Q62724
uniprot
Q62724
canonical
amino_acid_sequence
LRDEEQTAESIKNQMTVKEWEKVFEMSQDQNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVDEFSPRAVYTSGKASSASGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDMRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVSGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKRLRQRDGSGITKSSWRITVRQLESMIRLSESMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMETDEGPGGINGHADSPAPVNGFNGSGEDASQETVPKPSLRLAFAEYCRISNLIVLHLRKMEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVVHRLTHYDHVLIELTQAGLKGSSEGSESYEEDPYLVVNPNYLLED
uniprot
proteins
ec_number
3.6.4.12
uniprot
proteins
function
FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. 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. {ECO:0000250|UniProtKB:Q14566}.
uniprot
proteins
mass_dalton
57370
uniprot
proteins
post_translational_modification
PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250|UniProtKB:Q14566}.
uniprot
proteins
protein_family
MCM family
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7590274
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14566}. Chromosome {ECO:0000250|UniProtKB:Q14566}. Note=Binds to chromatin during G1 and detaches from it during S phase. {ECO:0000250|UniProtKB:Q14566}.
uniprot
proteins