MCM2

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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DNA replication licensing factor MCM2 is a protein that in humans is encoded by the MCM2 gene.[1][2]

Function

The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein forms a complex with MCM4, 6, and 7, and has been shown to regulate the helicase activity of the complex. This protein is phosphorylated, and thus regulated by, protein kinases CDC2 and CDC7.[3]

Interactions

MCM2 has been shown to interact with:

See also

References

  1. Todorov IT, Lavigne J, Sakr F, Kaneva R, Foisy S, Bibor-Hardy V (Jul 1991). "Nuclear matrix protein mitotin messenger RNA is expressed at constant levels during the cell cycle". Biochem Biophys Res Commun. 177 (1): 395–400. doi:10.1016/0006-291X(91)91996-P. PMID 1710453.
  2. Mincheva A, Todorov I, Werner D, Fink TM, Lichter P (Jan 1994). "The human gene for nuclear protein BM28 (CDCL1), a new member of the early S-phase family of proteins, maps to chromosome band 3q21". Cytogenet Cell Genet. 65 (4): 276–7. doi:10.1159/000133647. PMID 8258304.
  3. "Entrez Gene: MCM2 MCM2 minichromosome maintenance deficient 2, mitotin (S. cerevisiae)".
  4. Eide T, Taskén KA, Carlson C, Williams G, Jahnsen T, Taskén K, Collas P (Jul 2003). "Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication". J. Biol. Chem. 278 (29): 26750–6. doi:10.1074/jbc.M300765200. PMID 12740381.
  5. 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 Kneissl M, Pütter V, Szalay AA, Grummt F (Mar 2003). "Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells". J. Mol. Biol. 327 (1): 111–28. doi:10.1016/s0022-2836(03)00079-2. PMID 12614612.
  6. 6.0 6.1 6.2 Yabuta N, Kajimura N, Mayanagi K, Sato M, Gotow T, Uchiyama Y, Ishimi Y, Nojima H (May 2003). "Mammalian Mcm2/4/6/7 complex forms a toroidal structure". Genes Cells. 8 (5): 413–21. doi:10.1046/j.1365-2443.2003.00645.x. PMID 12694531.
  7. 7.0 7.1 7.2 You Z, Komamura Y, Ishimi Y (Dec 1999). "Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity". Mol. Cell. Biol. 19 (12): 8003–15. PMC 84885. PMID 10567526.
  8. Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (Sep 1996). "Binding of human minichromosome maintenance proteins with histone H3". J. Biol. Chem. 271 (39): 24115–22. doi:10.1074/jbc.271.39.24115. PMID 8798650.
  9. DaFonseca CJ, Shu F, Zhang JJ (Mar 2001). "Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3034–9. doi:10.1073/pnas.061487598. PMC 30602. PMID 11248027.
  10. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  11. 11.0 11.1 You Z, Ishimi Y, Masai H, Hanaoka F (Nov 2002). "Roles of Mcm7 and Mcm4 subunits in the DNA helicase activity of the mouse Mcm4/6/7 complex". J. Biol. Chem. 277 (45): 42471–9. doi:10.1074/jbc.M205769200. PMID 12207017.
  12. Fujita M, Kiyono T, Hayashi Y, Ishibashi M (Apr 1997). "In vivo interaction of human MCM heterohexameric complexes with chromatin. Possible involvement of ATP". J. Biol. Chem. 272 (16): 10928–35. doi:10.1074/jbc.272.16.10928. PMID 9099751.

Further reading