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 29-OCT-2014, entry version 153. 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; OC Saccharomycetes; 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 RT from G1 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., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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 RT alg1 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., RA Dephoure N., 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., RA Yates J.R. III, Wittenberg C.; RT "The SBF- and MBF-associated protein Msa1 is required for proper RT timing of 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-325; SER-326 RP AND SER-330, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT insights 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 CC the promoter of most DNA synthesis genes. Transcriptional CC activation by MBF has an important role in the transition from G1 CC to S phase. It may have a dual role in that it behaves as an CC activator of transcription at the G1-S boundary and as a repressor CC 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 P09959:SWI6; NbExp=5; IntAct=EBI-10485, EBI-18641; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Contains 2 ANK repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00023}. CC -!- SIMILARITY: Contains 1 HTH APSES-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00630}. 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 ProteinModelPortal; P39678; -. DR SMR; P39678; 2-124, 349-547. DR BioGrid; 32002; 95. DR DIP; DIP-2391N; -. DR IntAct; P39678; 28. DR MINT; MINT-616665; -. DR MaxQB; P39678; -. DR PaxDb; P39678; -. DR EnsemblFungi; YDL056W; YDL056W; YDL056W. DR GeneID; 851503; -. DR KEGG; sce:YDL056W; -. DR CYGD; YDL056w; -. DR SGD; S000002214; MBP1. DR eggNOG; COG0666; -. DR GeneTree; ENSGT00530000067565; -. DR HOGENOM; HOG000113493; -. DR InParanoid; P39678; -. DR KO; K06647; -. DR OMA; TGSIMKR; -. DR OrthoDB; EOG7ZSJ36; -. DR BioCyc; YEAST:G3O-29472-MONOMER; -. DR EvolutionaryTrace; P39678; -. DR NextBio; 968852; -. DR Genevestigator; P39678; -. DR GO; GO:0030907; C:MBF transcription complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IMP:SGD. DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD. DR Gene3D; 1.25.40.20; -; 1. DR Gene3D; 3.10.260.10; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR018004; KilA_N/APSES_HTH. DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type. DR Pfam; PF00023; Ank; 2. DR Pfam; PF04383; KilA-N; 1. DR SMART; SM00248; ANK; 3. DR SUPFAM; SSF48403; SSF48403; 1. DR SUPFAM; SSF54616; SSF54616; 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; Complete proteome; KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1 833 Transcription factor MBP1. FT /FTId=PRO_0000067062. FT DOMAIN 5 111 HTH APSES-type. {ECO:0000255|PROSITE- FT ProRule:PRU00630}. FT REPEAT 394 423 ANK 1. FT REPEAT 512 541 ANK 2. FT DNA_BIND 36 57 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00630}. FT MOD_RES 110 110 Phosphoserine. FT {ECO:0000269|PubMed:18407956, FT ECO:0000269|PubMed:19779198}. FT MOD_RES 325 325 Phosphothreonine. FT {ECO:0000269|PubMed:19779198}. FT MOD_RES 326 326 Phosphoserine. FT {ECO:0000269|PubMed:19779198}. FT MOD_RES 330 330 Phosphoserine. FT {ECO:0000269|PubMed:19779198}. FT MOD_RES 827 827 Phosphoserine. FT {ECO:0000269|PubMed:18407956}. FT STRAND 5 10 FT STRAND 13 19 FT STRAND 24 28 FT TURN 29 31 FT STRAND 33 35 FT HELIX 36 42 FT HELIX 47 57 FT TURN 58 60 FT STRAND 64 69 FT TURN 71 73 FT STRAND 75 78 FT HELIX 80 89 FT HELIX 93 101 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 //