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Q14566

- MCM6_HUMAN

UniProt

Q14566 - MCM6_HUMAN

Protein

DNA replication licensing factor MCM6

Gene

MCM6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi396 – 4038ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. DNA helicase activity Source: Ensembl
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB
    5. single-stranded DNA binding Source: Ensembl

    GO - Biological processi

    1. DNA replication Source: UniProtKB
    2. DNA replication initiation Source: InterPro
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. DNA unwinding involved in DNA replication Source: Ensembl
    5. G1/S transition of mitotic cell cycle Source: Reactome
    6. mitotic cell cycle Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    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 MCM6 (EC:3.6.4.12)
    Alternative name(s):
    p105MCM
    Gene namesi
    Name:MCM6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6949. MCM6.

    Subcellular locationi

    Nucleus
    Note: Binds to chromatin during G1 and detach from it during S phase.

    GO - Cellular componenti

    1. MCM complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi757 – 7571E → A or D: Impairs interaction with CTD1. 1 Publication
    Mutagenesisi763 – 7631E → A or D: Impairs interaction with CTD1. 1 Publication
    Mutagenesisi766 – 7661L → A: Impairs interaction with CTD1. 1 Publication

    Organism-specific databases

    MIMi223100. phenotype.
    Orphaneti319681. Lactase non-persistence in adulthood.
    PharmGKBiPA30696.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 821821DNA replication licensing factor MCM6PRO_0000194113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei271 – 2711Phosphoserine4 Publications
    Modified residuei643 – 6431N6-acetyllysineBy similarity
    Modified residuei762 – 7621Phosphoserine4 Publications
    Modified residuei791 – 7911Phosphothreonine1 Publication

    Post-translational modificationi

    O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ14566.
    PaxDbiQ14566.
    PeptideAtlasiQ14566.
    PRIDEiQ14566.

    PTM databases

    PhosphoSiteiQ14566.

    Miscellaneous databases

    PMAP-CutDBQ14566.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14566.
    BgeeiQ14566.
    CleanExiHS_MCM6.
    GenevestigatoriQ14566.

    Organism-specific databases

    HPAiCAB009577.
    HPA004818.

    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). May interact with MCM10. Interacts with TIPIN. Interacts with CDT1. Interacts with MCMBP.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-374900,EBI-374900
    Q763532EBI-374900,EBI-6248077From a different organism.
    CDKN2AP427714EBI-374900,EBI-375053
    CDT1Q9H2113EBI-374900,EBI-456953
    MCM10Q7L5902EBI-374900,EBI-374912
    MCM2P497369EBI-374900,EBI-374819
    MCM3P252052EBI-374900,EBI-355153
    MCM7P339935EBI-374900,EBI-355924
    MCMBPQ9BTE315EBI-374900,EBI-749378
    SSRP1Q089452EBI-374900,EBI-353771

    Protein-protein interaction databases

    BioGridi110343. 74 interactions.
    DIPiDIP-31727N.
    IntActiQ14566. 33 interactions.
    MINTiMINT-5004576.
    STRINGi9606.ENSP00000264156.

    Structurei

    Secondary structure

    1
    821
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi709 – 7113
    Beta strandi714 – 7163
    Helixi718 – 73720
    Beta strandi739 – 7413
    Helixi745 – 75612
    Turni757 – 7593
    Helixi763 – 78220
    Helixi793 – 7964

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KLQNMR-A708-821[»]
    2LE8NMR-A708-821[»]
    ProteinModelPortaliQ14566.
    SMRiQ14566. Positions 27-652, 708-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14566.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini346 – 553208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi528 – 5314Arginine finger

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    HOGENOMiHOG000224130.
    HOVERGENiHBG006334.
    InParanoidiQ14566.
    KOiK02542.
    OMAiGTNIRGE.
    OrthoDBiEOG7CCBQC.
    PhylomeDBiQ14566.
    TreeFamiTF105646.

    Family and domain databases

    Gene3Di2.20.28.10. 1 hit.
    2.40.50.140. 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.
    IPR004039. Rubredoxin-type_fold.
    [Graphical view]
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01662. MCMPROTEIN6.
    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.

    Q14566-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLAAAAEPG AGSQHLEVRD EVAEKCQKLF LDFLEEFQSS DGEIKYLQLA    50
    EELIRPERNT LVVSFVDLEQ FNQQLSTTIQ EEFYRVYPYL CRALKTFVKD 100
    RKEIPLAKDF YVAFQDLPTR HKIRELTSSR IGLLTRISGQ VVRTHPVHPE 150
    LVSGTFLCLD CQTVIRDVEQ QFKYTQPNIC RNPVCANRRR FLLDTNKSRF 200
    VDFQKVRIQE TQAELPRGSI PRSLEVILRA EAVESAQAGD KCDFTGTLIV 250
    VPDVSKLSTP GARAETNSRV SGVDGYETEG IRGLRALGVR DLSYRLVFLA 300
    CCVAPTNPRF GGKELRDEEQ TAESIKNQMT VKEWEKVFEM SQDKNLYHNL 350
    CTSLFPTIHG NDEVKRGVLL MLFGGVPKTT GEGTSLRGDI NVCIVGDPST 400
    AKSQFLKHVE EFSPRAVYTS GKASSAAGLT AAVVRDEESH EFVIEAGALM 450
    LADNGVCCID EFDKMDVRDQ VAIHEAMEQQ TISITKAGVK ATLNARTSIL 500
    AAANPISGHY DRSKSLKQNI NLSAPIMSRF DLFFILVDEC NEVTDYAIAR 550
    RIVDLHSRIE ESIDRVYSLD DIRRYLLFAR QFKPKISKES EDFIVEQYKH 600
    LRQRDGSGVT KSSWRITVRQ LESMIRLSEA MARMHCCDEV QPKHVKEAFR 650
    LLNKSIIRVE TPDVNLDQEE EIQMEVDEGA GGINGHADSP APVNGINGYN 700
    EDINQESAPK ASLRLGFSEY CRISNLIVLH LRKVEEEEDE SALKRSELVN 750
    WYLKEIESEI DSEEELINKK RIIEKVIHRL THYDHVLIEL TQAGLKGSTE 800
    GSESYEEDPY LVVNPNYLLE D 821
    Length:821
    Mass (Da):92,889
    Last modified:November 1, 1997 - v1
    Checksum:iF94968EB25A3E501
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti377 – 38711PKTTGEGTSLR → SKDNRRRDLSS in AAC50766. (PubMed:9516426)CuratedAdd
    BLAST
    Sequence conflicti495 – 4951A → T in AAC50766. (PubMed:9516426)Curated
    Sequence conflicti738 – 7381Missing in AAB48165. (PubMed:8977093)Curated
    Sequence conflicti790 – 7901L → P in AAC50766. (PubMed:9516426)Curated

    Polymorphismi

    Intronic variations in MCM6 upstream from the LCT gene are associated with adult-type hypolactasia [MIMi:223100] leading to lactose intolerance, or with lactase persistance. Lactose intolerance is a normal physiological phenomenon caused by developmental down-regulation of lactase activity during childhood or early adulthood. A non-coding variation in MCM6 affects the transcriptional regulation of the LCT gene resulting in down-regulation of lactase activity. However, the majority of Northern Europeans and some African populations have the ability to maintain lactase activity and digest lactose throughout life (lactase persistence).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351E → V.
    Corresponds to variant rs3087355 [ dbSNP | Ensembl ].
    VAR_014816
    Natural varianti806 – 8061E → K.1 Publication
    Corresponds to variant rs4988283 [ dbSNP | Ensembl ].
    VAR_016340

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84557 mRNA. Translation: BAA12699.1.
    U46838 mRNA. Translation: AAC50766.1.
    AY220757 Genomic DNA. Translation: AAO26043.1.
    AK312575 mRNA. Translation: BAG35469.1.
    CH471058 Genomic DNA. Translation: EAX11621.1.
    BC032374 mRNA. Translation: AAH32374.1.
    AH005100 Genomic DNA. Translation: AAB48165.1.
    CCDSiCCDS2179.1.
    RefSeqiNP_005906.2. NM_005915.5.
    UniGeneiHs.444118.

    Genome annotation databases

    EnsembliENST00000264156; ENSP00000264156; ENSG00000076003.
    GeneIDi4175.
    KEGGihsa:4175.
    UCSCiuc002tuw.4. human.

    Polymorphism databases

    DMDMi2497824.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84557 mRNA. Translation: BAA12699.1 .
    U46838 mRNA. Translation: AAC50766.1 .
    AY220757 Genomic DNA. Translation: AAO26043.1 .
    AK312575 mRNA. Translation: BAG35469.1 .
    CH471058 Genomic DNA. Translation: EAX11621.1 .
    BC032374 mRNA. Translation: AAH32374.1 .
    AH005100 Genomic DNA. Translation: AAB48165.1 .
    CCDSi CCDS2179.1.
    RefSeqi NP_005906.2. NM_005915.5.
    UniGenei Hs.444118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KLQ NMR - A 708-821 [» ]
    2LE8 NMR - A 708-821 [» ]
    ProteinModelPortali Q14566.
    SMRi Q14566. Positions 27-652, 708-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110343. 74 interactions.
    DIPi DIP-31727N.
    IntActi Q14566. 33 interactions.
    MINTi MINT-5004576.
    STRINGi 9606.ENSP00000264156.

    Chemistry

    DrugBanki DB01076. Atorvastatin.

    PTM databases

    PhosphoSitei Q14566.

    Polymorphism databases

    DMDMi 2497824.

    Proteomic databases

    MaxQBi Q14566.
    PaxDbi Q14566.
    PeptideAtlasi Q14566.
    PRIDEi Q14566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264156 ; ENSP00000264156 ; ENSG00000076003 .
    GeneIDi 4175.
    KEGGi hsa:4175.
    UCSCi uc002tuw.4. human.

    Organism-specific databases

    CTDi 4175.
    GeneCardsi GC02M136619.
    HGNCi HGNC:6949. MCM6.
    HPAi CAB009577.
    HPA004818.
    MIMi 223100. phenotype.
    601806. gene.
    neXtProti NX_Q14566.
    Orphaneti 319681. Lactase non-persistence in adulthood.
    PharmGKBi PA30696.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOGENOMi HOG000224130.
    HOVERGENi HBG006334.
    InParanoidi Q14566.
    KOi K02542.
    OMAi GTNIRGE.
    OrthoDBi EOG7CCBQC.
    PhylomeDBi Q14566.
    TreeFami TF105646.

    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

    ChiTaRSi MCM6. human.
    EvolutionaryTracei Q14566.
    GeneWikii MCM6.
    GenomeRNAii 4175.
    NextBioi 16446.
    PMAP-CutDB Q14566.
    PROi Q14566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14566.
    Bgeei Q14566.
    CleanExi HS_MCM6.
    Genevestigatori Q14566.

    Family and domain databases

    Gene3Di 2.20.28.10. 1 hit.
    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.
    IPR004039. Rubredoxin-type_fold.
    [Graphical view ]
    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. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HsMCM6: a new member of the human MCM/P1 family encodes a protein homologous to fission yeast Mis5."
      Tsuruga H., Yabuta N., Hosoya S., Tamura K., Endo Y., Nojima H.
      Genes Cells 2:381-399(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-806.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Cervix.
    7. "Characterisation of a human homologue of a yeast cell division cycle gene, MCM6, located adjacent to the 5' end of the lactase gene on chromosome 2q21."
      Harvey C.B., Wang Y., Darmoul D., Phillips A., Mantei N., Swallow D.M.
      FEBS Lett. 398:135-140(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-821.
    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, FUNCTION.
    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. "Identification of a variant associated with adult-type hypolactasia."
      Enattah N.S., Sahi T., Savilahti E., Terwilliger J.D., Peltonen L., Jaervelae I.
      Nat. Genet. 30:233-237(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ADULT-TYPE HYPOLACTASIA.
    11. "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: IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
    12. "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-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
      Chou D.M., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIPIN.
    14. "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: HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    15. Cited for: INVOLVEMENT IN ADULT-TYPE HYPOLACTASIA AND LACTASE PERSISTANCE.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-791, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
      Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
      Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    23. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6."
      Wei Z., Liu C., Wu X., Xu N., Zhou B., Liang C., Zhu G.
      J. Biol. Chem. 285:12469-12473(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 708-821, INTERACTION WITH CDT1, MUTAGENESIS OF GLU-757; GLU-763 AND LEU-766.

    Entry informationi

    Entry nameiMCM6_HUMAN
    AccessioniPrimary (citable) accession number: Q14566
    Secondary accession number(s): B2R6H2, Q13504, Q99859
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3