Aliases for MCM6 Gene
- Minichromosome Maintenance Complex Component 6 2 3 5
- Minichromosome Maintenance Deficient (Mis5, S. Pombe) 6 2 3
- P105MCM 3 4
- MCM6 Minichromosome Maintenance Deficient 6 (MIS5 Homolog, S. Pombe) (S. Cerevisiae) 2
- MCM6 Minichromosome Maintenance Deficient 6 (MIS5 Homolog, S. Pombe) 3
- Minichromosome Maintenance Deficient 6 Homolog (S. Cerevisiae) 2
External Ids for MCM6 Gene
Previous GeneCards Identifiers for MCM6 Gene
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the 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. The MCM complex consisting of this protein and MCM2, 4 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of the complex by CDC2 kinase reduces the helicase activity, suggesting a role in the regulation of DNA replication. Single nucleotide polymorphisms in the intron regions of this gene are associated with differential transcriptional activation of the promoter of the neighboring lactase gene and, thereby, influence lactose intolerance in early adulthood. [provided by RefSeq, May 2012]
GeneCards Summary for MCM6 Gene
MCM6 (Minichromosome Maintenance Complex Component 6) is a Protein Coding gene. Diseases associated with MCM6 include lactase persistence/nonpersistence and lactose intolerance. Among its related pathways are Cell cycle and DNA strand elongation. GO annotations related to this gene include identical protein binding and ATP-dependent DNA helicase activity.
UniProtKB/Swiss-Prot for MCM6 Gene
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.