ALPHASUITEATLASTM
MCM3 · P25205Homo sapiens
PROTEIN OVERVIEW

MCM3DNA replication licensing factor MCM3

P25205Homo sapiensReviewed · UniProt

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.

Sequence808 aa
Source mass90.98 kDa
Recorded PDB entries28
Isoforms listed2

UniProt locations Nucleus · Chromosome

01

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 [34, 36, 35, 33]. 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 [34]. Required for the entry in S phase and for cell division (Probable)

Experimental evidenceCurator inference 4 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "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:0000305",
          "source": "PubMed",
          "id": "35585232"
        }
      ],
      "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 (Probable)"
    }
  ],
  "commentType": "FUNCTION"
}

Additional functional context

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "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"
}

Catalytic activity

ATP + H2O = ADP + phosphate + H(+)

Evidence
Complete source annotation
{
  "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"
        }
      ]
    }
  ]
}

GO functions & biological processes

single-stranded DNA helicase activitycontributes toUniProtKB:P25205
GO
GO:0017116 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210414
    qualifier: contributes_to
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179711"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC211.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC25D12.03c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000406"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000003169"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000004264"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
DNA bindingenablesUniProtKB:P25205
GO
GO:0003677 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001208"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008046"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
  • ECO:0000304 PMID:1549468 ↗ TAS · PINC · 20030904
    qualifier: enables
DNA helicase activityenablesUniProtKB:P25205
GO
GO:0003678 · evidence & context
  • ECO:0000501 GO_REF:0000003 IEA · UniProt · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "EC", "id": "3.6.4.12"}]}]
single-stranded DNA bindingenablesUniProtKB:P25205
GO
GO:0003697 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20230110
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179711"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
protein bindingenablesUniProtKB:P25205 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:12364596 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:12364596 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13416"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:19862764 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62805"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
All recorded function and process assertions (15)
protein bindingenablesUniProtKB:P25205
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:16899510 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:19150984 ↗ IPI · UniProt · 20141114
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75179"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:26496610 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:29395061 ↗ IPI · UniProt · 20180319
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7Z7L1"}]}]
  • ECO:0000353 PMID:31467278 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
ATP bindingenablesUniProtKB:P25205
GO
GO:0005524 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001208"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008046"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
ATP hydrolysis activityenablesUniProtKB:P25205
GO
GO:0016887 · evidence & context
  • ECO:0007322 GO_REF:0000116 IEA · RHEA · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "RHEA", "id": "13065"}]}]
  • ECO:0000269 PMID:32453425 ↗ EXP · UniProt · 20240916
    qualifier: enables
double-strand break repair via break-induced replicationinvolved inUniProtKB:P25205
GO
GO:0000727 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190209
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179713"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}]
DNA metabolic processinvolved inUniProtKB:P25205
GO
GO:0006259 · evidence & context
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028839"}]}]
DNA replicationinvolved inUniProtKB:P25205
GO
GO:0006260 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}]
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: involved_in
DNA replication initiationinvolved inUniProtKB:P25205
GO
GO:0006270 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR008046"}]}]
  • ECO:0000304 PMID:1549468 ↗ TAS · PINC · 20030904
    qualifier: involved_in
DNA strand elongation involved in DNA replicationinvolved inUniProtKB:P25205
GO
GO:0006271 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179713"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}]
regulation of DNA-templated DNA replication initiationinvolved inUniProtKB:P25205
GO
GO:0030174 · evidence & context
mitotic DNA replication initiationinvolved inUniProtKB:P25205
GO
GO:1902975 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20220414
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179713"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC1682.02c"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}]
02

Names & Taxonomy

Recommended name
DNA replication licensing factor MCM3
Gene
MCM3
Accession / entry
P25205 · MCM3_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
DNA polymerase alpha holoenzyme-associated protein P1 · P1-MCM3 · RLF subunit beta · p102
Full taxonomy & recorded names

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

{
  "names": {
    "recommendedName": {
      "fullName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000305"
          }
        ],
        "value": "DNA replication licensing factor MCM3"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "32453425"
            }
          ],
          "value": "3.6.4.12"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "DNA polymerase alpha holoenzyme-associated protein P1"
        }
      },
      {
        "fullName": {
          "value": "P1-MCM3"
        }
      },
      {
        "fullName": {
          "value": "RLF subunit beta"
        }
      },
      {
        "fullName": {
          "value": "p102"
        }
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:6945"
          }
        ],
        "value": "MCM3"
      }
    }
  ]
}
03

Subcellular Location

UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.

NucleusReported location

Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses

UniProt
Curator inference 1 publication
Evidence & references
ChromosomeReported location

Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses

UniProt
Curator inference 1 publication
Evidence & references
nucleolusNOT|located in
GO
1 publication
Evidence & references
nucleusis active in
GO
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260528
    qualifier: is_active_in
    withFrom: [{"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT1G44900"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT2G07690"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT2G16440"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT4G02060"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT5G44635"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT5G46280"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003227"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0014861"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0015929"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0017577"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0020633"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0284442"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:101845"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:105380"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1298227"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1918817"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179712"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPAC1B2.05"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC25D12.03c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC4.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC1682.02c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000406"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000003169"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000004264"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP3"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P30664"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33991"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49739"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P55862"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q24849"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q381H2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q382V6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q383B6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q384N2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q385L1"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q389T6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q38E36"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q586W7"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5F310"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5FWY4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5XK83"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q6NRM6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q8ILR7"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91876"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJA3"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003154"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003155"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003156"}]}]
chromosome, telomeric regionlocated in
GO
1 publication
Evidence & references
nucleuslocated in
GO
3 publications
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25206"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000059192"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
  • ECO:0000314 PMID:20531406 ↗ IDA · BHF-UCL · 20101105
    qualifier: located_in
  • ECO:0000314 PMID:21383955 ↗ IDA · UniProt · 20170426
    qualifier: located_in
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: located_in
nucleoplasmlocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-176298 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-176318 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68916 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68917 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68918 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68919 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68940 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68944 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68954 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-69019 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9749253 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9757256 TAS · Reactome · 20130528
    qualifier: located_in
chromosomelocated in
GO
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00026361"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0468"}]}]
All recorded location assertions (14)
cytoplasmlocated in
GO
Evidence & references
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25206"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000059192"}]}]
membranelocated in
GO
1 publication
Evidence & references
perinuclear region of cytoplasmlocated in
GO
1 publication
Evidence & references
alpha DNA polymerase:primase complexpart of
GO
1 publication
Evidence & references
MCM complexpart of
GO
2 publications
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250902
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0014861"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0015929"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0017577"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0020633"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0025815"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0284442"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:103199"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:105380"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1298227"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1298398"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1913884"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1918817"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179711"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPAC1B2.05"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC211.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC25D12.03c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC4.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC1682.02c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000406"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000003169"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000004264"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP3"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P30664"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33991"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49739"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P55861"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P55862"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q381H2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q382V6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q383B6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q385L1"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q389T6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q498J7"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5FWY4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5XK83"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q7ZXB1"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q7ZXZ0"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q7ZY18"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91876"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NXL9"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJA3"}]}]
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027194"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008046"}]}]
  • ECO:0000314 PMID:17296731 ↗ IDA · UniProt · 20110124
    qualifier: part_of
  • ECO:0000353 PMID:22540012 ↗ IPI · ComplexPortal · 20251229
    qualifier: part_of
CMG complexpart of
GO
By similarity 1 publication
Evidence & references
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20200807
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49739"}]}]
  • ECO:0000353 PMID:22474384 ↗ IPI · ComplexPortal · 20251015
    qualifier: part_of

Membrane topology 0

No annotation is recorded in this UniProt entry.

04

Disease & Variants

Source annotations; a recorded variant is not automatically a clinical classification.

No annotation is recorded in this UniProt entry.

Natural variants 6

Scroll across the table for evidence and actions.

6 recorded rows

FeaturePositionDescriptionEvidenceInspect
S105GVAR_014810105in dbSNP:rs2307332
S → G
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
D280VVAR_014811280in dbSNP:rs2307329
D → V
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.5
No verified residues in this structure
F287LVAR_014812287in dbSNP:rs2307328
F → L
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.5
No verified residues in this structure
I590LVAR_020516590in dbSNP:rs17240063
I → L
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.5
No verified residues in this structure
R774WVAR_020517774in dbSNP:rs2230239
R → W
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.5
No verified residues in this structure
E777KVAR_020427777in dbSNP:rs2230240
E → K
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.5
No verified residues in this structure

Laboratory mutagenesis 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
S535A53550% reduction in phosphorylation by ATM or ATR.
S → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
05

PTM/Processing

Acetylated by MCM3AP

Experimental evidence 2 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11258703"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12226073"
        }
      ],
      "value": "Acetylated by MCM3AP"
    }
  ],
  "commentType": "PTM"
}

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22967762"
        }
      ],
      "value": "O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Initiator methionine1Removed
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
ChainPRO_00001940932–808DNA replication licensing factor MCM3
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure

Modifications 18

Scroll across the table for evidence and actions.

18 recorded rows

FeaturePositionDescriptionEvidenceInspect
Modified residue2N-acetylalanine
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Modified residue160Phosphoserine
2 publications
Evidence & references
No verified residues in this structure
Modified residue275Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue293N6-acetyllysine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P25206
No verified residues in this structure
Modified residue535Phosphoserine; by ATM
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue547N6-acetyllysine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P25206
No verified residues in this structure
Modified residue611Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue668Phosphoserine
2 publications
Evidence & references
No verified residues in this structure
Modified residue672Phosphoserine
6 publications
Evidence & references
No verified residues in this structure
Modified residue674Phosphothreonine
5 publications
Evidence & references
No verified residues in this structure
Modified residue681Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue708Phosphotyrosine
1 publication
Evidence & references
No verified residues in this structure
Modified residue711Phosphoserine
4 publications
Evidence & references
No verified residues in this structure
Modified residue713Phosphothreonine
2 publications
Evidence & references
No verified residues in this structure
Modified residue722Phosphothreonine
8 publications
Evidence & references
No verified residues in this structure
Modified residue725Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue728Phosphoserine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P25206
No verified residues in this structure
Modified residue734Phosphoserine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P25206
No verified residues in this structure
06

Expression

No annotation is recorded in this UniProt entry.

07

Interaction

Documented interaction partners

UniProt’s filtered IntAct records. Experiment counts describe reported experiments, not binding strength or independent publications. Separate products remain separate rows.

6 records
Partner / productSpeciesExperimentsEvidence & actions
H4C9P62805With P25205Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: P62805. Reported experiment count: 2.

Open protein ↗
MCM2P49736With P25205Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: P49736. Reported experiment count: 9.

Open protein ↗
MCM5P33992With P25205Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: P33992. Reported experiment count: 8.

Open protein ↗
MCM6Q14566With P25205Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: Q14566. Reported experiment count: 5.

Open protein ↗
MCMBPQ9BTE3With P25205Homo sapiens13
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: Q9BTE3. Reported experiment count: 13.

Open protein ↗
ORC2Q13416With P25205Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P25205. Partner: Q13416. Reported experiment count: 2.

Open protein ↗

Complex membership & assembly descriptions

Co-membership does not by itself prove direct binding between every pair.

MCM complex CPX-2940 Complex Portal

Homo sapiens; 9606 · Heterohexamer

Evidence: physical interaction evidence

  • MCM3 · P25205 · minValue: 1, maxValue: 1
  • MCM7 · P33993 · minValue: 1, maxValue: 1
  • MCM5 · P33992 · minValue: 1, maxValue: 1
  • MCM2 · P49736 · minValue: 1, maxValue: 1
  • MCM6 · Q14566 · minValue: 1, maxValue: 1
  • MCM4 · P33991 · minValue: 1, maxValue: 1

Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. Activation of the MCM complex at origins by cyclin-dependent kinases and the Cdc7 protein kinase leads to initiation of DNA synthesis. MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.

Source & references ↗

UniProt subunit description

Component of the MCM2-7 complex [16, 19]. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 [16, 19, 34, 36, 35]. Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex [34, 36, 35].

Associated with the replication-specific DNA polymerase alpha (By similarity). Interacts with MCMBP [19]. Interacts with ANKRD17 [31].

Interacts with MCM3AP isoform MCM3AP; this interaction leads to MCM3 acetylation [12, 13, 11]

By similarityExperimental evidence 9 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P25206"
        },
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P49739"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11258703"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12226073"
        },
        {
          "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": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9712829"
        }
      ],
      "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, PubMed:34694004, PubMed:34700328). 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). Associated with the replication-specific DNA polymerase alpha (By similarity). Interacts with MCMBP (PubMed:17296731). Interacts with ANKRD17 (PubMed:23711367). Interacts with MCM3AP isoform MCM3AP; this interaction leads to MCM3 acetylation (PubMed:11258703, PubMed:12226073, PubMed:9712829)"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

Resource links only; their association networks and counts are not added to the partner table.

BioGRID · 110340 ↗IntAct · P25205 ↗STRING · 9606.ENSP00000480987 ↗
08

Structure

7W1Y · Human MCM double hexamer bound to natural DNA duplex (polyAT/polyTA)

ELECTRON MICROSCOPY · 2.59 Å

Recorded components

ComponentSpeciesChainsProtein identities
DNA replication licensing factor MCM2protein · Entity 1Homo sapiensA, GP49736
Isoform 2 of DNA replication licensing factor MCM3protein · Entity 2Homo sapiensB, HP25205
DNA replication licensing factor MCM4protein · Entity 3Homo sapiensC, IP33991
DNA replication licensing factor MCM5protein · Entity 4Homo sapiensD, JP33992
DNA replication licensing factor MCM6protein · Entity 5Homo sapiensE, KQ14566
DNA replication licensing factor MCM7protein · Entity 6Homo sapiensF, LP33993
DNA (49-MER)dna · Entity 7Homo sapiensMNo verified protein mapping
DNA (49-MER)dna · Entity 8Homo sapiensNNo verified protein mapping
ZINC IONligand · Entity 9CA, FA, KA, NA, O, QA, T, TA, W, ZNo verified protein mapping
MAGNESIUM IONligand · Entity 10AA, DA, GA, IA, LA, OA, P, R, RA, U, UA, XNo verified protein mapping
ADENOSINE-5'-TRIPHOSPHATEligand · Entity 11EA, HA, JA, MA, Q, S, V, VANo verified protein mapping
ADENOSINE-5'-DIPHOSPHATEligand · Entity 12BA, PA, SA, YNo verified protein mapping

Biological assemblies

Assembly 1 · author_defined_assembly
Recorded chains: A, AA, B, BA, C, CA, D, DA, E, EA, F, FA, G, GA, H, HA, I, IA, J, JA, K, KA, L, LA, M, MA, N, NA, O, OA, P, PA, Q, QA, R, RA, S, SA, T, TA, U, UA, V, VA, W, X, Y, Z

Assembly membership does not establish direct binding. Observed residue coverage is checked against the loaded coordinates; it is not inferred from construct metadata.

Publication

The human pre-replication complex is an open complex.

05/01/2023 · Read publication ↗

Detailed validation, construct lengths and deposition dates are not included in this published record. See the source record for those details.

PDB source record ↗

Structure references are from the dated source record. Opening another structure follows your existing Atlas account permissions.

Available structures 29

Scroll across the table for evidence and actions.

29 recorded rows

RecordEvidence typeMethodResolutionOpen
7W1YexperimentalEM2.59 AOpen in Atlas ↗
9E2ZexperimentalEM2.60 AOpen in Atlas ↗
7PLOexperimentalEM2.80 AOpen in Atlas ↗
8W0FexperimentalEM2.80 AOpen in Atlas ↗
8S09experimentalEM3.10 AOpen in Atlas ↗
7PFOexperimentalEM3.20 AOpen in Atlas ↗
8S0AexperimentalEM3.20 AOpen in Atlas ↗
9CAQexperimentalEM3.20 AOpen in Atlas ↗
9LXDexperimentalEM3.27 AOpen in Atlas ↗
6XTXexperimentalEM3.29 AOpen in Atlas ↗
22VTexperimentalEM3.30 AOpen in Atlas ↗
8B9DexperimentalEM3.40 AOpen in Atlas ↗
8W0EexperimentalEM3.40 AOpen in Atlas ↗
9UQ0experimentalEM3.47 AOpen in Atlas ↗
8W0IexperimentalEM3.50 AOpen in Atlas ↗
8S0BexperimentalEM3.60 AOpen in Atlas ↗
8S0DexperimentalEM3.60 AOpen in Atlas ↗
8S0EexperimentalEM3.80 AOpen in Atlas ↗
8W0GexperimentalEM3.80 AOpen in Atlas ↗
9LXFexperimentalEM3.86 AOpen in Atlas ↗
9LXEexperimentalEM3.96 AOpen in Atlas ↗
8S0FexperimentalEM4.10 AOpen in Atlas ↗
9C6GexperimentalEM4.26 AOpen in Atlas ↗
7W68experimentalEM4.40 AOpen in Atlas ↗
8RWVexperimentalEM6.68 AOpen in Atlas ↗
6XTYexperimentalEM6.77 AOpen in Atlas ↗
9VLNexperimentalEM3.42 AOpen in Atlas ↗
9VLWexperimentalEM4.06 AOpen in Atlas ↗
AF-P25205-F1predictedAlphaFoldNot applicableOpen in Atlas ↗
09

Family & Domains

Belongs to the MCM family

Curator inference
Evidence & references
  • ECO:0000305
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Belongs to the MCM family"
    }
  ],
  "commentType": "SIMILARITY"
}

Domain architecture

Canonical sequence1808 aa
Coverage
Domains & repeats
Variants
Processing

Canonical coordinates. Overlapping marks share a lane; individual records and evidence are in the tables below. Gaps in coverage are not selectable in 3D. Use the track links and tables for keyboard inspection.

Atlas domains, motifs & repeats 6

Scroll across the table for evidence and actions.

6 recorded rows

AnnotationPositionSource & interpretationInspect
MCM, N-terminal domainIPR02792516–103INTERPROdomain

This entry represents the N-terminal region of MCM proteins. This region is composed of three structural domains.

Full source description

This entry represents the N-terminal region of MCM proteins. This region is composed of three structural domains. Firstly a four helical bundle, secondly a zinc binding motif and thirdly an OB-like fold. MCM proteins are DNA-dependent ATPases required for the initiation of eukaryotic DNA replication. In eukaryotes there is a family of six proteins, MCM2 to MCM7. They were first identified in yeast where most of them have a direct role in the initiation of chromosomal DNA replication by interacting directly with autonomously replicating sequences (ARS). They were thus called minichromosome maintenance proteins, MCM proteins.

Source entry ↗		No verified residues in this structure
MCM OB domainIPR033762114–244INTERPROdomain

This OB-fold domain is found within MCM (mini-chromosome maintenance) proteins, which are components if the MCM complex involved in chromosome replication. This domain, found at the N terminus, contains an insertion at the zinc binding motif.

Source entry ↗		No verified residues in this structure
MCM domainIPR001208276–659INTERPROdomain

Proteins shown to be required for the initiation of eukaryotic DNA replication share a highly conserved domain of about 210 amino-acid residues. The latter shows some similarities with that of various other families of DNA-dependent ATPases.

Full source description

Proteins shown to be required for the initiation of eukaryotic DNA replication share a highly conserved domain of about 210 amino-acid residues. The latter shows some similarities with that of various other families of DNA-dependent ATPases. Eukaryotes seem to possess a family of eight proteins that contain this domain. They were first identified in yeast where most of them have a direct role in the initiation of chromosomal DNA replication by interacting directly with autonomously replicating sequences (ARS). They were thus called 'minichromosome maintenance proteins' with gene symbols prefixed by MCM. These six proteins are: MCM2, also known as cdc19 (in S.pombe). MCM3, also known as DNA polymerase alpha holoenzyme-associated protein P1, RLF beta subunit or ROA. MCM4, also known as CDC54, cdc21 (in S.pombe) or dpa (in Drosophila). MCM5, also known as CDC46 or nda4 (in S.pombe). MCM6, also known as mis5 (in S.pombe). MCM7, also known as CDC47 or Prolifera (in A.thaliana). MCM8, also known as as REC (in Drosophila). MCM These proteins are evolutionarily related and belong to the AAA+ superfamily. They contain the Mcm family domain, which includes motifs that are required for ATP hydrolysis (such as the Walker A and B, and R-finger motifs). Mcm2-7 forms a hexameric complex which is the replicative helicase involved in replication initiation and elongation, whereas Mcm8 and Mcm9 from and separate one, conserved among many eukaryotes except yeast and C. elegans. Mcm8/9 complex play a role during replication elongation or recombination, being involved in the repair of double-stranded DNA breaks and DNA interstrand cross-links by homologous recombination. Drosophila is the only organism that has MCM8 without MCM9, involved in meiotic recombination.

Source entry ↗		No verified residues in this structure
AAA+ ATPase domainIPR003593337–490INTERPROdomain

This entry represents the AAA+ ATPase domain found in a range of proteins, including Holliday junction ATP-dependent DNA helicase RuvB from Mycobacterium sp, ATP synthases, and related ATP-dependent proteins. The proteins in this superfamily are characterised by the structural conservation of a central ATPase domain of about 250 amino acids called the AAA module.

Full source description

This entry represents the AAA+ ATPase domain found in a range of proteins, including Holliday junction ATP-dependent DNA helicase RuvB from Mycobacterium sp, ATP synthases, and related ATP-dependent proteins. The proteins in this superfamily are characterised by the structural conservation of a central ATPase domain of about 250 amino acids called the AAA module. Typically, the AAA domain can be divided into two structural subdomains, an N-terminal P-loop NTPase α-β-α subdomain that is connected to a smaller C-terminal all-α subdomain. The α-β-α subdomain adopts a Rossman fold and contains several motifs involved in ATP binding and hydrolysis, including classical motifs Walker A and Walker B. The all-α subdomain, is much less conserved across AAA proteins. The AAA+ superfamily of ATPases is found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Although the terms AAA+ and AAA are often used loosely and interchangeably, the classical AAA family members are distinguished by their possession of the SRH region in the AAA module. Many AAA+ proteins are involved in similar processes to those of AAA proteins (facilitation of protein folding and unfolding, assembly or disassembly of proteins complexes, protein transport and degradation), but others function in replication, recombination, repair and transcription. For a review see.

Source entry ↗		No verified residues in this structure
MCM, AAA-lid domainIPR041562567–650INTERPROdomain

This entry represents the AAA-lid domain found in MCM proteins. MCM proteins are DNA-dependent ATPases required for the initiation of eukaryotic DNA replication.

Full source description

This entry represents the AAA-lid domain found in MCM proteins. MCM proteins are DNA-dependent ATPases required for the initiation of eukaryotic DNA replication. In eukaryotes there is a family of six proteins, MCM2 to MCM7. They were first identified in yeast where most of them have a direct role in the initiation of chromosomal DNA replication by interacting directly with autonomously replicating sequences (ARS). They were thus called minichromosome maintenance proteins, MCM proteins.

Source entry ↗		No verified residues in this structure
MCM3-like, winged helix domainIPR056575738–808INTERPROdomain

This small C-terminal winged helix (WH) domain is found in the human DNA replication licensing factor MCM3 and similar eukaryotic sequences. MCM3 is a minichromosome maintenance (MCM) protein, 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.

Full source description

This small C-terminal winged helix (WH) domain is found in the human DNA replication licensing factor MCM3 and similar eukaryotic sequences. MCM3 is a minichromosome maintenance (MCM) protein, 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. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighbouring subunits.

Source entry ↗		No verified residues in this structure

UniProt domains, repeats & motifs 3

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3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Domain276–659MCM C-terminal AAA(+) ATPase
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif345–352Walker A
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif409–412Walker B
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Functional sites 8

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8 recorded rows

FeaturePositionDescriptionEvidenceInspect
Binding site353Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site393Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site394Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site395Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site397Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site523Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site664Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Site478Arginine finger
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Sequence regions 4

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4 recorded rows

FeaturePositionDescriptionEvidenceInspect
Region662–739Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias670–681Acidic residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias704–717Acidic residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias727–739Basic and acidic residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
10

Sequence & Isoforms

Sequence & isoforms

UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.

UniProt’s canonical sequence · P25205-1808 aa90,981 Da · source sequence mass

The mass describes this unmodified source sequence, not every mature or modified product.

MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQSKVRELISDNQYRLIVNVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI

Source isoform notes & selection

Alternative splicing

Complete source annotation
{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "isoformIds": [
        "P25205-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "isoformIds": [
        "P25205-2"
      ],
      "sequenceIds": [
        "VSP_057050"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}
  • P25205-1 · 1 · Displayed
    Complete source annotation
    {
  "name": {
    "value": "1"
  },
  "isoformIds": [
    "P25205-1"
  ],
  "isoformSequenceStatus": "Displayed"
}
  • P25205-2 · 2 · Described · VSP_057050
    Complete source annotation
    {
  "name": {
    "value": "2"
  },
  "isoformIds": [
    "P25205-2"
  ],
  "sequenceIds": [
    "VSP_057050"
  ],
  "isoformSequenceStatus": "Described"
}

Isoform sequence differences 1

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1 recorded rows

FeaturePositionDescriptionEvidenceInspect
Alternative sequenceVSP_0570501in isoform 2
M → MLPRSPPLPRGNLWWREEFGSFRAGVESSWEPPRDFGGGSSLAAGM
Published statement 1 publication
Evidence & references
No verified residues in this structure

Sequence conflicts & cautions 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
Sequence conflict230–231in Ref. 3; BAA07267
KP → NA
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure

Recorded secondary structure 80

Scroll across the table for evidence and actions.

80 recorded rows

FeaturePositionDescriptionEvidenceInspect
Beta strand4–8Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix10–23Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand26–28Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix31–42Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand46–50Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix51–57Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix59–67Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix69–87Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix89–94Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand99–104Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn107–109Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn113–115Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix118–120Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand123–134Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand138–148Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn149–152Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand153–158Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand163–165Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix169–172Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand179–181Beta strand
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Beta strand185–202Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn205–207Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand210–212Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand216–222Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix223–225Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix226–228Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand234–244Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix245–248Helix
Evidence & references
  • ECO:0007829 PDB:8S09
No verified residues in this structure
Beta strand250–268Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand270–273Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix278–290Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn291–294Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix295–301Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix311–322Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand330–332Beta strand
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Beta strand341–345Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand347–350Beta strand
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix351–361Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand365–368Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand370–373Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix375–377Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand381–384Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand386–388Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand391–394Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix397–400Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn401–403Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand404–410Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix411–413Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix416–428Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand430–435Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand438–443Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand446–452Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix455–457Helix
Evidence & references
  • ECO:0007829 PDB:9CAQ
No verified residues in this structure
Beta strand461–463Beta strand
Evidence & references
  • ECO:0007829 PDB:8S09
No verified residues in this structure
Helix465–468Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix473–478Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand480–485Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix491–506Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn510–512Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand514–516Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix517–521Helix
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Beta strand523–525Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn526–528Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix532–534Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand552–560Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix565–576Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix584–598Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix600–602Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand607–611Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix615–631Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand635–637Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix639–652Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand654–656Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix741–757Helix
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand761–764Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Helix765–773Helix
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand775–778Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Helix782–794Helix
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand797–801Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand804–807Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
12

Homologs

OMA orthologs

Evolutionary relationships assigned by OMA, kept separate from sequence clusters. “1:1” describes an orthology relationship, not percentage identity.

Recorded preview of up to 12 orthologs; not an exhaustive list. Entries without a verified UniProt mapping open their OMA record.

Q2FML6Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)m:1OMA record ↗
E1RK23Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)m:1OMA record ↗
Q12TE3Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)m:1OMA record ↗
A0A384KKF2Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)m:1OMA record ↗
M0AKM2Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM P-10747 / NBRC 102637 / 172P1)m:1OMA record ↗
L0IHG4Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70)m:1OMA record ↗
OKY78610.1Candidatus Methanohalarchaeum thermophilum HMET1m:nOMA record ↗
OKY78628.1Candidatus Methanohalarchaeum thermophilum HMET1m:nOMA record ↗
Q74MT7Nanoarchaeum equitans (strain Kin4-M)m:1OMA record ↗
NHV98752.1Thaumarchaeota archaeon SJ3.Bin56m:1OMA record ↗
MBM1154563.1archaeon B48_G17m:1OMA record ↗
A2BL91Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)m:1OMA record ↗
13

Sources & References

Scientific descriptions and evidence come from the named sources. Atlas assembles the presentation and verifies residue mappings; it does not independently curate these claims.

UniProt ↗QuickGO ↗InterPro ↗PDB / PDBe ↗Complex Portal ↗UniRef ↗OMA ↗
Source dates & provenance

Recorded 2026-11-10. Source dates and identifiers are retained below.

Publications in this UniProt entry

1 · The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins.

1993 · Nucleic Acids Res.

PubMed 8265339 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)

Hu B., Burkhart R., Schulte D., Musahl C., Knippers R.

· Reference

AUG-1999 ·

Scope & authors

SEQUENCE REVISION

Goehring F., Jehnichen P., Hemmer W.H.

3 · Identification of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor.

1995 · Cell

PubMed 7758114 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)

Kubota Y., Mimura S., Nishimoto S., Takisawa H., Nojima H.

4 · Complete sequencing and characterization of 21,243 full-length human cDNAs.

2004 · Nat. Genet.

PubMed 14702039 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)

Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.

All source publications (36)
· Reference

MAY-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS VAL-280; LEU-287; LEU-590; TRP-774 AND LYS-777

6 · The DNA sequence and analysis of human chromosome 6.

2003 · Nature

PubMed 14574404 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.

· Reference

JUL-2005 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.

8 · The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

2004 · Genome Res.

PubMed 15489334 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

· Reference

JUL-2007 ·

Scope & authors

PROTEIN SEQUENCE OF 2-13; 47-55; 337-351 AND 749-756; CLEAVAGE OF INITIATOR METHIONINE; ACETYLATION AT ALA-2; IDENTIFICATION BY MASS SPECTROMETRY

Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.

10 · Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein.

1992 · Nucleic Acids Res.

PubMed 1549468 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 563-808 (ISOFORM 1)

Thoemmes P., Fett R., Schray B., Burkhart R., Barnes M., Kennedy C., Brown N.C., Knippers R.

11 · Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization.

1998 · J. Biol. Chem.

PubMed 9712829 ↗
Scope & authors

INTERACTION WITH MCM3AP

Takei Y., Tsujimoto G.

12 · MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3.

2001 · EMBO Rep.

PubMed 11258703 ↗
Scope & authors

INTERACTION WITH MCM3AP; ACETYLATION

Takei Y., Swietlik M., Tanoue A., Tsujimoto G., Kouzarides T., Laskey R.

13 · The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA replication via interaction with MCM3.

2002 · J. Biol. Chem.

PubMed 12226073 ↗
Scope & authors

INTERACTION WITH MCM3AP; ACETYLATION

Takei Y., Assenberg M., Tsujimoto G., Laskey R.

14 · Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases.

2004 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 15210935 ↗
Scope & authors

PHOSPHORYLATION AT SER-535; MUTAGENESIS OF SER-535

Cortez D., Glick G., Elledge S.J.

15 · Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

2006 · Cell

PubMed 17081983 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.

16 · Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells.

2006 · Mol. Biol. Cell

PubMed 16899510 ↗
Scope & authors

IDENTIFICATION IN THE MCM2-7 COMPLEX; ATPASE ACTIVITY OF THE MCM2-7 COMPLEX

Tsuji T., Ficarro S.B., Jiang W.

17 · A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

2006 · Nat. Biotechnol.

PubMed 16964243 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND THR-674; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.

18 · Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

2007 · Electrophoresis

PubMed 17487921 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.

19 · Identification and characterization of a novel component of the human minichromosome maintenance complex.

2007 · Mol. Cell. Biol.

PubMed 17296731 ↗
Scope & authors

IDENTIFICATION IN THE MCM2-7 COMPLEX; INTERACTION WITH MCMBP; IDENTIFICATION BY MASS SPECTROMETRY

Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.

20 · Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

2008 · Mol. Cell

PubMed 18691976 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.

21 · A quantitative atlas of mitotic phosphorylation.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18669648 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-668; SER-672; THR-674; SER-681; SER-711; THR-713 AND THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.

22 · Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

2009 · Anal. Chem.

PubMed 19413330 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.

23 · Large-scale proteomics analysis of the human kinome.

2009 · Mol. Cell. Proteomics

PubMed 19369195 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.

24 · Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

2009 · Sci. Signal.

PubMed 19690332 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-674; TYR-708; SER-711; THR-713; THR-722 AND THR-725; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.

25 · Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

2010 · Sci. Signal.

PubMed 20068231 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668; SER-672; SER-711 AND THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.

26 · Initial characterization of the human central proteome.

2011 · BMC Syst. Biol.

PubMed 21269460 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.

27 · System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

2011 · Sci. Signal.

PubMed 21406692 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-672; THR-674 AND SER-711; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.

28 · Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.

2012 · Biochim. Biophys. Acta

PubMed 22967762 ↗
Scope & authors

GLYCOSYLATION

Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.

29 · Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

2012 · Mol. Cell. Proteomics

PubMed 22223895 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.

30 · N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

2012 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 22814378 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.

31 · A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and Nod2-mediated inflammatory responses.

2013 · FEBS Lett.

PubMed 23711367 ↗
Scope & authors

INTERACTION WITH ANKRD17

Menning M., Kufer T.A.

32 · Toward a comprehensive characterization of a human cancer cell phosphoproteome.

2013 · J. Proteome Res.

PubMed 23186163 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-611; SER-672; THR-674 AND THR-722; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.

33 · Fast and efficient DNA replication with purified human proteins.

2022 · Nature

PubMed 35585232 ↗
Scope & authors

FUNCTION; SUBCELLULAR LOCATION

Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.

34 · CryoEM structures of human CMG-ATPgammaS-DNA and CMG-AND-1 complexes.

2020 · Nucleic Acids Res.

PubMed 32453425 ↗
Scope & authors

STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEXES WITH ADP; ATP ANALOG AND WDHD1 IN CMG COMPLEX; SUBUNIT; FUNCTION

Rzechorzek N.J., Hardwick S.W., Jatikusumo V.A., Chirgadze D.Y., Pellegrini L.

35 · A conserved mechanism for regulating replisome disassembly in eukaryotes.

2021 · Nature

PubMed 34700328 ↗
Scope & authors

STRUCTURE BY ELECTRON MICROSCOPY IN REPLISOME; SUBUNIT; FUNCTION

Jenkyn-Bedford M., Jones M.L., Baris Y., Labib K.P.M., Cannone G., Yeeles J.T.P., Deegan T.D.

36 · Structure of a human replisome shows the organisation and interactions of a DNA replication machine.

2021 · EMBO J.

PubMed 34694004 ↗
Scope & authors

STRUCTURE BY ELECTRON MICROSCOPY IN REPLISOME; SUBUNIT; FUNCTION

Jones M.L., Baris Y., Taylor M.R.G., Yeeles J.T.P.

Annotation coverage audit

Every recorded UniProt comment and feature has a destination in this page. GO, Atlas annotations and interaction rows retain their separate source counts.

134 source comments and features accounted for.

View annotation inventory
Source recordTypeSection
FUNCTION:0FUNCTIONfunction
CATALYTIC ACTIVITY:0CATALYTIC ACTIVITYfunction
SUBUNIT:0SUBUNITinteractions
INTERACTION:0INTERACTIONinteractions
SUBCELLULAR LOCATION:0SUBCELLULAR LOCATIONlocation
ALTERNATIVE PRODUCTS:0ALTERNATIVE PRODUCTSsequence
PTM:0PTMprocessing
PTM:1PTMprocessing
MISCELLANEOUS:0MISCELLANEOUSfunction
SIMILARITY:0SIMILARITYdomains
feature-0Initiator methionineprocessing
feature-1Chainprocessing
feature-2Domaindomains
feature-3Regiondomains
feature-4Motifdomains
feature-5Motifdomains
feature-6Compositional biasdomains
feature-7Compositional biasdomains
feature-8Compositional biasdomains
feature-9Binding sitedomains
feature-10Binding sitedomains
feature-11Binding sitedomains
feature-12Binding sitedomains
feature-13Binding sitedomains
feature-14Binding sitedomains
feature-15Binding sitedomains
feature-16Sitedomains
feature-17Modified residueprocessing
feature-18Modified residueprocessing
feature-19Modified residueprocessing
feature-20Modified residueprocessing
feature-21Modified residueprocessing
feature-22Modified residueprocessing
feature-23Modified residueprocessing
feature-24Modified residueprocessing
feature-25Modified residueprocessing
feature-26Modified residueprocessing
feature-27Modified residueprocessing
feature-28Modified residueprocessing
feature-29Modified residueprocessing
feature-30Modified residueprocessing
feature-31Modified residueprocessing
feature-32Modified residueprocessing
feature-33Modified residueprocessing
feature-34Modified residueprocessing
feature-35Alternative sequencesequence
feature-36Natural variantdisease
feature-37Natural variantdisease
feature-38Natural variantdisease
feature-39Natural variantdisease
feature-40Natural variantdisease
feature-41Natural variantdisease
feature-42Mutagenesisdisease
feature-43Sequence conflictsequence
feature-44Beta strandsequence
feature-45Helixsequence
feature-46Beta strandsequence
feature-47Helixsequence
feature-48Beta strandsequence
feature-49Helixsequence
feature-50Helixsequence
feature-51Helixsequence
feature-52Helixsequence
feature-53Beta strandsequence
feature-54Turnsequence
feature-55Turnsequence
feature-56Helixsequence
feature-57Beta strandsequence
feature-58Beta strandsequence
feature-59Turnsequence
feature-60Beta strandsequence
feature-61Beta strandsequence
feature-62Helixsequence
feature-63Beta strandsequence
feature-64Beta strandsequence
feature-65Turnsequence
feature-66Beta strandsequence
feature-67Beta strandsequence
feature-68Helixsequence
feature-69Helixsequence
feature-70Beta strandsequence
feature-71Helixsequence
feature-72Beta strandsequence
feature-73Beta strandsequence
feature-74Helixsequence
feature-75Turnsequence
feature-76Helixsequence
feature-77Helixsequence
feature-78Beta strandsequence
feature-79Beta strandsequence
feature-80Beta strandsequence
feature-81Helixsequence
feature-82Beta strandsequence
feature-83Beta strandsequence
feature-84Helixsequence
feature-85Beta strandsequence
feature-86Beta strandsequence
feature-87Beta strandsequence
feature-88Helixsequence
feature-89Turnsequence
feature-90Beta strandsequence
feature-91Helixsequence
feature-92Helixsequence
feature-93Beta strandsequence
feature-94Beta strandsequence
feature-95Beta strandsequence
feature-96Helixsequence
feature-97Beta strandsequence
feature-98Helixsequence
feature-99Helixsequence
feature-100Beta strandsequence
feature-101Helixsequence
feature-102Turnsequence
feature-103Beta strandsequence
feature-104Helixsequence
feature-105Beta strandsequence
feature-106Turnsequence
feature-107Helixsequence
feature-108Beta strandsequence
feature-109Helixsequence
feature-110Helixsequence
feature-111Helixsequence
feature-112Beta strandsequence
feature-113Helixsequence
feature-114Beta strandsequence
feature-115Helixsequence
feature-116Beta strandsequence
feature-117Helixsequence
feature-118Beta strandsequence
feature-119Helixsequence
feature-120Beta strandsequence
feature-121Helixsequence
feature-122Beta strandsequence
feature-123Beta strandsequence