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Protein

Transcription factor MBP1

Gene

MBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi36 – 5722H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: SGD

GO - Biological processi

  1. positive regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29472-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor MBP1
Alternative name(s):
MBF subunit p120
Gene namesi
Name:MBP1
Ordered Locus Names:YDL056W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL056w.
SGDiS000002214. MBP1.

Subcellular locationi

GO - Cellular componenti

  1. MBF transcription complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Transcription factor MBP1PRO_0000067062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphoserine2 Publications
Modified residuei325 – 3251Phosphothreonine1 Publication
Modified residuei326 – 3261Phosphoserine1 Publication
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei827 – 8271Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39678.
PaxDbiP39678.

Expressioni

Gene expression databases

GenevestigatoriP39678.

Interactioni

Subunit structurei

Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Interacts with MSA1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SWI6P099595EBI-10485,EBI-18641

Protein-protein interaction databases

BioGridi32002. 95 interactions.
DIPiDIP-2391N.
IntActiP39678. 28 interactions.
MINTiMINT-616665.

Structurei

Secondary structure

1
833
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi13 – 197Combined sources
Beta strandi24 – 285Combined sources
Turni29 – 313Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 427Combined sources
Helixi47 – 5711Combined sources
Turni58 – 603Combined sources
Beta strandi64 – 696Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 784Combined sources
Helixi80 – 8910Combined sources
Helixi93 – 1019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BM8X-ray1.71A4-102[»]
1L3GNMR-A2-124[»]
1MB1X-ray2.10A1-124[»]
ProteinModelPortaliP39678.
SMRiP39678. Positions 2-124, 349-547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 111107HTH APSES-typePROSITE-ProRule annotationAdd
BLAST
Repeati394 – 42330ANK 1Add
BLAST
Repeati512 – 54130ANK 2Add
BLAST

Sequence similaritiesi

Contains 2 ANK repeats.PROSITE-ProRule annotation
Contains 1 HTH APSES-type DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00530000067565.
HOGENOMiHOG000113493.
InParanoidiP39678.
KOiK06647.
OMAiTGSIMKR.
OrthoDBiEOG7ZSJ36.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.10.260.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR018004. KilA_N/APSES_HTH.
IPR029793. Mbp1/Res1/Res2.
IPR003163. Tscrpt_reg_HTH_APSES-type.
[Graphical view]
PANTHERiPTHR11707:SF26. PTHR11707:SF26. 1 hit.
PfamiPF00023. Ank. 2 hits.
PF04383. KilA-N. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF54616. SSF54616. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS51299. HTH_APSES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39678-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNQIYSARY SGVDVYEFIH STGSIMKRKK DDWVNATHIL KAANFAKAKR
60 70 80 90 100
TRILEKEVLK ETHEKVQGGF GKYQGTWVPL NIAKQLAEKF SVYDQLKPLF
110 120 130 140 150
DFTQTDGSAS PPPAPKHHHA SKVDRKKAIR SASTSAIMET KRNNKKAEEN
160 170 180 190 200
QFQSSKILGN PTAAPRKRGR PVGSTRGSRR KLGVNLQRSQ SDMGFPRPAI
210 220 230 240 250
PNSSISTTQL PSIRSTMGPQ SPTLGILEEE RHDSRQQQPQ QNNSAQFKEI
260 270 280 290 300
DLEDGLSSDV EPSQQLQQVF NQNTGFVPQQ QSSLIQTQQT ESMATSVSSS
310 320 330 340 350
PSLPTSPGDF ADSNPFEERF PGGGTSPIIS MIPRYPVTSR PQTSDINDKV
360 370 380 390 400
NKYLSKLVDY FISNEMKSNK SLPQVLLHPP PHSAPYIDAP IDPELHTAFH
410 420 430 440 450
WACSMGNLPI AEALYEAGTS IRSTNSQGQT PLMRSSLFHN SYTRRTFPRI
460 470 480 490 500
FQLLHETVFD IDSQSQTVIH HIVKRKSTTP SAVYYLDVVL SKIKDFSPQY
510 520 530 540 550
RIELLLNTQD KNGDTALHIA SKNGDVVFFN TLVKMGALTT ISNKEGLTAN
560 570 580 590 600
EIMNQQYEQM MIQNGTNQHV NSSNTDLNIH VNTNNIETKN DVNSMVIMSP
610 620 630 640 650
VSPSDYITYP SQIATNISRN IPNVVNSMKQ MASIYNDLHE QHDNEIKSLQ
660 670 680 690 700
KTLKSISKTK IQVSLKTLEV LKESSKDENG EAQTNDDFEI LSRLQEQNTK
710 720 730 740 750
KLRKRLIRYK RLIKQKLEYR QTVLLNKLIE DETQATTNNT VEKDNNTLER
760 770 780 790 800
LELAQELTML QLQRKNKLSS LVKKFEDNAK IHKYRRIIRE GTEMNIEEVD
810 820 830
SSLDVILQTL IANNNKNKGA EQIITISNAN SHA
Length:833
Mass (Da):93,908
Last modified:February 1, 1995 - v1
Checksum:iBB7C35E29802BBD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74158 Genomic DNA. Translation: CAA52271.1.
Z74104 Genomic DNA. Translation: CAA98618.1.
U19608 Genomic DNA. Translation: AAC49290.1.
BK006938 Genomic DNA. Translation: DAA11800.1.
PIRiA47528.
RefSeqiNP_010227.1. NM_001180115.1.

Genome annotation databases

EnsemblFungiiYDL056W; YDL056W; YDL056W.
GeneIDi851503.
KEGGisce:YDL056W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74158 Genomic DNA. Translation: CAA52271.1.
Z74104 Genomic DNA. Translation: CAA98618.1.
U19608 Genomic DNA. Translation: AAC49290.1.
BK006938 Genomic DNA. Translation: DAA11800.1.
PIRiA47528.
RefSeqiNP_010227.1. NM_001180115.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BM8X-ray1.71A4-102[»]
1L3GNMR-A2-124[»]
1MB1X-ray2.10A1-124[»]
ProteinModelPortaliP39678.
SMRiP39678. Positions 2-124, 349-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32002. 95 interactions.
DIPiDIP-2391N.
IntActiP39678. 28 interactions.
MINTiMINT-616665.

Proteomic databases

MaxQBiP39678.
PaxDbiP39678.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL056W; YDL056W; YDL056W.
GeneIDi851503.
KEGGisce:YDL056W.

Organism-specific databases

CYGDiYDL056w.
SGDiS000002214. MBP1.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00530000067565.
HOGENOMiHOG000113493.
InParanoidiP39678.
KOiK06647.
OMAiTGSIMKR.
OrthoDBiEOG7ZSJ36.

Enzyme and pathway databases

BioCyciYEAST:G3O-29472-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39678.
NextBioi968852.

Gene expression databases

GenevestigatoriP39678.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.10.260.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR018004. KilA_N/APSES_HTH.
IPR029793. Mbp1/Res1/Res2.
IPR003163. Tscrpt_reg_HTH_APSES-type.
[Graphical view]
PANTHERiPTHR11707:SF26. PTHR11707:SF26. 1 hit.
PfamiPF00023. Ank. 2 hits.
PF04383. KilA-N. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF54616. SSF54616. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS51299. HTH_APSES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiMBP1_YEAST
AccessioniPrimary (citable) accession number: P39678
Secondary accession number(s): D6VRU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.