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P29469

- MCM2_YEAST

UniProt

P29469 - MCM2_YEAST

Protein

DNA replication licensing factor MCM2

Gene

MCM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri341 – 36727C4-typeSequence AnalysisAdd
    BLAST
    Nucleotide bindingi543 – 5508ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: SGD
    3. DNA helicase activity Source: InterPro
    4. DNA replication origin binding Source: SGD
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: SGD
    2. DNA duplex unwinding Source: GOC
    3. DNA replication initiation Source: InterPro
    4. DNA strand elongation involved in DNA replication Source: SGD
    5. double-strand break repair via break-induced replication Source: SGD
    6. negative regulation of ATP-dependent DNA helicase activity Source: SGD
    7. nuclear cell cycle DNA replication Source: SGD
    8. pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28926-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM2 (EC:3.6.4.12)
    Alternative name(s):
    Minichromosome maintenance protein 2
    Gene namesi
    Name:MCM2
    Ordered Locus Names:YBL023C
    ORF Names:YBL0438
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL023c.
    SGDiS000000119. MCM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. DNA replication preinitiation complex Source: SGD
    3. MCM complex Source: SGD
    4. nuclear pre-replicative complex Source: SGD
    5. nucleoplasm Source: Reactome
    6. nucleus Source: SGD
    7. replication fork protection complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi364 – 3641C → Y, F, S or H: Loss of activity. 1 Publication
    Mutagenesisi367 – 3671C → Y, F, S or H: Loss of activity. 1 Publication
    Mutagenesisi549 – 5491K → 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. 1 Publication
    Mutagenesisi676 – 6761R → A: Loss of MCM2-7 complex helicase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 868868DNA replication licensing factor MCM2PRO_0000194091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei23 – 231Phosphoserine1 Publication
    Modified residuei164 – 1641Phosphoserine1 Publication
    Modified residuei170 – 1701Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29469.
    PaxDbiP29469.
    PeptideAtlasiP29469.

    Expressioni

    Gene expression databases

    GenevestigatoriP29469.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DIA2Q084963EBI-10533,EBI-31943
    MCM4P306657EBI-10533,EBI-4326

    Protein-protein interaction databases

    BioGridi32675. 106 interactions.
    DIPiDIP-2291N.
    IntActiP29469. 47 interactions.
    MINTiMINT-469073.
    STRINGi4932.YBL023C.

    Structurei

    3D structure databases

    ProteinModelPortaliP29469.
    SMRiP29469. Positions 214-841.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini493 – 700208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi675 – 6784Arginine finger

    Sequence similaritiesi

    Belongs to the MCM family.Curated
    Contains 1 MCM domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri341 – 36727C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1241.
    GeneTreeiENSGT00740000115337.
    HOGENOMiHOG000224124.
    KOiK02540.
    OMAiNMEETVY.
    OrthoDBiEOG7B5X4C.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR008045. MCM2.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00493. MCM. 1 hit.
    PF12619. MCM2_N. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01658. MCMPROTEIN2.
    SMARTiSM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29469-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG    50
    DDNEVDDVPD IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE 100
    QQELSLSERR RIDAQLNERD RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ 150
    RRRRRRQYED LENSDDDLLS DMDIDPLREE LTLESLSNVK ANSYSEWITQ 200
    PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE SLEVNYRHLA 250
    ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF 300
    PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP 350
    FFQDSNEEIR ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG 400
    RLPRHREVIL LADLVDVSKP GEEVEVTGIY KNNYDGNLNA KNGFPVFATI 450
    IEANSIKRRE GNTANEGEEG LDVFSWTEEE EREFRKISRD RGIIDKIISS 500
    MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL LLGDPGTAKS 550
    QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD 600
    KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA 650
    NPNGGRYNST LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV 700
    DSHVRSHPEN DEDREGEELK NNGESAIEQG EDEINEQLNA RQRRLQRQRK 750
    KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ MDMDKVSRVY ADLRRESIST 800
    GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV VVDSFVDAQK 850
    VSVRRQLRRS FAIYTLGH 868
    Length:868
    Mass (Da):98,780
    Last modified:October 1, 1994 - v2
    Checksum:iF38FF682581B0EC0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641S → T in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti172 – 1732MD → IH in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti529 – 5291G → P in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti578 – 5781A → R in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti583 – 5831D → H in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti712 – 7121E → Q in CAA37615. (PubMed:2044961)Curated
    Sequence conflicti733 – 74715Missing in CAA37615. (PubMed:2044961)CuratedAdd
    BLAST
    Sequence conflicti859 – 86810RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615. (PubMed:2044961)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti392 – 3921E → K in allele MCM2-1.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS45757.
    RefSeqiNP_009530.1. NM_001178263.1.

    Genome annotation databases

    EnsemblFungiiYBL023C; YBL023C; YBL023C.
    GeneIDi852258.
    KEGGisce:YBL023C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S45757.
    RefSeqi NP_009530.1. NM_001178263.1.

    3D structure databases

    ProteinModelPortali P29469.
    SMRi P29469. Positions 214-841.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32675. 106 interactions.
    DIPi DIP-2291N.
    IntActi P29469. 47 interactions.
    MINTi MINT-469073.
    STRINGi 4932.YBL023C.

    Proteomic databases

    MaxQBi P29469.
    PaxDbi P29469.
    PeptideAtlasi P29469.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL023C ; YBL023C ; YBL023C .
    GeneIDi 852258.
    KEGGi sce:YBL023C.

    Organism-specific databases

    CYGDi YBL023c.
    SGDi S000000119. MCM2.

    Phylogenomic databases

    eggNOGi COG1241.
    GeneTreei ENSGT00740000115337.
    HOGENOMi HOG000224124.
    KOi K02540.
    OMAi NMEETVY.
    OrthoDBi EOG7B5X4C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28926-MONOMER.

    Miscellaneous databases

    NextBioi 970844.
    PROi P29469.

    Gene expression databases

    Genevestigatori P29469.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR008045. MCM2.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00493. MCM. 1 hit.
    PF12619. MCM2_N. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01658. MCMPROTEIN2.
    SMARTi SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiMCM2_YEAST
    AccessioniPrimary (citable) accession number: P29469
    Secondary accession number(s): D6VPX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 142 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 1690 molecules/cell in log phase SD medium.1 Publication
    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.

    Keywords - Technical termi

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

    External Data

    Dasty 3