sum1 and Hst1 repress middle sporulation-specific gene expression during
RT mitosis in Saccharomyces cerevisiae.";
RL EMBO J. 18:6448-6454(1999).
RN [5]
RP INTERACTION WITH RFM1.
RX PubMed=12612074; DOI=10.1128/mcb.23.6.2009-2016.2003;
RA McCord R., Pierce M., Xie J., Wonkatal S., Mickel C., Vershon A.K.;
RT "Rfm1, a novel tethering factor required to recruit the hst1 histone
RT deacetylase for repression of middle sporulation genes.";
RL Mol. Cell. Biol. 23:2009-2016(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, 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-628; SER-681; THR-697;
RP SER-738 AND THR-817, 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-378; SER-379; SER-628;
RP THR-697; SER-712; SER-738 AND THR-817, AND IDENTIFICATION BY MASS
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: DNA-binding protein that specifically binds the regulatory
CC region of middle sporulation genes (MSE). Required for the repression
CC of middle sporulation genes during vegetative growth. Represses
CC expression via the recruitment of histone deacetylase HST1.
CC {ECO:0000269|PubMed:10562556}.
CC -!- SUBUNIT: Interacts with RFM1. This interaction is required to recruit
CC HST1. {ECO:0000269|PubMed:12612074}.
CC -!- INTERACTION:
CC P46676; P38074: HMT1; NbExp=2; IntAct=EBI-18547, EBI-8394;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8754829}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U34832; AAB38222.1; -; Genomic_DNA.
DR EMBL; U28374; AAB64746.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12149.1; -; Genomic_DNA.
DR PIR; S61196; S61196.
DR RefSeq; NP_010596.1; NM_001180618.1.
DR AlphaFoldDB; P46676; -.
DR SMR; P46676; -.
DR BioGRID; 32363; 524.
DR ComplexPortal; CPX-1384; SUM1-RFM1-HST1 histone deacetylase complex.
DR DIP; DIP-6438N; -.
DR IntAct; P46676; 21.
DR MINT; P46676; -.
DR STRING; 4932.YDR310C; -.
DR iPTMnet; P46676; -.
DR MaxQB; P46676; -.
DR PaxDb; P46676; -.
DR PRIDE; P46676; -.
DR EnsemblFungi; YDR310C_mRNA; YDR310C; YDR310C.
DR GeneID; 851905; -.
DR KEGG; sce:YDR310C; -.
DR SGD; S000002718; SUM1.
DR VEuPathDB; FungiDB:YDR310C; -.
DR eggNOG; ENOG502QTPX; Eukaryota.
DR HOGENOM; CLU_012589_0_0_1; -.
DR InParanoid; P46676; -.
DR OMA; FALFEFW; -.
DR BioCyc; YEAST:G3O-29869-MON; -.
DR PRO; PR:P46676; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P46676; protein.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0110029; P:negative regulation of meiosis I; IMP:CACAO.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR GO; GO:0043937; P:regulation of sporulation; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Sporulation; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1062
FT /note="Suppressor of mar1-1 protein"
FT /id="PRO_0000072311"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 697
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 712
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 817
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 988
FT /note="T->I: Loss of function."
FT /evidence="ECO:0000269|PubMed:8754829"
FT CONFLICT 1..20
FT /note="MSENTTAPSDNITNEQRLPS -> MNRDFRL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="A -> R (in Ref. 1; AAB38222)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="A -> G (in Ref. 1; AAB38222)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="Missing (in Ref. 1; AAB38222)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="G -> A (in Ref. 1; AAB38222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1062 AA; 118201 MW; 08A43263CCCFC1C8 CRC64;
MSENTTAPSD NITNEQRLPS GPKDDVDTLA LTSAQNQANS LRKLDTDANA KALPSITDIP
VSDDSDIKRQ VGSGFGSNPL HIKDSEAFPH SSIEALKEGM DKVTKQCNDL KTALLSKDTS
LTDSVQDLFN SLKVLSHNQS VLENKLDDVM KNQVNTDILV NNLNERLNKL STMLQNTSKV
NHSNLLIENS SNNTSSQHNT SSSRRGPGRP RKDASTSTMN KLVSNAASVN LKSASNQGAP
FSPVNITLPT AVVQTSKSKR YFVEPSTKQE SLLLSAPSSS RDDADMSLTS VPQRTNNENG
KERPSTANSS SITPTPVTPN NLIQIKRKRG RPPKKRTVET MISNSTDTID KSDASNRIKN
EIPINSLLPS SKFHQIPSSP SNPVSQPAPV RTSRSATQEI DIKSLELASL ISTNGDPNAE
DSNTTDTVHN NVEGKVNVEE NKTEKEKIIT IKSSSENSGN NTTNNNNTDN VIKFSANSDI
NSDIRRLMVN DQFSLSYDAS GNITVKLPPV SSPAAATAAA AAAVTSEMNR QQRELDKRRD
SREKMLVNMK YNDRDKAKSF MESNKKLLKA MKEEERRKRM TSIIHDNHLN LNLNEISTRS
KIKSAEKPTT KGSSMSPKPR SASISGISDH QQEGYQPLEQ EKLVDIDNEG SNANSDSLKM
GLTISAADTV HKVGIQSMLN SGEEAITKEN AEYERKTPGD EETTTFVPLE NSQPSDTIRK
RTAGDDGALD QTENTSISPK KRRTEDHTKG EEDEGERGVG NSGTLATVEN VSGDISADLS
KGTSSIHNDT ESANDSSNGN GNLGLGTESR NTLLTATPIE LICREGFFYR RDIPDVPITT
GAYLEFKFKA KEEELINSSI NEEDYAAKSK HEKMNAHFFK PDIQEETELA FEILSKTTLT
EKYVNSLEYF LMEFRWENKL VGLGLKLRES KRTWQRRKAL FALFEFWRDQ SRDKRRFHNY
TILHAVKEME NYRIFINRSV SWFYNHITLL KMILYDLCDN VTTQWREWMF PHNETLPALG
QDGINEDNLN ETIDNMLIFD FLDDGSENNQ VKYSRIIPPD IR
