STB1_YEAST
ID STB1_YEAST Reviewed; 420 AA.
AC P42845; D6W0N6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein STB1;
DE AltName: Full=SIN3-binding protein 1;
GN Name=STB1; OrderedLocusNames=YNL309W; ORFNames=N0384;
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], AND INTERACTION WITH SIN3.
RX PubMed=9393435; DOI=10.1007/s004380050581;
RA Kasten M.M., Stillman D.J.;
RT "Identification of the Saccharomyces cerevisiae genes STB1-STB5 encoding
RT Sin3p binding proteins.";
RL Mol. Gen. Genet. 256:376-386(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7502583; DOI=10.1002/yea.320111109;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT identifies six known genes, a new member of the hexose transporter family
RT and ten new open reading frames.";
RL Yeast 11:1077-1085(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 PROTEIN SEQUENCE OF 249-259, INTERACTION WITH SWI6, AND PHOSPHORYLATION BY
RP CDC28.
RX PubMed=10409718; DOI=10.1128/mcb.19.8.5267;
RA Ho Y., Costanzo M., Moore L., Kobayashi R., Andrews B.J.;
RT "Regulation of transcription at the Saccharomyces cerevisiae start
RT transition by Stb1, a Swi6-binding protein.";
RL Mol. Cell. Biol. 19:5267-5278(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH SWI6.
RX PubMed=12832490; DOI=10.1128/mcb.23.14.5064-5077.2003;
RA Costanzo M., Schub O., Andrews B.J.;
RT "G1 transcription factors are differentially regulated in Saccharomyces
RT cerevisiae by the Swi6-binding protein Stb1.";
RL Mol. Cell. Biol. 23:5064-5077(2003).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
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 [9]
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-99, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-99 AND THR-419, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; THR-99 AND SER-102, 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).
CC -!- FUNCTION: Involved in the regulation and timing of MBF-dependent
CC transcription in late G1 of the cell cycle.
CC {ECO:0000269|PubMed:12832490}.
CC -!- SUBUNIT: Interacts with the ANK repeats of SWI6. The interaction with
CC SWI6 is required for function. Interacts with SIN3.
CC {ECO:0000269|PubMed:10409718, ECO:0000269|PubMed:12832490,
CC ECO:0000269|PubMed:9393435}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by CDC28 in a cell cycle-dependent manner,
CC inhibiting the interaction with SWI6. {ECO:0000269|PubMed:10409718,
CC ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA86386.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA96238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U33439; AAA75482.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z46259; CAA86386.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71585; CAA96238.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006947; DAA10252.1; -; Genomic_DNA.
DR PIR; S51302; S51302.
DR RefSeq; NP_014090.2; NM_001183147.1.
DR AlphaFoldDB; P42845; -.
DR SMR; P42845; -.
DR BioGRID; 35530; 110.
DR DIP; DIP-2485N; -.
DR IntAct; P42845; 4.
DR MINT; P42845; -.
DR STRING; 4932.YNL309W; -.
DR iPTMnet; P42845; -.
DR MaxQB; P42845; -.
DR PaxDb; P42845; -.
DR PRIDE; P42845; -.
DR EnsemblFungi; YNL309W_mRNA; YNL309W; YNL309W.
DR GeneID; 855407; -.
DR KEGG; sce:YNL309W; -.
DR SGD; S000005253; STB1.
DR VEuPathDB; FungiDB:YNL309W; -.
DR eggNOG; ENOG502S5ZX; Eukaryota.
DR HOGENOM; CLU_048305_0_0_1; -.
DR InParanoid; P42845; -.
DR OMA; NMNDYVH; -.
DR BioCyc; YEAST:G3O-33296-MON; -.
DR PRO; PR:P42845; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42845; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0030907; C:MBF transcription complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0033309; C:SBF transcription complex; IDA:SGD.
DR GO; GO:0070822; C:Sin3-type complex; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IPI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..420
FT /note="Protein STB1"
FT /id="PRO_0000072251"
FT REGION 2..70
FT /note="Interaction with SWI6"
FT REGION 30..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 420 AA; 45684 MW; B1F5E52C8A920400 CRC64;
MSQPQMSPEK EQELASKILH RAELAQMTRQ LKLGLSNVPS TKRKQDSTTK KRSGEDAEDV
DEDHKTLLEA ISPAKKPLHD DTNKMTVISP VKFVEKPNTP PSSRQRKAED RSQQIKPRKE
DTPSTPRASA TPIILPHASS HYQRPHDKNF MTPKRNNNNS SNHSNNNNNI KKKAAGSKDA
PQDSDNTAGA DLLMYLATSP YNKSSHHGTP MAVRMPTTPR SYHYASQLSL NGNTASTSND
AVRFSHIKPS ASSPQSTFKS NLLPNFPDES LMDSPSLYLS NNNGSVQATL SPQQRRKPTT
NTLHPPSNVP TTPSRELNGT NFNLLRTPNF NMGDYLHNLF SPSPRVPAQQ GASNTSASIP
SVPAMVPGSS SNTSAIATAA ISSHTTNNFL DMNANGIPLI VGPGTDRIGE GESIDDKLTD
