MCM7DNA replication licensing factor MCM7

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15210935"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15538388"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25661590"
        },
        {
          "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": "9305914"
        }
      ],
      "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:25661590, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:9305914). 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 S-phase checkpoint activation upon UV-induced damage"
    }
  ],
  "commentType": "FUNCTION"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q61881"
        }
      ],
      "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"
}

{
  "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": "25661590"
      }
    ]
  },
  "physiologicalReactions": [
    {
      "directionType": "left-to-right",
      "reactionCrossReference": {
        "database": "Rhea",
        "id": "RHEA:13066"
      },
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25661590"
        }
      ]
    }
  ]
}

Eukaryota → Metazoa → Chordata → Craniata → Vertebrata → Euteleostomi → Mammalia → Eutheria → Euarchontoglires → Primates → Haplorrhini → Catarrhini → Hominidae → Homo

{
  "names": {
    "recommendedName": {
      "fullName": {
        "value": "DNA replication licensing factor MCM7"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "25661590"
            }
          ],
          "value": "3.6.4.12"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "CDC47 homolog"
        }
      },
      {
        "fullName": {
          "value": "P1.1-MCM3"
        }
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:6950"
          }
        ],
        "value": "MCM7"
      },
      "synonyms": [
        {
          "value": "CDC47"
        },
        {
          "value": "MCM2"
        }
      ]
    }
  ]
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22967762"
        }
      ],
      "value": "O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q61881"
        },
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q91876"
        }
      ],
      "value": "Ubiquitinated by ECS(LRR1) E3 ubiquitin-protein ligase complex when forks converge following formation of DNA interstrand cross-links. During mitosis, ubiquitinated by TRAIP when forks converge following formation of DNA interstrand cross-links (By similarity). Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By similarity). If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase (By similarity)"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q91876"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15210935"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15538388"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17116885"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17296731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23711367"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "28191891"
        },
        {
          "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": "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: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 the ATR-ATRIP complex and with RAD17 (PubMed:15210935, PubMed:15538388). Interacts with TIPIN (PubMed:17116885). Interacts with MCMBP (PubMed:17296731). Interacts with ANKRD17 (PubMed:23711367). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (PubMed:28191891)"
    }
  ],
  "commentType": "SUBUNIT"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Belongs to the MCM family"
    }
  ],
  "commentType": "SIMILARITY"
}

Alternative splicing

{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "isoformIds": [
        "P33993-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "isoformIds": [
        "P33993-2"
      ],
      "sequenceIds": [
        "VSP_003205"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "3"
      },
      "isoformIds": [
        "P33993-3"
      ],
      "sequenceIds": [
        "VSP_044310"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}

• P33993-1 · 1 · Displayed
  Complete source annotation

  {
    "name": {
      "value": "1"
    },
    "isoformIds": [
      "P33993-1"
    ],
    "isoformSequenceStatus": "Displayed"
  }

• P33993-2 · 2 · Described · VSP_003205
  Complete source annotation

  {
    "name": {
      "value": "2"
    },
    "isoformIds": [
      "P33993-2"
    ],
    "sequenceIds": [
      "VSP_003205"
    ],
    "isoformSequenceStatus": "Described"
  }

• P33993-3 · 3 · Described · VSP_044310
  Complete source annotation

  {
    "name": {
      "value": "3"
    },
    "isoformIds": [
      "P33993-3"
    ],
    "sequenceIds": [
      "VSP_044310"
    ],
    "isoformSequenceStatus": "Described"
  }

• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:20.960692+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:20.953669+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:22.866492+00:00
• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:20.960692+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:20.953669+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:22.866492+00:00
• UniProt overview ↗ · 2026-11-10T20:42:47.242541+00:00
• www.ebi.ac.uk ↗ · 2026-11-10T21:11:58.093363+00:00
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• rest.uniprot.org ↗ · 2026-11-10T21:11:59.377265+00:00
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