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P39678 (MBP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor MBP1
Alternative name(s):
MBF subunit p120
Gene names
Name:MBP1
Ordered Locus Names:YDL056W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle.

Subunit structure

Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Interacts with MSA1. Ref.7

Subcellular location

Nucleus.

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.

Sequence similarities

Contains 2 ANK repeats.

Contains 1 HTH APSES-type DNA-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SWI6P099595EBI-10485,EBI-18641

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 833833Transcription factor MBP1
PRO_0000067062

Regions

Domain5 – 111107HTH APSES-type
Repeat394 – 42330ANK 1
Repeat512 – 54130ANK 2
DNA binding36 – 5722H-T-H motif

Amino acid modifications

Modified residue1101Phosphoserine Ref.8 Ref.9
Modified residue3251Phosphothreonine Ref.9
Modified residue3261Phosphoserine Ref.9
Modified residue3301Phosphoserine Ref.9
Modified residue8271Phosphoserine Ref.8

Secondary structure

........................ 833
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39678 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BB7C35E29802BBD5

FASTA83393,908
        10         20         30         40         50         60 
MSNQIYSARY SGVDVYEFIH STGSIMKRKK DDWVNATHIL KAANFAKAKR TRILEKEVLK 

        70         80         90        100        110        120 
ETHEKVQGGF GKYQGTWVPL NIAKQLAEKF SVYDQLKPLF DFTQTDGSAS PPPAPKHHHA 

       130        140        150        160        170        180 
SKVDRKKAIR SASTSAIMET KRNNKKAEEN QFQSSKILGN PTAAPRKRGR PVGSTRGSRR 

       190        200        210        220        230        240 
KLGVNLQRSQ SDMGFPRPAI PNSSISTTQL PSIRSTMGPQ SPTLGILEEE RHDSRQQQPQ 

       250        260        270        280        290        300 
QNNSAQFKEI DLEDGLSSDV EPSQQLQQVF NQNTGFVPQQ QSSLIQTQQT ESMATSVSSS 

       310        320        330        340        350        360 
PSLPTSPGDF ADSNPFEERF PGGGTSPIIS MIPRYPVTSR PQTSDINDKV NKYLSKLVDY 

       370        380        390        400        410        420 
FISNEMKSNK SLPQVLLHPP PHSAPYIDAP IDPELHTAFH WACSMGNLPI AEALYEAGTS 

       430        440        450        460        470        480 
IRSTNSQGQT PLMRSSLFHN SYTRRTFPRI FQLLHETVFD IDSQSQTVIH HIVKRKSTTP 

       490        500        510        520        530        540 
SAVYYLDVVL SKIKDFSPQY RIELLLNTQD KNGDTALHIA SKNGDVVFFN TLVKMGALTT 

       550        560        570        580        590        600 
ISNKEGLTAN EIMNQQYEQM MIQNGTNQHV NSSNTDLNIH VNTNNIETKN DVNSMVIMSP 

       610        620        630        640        650        660 
VSPSDYITYP SQIATNISRN IPNVVNSMKQ MASIYNDLHE QHDNEIKSLQ KTLKSISKTK 

       670        680        690        700        710        720 
IQVSLKTLEV LKESSKDENG EAQTNDDFEI LSRLQEQNTK KLRKRLIRYK RLIKQKLEYR 

       730        740        750        760        770        780 
QTVLLNKLIE DETQATTNNT VEKDNNTLER LELAQELTML QLQRKNKLSS LVKKFEDNAK 

       790        800        810        820        830 
IHKYRRIIRE GTEMNIEEVD SSLDVILQTL IANNNKNKGA EQIITISNAN SHA 

« Hide

References

« Hide 'large scale' references
[1]"A role for the transcription factors Mbp1 and Swi4 in progression from G1 to S phase."
Koch C., Moll T., Neuberg M., Ahorn H., Nasmyth K.
Science 261:1551-1557(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 372-387.
Strain: K1107.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1 N-glycosylation mutants."
Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.
Curr. Genet. 29:106-113(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-833.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"The SBF- and MBF-associated protein Msa1 is required for proper timing of G1-specific transcription in Saccharomyces cerevisiae."
Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III, Wittenberg C.
J. Biol. Chem. 283:6040-6049(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MSA1.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-325; SER-326 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1-A resolution."
Taylor I.A., Treiber M.K., Olivi L., Smerdon S.J.
J. Mol. Biol. 272:1-8(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100.
[11]"Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis."
Xu R.M., Koch C., Liu Y., Horton J.R., Knapp D., Nasmyth K., Cheng X.
Structure 5:349-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74158 Genomic DNA. Translation: CAA52271.1.
Z74104 Genomic DNA. Translation: CAA98618.1.
U19608 Genomic DNA. Translation: AAC49290.1.
BK006938 Genomic DNA. Translation: DAA11800.1.
PIRA47528.
RefSeqNP_010227.1. NM_001180115.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BM8X-ray1.71A4-102[»]
1L3GNMR-A2-124[»]
1MB1X-ray2.10A1-124[»]
ProteinModelPortalP39678.
SMRP39678. Positions 2-124, 349-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32002. 92 interactions.
DIPDIP-2391N.
IntActP39678. 28 interactions.
MINTMINT-616665.

Proteomic databases

MaxQBP39678.
PaxDbP39678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL056W; YDL056W; YDL056W.
GeneID851503.
KEGGsce:YDL056W.

Organism-specific databases

CYGDYDL056w.
SGDS000002214. MBP1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00530000067565.
HOGENOMHOG000113493.
KOK06647.
OMATGSIMKR.
OrthoDBEOG7ZSJ36.

Enzyme and pathway databases

BioCycYEAST:G3O-29472-MONOMER.

Gene expression databases

GenevestigatorP39678.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.10.260.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR018004. KilA_N/APSES_HTH.
IPR003163. Tscrpt_reg_HTH_APSES-type.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF04383. KilA-N. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF54616. SSF54616. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS51299. HTH_APSES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP39678.
NextBio968852.

Entry information

Entry nameMBP1_YEAST
AccessionPrimary (citable) accession number: P39678
Secondary accession number(s): D6VRU0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references