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P49736

- MCM2_HUMAN

UniProt

P49736 - MCM2_HUMAN

Protein

DNA replication licensing factor MCM2

Gene

MCM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (16 Jan 2004)
      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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
    BLAST
    Nucleotide bindingi523 – 5308ATPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: ProtInc
    2. cellular response to interleukin-4 Source: Ensembl
    3. DNA replication Source: Reactome
    4. DNA replication initiation Source: UniProtKB
    5. DNA strand elongation involved in DNA replication Source: Reactome
    6. DNA unwinding involved in DNA replication Source: Ensembl
    7. G1/S transition of mitotic cell cycle Source: Reactome
    8. mitotic cell cycle Source: Reactome
    9. nucleosome assembly Source: Ensembl

    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

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_207. Removal of licensing factors from origins.
    REACT_2148. Switching of origins to a post-replicative state.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_6776. Unwinding of DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM2 (EC:3.6.4.12)
    Alternative name(s):
    Minichromosome maintenance protein 2 homolog
    Nuclear protein BM28
    Gene namesi
    Name:MCM2
    Synonyms:BM28, CCNL1, CDCL1, KIAA0030
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6944. MCM2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. cytoplasm Source: HPA
    3. MCM complex Source: UniProtKB
    4. microtubule cytoskeleton Source: HPA
    5. nuclear origin of replication recognition complex Source: Ensembl
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139. 1 Publication
    Mutagenesisi41 – 411S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139. 1 Publication
    Mutagenesisi108 – 1081S → A: Reduces phosphorylation by ATR. 1 Publication
    Mutagenesisi139 – 1391S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41. 1 Publication

    Organism-specific databases

    PharmGKBiPA164742061.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 904903DNA replication licensing factor MCM2PRO_0000194087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei13 – 131Phosphoserine2 Publications
    Modified residuei26 – 261Phosphoserine2 Publications
    Modified residuei27 – 271Phosphoserine5 Publications
    Modified residuei39 – 391Phosphothreonine1 Publication
    Modified residuei40 – 401Phosphoserine; by CDC72 Publications
    Modified residuei41 – 411Phosphoserine5 Publications
    Modified residuei53 – 531Phosphoserine; by CDC73 Publications
    Modified residuei59 – 591Phosphothreonine1 Publication
    Modified residuei108 – 1081Phosphoserine; by ATR5 Publications
    Modified residuei139 – 1391Phosphoserine5 Publications
    Modified residuei216 – 2161N6-acetyllysine1 Publication
    Modified residuei381 – 3811Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49736.
    PaxDbiP49736.
    PeptideAtlasiP49736.
    PRIDEiP49736.

    PTM databases

    PhosphoSiteiP49736.

    Miscellaneous databases

    PMAP-CutDBP49736.

    Expressioni

    Gene expression databases

    ArrayExpressiP49736.
    BgeeiP49736.
    CleanExiHS_CCNL1.
    HS_MCM2.
    GenevestigatoriP49736.

    Organism-specific databases

    HPAiCAB000303.
    HPA031495.
    HPA031496.

    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 (By simililarity). Interacts with DBF4 By similarity. Interacts with KAT7. May interact with MCM10.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628053EBI-374819,EBI-302023
    MCM3P252055EBI-374819,EBI-355153
    MCM5P339925EBI-374819,EBI-359410
    MCM6Q145669EBI-374819,EBI-374900
    MCM7P3399321EBI-374819,EBI-355924
    MCMBPQ9BTE34EBI-374819,EBI-749378
    SNF8Q96H208EBI-374819,EBI-747719

    Protein-protein interaction databases

    BioGridi110339. 85 interactions.
    DIPiDIP-31732N.
    IntActiP49736. 45 interactions.
    MINTiMINT-5004296.
    STRINGi9606.ENSP00000265056.

    Structurei

    3D structure databases

    ProteinModelPortaliP49736.
    SMRiP49736. Positions 199-798.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini473 – 679207MCMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 257256Interaction with KAT7By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi655 – 6584Arginine finger

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1241.
    HOVERGENiHBG106398.
    InParanoidiP49736.
    KOiK02540.
    OMAiNMEETVY.
    OrthoDBiEOG71VSRZ.
    PhylomeDBiP49736.
    TreeFamiTF300772.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49736-1 [UniParc]FASTAAdd to Basket

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    MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE    50
    DESEGLLGTE GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE 100
    DVEELTASQR EAAERAMRQR DREAGRGLGR MRRGLLYDSD EEDEERPARK 150
    RRQVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK 200
    NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE 250
    APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL 300
    HLNQLIRTSG VVTSCTGVLP QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG 350
    SCPECQSAGP FEVNMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA 400
    DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATVIL ANHVAKKDNK 450
    VAVGELTDED VKMITSLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF 500
    GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG 550
    ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI 600
    HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT 650
    EPIISRFDIL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS 700
    AAEPAMPNTY GVEPLPQEVL KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL 750
    RKESMATGSI PITVRHIESM IRMAEAHARI HLRDYVIEDD VNMAIRVMLE 800
    SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV AEQVTYQRNR 850
    FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI 900
    LQQF 904
    Length:904
    Mass (Da):101,896
    Last modified:January 16, 2004 - v4
    Checksum:i52C6DC61F128B404
    GO

    Sequence cautioni

    The sequence CAA47749.1 differs from that shown. Reason: Frameshift at positions 115, 124, 127, 129, 154, 158, 773 and 811.
    The sequence BAA04642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA12177.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA47749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → S in CAA47749. (PubMed:8175912)Curated
    Sequence conflicti109 – 1091Q → R in CAA47749. (PubMed:8175912)Curated
    Sequence conflicti388 – 3881G → R in CAA47749. (PubMed:8175912)Curated
    Sequence conflicti407 – 4082KP → NA in CAA47749. (PubMed:8175912)Curated
    Sequence conflicti407 – 4082KP → NA in BAA12177. 1 PublicationCurated
    Sequence conflicti495 – 4951L → P in CAA47749. (PubMed:8175912)Curated
    Sequence conflicti555 – 5562GL → AV in CAA47749. (PubMed:8175912)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681D → E.1 Publication
    Corresponds to variant rs3087452 [ dbSNP | Ensembl ].
    VAR_021111
    Natural varianti135 – 1351L → F.1 Publication
    Corresponds to variant rs2307314 [ dbSNP | Ensembl ].
    VAR_021112
    Natural varianti166 – 1661E → Q.1 Publication
    Corresponds to variant rs1048225 [ dbSNP | Ensembl ].
    VAR_033298
    Natural varianti396 – 3961A → T.1 Publication
    Corresponds to variant rs3087450 [ dbSNP | Ensembl ].
    VAR_016137
    Natural varianti501 – 5011G → R.1 Publication
    Corresponds to variant rs13087457 [ dbSNP | Ensembl ].
    VAR_033299
    Natural varianti667 – 6671V → M.1 Publication
    Corresponds to variant rs2307311 [ dbSNP | Ensembl ].
    VAR_016138
    Natural varianti727 – 7271A → T.2 Publications
    Corresponds to variant rs2307313 [ dbSNP | Ensembl ].
    VAR_016139

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67334 mRNA. Translation: CAA47749.1. Sequence problems.
    D21063 mRNA. Translation: BAA04642.1. Different initiation.
    AY675259 Genomic DNA. Translation: AAT70723.1.
    BC006165 mRNA. Translation: AAH06165.3.
    BC007670 mRNA. Translation: AAH07670.2.
    BC007938 mRNA. Translation: AAH07938.2.
    BC014272 mRNA. Translation: AAH14272.2.
    BC017258 mRNA. Translation: AAH17258.2.
    BC017490 mRNA. Translation: AAH17490.2.
    BC030131 mRNA. Translation: AAH30131.2.
    D83987 mRNA. Translation: BAA12177.1. Different initiation.
    BT009734 mRNA. Translation: AAP88736.1.
    CCDSiCCDS3043.1.
    PIRiS42228.
    RefSeqiNP_004517.2. NM_004526.3.
    UniGeneiHs.477481.

    Genome annotation databases

    EnsembliENST00000265056; ENSP00000265056; ENSG00000073111.
    GeneIDi4171.
    KEGGihsa:4171.
    UCSCiuc003ejp.4. human.

    Polymorphism databases

    DMDMi41019490.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67334 mRNA. Translation: CAA47749.1 . Sequence problems.
    D21063 mRNA. Translation: BAA04642.1 . Different initiation.
    AY675259 Genomic DNA. Translation: AAT70723.1 .
    BC006165 mRNA. Translation: AAH06165.3 .
    BC007670 mRNA. Translation: AAH07670.2 .
    BC007938 mRNA. Translation: AAH07938.2 .
    BC014272 mRNA. Translation: AAH14272.2 .
    BC017258 mRNA. Translation: AAH17258.2 .
    BC017490 mRNA. Translation: AAH17490.2 .
    BC030131 mRNA. Translation: AAH30131.2 .
    D83987 mRNA. Translation: BAA12177.1 . Different initiation.
    BT009734 mRNA. Translation: AAP88736.1 .
    CCDSi CCDS3043.1.
    PIRi S42228.
    RefSeqi NP_004517.2. NM_004526.3.
    UniGenei Hs.477481.

    3D structure databases

    ProteinModelPortali P49736.
    SMRi P49736. Positions 199-798.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110339. 85 interactions.
    DIPi DIP-31732N.
    IntActi P49736. 45 interactions.
    MINTi MINT-5004296.
    STRINGi 9606.ENSP00000265056.

    PTM databases

    PhosphoSitei P49736.

    Polymorphism databases

    DMDMi 41019490.

    Proteomic databases

    MaxQBi P49736.
    PaxDbi P49736.
    PeptideAtlasi P49736.
    PRIDEi P49736.

    Protocols and materials databases

    DNASUi 4171.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265056 ; ENSP00000265056 ; ENSG00000073111 .
    GeneIDi 4171.
    KEGGi hsa:4171.
    UCSCi uc003ejp.4. human.

    Organism-specific databases

    CTDi 4171.
    GeneCardsi GC03P127317.
    HGNCi HGNC:6944. MCM2.
    HPAi CAB000303.
    HPA031495.
    HPA031496.
    MIMi 116945. gene.
    neXtProti NX_P49736.
    PharmGKBi PA164742061.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOVERGENi HBG106398.
    InParanoidi P49736.
    KOi K02540.
    OMAi NMEETVY.
    OrthoDBi EOG71VSRZ.
    PhylomeDBi P49736.
    TreeFami TF300772.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_207. Removal of licensing factors from origins.
    REACT_2148. Switching of origins to a post-replicative state.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_6776. Unwinding of DNA.

    Miscellaneous databases

    GeneWikii MCM2.
    GenomeRNAii 4171.
    NextBioi 16428.
    PMAP-CutDB P49736.
    PROi P49736.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49736.
    Bgeei P49736.
    CleanExi HS_CCNL1.
    HS_MCM2.
    Genevestigatori P49736.

    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. "A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division."
      Todorov I.T., Pepperkok R., Philipova R.N., Kearsey S.E., Ansorge W., Werner D.
      J. Cell Sci. 107:253-265(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, VARIANT GLN-166.
      Tissue: Colon carcinoma.
    2. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-68; PHE-135; THR-396; MET-667 AND THR-727.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-501 AND THR-727.
      Tissue: Brain, Lung, Lymph, Muscle, Placenta and Uterus.
    5. "Homo sapiens DNA replication licensing factor (huMCM2)."
      Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-904.
      Tissue: Cervix carcinoma.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-904.
    7. "The human gene for nuclear protein BM28 (CDCL1), a new member of the early S-phase family of proteins, maps to chromosome band 3q21."
      Mincheva A., Todorov I.T., Werner D., Fink T.M., Lichter P.
      Cytogenet. Cell Genet. 65:276-277(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL LOCATION.
    8. "A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex."
      Ishimi Y.
      J. Biol. Chem. 272:24508-24513(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX.
    9. "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase."
      Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., Hurwitz J., Yatagai F., Hanaoka F.
      Nucleic Acids Res. 28:4769-4777(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM10.
    10. "Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases."
      Cortez D., Glick G., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-108, MUTAGENESIS OF SER-108.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells."
      Tsuji T., Ficarro S.B., Jiang W.
      Mol. Biol. Cell 17:4459-4472(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-27; SER-41; SER-53; SER-108 AND SER-139, MUTAGENESIS OF SER-27; SER-41 AND SER-139, IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
    13. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT7.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    16. "Cdc7 is an active kinase in human cancer cells undergoing replication stress."
      Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.
      J. Biol. Chem. 282:208-215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-40 AND SER-53.
    17. "Identification and characterization of a novel component of the human minichromosome maintenance complex."
      Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.
      Mol. Cell. Biol. 27:3044-3055(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    21. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-39; SER-40; SER-41; SER-53 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-59; SER-108 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; SER-41; SER-108 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-26; SER-27; SER-41; SER-139 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM2_HUMAN
    AccessioniPrimary (citable) accession number: P49736
    Secondary accession number(s): Q14577
    , Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    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. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3