ID MBP1_YEAST STANDARD; PRT; 833 AA. AC P39678; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE TRANSCRIPTION FACTOR MBP1 (MBF SUBUNIT P120). GN MBP1 OR YDL056W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A., AND 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 SEQUENCE FROM N.A. RA Bloecker H., Brandt P.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 460-833 FROM N.A. RA Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100. RX MEDLINE=97446148; PubMed=9299332; 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 RT resolution."; RL J. Mol. Biol. 272:1-8(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102. RX MEDLINE=97238931; PubMed=9083114; 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: NUCLEAR. 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; -. DR EMBL; Z74104; CAA98618.1; -. DR EMBL; U19608; AAC49290.1; -. DR PIR; A47528; A47528. DR PIR; S37404; S37404. DR PDB; 1MB1; 29-JUL-98. DR PDB; 1BM8; 02-MAR-99. DR SGD; S0002214; MBP1. DR InterPro; IPR002110; ANK. DR InterPro; IPR003163; Yeast_DNA_bind. DR Pfam; PF00023; ank; 2. DR Pfam; PF02292; Yeast_DNA_bind; 1. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50088; ANK_REPEAT; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. KW Transcription regulation; Activator; Nuclear protein; DNA-binding; KW ANK repeat; Repeat; 3D-structure. FT DNA_BIND 1 94 FT REPEAT 394 423 ANK 1. FT REPEAT 512 541 ANK 2. SQ SEQUENCE 833 AA; 93907 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 //