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P53091

- MCM6_YEAST

UniProt

P53091 - MCM6_YEAST

Protein

DNA replication licensing factor MCM6

Gene

MCM6

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 126 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi575 – 5828ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA helicase activity Source: InterPro
    3. DNA replication origin binding Source: SGD
    4. protein binding Source: IntAct
    5. single-stranded DNA-dependent ATPase activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA replication initiation Source: SGD
    3. DNA strand elongation involved in DNA replication Source: SGD
    4. DNA unwinding involved in DNA replication Source: SGD
    5. double-strand break repair via break-induced replication Source: SGD
    6. nuclear cell cycle DNA replication Source: SGD
    7. 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, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30681-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM6 (EC:3.6.4.12)
    Alternative name(s):
    Minichromosome maintenance protein 6
    Gene namesi
    Name:MCM6
    Ordered Locus Names:YGL201C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000003169. MCM6.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi581 – 5811K → A: Loss of MCM2-7 complex helicase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10171017DNA replication licensing factor MCM6PRO_0000194117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei78 – 781Phosphoserine1 Publication
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei372 – 3721Phosphoserine1 Publication
    Modified residuei766 – 7661Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53091.
    PaxDbiP53091.
    PeptideAtlasiP53091.
    PRIDEiP53091.

    Expressioni

    Gene expression databases

    GenevestigatoriP53091.

    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. Interacts with MCM10.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MCM10P323545EBI-10556,EBI-5965
    MCM4P306655EBI-10556,EBI-4326

    Protein-protein interaction databases

    BioGridi33056. 65 interactions.
    DIPiDIP-1294N.
    IntActiP53091. 54 interactions.
    MINTiMINT-397018.
    STRINGi4932.YGL201C.

    Structurei

    3D structure databases

    ProteinModelPortaliP53091.
    SMRiP53091. Positions 264-400, 508-832.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini525 – 732208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi707 – 7104Arginine finger

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    GeneTreeiENSGT00550000074860.
    HOGENOMiHOG000224130.
    KOiK02542.
    OMAiLHNMIAK.
    OrthoDBiEOG7Z69MX.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR008049. MCM6.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11630:SF43. PTHR11630:SF43. 1 hit.
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01662. MCMPROTEIN6.
    SMARTiSM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53091-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ     50
    PHVSNSQTGP FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV 100
    KKVDDVTGEK VREAFEQFLE DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT 150
    IYIDYQHLSM RENGALAMAI SEQYYRFLPF LQKGLRRVVR KYAPELLNTS 200
    DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN GTSAMATRSI 250
    TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV 300
    RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR 350
    SRFLDWQKVR IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV 400
    EIVVPDVTQL GLPGVKPSST LDTRGISKTT EGLNSGVTGL RSLGVRDLTY 450
    KISFLACHVI SIGSNIGASS PDANSNNRET ELQMAANLQA NNVYQDNERD 500
    QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH EAVKKGILLQ 550
    MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG 600
    KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV 650
    AIHEAMEQQT ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN 700
    MTAPIMSRFD LFFVILDDCN EKIDTELASH IVDLHMKRDE AIEPPFSAEQ 750
    LRRYIKYART FKPILTKEAR SYLVEKYKEL RKDDAQGFSR SSYRITVRQL 800
    ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV DDVEMDEEFD 850
    NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK 900
    KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS 950
    LAEYWEERRL AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV 1000
    IHPNCEVLDQ LEPQDSS 1017
    Length:1,017
    Mass (Da):112,978
    Last modified:October 5, 2010 - v2
    Checksum:i03AB793134E64A50
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791P → A in CAA96913. (PubMed:9169869)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY258324 Genomic DNA. Translation: AAO89010.1.
    Z72723 Genomic DNA. Translation: CAA96913.1.
    Y13624 Genomic DNA. Translation: CAA73947.1.
    BK006941 Genomic DNA. Translation: DAA07914.1.
    PIRiS64219.
    RefSeqiNP_011314.2. NM_001181066.1.

    Genome annotation databases

    EnsemblFungiiYGL201C; YGL201C; YGL201C.
    GeneIDi852673.
    KEGGisce:YGL201C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY258324 Genomic DNA. Translation: AAO89010.1 .
    Z72723 Genomic DNA. Translation: CAA96913.1 .
    Y13624 Genomic DNA. Translation: CAA73947.1 .
    BK006941 Genomic DNA. Translation: DAA07914.1 .
    PIRi S64219.
    RefSeqi NP_011314.2. NM_001181066.1.

    3D structure databases

    ProteinModelPortali P53091.
    SMRi P53091. Positions 264-400, 508-832.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33056. 65 interactions.
    DIPi DIP-1294N.
    IntActi P53091. 54 interactions.
    MINTi MINT-397018.
    STRINGi 4932.YGL201C.

    Proteomic databases

    MaxQBi P53091.
    PaxDbi P53091.
    PeptideAtlasi P53091.
    PRIDEi P53091.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL201C ; YGL201C ; YGL201C .
    GeneIDi 852673.
    KEGGi sce:YGL201C.

    Organism-specific databases

    SGDi S000003169. MCM6.

    Phylogenomic databases

    eggNOGi COG1241.
    GeneTreei ENSGT00550000074860.
    HOGENOMi HOG000224130.
    KOi K02542.
    OMAi LHNMIAK.
    OrthoDBi EOG7Z69MX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30681-MONOMER.

    Miscellaneous databases

    NextBioi 971976.
    PROi P53091.

    Gene expression databases

    Genevestigatori P53091.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR008049. MCM6.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR11630:SF43. PTHR11630:SF43. 1 hit.
    Pfami PF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01662. MCMPROTEIN6.
    SMARTi SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the Saccharomyces cerevisiae MCM6 gene."
      Duina A.A., Winston F.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    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-581.
    5. "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-78 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "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.
    7. "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.
    8. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    9. "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily."
      Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.
      Mol. Gen. Genet. 257:238-248(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017.
      Strain: Sigma 1278B.
    10. "A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae."
      Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.
      Mol. Cell. Biol. 17:3261-3271(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM10.
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "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-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM6_YEAST
    AccessioniPrimary (citable) accession number: P53091
    Secondary accession number(s): D6VTV3, Q870M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 126 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 13400 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3