{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P49736","secondaryAccessions":["Q14577","Q15023","Q8N2V1","Q969W7","Q96AE1","Q9BRM7"],"uniProtkbId":"MCM2_HUMAN","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-01-16","entryVersion":249,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA replication licensing factor MCM2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32453425"}],"value":"3.6.4.12"}]},"alternativeNames":[{"fullName":{"value":"Minichromosome maintenance protein 2 homolog"}},{"fullName":{"value":"Nuclear protein BM28"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6944"}],"value":"MCM2"},"synonyms":[{"value":"BM28"},{"value":"CCNL1"},{"value":"CDCL1"},{"value":"KIAA0030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26196677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32453425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34694004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34700328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35585232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8175912"}],"value":"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 (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). 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 (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"3.6.4.12","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32453425"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:13066"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32453425"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P55861"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11095689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16899510"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17296731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28191891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32453425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33857403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34694004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34700328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36807739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9305914"}],"value":"Component of the MCM2-7 complex (PubMed:16899510, PubMed:17296731, PubMed:9305914). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:17296731, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:9305914). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex (PubMed:32453425, PubMed:34694004, PubMed:34700328). Interacts with DBF4 (By similarity). Interacts with KAT7 (PubMed:16387653). May interact with MCM10 (PubMed:11095689). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (PubMed:28191891). Forms a co-chaperone complex with DNAJC9 and histone H3.3-H4 heterodimers (PubMed:33857403). Within the complex, interacts (via N-terminus) with DNAJC9 (via C-terminus); the interaction is histone-dependent (PubMed:33857403). Interacts with histones H3.1 and H3.3 (PubMed:33857403). Interacts with AGER/RAGE; the interaction is increased following DNA replication stress and stabilizes the MCM2-7 complex at replication forks 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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"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Deafness, autosomal dominant, 70","diseaseAccession":"DI-04728","acronym":"DFNA70","description":"A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA70 is characterized by slowly progressive, postlingual hearing impairment.","diseaseCrossReference":{"database":"MIM","id":"616968"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26196677"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"value":"Early 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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MCM family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA04642.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA12177.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA47749.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"CAA47749.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Initiator 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