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MGP001885

UniProt Annotations

Entry Information
Gene Nameminichromosome maintenance complex component 2
Protein EntryMCM2_HUMAN
UniProt IDP49736
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityATP + H(2)O = ADP + phosphate.
FunctionActs 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. Required for the entry in S phase and for cell division. {ECO:0000269|PubMed:8175912}.
InteractionP62805:HIST2H4B; NbExp=3; IntAct=EBI-374819, EBI-302023; P25205:MCM3; NbExp=5; IntAct=EBI-374819, EBI-355153; P33992:MCM5; NbExp=5; IntAct=EBI-374819, EBI-359410; Q14566:MCM6; NbExp=9; IntAct=EBI-374819, EBI-374900; P33993:MCM7; NbExp=21; IntAct=EBI-374819, EBI-355924; Q9BTE3:MCMBP; NbExp=4; IntAct=EBI-374819, EBI-749378; Q96H20:SNF8; NbExp=8; IntAct=EBI-374819, EBI-747719;
MiscellaneousEarly 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.
PtmPhosphorylated on Ser-108 by ATR in proliferating cells. Ser- 108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication. {ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:16964243, ECO:0000269|PubMed:17062569, ECO:0000269|PubMed:17525332, ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:21406692}.
Sequence CautionSequence=BAA04642.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=BAA12177.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=CAA47749.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=CAA47749.1; Type=Frameshift; Positions=115, 124, 127, 129, 154, 158, 773, 811; Evidence={ECO:0000305};
SimilarityBelongs to the MCM family. {ECO:0000305}.
SimilarityContains 1 MCM domain. {ECO:0000305}.
Subcellular LocationNucleus {ECO:0000269|PubMed:8175912}.
SubunitComponent 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). Interacts with DBF4 (By similarity). Interacts with KAT7. May interact with MCM10. {ECO:0000250, ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:17296731, ECO:0000269|PubMed:9305914}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mcm2/";
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