ID MBP1_YEAST STANDARD; PRT; 833 AA. AC P39678; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 18-APR-2006, entry version 63. DE Transcription factor MBP1 (MBF subunit p120). GN Name=MBP1; OrderedLocusNames=YDL056W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC 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=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. 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 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 [6] 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. CC -!- SIMILARITY: Contains 2 ANK repeats. 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 PDB; 1BM8; X-ray; @=4-102. DR PDB; 1L3G; NMR; A=2-124. DR PDB; 1MB1; X-ray; @=1-124. DR IntAct; P39678; -. DR GermOnline; 140298; -. DR TRANSFAC; T03480; -. DR Ensembl; YDL056W; Saccharomyces cerevisiae. DR GenomeReviews; Z71256_GR; YDL056W. DR SGD; S000002214; MBP1. DR BioCyc; SCER-S28-01:SCER-S28-01-000804-MONOMER; -. DR LinkHub; P39678; -. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003700; F:transcription factor activity; IMP. DR GO; GO:0006260; P:DNA replication; IMP. DR GO; GO:0000074; P:regulation of progression through cell cycle; IGI. DR InterPro; IPR002110; ANK. DR InterPro; IPR003163; Yeast_DNA_bd. DR Pfam; PF00023; Ank; 3. DR Pfam; PF02292; APSES; 1. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. KW 3D-structure; Activator; ANK repeat; Complete proteome; KW Direct protein sequencing; DNA-binding; Nuclear protein; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1 833 Transcription factor MBP1. FT /FTId=PRO_0000067062. FT REPEAT 394 423 ANK 1. FT REPEAT 512 541 ANK 2. FT DNA_BIND 1 94 FT STRAND 5 10 FT TURN 11 12 FT STRAND 13 19 FT STRAND 21 22 FT STRAND 24 28 FT TURN 29 31 FT STRAND 34 35 FT HELIX 36 42 FT TURN 43 44 FT HELIX 47 57 FT TURN 58 60 FT STRAND 61 62 FT STRAND 64 69 FT STRAND 71 71 FT TURN 72 73 FT STRAND 75 78 FT HELIX 80 89 FT TURN 90 91 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 //