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P24279

- MCM3_YEAST

UniProt

P24279 - MCM3_YEAST

Protein

DNA replication licensing factor MCM3

Gene

MCM3

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 144 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      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. Necessary for cell growth.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi409 – 4168ATPSequence 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. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromatin silencing at silent mating-type cassette Source: SGD
    3. chromatin silencing at telomere Source: SGD
    4. DNA duplex unwinding Source: GOC
    5. DNA replication initiation Source: SGD
    6. DNA strand elongation involved in DNA replication Source: SGD
    7. double-strand break repair via break-induced replication Source: SGD
    8. nuclear cell cycle DNA replication Source: SGD
    9. pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30154-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM3 (EC:3.6.4.12)
    Alternative name(s):
    Minichromosome maintenance protein 3
    Gene namesi
    Name:MCM3
    Ordered Locus Names:YEL032W
    ORF Names:SYGP-ORF23
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYEL032w.
    SGDiS000000758. MCM3.

    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
    Mutagenesisi415 – 4151K → A: No effect on MCM2-7 complex helicase activity. Loss of MCM2-7 complex helicase activity; when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity; when asscociated with MCM2 A-549. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 971971DNA replication licensing factor MCM3PRO_0000194099Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei761 – 7611Phosphoserine1 Publication
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei781 – 7811Phosphoserine2 Publications
    Modified residuei868 – 8681Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP24279.
    PaxDbiP24279.
    PeptideAtlasiP24279.

    Expressioni

    Gene expression databases

    GenevestigatoriP24279.

    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 CSM1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSM1P256512EBI-10541,EBI-22001
    MCM5P294964EBI-10541,EBI-10549

    Protein-protein interaction databases

    BioGridi36697. 51 interactions.
    DIPiDIP-2407N.
    IntActiP24279. 30 interactions.
    MINTiMINT-699197.
    STRINGi4932.YEL032W.

    Structurei

    3D structure databases

    ProteinModelPortaliP24279.
    SMRiP24279. Positions 96-569.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini359 – 566208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi541 – 5444Arginine finger

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    GeneTreeiENSGT00550000075022.
    HOGENOMiHOG000224126.
    KOiK02541.
    OMAiVLRTHRY.
    OrthoDBiEOG7B5X4C.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR008046. Mcm3.
    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.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01659. MCMPROTEIN3.
    SMARTiSM00382. AAA. 1 hit.
    SM00350. 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.

    P24279-1 [UniParc]FASTAAdd to Basket

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    MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS    50
    NNAANYNDDQ DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL 100
    DDLREFDRSF WSGILVEPAY FIPPAEKALT DLADSMDDVP HPNASAVSSR 150
    HPWKLSFKGS FGAHALSPRT LTAQHLNKLV SVEGIVTKTS LVRPKLIRSV 200
    HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK LTTEYGYSTF 250
    IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS 300
    LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI 350
    NKLSKKKDIF DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR 400
    GDINILMVGD PSTAKSQLLR FVLNTASLAI ATTGRGSSGV GLTAAVTTDR 450
    ETGERRLEAG AMVLADRGVV CIDEFDKMTD VDRVAIHEVM EQQTVTIAKA 500
    GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL SRFDLLFVVT 550
    DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP 600
    EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL 650
    VTIPFLRKYV QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR 700
    TLETLIRLAT AHAKVRLSKT VNKVDAKVAA NLLRFALLGE DIGNDIDEEE 750
    SEYEEALSKR SPQKSPKKRQ RVRQPASNSG SPIKSTPRRS TASSVNATPS 800
    SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL GLRVSPRRRE 850
    HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST 900
    GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA 950
    GLKIMSDRNN LMVADDKVWR V 971
    Length:971
    Mass (Da):107,518
    Last modified:March 1, 1992 - v1
    Checksum:i43DD4DACAF4456DC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53540 Genomic DNA. Translation: CAA37616.1.
    U18779 Genomic DNA. Translation: AAB65010.1.
    BK006939 Genomic DNA. Translation: DAA07621.1.
    PIRiA36376.
    RefSeqiNP_010882.1. NM_001178847.1.

    Genome annotation databases

    EnsemblFungiiYEL032W; YEL032W; YEL032W.
    GeneIDi856680.
    KEGGisce:YEL032W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53540 Genomic DNA. Translation: CAA37616.1 .
    U18779 Genomic DNA. Translation: AAB65010.1 .
    BK006939 Genomic DNA. Translation: DAA07621.1 .
    PIRi A36376.
    RefSeqi NP_010882.1. NM_001178847.1.

    3D structure databases

    ProteinModelPortali P24279.
    SMRi P24279. Positions 96-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36697. 51 interactions.
    DIPi DIP-2407N.
    IntActi P24279. 30 interactions.
    MINTi MINT-699197.
    STRINGi 4932.YEL032W.

    Proteomic databases

    MaxQBi P24279.
    PaxDbi P24279.
    PeptideAtlasi P24279.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL032W ; YEL032W ; YEL032W .
    GeneIDi 856680.
    KEGGi sce:YEL032W.

    Organism-specific databases

    CYGDi YEL032w.
    SGDi S000000758. MCM3.

    Phylogenomic databases

    eggNOGi COG1241.
    GeneTreei ENSGT00550000075022.
    HOGENOMi HOG000224126.
    KOi K02541.
    OMAi VLRTHRY.
    OrthoDBi EOG7B5X4C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30154-MONOMER.

    Miscellaneous databases

    NextBioi 982707.
    PROi P24279.

    Gene expression databases

    Genevestigatori P24279.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR008046. Mcm3.
    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.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01659. MCMPROTEIN3.
    SMARTi SM00382. AAA. 1 hit.
    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. "The phenotype of the minichromosome maintenance mutant mcm3 is characteristic of mutants defective in DNA replication."
      Gibson S.T., Suroski R.T., Tye B.K.
      Mol. Cell. Biol. 10:5707-5720(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. 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-868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    4. "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(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "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-415.
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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.
    8. "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.
    9. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex."
      Wysocka M., Rytka J., Kurlandzka A.
      Exp. Cell Res. 294:592-602(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSM1.
    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-761 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM3_YEAST
    AccessioniPrimary (citable) accession number: P24279
    Secondary accession number(s): D3DLL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 35100 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. 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3