MCM3

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Minichromosome maintenance complex component 3
Identifiers
Symbols MCM3 ; HCC5; P1-MCM3; P1.h; RLFB
External IDs OMIM602693 MGI101845 HomoloGene1791 GeneCards: MCM3 Gene
EC number 3.6.4.12
RNA expression pattern
PBB GE MCM3 201555 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4172 17215
Ensembl ENSG00000112118 ENSMUSG00000041859
UniProt P25205 P25206
RefSeq (mRNA) NM_001270472 NM_008563
RefSeq (protein) NP_001257401 NP_032589
Location (UCSC) Chr 6:
52.13 – 52.15 Mb
Chr 1:
20.8 – 20.82 Mb
PubMed search [1] [2]

DNA replication licensing factor MCM3 is a protein that in humans is encoded by the MCM3 gene.[1]

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 is a subunit of the protein complex that consists of MCM2-7. It has been shown to interact directly with MCM5/CDC46. This protein also interacts with, and thus is acetlyated by MCM3AP, a chromatin-associated acetyltransferase. The acetylation of this protein inhibits the initiation of DNA replication and cell cycle progression.[2]

See also[edit]

Interactions[edit]

MCM3 has been shown to interact with:

References[edit]

  1. ^ Thommes P, Fett R, Schray B, Burkhart R, Barnes M, Kennedy C, Brown NC, Knippers R (April 1992). "Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein". Nucleic Acids Res 20 (5): 1069–74. doi:10.1093/nar/20.5.1069. PMC 312092. PMID 1549468. 
  2. ^ "Entrez Gene: MCM3 MCM3 minichromosome maintenance deficient 3 (S. cerevisiae)". 
  3. ^ a b c d e f g Kneissl M, Pütter V, Szalay AA, Grummt F (March 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. 
  4. ^ a b Fujita M, Yamada C, Goto H, Yokoyama N, Kuzushima K, Inagaki M, Tsurumi T (September 1999). "Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation". J. Biol. Chem. 274 (36): 25927–32. doi:10.1074/jbc.274.36.25927. PMID 10464337. 
  5. ^ Méndez J, Stillman B (November 2000). "Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis". Mol. Cell. Biol. 20 (22): 8602–12. doi:10.1128/mcb.20.22.8602-8612.2000. PMC 102165. PMID 11046155. 
  6. ^ Takei Y, Assenberg M, Tsujimoto G, Laskey R (November 2002). "The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA replication via interaction with MCM3". J. Biol. Chem. 277 (45): 43121–5. doi:10.1074/jbc.C200442200. PMID 12226073. 
  7. ^ Kuwahara K, Yoshida M, Kondo E, Sakata A, Watanabe Y, Abe E, Kouno Y, Tomiyasu S, Fujimura S, Tokuhisa T, Kimura H, Ezaki T, Sakaguchi N (April 2000). "A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein essential for DNA replication". Blood 95 (7): 2321–8. PMID 10733502. 
  8. ^ Takei Y, Tsujimoto G (August 1998). "Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization". J. Biol. Chem. 273 (35): 22177–80. doi:10.1074/jbc.273.35.22177. PMID 9712829. 
  9. ^ DaFonseca CJ, Shu F, Zhang JJ (March 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. ^ Fujita M, Kiyono T, Hayashi Y, Ishibashi M (April 1997). "In vivo interaction of human MCM heterohexameric complexes with chromatin. Possible involvement of ATP". J. Biol. Chem. 272 (16): 10928–35. PMID 9099751. 
  11. ^ Fujita M, Ishimi Y, Nakamura H, Kiyono T, Tsurumi T (March 2002). "Nuclear organization of DNA replication initiation proteins in mammalian cells". J. Biol. Chem. 277 (12): 10354–61. doi:10.1074/jbc.M111398200. PMID 11779870. 

Further reading[edit]