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Protein

Multiprotein-bridging factor 1

Gene

MBF1

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

Functioni

Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi96 – 11520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. transcription coactivator activity Source: SGD

GO - Biological processi

  1. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33879-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiprotein-bridging factor 1
Alternative name(s):
Suppressor of frameshift mutations protein 13
Gene namesi
Name:MBF1
Synonyms:SUF13
Ordered Locus Names:YOR298C-A
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR298c-a.
SGDiS000007253. MBF1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121D → A: Reduces interaction to TBP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Multiprotein-bridging factor 1PRO_0000149814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14467.
PaxDbiO14467.
PeptideAtlasiO14467.

Expressioni

Gene expression databases

GenevestigatoriO14467.

Interactioni

Subunit structurei

Interacts with TBP and the transcription factor GCN4.1 Publication

Protein-protein interaction databases

BioGridi34687. 72 interactions.
DIPiDIP-8708N.
IntActiO14467. 2 interactions.
MINTiMINT-8285541.

Structurei

3D structure databases

ProteinModelPortaliO14467.
SMRiO14467. Positions 55-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 13955HTH cro/C1-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 11979Essential for TBP-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the MBF1 family.Curated
Contains 1 HTH cro/C1-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1813.
GeneTreeiENSGT00390000008519.
HOGENOMiHOG000195726.
InParanoidiO14467.
KOiK03627.
OMAiGRGIPNN.
OrthoDBiEOG7NGQQW.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
IPR013729. MBF1_N.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
PF08523. MBF1. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDWDTNTII GSRARAGGSG PRANVARSQG QINAARRQGL VVSVDKKYGS
60 70 80 90 100
TNTRGDNEGQ RLTKVDRETD IVKPKKLDPN VGRAISRART DKKMSQKDLA
110 120 130 140 150
TKINEKPTVV NDYEAARAIP NQQVLSKLER ALGVKLRGNN IGSPLGAPKK

K
Length:151
Mass (Da):16,404
Last modified:May 1, 1999 - v2
Checksum:iE687ED8768ACD1DF
GO

Sequence cautioni

The sequence CAA99527.1 differs from that shown. Reason: Frameshift at position 20. Curated
The sequence CAA99530.1 differs from that shown. Reason: Frameshift at position 20. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017593 Genomic DNA. Translation: BAA33217.1.
Z75206 Genomic DNA. Translation: CAA99527.1. Frameshift.
Z75207 Genomic DNA. Translation: CAA99530.1. Frameshift.
AY260886 Genomic DNA. Translation: AAP21754.1.
AY692753 Genomic DNA. Translation: AAT92772.1.
BK006948 Genomic DNA. Translation: DAA11064.1.
PIRiS72394.
RefSeqiNP_014942.4. NM_001184346.3.

Genome annotation databases

EnsemblFungiiYOR298C-A; YOR298C-A; YOR298C-A.
GeneIDi854474.
KEGGisce:YOR298C-A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017593 Genomic DNA. Translation: BAA33217.1.
Z75206 Genomic DNA. Translation: CAA99527.1. Frameshift.
Z75207 Genomic DNA. Translation: CAA99530.1. Frameshift.
AY260886 Genomic DNA. Translation: AAP21754.1.
AY692753 Genomic DNA. Translation: AAT92772.1.
BK006948 Genomic DNA. Translation: DAA11064.1.
PIRiS72394.
RefSeqiNP_014942.4. NM_001184346.3.

3D structure databases

ProteinModelPortaliO14467.
SMRiO14467. Positions 55-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34687. 72 interactions.
DIPiDIP-8708N.
IntActiO14467. 2 interactions.
MINTiMINT-8285541.

Proteomic databases

MaxQBiO14467.
PaxDbiO14467.
PeptideAtlasiO14467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR298C-A; YOR298C-A; YOR298C-A.
GeneIDi854474.
KEGGisce:YOR298C-A.

Organism-specific databases

CYGDiYOR298c-a.
SGDiS000007253. MBF1.

Phylogenomic databases

eggNOGiCOG1813.
GeneTreeiENSGT00390000008519.
HOGENOMiHOG000195726.
InParanoidiO14467.
KOiK03627.
OMAiGRGIPNN.
OrthoDBiEOG7NGQQW.

Enzyme and pathway databases

BioCyciYEAST:G3O-33879-MONOMER.

Miscellaneous databases

NextBioi976777.
PROiO14467.

Gene expression databases

GenevestigatoriO14467.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
IPR013729. MBF1_N.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
PF08523. MBF1. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast coactivator MBF1 mediates GCN4-dependent transcriptional activation."
    Takemaru K., Harashima S., Ueda H., Hirose S.
    Mol. Cell. Biol. 18:4971-4976(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH GCN4 AND TBP, MUTAGENESIS OF ASP-112, FUNCTION.
    Strain: KT130.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1996) [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. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
    Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
    Genome Biol. 4:R45.1-R45.13(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
    Strain: ATCC 204511 / S288c / AB972.
  5. Bienvenut W.V., Peters C.
    Submitted (APR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 76-83; 103-117 AND 138-149, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-151.
    Strain: ATCC 204508 / S288c.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMBF1_YEAST
AccessioniPrimary (citable) accession number: O14467
Secondary accession number(s): D6W2Z8, Q7LGJ8, Q86ZS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 47277 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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