ID MBP1_YEAST Reviewed; 833 AA. AC P39678; D6VRU0; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 14-DEC-2022, entry version 209. DE RecName: Full=Transcription factor MBP1; DE AltName: Full=MBF subunit p120; GN Name=MBP1; OrderedLocusNames=YDL056W; 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 PROTEIN SEQUENCE OF 372-387. RC STRAIN=K1107; RX PubMed=8372350; DOI=10.1126/science.8372350; RA Koch C., Moll T., Neuberg M., Ahorn H., Nasmyth K.; RT "A role for the transcription factors Mbp1 and Swi4 in progression from G1 RT to S phase."; RL Science 261:1551-1557(1993). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-833. RX PubMed=8821656; DOI=10.1007/bf02221573; RA Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.; RT "Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1 RT N-glycosylation mutants."; RL Curr. Genet. 29:106-113(1996). RN [5] 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 [6] RP 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 [7] RP INTERACTION WITH MSA1. RX PubMed=18160399; DOI=10.1074/jbc.m708248200; RA Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III, RA Wittenberg C.; RT "The SBF- and MBF-associated protein Msa1 is required for proper timing of RT G1-specific transcription in Saccharomyces cerevisiae."; RL J. Biol. Chem. 283:6040-6049(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-827, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-325; SER-326 AND RP SER-330, 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 [10] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100. RX PubMed=9299332; DOI=10.1006/jmbi.1997.1229; RA Taylor I.A., Treiber M.K., Olivi L., Smerdon S.J.; RT "The X-ray structure of the DNA-binding domain from the Saccharomyces RT cerevisiae cell-cycle transcription factor Mbp1 at 2.1-A resolution."; RL J. Mol. Biol. 272:1-8(1997). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102. RX PubMed=9083114; DOI=10.1016/s0969-2126(97)00192-5; RA Xu R.M., Koch C., Liu Y., Horton J.R., Knapp D., Nasmyth K., Cheng X.; RT "Crystal structure of the DNA-binding domain of Mbp1, a transcription RT factor important in cell-cycle control of DNA synthesis."; RL Structure 5:349-358(1997). CC -!- FUNCTION: Binds to MCB elements (Mlu I cell cycle box) found in the CC promoter of most DNA synthesis genes. Transcriptional activation by MBF CC has an important role in the transition from G1 to S phase. It may have CC a dual role in that it behaves as an activator of transcription at the CC G1-S boundary and as a repressor during other stages of the cell cycle. CC -!- SUBUNIT: Component of the transcription complex MCB-binding factor CC (MBF) composed of SWI6 and MBP1. Interacts with MSA1. CC {ECO:0000269|PubMed:18160399}. CC -!- INTERACTION: CC P39678; P09959: SWI6; NbExp=4; IntAct=EBI-10485, EBI-18641; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 521 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; X74158; CAA52271.1; -; Genomic_DNA. DR EMBL; Z74104; CAA98618.1; -; Genomic_DNA. DR EMBL; U19608; AAC49290.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11800.1; -; Genomic_DNA. DR PIR; A47528; A47528. DR RefSeq; NP_010227.1; NM_001180115.1. DR PDB; 1BM8; X-ray; 1.71 A; A=4-102. DR PDB; 1L3G; NMR; -; A=2-124. DR PDB; 1MB1; X-ray; 2.10 A; A=1-124. DR PDBsum; 1BM8; -. DR PDBsum; 1L3G; -. DR PDBsum; 1MB1; -. DR AlphaFoldDB; P39678; -. DR BMRB; P39678; -. DR SMR; P39678; -. DR BioGRID; 32002; 163. DR ComplexPortal; CPX-950; MBP transcription complex. DR DIP; DIP-2391N; -. DR IntAct; P39678; 29. DR MINT; P39678; -. DR STRING; 4932.YDL056W; -. DR iPTMnet; P39678; -. DR MaxQB; P39678; -. DR PaxDb; P39678; -. DR PeptideAtlas; P39678; -. DR EnsemblFungi; YDL056W_mRNA; YDL056W; YDL056W. DR GeneID; 851503; -. DR KEGG; sce:YDL056W; -. DR AGR; SGD:S000002214; -. DR SGD; S000002214; MBP1. DR VEuPathDB; FungiDB:YDL056W; -. DR eggNOG; KOG4177; Eukaryota. DR HOGENOM; CLU_009666_3_0_1; -. DR InParanoid; P39678; -. DR OMA; QRNARKC; -. DR BioCyc; YEAST:G3O-29472-MON; -. DR EvolutionaryTrace; P39678; -. DR PRO; PR:P39678; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P39678; protein. 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; IBA:GO_Central. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD. DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal. DR Gene3D; 1.25.40.20; -; 1. DR Gene3D; 3.10.260.10; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR036887; HTH_APSES_sf. DR InterPro; IPR018004; KilA_N/APSES_HTH. DR InterPro; IPR029793; Mbp1/Res1/Res2. DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type. DR PANTHER; PTHR43828:SF1; TRANSCRIPTION FACTOR MBP1; 1. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF04383; KilA-N; 1. DR SMART; SM00248; ANK; 3. DR SMART; SM01252; KilA-N; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. DR PROSITE; PS51299; HTH_APSES; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; ANK repeat; Direct protein sequencing; KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1..833 FT /note="Transcription factor MBP1" FT /id="PRO_0000067062" FT DOMAIN 5..111 FT /note="HTH APSES-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630" FT REPEAT 394..423 FT /note="ANK 1" FT REPEAT 512..541 FT /note="ANK 2" FT DNA_BIND 36..57 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630" FT REGION 104..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 280..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 180..222 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 280..309 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 325 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 827 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:1BM8" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:1BM8" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:1BM8" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:1BM8" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:1L3G" FT HELIX 36..42 FT /evidence="ECO:0007829|PDB:1BM8" FT HELIX 47..57 FT /evidence="ECO:0007829|PDB:1BM8" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:1BM8" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:1BM8" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:1MB1" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:1BM8" FT HELIX 80..89 FT /evidence="ECO:0007829|PDB:1BM8" FT HELIX 93..101 FT /evidence="ECO:0007829|PDB:1BM8" SQ SEQUENCE 833 AA; 93908 MW; BB7C35E29802BBD5 CRC64; MSNQIYSARY SGVDVYEFIH STGSIMKRKK DDWVNATHIL KAANFAKAKR TRILEKEVLK ETHEKVQGGF GKYQGTWVPL NIAKQLAEKF SVYDQLKPLF DFTQTDGSAS PPPAPKHHHA SKVDRKKAIR SASTSAIMET KRNNKKAEEN QFQSSKILGN PTAAPRKRGR PVGSTRGSRR KLGVNLQRSQ SDMGFPRPAI PNSSISTTQL PSIRSTMGPQ SPTLGILEEE RHDSRQQQPQ QNNSAQFKEI DLEDGLSSDV EPSQQLQQVF NQNTGFVPQQ QSSLIQTQQT ESMATSVSSS PSLPTSPGDF ADSNPFEERF PGGGTSPIIS MIPRYPVTSR PQTSDINDKV NKYLSKLVDY FISNEMKSNK SLPQVLLHPP PHSAPYIDAP IDPELHTAFH WACSMGNLPI AEALYEAGTS IRSTNSQGQT PLMRSSLFHN SYTRRTFPRI FQLLHETVFD IDSQSQTVIH HIVKRKSTTP SAVYYLDVVL SKIKDFSPQY RIELLLNTQD KNGDTALHIA SKNGDVVFFN TLVKMGALTT ISNKEGLTAN EIMNQQYEQM MIQNGTNQHV NSSNTDLNIH VNTNNIETKN DVNSMVIMSP VSPSDYITYP SQIATNISRN IPNVVNSMKQ MASIYNDLHE QHDNEIKSLQ KTLKSISKTK IQVSLKTLEV LKESSKDENG EAQTNDDFEI LSRLQEQNTK KLRKRLIRYK RLIKQKLEYR QTVLLNKLIE DETQATTNNT VEKDNNTLER LELAQELTML QLQRKNKLSS LVKKFEDNAK IHKYRRIIRE GTEMNIEEVD SSLDVILQTL IANNNKNKGA EQIITISNAN SHA //