PLM2_YEAST
ID PLM2_YEAST Reviewed; 521 AA.
AC Q04383; D6VTC3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein PLM2;
DE AltName: Full=Plasmid maintenance protein 2;
GN Name=PLM2; OrderedLocusNames=YDR501W;
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 INDUCTION.
RX PubMed=11206552; DOI=10.1038/35054095;
RA Iyer V.R., Horak C.E., Scafe C.S., Botstein D., Snyder M., Brown P.O.;
RT "Genomic binding sites of the yeast cell-cycle transcription factors SBF
RT and MBF.";
RL Nature 409:533-538(2001).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=12464632; DOI=10.1101/gad.1039602;
RA Horak C.E., Luscombe N.M., Qian J., Bertone P., Piccirrillo S.,
RA Gerstein M., Snyder M.;
RT "Complex transcriptional circuitry at the G1/S transition in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 16:3017-3033(2002).
RN [5]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [6]
RP INDUCTION.
RX PubMed=15965243; DOI=10.1534/genetics.105.044560;
RA Bean J.M., Siggia E.D., Cross F.R.;
RT "High functional overlap between MluI cell-cycle box binding factor and
RT Swi4/6 cell-cycle box binding factor in the G1/S transcriptional program in
RT Saccharomyces cerevisiae.";
RL Genetics 171:49-61(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-295; SER-302 AND
RP SER-384, AND 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).
CC -!- FUNCTION: Binds to the promoters of genes with functions important for
CC the G1/S (start) transition; primarily genes involved in DNA synthesis
CC and repair, chromosome segregation, nuclear division and transcription.
CC {ECO:0000269|PubMed:12464632}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Regulated in a cell cycle-dependent manner, peaking in G1
CC phase. Negatively regulated by transcription factor SBF (SWI4-SWI6
CC cell-cycle box binding factor). {ECO:0000269|PubMed:11206552,
CC ECO:0000269|PubMed:12464632, ECO:0000269|PubMed:15965243}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- SIMILARITY: Belongs to the PLM2/TOS4 family. {ECO:0000305}.
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DR EMBL; U33057; AAB64943.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12333.1; -; Genomic_DNA.
DR PIR; S69559; S69559.
DR RefSeq; NP_010789.1; NM_001180809.1.
DR AlphaFoldDB; Q04383; -.
DR BioGRID; 32552; 96.
DR DIP; DIP-8546N; -.
DR IntAct; Q04383; 31.
DR MINT; Q04383; -.
DR STRING; 4932.YDR501W; -.
DR iPTMnet; Q04383; -.
DR MaxQB; Q04383; -.
DR PaxDb; Q04383; -.
DR PRIDE; Q04383; -.
DR EnsemblFungi; YDR501W_mRNA; YDR501W; YDR501W.
DR GeneID; 852112; -.
DR KEGG; sce:YDR501W; -.
DR SGD; S000002909; PLM2.
DR VEuPathDB; FungiDB:YDR501W; -.
DR eggNOG; ENOG502RZJP; Eukaryota.
DR GeneTree; ENSGT00940000176669; -.
DR HOGENOM; CLU_027153_0_0_1; -.
DR InParanoid; Q04383; -.
DR OMA; KCIGVIY; -.
DR BioCyc; YEAST:G3O-30024-MON; -.
DR PRO; PR:Q04383; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04383; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..521
FT /note="Protein PLM2"
FT /id="PRO_0000262747"
FT DOMAIN 102..156
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 521 AA; 58202 MW; 3A07FBED570FA9F7 CRC64;
MSHLFPPSSP VAGKPLESPQ KEPGKLANTS VLTLGRKRYN YELEEYPTPD PSSSIGRQSS
PVKDITSRLN ETKSALSSPS KQEKVLAGPI EIELDASDPS RLAIGRKKSV CNIILPCRKN
ISRQHAFISY AADRNEIKLE CNGTNGLSVH LPYSMQLHLV KPFPTRNFYK LVAEEPLTSQ
NTKQSHGKTL QKNQNFISFV LAKGETVTFP YIQGSFINFT GVTVCLSLKK VAPYPGDGNN
NFDEENSTET EDELCLLTTT SDDFSWQKET PSMKFVPVEH SPRTEQISKP LLIASPALVK
NSPISYRTTP QTSFVINQPS TPKKLKRKSI SLKNNTIQET PLPKDKIIGT LSASTRSGGI
NEEESFAAVA KKTKELSSTT AIVSPAQKRL KTSLNIIPEI SRSLSERGIR FDDLVHVLCN
HLAFSNLQQT PLSQLQNINS NTSQLSKDEL KKVLETISCI GIIVREGKDA SGKPLEDEYY
YDVENDDSDE RKILYNSLKG RSRLRSCRKK HKQYFWKRPT K
