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P11746 (MCM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pheromone receptor transcription factor
Alternative name(s):
GRM/PRTF protein
Gene names
Name:MCM1
Synonyms:FUN80
Ordered Locus Names:YMR043W
ORF Names:YM9532.08
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.

Subunit structure

Homodimer. Binds DNA with a high specificity in complex with mating-type protein ALPHA1. Also binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Interacts with YHP1 and YOX1, possibly leading to its inactivation. Interacts with ARG80 and ARG82. Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus.

Miscellaneous

Present with 8970 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 MADS-box domain.

Ontologies

Keywords
   Biological processArginine metabolism
Cell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication initiation

Inferred from mutant phenotype PubMed 12473677. Source: SGD

arginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of arginine catabolic process by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 8455631. Source: SGD

negative regulation of mating-type specific transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 1961765. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9121436. Source: SGD

positive regulation of arginine biosynthetic process by positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19233144. Source: SGD

positive regulation of mating-type specific transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11060038. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9121436. Source: SGD

positive regulation of transcription involved in G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 7565744PubMed 9171372. Source: SGD

regulation of mating type switching

Inferred from mutant phenotype PubMed 9620858. Source: SGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 22932476. Source: SGD

nuclear chromatin

Inferred from direct assay PubMed 12473677. Source: SGD

nucleus

Inferred from direct assay PubMed 22932476. Source: SGD

   Molecular_functionDNA replication origin binding

Inferred from direct assay PubMed 12473677. Source: SGD

RNA polymerase II activating transcription factor binding

Inferred from mutant phenotype PubMed 12052870PubMed 12711672. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 12738768PubMed 1752436PubMed 2673922. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 9121436. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 12052870PubMed 9121436. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding, bending

Inferred from direct assay PubMed 12509445PubMed 7739902PubMed 9121436Ref.15. Source: SGD

RNA polymerase II repressing transcription factor binding

Inferred from direct assay Ref.15. Source: SGD

sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity

Inferred from direct assay PubMed 11562353. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 286285Pheromone receptor transcription factor
PRO_0000199439

Regions

Domain18 – 7255MADS-box
Compositional bias98 – 12023Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue21Phosphoserine Ref.12
Modified residue1441Phosphoserine Ref.13

Experimental info

Sequence conflict91P → S in AAA34609. Ref.3
Sequence conflict371S → F in AAA34609. Ref.3
Sequence conflict156 – 1572GA → AR in AAA34609. Ref.3
Sequence conflict158 – 286129Missing in AAA34609. Ref.3

Secondary structure

............ 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11746 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: FD75B4BF549E9E3B

FASTA28632,802
        10         20         30         40         50         60 
MSDIEEGTPT NNGQQKERRK IEIKFIENKT RRHVTFSKRK HGIMKKAFEL SVLTGTQVLL 

        70         80         90        100        110        120 
LVVSETGLVY TFSTPKFEPI VTQQEGRNLI QACLNAPDDE EEDEEEDGDD DDDDDDDGND 

       130        140        150        160        170        180 
MQRQQPQQQQ PQQQQQVLNA HANSLGHLNQ DQVPAGALKQ EVKSQLLGGA NPNQNSMIQQ 

       190        200        210        220        230        240 
QQHHTQNSQP QQQQQQQPQQ QMSQQQMSQH PRPQQGIPHP QQSQPQQQQQ QQQQLQQQQQ 

       250        260        270        280 
QQQQQPLTGI HQPHQQAFAN AASPYLNAEQ NAAYQQYFQE PQQGQY 

« Hide

References

« Hide 'large scale' references
[1]"Identification, purification, and cloning of a polypeptide (PRTF/GRM) that binds to mating-specific promoter elements in yeast."
Ammerer G.
Genes Dev. 4:299-312(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells."
Passmore S., Maine G.T., Elble R., Christ C., Tye B.K.
J. Mol. Biol. 204:593-606(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Characterization of two new genes essential for vegetative growth in Saccharomyces cerevisiae: nucleotide sequence determination and chromosome mapping."
Dubois E., Bercy J., Descamps F., Messenguy F.
Gene 55:265-275(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins."
Primig M., Winkler H., Ammerer G.
EMBO J. 10:4209-4218(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALPHA1 AND ALPHA2.
[8]"The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes."
Mead J., Zhong H., Acton T.B., Vershon A.K.
Mol. Cell. Biol. 16:2135-2143(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALPHA2.
[9]"Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the pleiotropic factor ArgRIII is required for their stability."
El Bakkoury M., Dubois E., Messenguy F.
Mol. Microbiol. 35:15-31(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARG81 AND ARG82.
[10]"Conserved homeodomain proteins interact with MADS box protein Mcm1 to restrict ECB-dependent transcription to the M/G1 phase of the cell cycle."
Pramila T., Miles S., GuhaThakurta D., Jemiolo D., Breeden L.L.
Genes Dev. 16:3034-3045(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YHP1 AND YOX1.
[11]"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].
[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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex."
Tan S., Richmond T.J.
Nature 391:660-666(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-100 IN COMPLEX WITH ALPHA2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52453 Genomic DNA. Translation: CAA36691.1.
X14187 Genomic DNA. Translation: CAA32389.1.
M17511 Genomic DNA. Translation: AAA34609.1.
Z48502 Genomic DNA. Translation: CAA88409.1.
AY557985 Genomic DNA. Translation: AAS56311.1.
BK006946 Genomic DNA. Translation: DAA09942.1.
PIRA34599.
RefSeqNP_013757.1. NM_001182540.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MNMX-ray2.25A/B1-100[»]
ProteinModelPortalP11746.
SMRP11746. Positions 18-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35216. 39 interactions.
DIPDIP-72N.
IntActP11746. 51 interactions.
MINTMINT-478633.
STRING4932.YMR043W.

Proteomic databases

PaxDbP11746.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR043W; YMR043W; YMR043W.
GeneID855060.
KEGGsce:YMR043W.

Organism-specific databases

CYGDYMR043w.
SGDS000004646. MCM1.

Phylogenomic databases

eggNOGCOG5068.
GeneTreeENSGT00400000022158.
KOK12412.
OMACLNAPDD.
OrthoDBEOG7M0P1S.

Enzyme and pathway databases

BioCycYEAST:G3O-32748-MONOMER.

Gene expression databases

GenevestigatorP11746.

Family and domain databases

InterProIPR002100. TF_MADSbox.
[Graphical view]
PfamPF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSPR00404. MADSDOMAIN.
SMARTSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMSSF55455. SSF55455. 1 hit.
PROSITEPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11746.
NextBio978315.
PROP11746.

Entry information

Entry nameMCM1_YEAST
AccessionPrimary (citable) accession number: P11746
Secondary accession number(s): D6VZL8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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