ID MBP1_YEAST Reviewed; 833 AA. AC P39678; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 10-FEB-2009, entry version 93. DE RecName: Full=Transcription factor MBP1; DE AltName: Full=MBF subunit p120; GN Name=MBP1; OrderedLocusNames=YDL056W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 372-387. RC STRAIN=K1107; RX MEDLINE=93383264; PubMed=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 MEDLINE=97313263; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-833. RX MEDLINE=96418871; PubMed=8821656; DOI=10.1007/s002940050024; 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 [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-133; SER-135; RP SER-191; SER-212; SER-221; SER-326; SER-602 AND SER-827, AND MASS RP SPECTROMETRY. 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 [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100. RX MEDLINE=97446148; 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102. RX MEDLINE=97238931; 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: MBF contains SWI6 and MBP1. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Contains 2 ANK repeats. CC -!- SIMILARITY: Contains 1 HTH APSES-type DNA-binding domain. 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 PIR; A47528; A47528. DR RefSeq; NP_010227.1; -. 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 DIP; DIP:2391N; -. DR IntAct; P39678; 20. DR Ensembl; YDL056W; Saccharomyces cerevisiae. DR GeneID; 851503; -. DR GenomeReviews; Z71256_GR; YDL056W. DR KEGG; sce:YDL056W; -. DR NMPDR; fig|4932.3.peg.967; -. DR CYGD; YDL056w; -. DR SGD; S000002214; MBP1. DR HOGENOM; P39678; -. DR LinkHub; P39678; -. DR NextBio; 968852; -. DR ArrayExpress; P39678; -. DR GermOnline; YDL056W; Saccharomyces cerevisiae. DR GO; GO:0030907; C:MBF transcription complex; IPI:SGD. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. DR GO; GO:0016564; F:transcription repressor activity; IMP:SGD. DR GO; GO:0006260; P:DNA replication; IMP:SGD. DR GO; GO:0043193; P:positive regulation of gene-specific transc...; IDA:SGD. DR GO; GO:0051726; P:regulation of cell cycle; IGI:SGD. DR InterPro; IPR002110; ANK. DR InterPro; IPR016144; Mlu1-box-bd_prot_DNA-bd. DR InterPro; IPR003163; Yeast_DNA_bd. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Gene3D; G3DSA:3.10.260.10; Mlu1-box-bd_prot_DNA-bd; 1. DR Pfam; PF00023; Ank; 3. DR Pfam; PF02292; APSES; 1. DR SMART; SM00248; ANK; 3. 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 Repeat; Transcription; Transcription regulation. FT CHAIN 1 833 Transcription factor MBP1. FT /FTId=PRO_0000067062. FT DOMAIN 5 111 HTH APSES-type. FT REPEAT 394 423 ANK 1. FT REPEAT 512 541 ANK 2. FT DNA_BIND 36 57 H-T-H motif. FT MOD_RES 110 110 Phosphoserine. FT MOD_RES 133 133 Phosphoserine. FT MOD_RES 135 135 Phosphoserine. FT MOD_RES 191 191 Phosphoserine. FT MOD_RES 212 212 Phosphoserine. FT MOD_RES 221 221 Phosphoserine. FT MOD_RES 326 326 Phosphoserine. FT MOD_RES 602 602 Phosphoserine. FT MOD_RES 827 827 Phosphoserine. FT STRAND 6 10 FT STRAND 13 20 FT STRAND 23 25 FT TURN 29 31 FT STRAND 33 35 FT HELIX 36 39 FT HELIX 41 44 FT HELIX 48 58 FT TURN 59 62 FT TURN 72 74 FT STRAND 75 79 FT HELIX 80 90 FT TURN 93 96 FT HELIX 97 101 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 //