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P29469 (MCM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
DNA replication licensing factor MCM2

EC=3.6.4.12
Alternative name(s):
Minichromosome maintenance protein 2
Gene names
Name:MCM2
Ordered Locus Names:YBL023C
ORF Names:YBL0438
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length868 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth. Ref.5 Ref.6

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Ref.5 Ref.6

Subcellular location

Nucleus.

Miscellaneous

Present with 1690 molecules/cell in log phase SD medium.

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Ontologies

Keywords
   Biological processCell cycle
DNA replication
   Cellular componentNucleus
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA duplex unwinding

Inferred from direct assay Ref.4. Source: GOC

DNA replication initiation

Inferred from electronic annotation. Source: InterPro

DNA strand elongation involved in DNA replication

Inferred from mutant phenotype PubMed 10834843. Source: SGD

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 22564307. Source: SGD

double-strand break repair via break-induced replication

Inferred from mutant phenotype PubMed 20516198. Source: SGD

negative regulation of ATP-dependent DNA helicase activity

Inferred from direct assay PubMed 13679365. Source: SGD

nuclear cell cycle DNA replication

Inferred from mutant phenotype PubMed 10834843. Source: SGD

pre-replicative complex assembly involved in nuclear cell cycle DNA replication

Inferred from direct assay PubMed 16824194. Source: SGD

   Cellular_componentDNA replication preinitiation complex

Inferred from direct assay PubMed 9554851. Source: SGD

MCM complex

Inferred from direct assay PubMed 12480933. Source: SGD

cytoplasm

Inferred from direct assay PubMed 10704410. Source: SGD

nuclear pre-replicative complex

Inferred from direct assay PubMed 16824194PubMed 9335335. Source: SGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10704410. Source: SGD

replication fork protection complex

Inferred from direct assay PubMed 16531994. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA replication origin binding

Inferred from direct assay PubMed 11756674PubMed 16824194. Source: SGD

chromatin binding

Inferred from direct assay PubMed 10783164. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12480933PubMed 18719252Ref.5PubMed 19910927PubMed 22433841. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DIA2Q084963EBI-10533,EBI-31943
MCM4P306657EBI-10533,EBI-4326

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 868868DNA replication licensing factor MCM2
PRO_0000194091

Regions

Domain493 – 700208MCM
Zinc finger341 – 36727C4-type Potential
Nucleotide binding543 – 5508ATP Potential
Motif675 – 6784Arginine finger

Amino acid modifications

Modified residue141Phosphoserine Ref.10
Modified residue161Phosphoserine Ref.10
Modified residue231Phosphoserine Ref.10
Modified residue1641Phosphoserine Ref.10
Modified residue1701Phosphoserine Ref.10

Natural variations

Natural variant3921E → K in allele MCM2-1.

Experimental info

Mutagenesis3641C → Y, F, S or H: Loss of activity. Ref.1
Mutagenesis3671C → Y, F, S or H: Loss of activity. Ref.1
Mutagenesis5491K → A: Reduces MCM2-7 complex helicase activity. Abolishes MCM2-7 complex helicase activity; when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity; when associated with MCM3 A-415. Ref.4
Mutagenesis6761R → A: Loss of MCM2-7 complex helicase activity. Ref.4
Sequence conflict1641S → T in CAA37615. Ref.1
Sequence conflict172 – 1732MD → IH in CAA37615. Ref.1
Sequence conflict5291G → P in CAA37615. Ref.1
Sequence conflict5781A → R in CAA37615. Ref.1
Sequence conflict5831D → H in CAA37615. Ref.1
Sequence conflict7121E → Q in CAA37615. Ref.1
Sequence conflict733 – 74715Missing in CAA37615. Ref.1
Sequence conflict859 – 86810RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29469 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: F38FF682581B0EC0

FASTA86898,780
        10         20         30         40         50         60 
MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG DDNEVDDVPD 

        70         80         90        100        110        120 
IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE QQELSLSERR RIDAQLNERD 

       130        140        150        160        170        180 
RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ RRRRRRQYED LENSDDDLLS DMDIDPLREE 

       190        200        210        220        230        240 
LTLESLSNVK ANSYSEWITQ PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE 

       250        260        270        280        290        300 
SLEVNYRHLA ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF 

       310        320        330        340        350        360 
PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP FFQDSNEEIR 

       370        380        390        400        410        420 
ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG RLPRHREVIL LADLVDVSKP 

       430        440        450        460        470        480 
GEEVEVTGIY KNNYDGNLNA KNGFPVFATI IEANSIKRRE GNTANEGEEG LDVFSWTEEE 

       490        500        510        520        530        540 
EREFRKISRD RGIIDKIISS MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL 

       550        560        570        580        590        600 
LLGDPGTAKS QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD 

       610        620        630        640        650        660 
KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA NPNGGRYNST 

       670        680        690        700        710        720 
LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV DSHVRSHPEN DEDREGEELK 

       730        740        750        760        770        780 
NNGESAIEQG EDEINEQLNA RQRRLQRQRK KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ 

       790        800        810        820        830        840 
MDMDKVSRVY ADLRRESIST GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV 

       850        860 
VVDSFVDAQK VSVRRQLRRS FAIYTLGH 

« Hide

References

« Hide 'large scale' references
[1]"Mcm2 and Mcm3, two proteins important for ARS activity, are related in structure and function."
Yan H., Gibson S., Tye B.K.
Genes Dev. 5:944-957(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-364 AND CYS-367.
[2]"Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen."
van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.
Yeast 10:1663-1673(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The Mcm2-7 complex has in vitro helicase activity."
Bochman M.L., Schwacha A.
Mol. Cell 31:287-293(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-549 AND ARG-676.
[5]"Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing."
Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.
Cell 139:719-730(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[6]"A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication."
Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B., Speck C.
Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[7]"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.
[8]"PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae."
van Dyck L., Pearce D.A., Sherman F.
J. Biol. Chem. 269:238-242(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
Strain: ATCC 204508 / S288c.
[9]"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].
[10]"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-14; SER-16; SER-23; SER-164 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77291 Genomic DNA. Translation: CAA54503.1.
X53539 Genomic DNA. Translation: CAA37615.1.
Z35784 Genomic DNA. Translation: CAA84842.1.
X74544 Genomic DNA. Translation: CAA52635.1.
BK006936 Genomic DNA. Translation: DAA07097.1.
PIRS45757.
RefSeqNP_009530.1. NM_001178263.1.

3D structure databases

ProteinModelPortalP29469.
SMRP29469. Positions 214-841.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32675. 106 interactions.
DIPDIP-2291N.
IntActP29469. 46 interactions.
MINTMINT-469073.
STRING4932.YBL023C.

Proteomic databases

MaxQBP29469.
PaxDbP29469.
PeptideAtlasP29469.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL023C; YBL023C; YBL023C.
GeneID852258.
KEGGsce:YBL023C.

Organism-specific databases

CYGDYBL023c.
SGDS000000119. MCM2.

Phylogenomic databases

eggNOGCOG1241.
GeneTreeENSGT00740000115337.
HOGENOMHOG000224124.
KOK02540.
OMANMEETVY.
OrthoDBEOG7B5X4C.

Enzyme and pathway databases

BioCycYEAST:G3O-28926-MONOMER.
ReactomeREACT_190740. Cell Cycle.

Gene expression databases

GenevestigatorP29469.

Family and domain databases

Gene3D2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970844.
PROP29469.

Entry information

Entry nameMCM2_YEAST
AccessionPrimary (citable) accession number: P29469
Secondary accession number(s): D6VPX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 140 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 II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families