MCM5DNA replication licensing factor MCM5

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "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": "40940420"
        }
      ],
      "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 (PubMed:40940420). 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:16899510, 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)"
    }
  ],
  "commentType": "FUNCTION"
}

{
  "texts": [
    {
      "value": "Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. 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:0000305",
        "source": "PubMed",
        "id": "32453425"
      }
    ]
  },
  "physiologicalReactions": [
    {
      "directionType": "left-to-right",
      "reactionCrossReference": {
        "database": "Rhea",
        "id": "RHEA:13066"
      },
      "evidences": [
        {
          "evidenceCode": "ECO:0000305",
          "source": "PubMed",
          "id": "32453425"
        }
      ]
    }
  ]
}

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

{
  "names": {
    "recommendedName": {
      "fullName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000303",
            "source": "Reference",
            "id": "Ref.3"
          }
        ],
        "value": "DNA replication licensing factor MCM5"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000305",
              "source": "PubMed",
              "id": "32453425"
            }
          ],
          "value": "3.6.4.12"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "evidences": [
            {
              "evidenceCode": "ECO:0000250",
              "source": "UniProtKB",
              "id": "P49718"
            }
          ],
          "value": "CDC46 homolog"
        }
      },
      {
        "fullName": {
          "evidences": [
            {
              "evidenceCode": "ECO:0000303",
              "source": "PubMed",
              "id": "8265339"
            }
          ],
          "value": "P1-CDC46"
        }
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "value": "MCM5"
      },
      "synonyms": [
        {
          "value": "CDC46"
        }
      ]
    }
  ]
}

{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Meier-Gorlin syndrome 8",
    "diseaseAccession": "DI-05038",
    "acronym": "MGORS8",
    "description": "A form of Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. MGORS8 inheritance is autosomal recessive.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "617564"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "28198391"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "40940420"
        }
      ],
      "value": "UFMylated at Lys-583; UFMylation occurs at the ongoing replication fork and promotes the CMG replicative DNA helicase complex formation"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17296731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23711367"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26527279"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        }
      ],
      "value": "Component of the MCM2-7 complex (PubMed:16899510, PubMed:17296731). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:17296731, PubMed:32453425). 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 ANKRD17 (PubMed:23711367). Interacts with MCMBP (PubMed:17296731). Interacts with TONSL; the interaction is direct (PubMed:26527279)"
    }
  ],
  "commentType": "SUBUNIT"
}

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

• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:19.319673+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:19.316856+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:20.843213+00:00
• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:19.319673+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:19.316856+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:20.843213+00:00
• UniProt overview ↗ · 2026-11-10T20:42:47.155334+00:00
• www.ebi.ac.uk ↗ · 2026-11-10T21:11:57.417885+00:00
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• rest.uniprot.org ↗ · 2026-11-10T21:11:58.315470+00:00
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