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P55861

- MCM2_XENLA

UniProt

P55861 - MCM2_XENLA

Protein

DNA replication licensing factor mcm2

Gene

mcm2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      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. Required for the entry in S phase and for cell division.3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri314 – 34027C4-typeSequence AnalysisAdd
    BLAST
    Nucleotide bindingi508 – 5158ATPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell cycle Source: UniProtKB-KW
    3. DNA replication initiation Source: InterPro
    4. DNA unwinding involved in DNA replication Source: UniProtKB
    5. regulation of DNA-dependent DNA replication initiation Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor mcm2 (EC:3.6.4.12)
    Alternative name(s):
    BM28-homolog
    Minichromosome maintenance protein 2
    Short name:
    xMCM2
    p112
    Gene namesi
    Name:mcm2
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-999979. mcm2.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses.

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. MCM complex Source: UniProtKB
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 886886DNA replication licensing factor mcm2PRO_0000194089Add
    BLAST

    Post-translational modificationi

    May be in a phosphorylated state in the mitotic mcm complex. Phosphorylated in the interphase mcm complex. Phosphorylated by the cdc7-dbf4 and cdc7-dbf4b complexes.2 Publications

    Proteomic databases

    PRIDEiP55861.

    Interactioni

    Subunit structurei

    Component of the mcm2-7 complex (RLF-M). The complex forms a toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (By simililarity).5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mmcm3P497399EBI-876864,EBI-491720

    Protein-protein interaction databases

    BioGridi98693. 9 interactions.
    IntActiP55861. 7 interactions.
    MINTiMINT-6540654.

    Structurei

    3D structure databases

    ProteinModelPortaliP55861.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 665208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi640 – 6434Arginine finger

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri314 – 34027C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    HOVERGENiHBG106398.
    KOiK02540.

    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. 1 hit.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P55861-1 [UniParc]FASTAAdd to Basket

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    MADSSESFNI ATSPRAGSRR DALTSSPGRD LPPFEDESEG MFGDGVVPEE    50
    EEDGEELIGD AMERDYRPIS ELDRYEVEGL DDEEDVEDLT ASQREAAEQS 100
    MRMRDREMGR ELGRMRRGLL YDSDEEEEDR PARKRRMAER AAEGAPEEDE 150
    EMIESIENLE DMKGHTVREW VSMAATRLEI YHRFKNFLRT HVDEHGHNVF 200
    KEKISDMCKE NKESLPVNYE DLAAREHVLA YFLPEAPAEM LKIFDEAAKE 250
    VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC 300
    TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVRPGSCPEC QSFGPFEINM 350
    EETVYQNYQR ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT 400
    GIYHNNYDGS LNTANGFPVF ATVILANHIT KKDDKVAVGE LTDEDVKAIV 450
    ALSKDERIGE RIFASIAPSI YGHEDIKRGL ALALFGGEAK NPGGKHKVRG 500
    DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG LTAYVQRHPV 550
    TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG 600
    IVTSLQARCT VIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD 650
    TVDPVQDEML ARFVVSSHIK HHPSSKDIAN GDAAEFALPN TFGVEALPQE 700
    VLKKYIMYAK EKIRPKLNQM DQDKVAKMYS DLRKESMATG SIPITVRHIE 750
    SMIRMAEAHA RMHLRDYVVE DDVNMAIRVM LESFIDTQKF SVMRSMRKTF 800
    ARYLAFRRDN NELLLFVLKQ LIAEQVTYQR NRYGAQQDTI EVPEKDLVDK 850
    ARQINIHNLS AFYDSDLFKM NKFTHDVKKK LIIQQF 886
    Length:886
    Mass (Da):100,262
    Last modified:June 13, 2006 - v2
    Checksum:i524C7B3673E2B2DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691E → K in AAC60223. (PubMed:9214647)Curated
    Sequence conflicti439 – 4391G → R in BAA09948. (PubMed:8917078)Curated
    Sequence conflicti563 – 5631L → F in BAA09948. (PubMed:8917078)Curated
    Sequence conflicti728 – 7281M → I in BAA09948. (PubMed:8917078)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63919 mRNA. Translation: BAA09948.1.
    U44047 mRNA. Translation: AAC60223.1.
    BC046274 mRNA. Translation: AAH46274.1.
    PIRiJC5085.
    RefSeqiNP_001080759.1. NM_001087290.1.
    UniGeneiXl.382.

    Genome annotation databases

    GeneIDi380451.
    KEGGixla:380451.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63919 mRNA. Translation: BAA09948.1 .
    U44047 mRNA. Translation: AAC60223.1 .
    BC046274 mRNA. Translation: AAH46274.1 .
    PIRi JC5085.
    RefSeqi NP_001080759.1. NM_001087290.1.
    UniGenei Xl.382.

    3D structure databases

    ProteinModelPortali P55861.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 98693. 9 interactions.
    IntActi P55861. 7 interactions.
    MINTi MINT-6540654.

    Proteomic databases

    PRIDEi P55861.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 380451.
    KEGGi xla:380451.

    Organism-specific databases

    CTDi 4171.
    Xenbasei XB-GENE-999979. mcm2.

    Phylogenomic databases

    HOVERGENi HBG106398.
    KOi K02540.

    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. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of two Xenopus laevis genes, xMCM2 and xCDC46, with sequence homology to MCM genes involved in DNA replication."
      Miyake S., Saito I., Kobayashi H., Yamashita S.
      Gene 175:71-75(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH MCM5.
      Tissue: Oocyte.
    2. "Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins in Xenopus eggs."
      Kubota Y., Mimura S., Nishimoto S., Masuda T., Nojima H., Takisawa H.
      EMBO J. 16:3320-3331(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7, SUBCELLULAR LOCATION.
      Tissue: Oocyte.
    3. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    4. "The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides."
      Thommes P., Kubota Y., Takisawa H., Blow J.J.
      EMBO J. 16:3312-3319(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, SUBCELLULAR LOCATION.
    5. "Evidence for different MCM subcomplexes with differential binding to chromatin in Xenopus."
      Coue M., Amariglio F., Maiorano D., Bocquet S., Mechali M.
      Exp. Cell Res. 245:282-289(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN MCM COMPLEXES.
    6. "Distinct phosphoisoforms of the Xenopus Mcm4 protein regulate the function of the Mcm complex."
      Pereverzeva I., Whitmire E., Khan B., Coue M.
      Mol. Cell. Biol. 20:3667-3676(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    7. "The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding."
      Ying C.Y., Gautier J.
      EMBO J. 24:4334-4344(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE MCM2-7 COMPLEX, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7.
    8. "Cdc7-Drf1 is a developmentally regulated protein kinase required for the initiation of vertebrate DNA replication."
      Takahashi T.S., Walter J.C.
      Genes Dev. 19:2295-2300(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.

    Entry informationi

    Entry nameiMCM2_XENLA
    AccessioniPrimary (citable) accession number: P55861
    Secondary accession number(s): O42588, Q7ZX05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3