ALPHASUITEATLASTM
MCM2 · P49736Homo sapiens
PROTEIN OVERVIEW

MCM2DNA replication licensing factor MCM2

P49736Homo 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.

Sequence904 aa
Source mass101.90 kDa
Recorded PDB entries39
Isoforms listed1

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 [38, 40, 41, 36]. 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 [38]. Required for the entry in S phase and for cell division [1]. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis [42]

Experimental evidence 6 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26196677"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "35585232"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8175912"
        }
      ],
      "value": "Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677)"
    }
  ],
  "commentType": "FUNCTION"
}

Additional functional context

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex

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. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex"
    }
  ],
  "commentType": "MISCELLANEOUS"
}

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:P49736
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"}]}]
3'-5' DNA helicase activitycontributes toUniProtKB:P49736
GO
GO:0043138 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210
    qualifier: contributes_to
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0014861"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179907"}]}]
DNA bindingenablesUniProtKB:P49736
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": "IPR008045"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
  • ECO:0000304 PMID:8175912 ↗ TAS · PINC · 20030904
    qualifier: enables
DNA helicase activityenablesUniProtKB:P49736
GO
GO:0003678 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}, {"connectedXrefs": [{"db": "EC", "id": "3.6.4.12"}]}]
DNA replication origin bindingenablesUniProtKB:P49736
GO
GO:0003688 · evidence & context
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}]
All recorded function and process assertions (20)
single-stranded DNA bindingenablesUniProtKB:P49736
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:P49736
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:11095689 ↗ IPI · UniProt · 20070220
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7L590"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:15654075 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P53350"}]}]
  • ECO:0000353 PMID:16189514 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:16387653 ↗ IPI · UniProt · 20090529
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95251"}]}]
  • ECO:0000353 PMID:16899510 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:16899510 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
  • ECO:0000353 PMID:16899510 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:16899510 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:16902406 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:19805216 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75419"}]}]
  • ECO:0000353 PMID:19805216 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BRX5"}]}]
  • ECO:0000353 PMID:19819239 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96H20"}]}]
  • ECO:0000353 PMID:20211142 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:21044950 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NYB0"}]}]
  • ECO:0000353 PMID:21149733 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y468"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:23764002 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:24981860 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • ECO:0000353 PMID:24981860 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y294"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:25416956 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75419"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49450"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P68431"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y294"}]}]
  • ECO:0000353 PMID:26496610 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}]
  • ECO:0000353 PMID:27173435 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P53350"}]}]
  • ECO:0000353 PMID:28191891 ↗ IPI · UniProt · 20171006
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12004"}, {"db": "UniProtKB", "id": "P33993"}, {"db": "UniProtKB", "id": "Q7Z2Z1"}, {"db": "UniProtKB", "id": "Q9NYP3"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P68431"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y294"}]}]
  • ECO:0000353 PMID:31467278 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y294"}]}]
  • ECO:0000353 PMID:32769987 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IYD8"}]}]
  • ECO:0000353 PMID:32769987 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NYP3"}]}]
  • ECO:0000353 PMID:33654309 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:33857403 ↗ IPI · UniProt · 20210528
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8WXX5"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P68431"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • 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": "Q9BRX5"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y294"}]}]
  • ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y468"}]}]
  • ECO:0000353 PMID:35271311 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • ECO:0000353 PMID:36807739 ↗ IPI · UniProt · 20241115
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15109"}]}]
  • ECO:0000353 PMID:40205054 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
protein bindingenablesUniProtKB:P49736 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:12740381 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43823"}]}]
    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:26167883 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62805"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62805"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
ATP bindingenablesUniProtKB:P49736
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": "IPR008045"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
ATP hydrolysis activityenablesUniProtKB:P49736
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 · 20251027
    qualifier: enables
enzyme bindingenablesUniProtKB:P49736
GO
GO:0019899 · evidence & context
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}]
histone bindingenablesUniProtKB:P49736
GO
GO:0042393 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028931"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}]
  • ECO:0000353 PMID:25618846 ↗ IPI · DisProt · 20240220
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P02299"}, {"db": "UniProtKB", "id": "P84040"}]}]
histone bindingenablesUniProtKB:P49736 · Context-qualified assertion; see evidence
GO
GO:0042393 · evidence & context
  • ECO:0000269 PMID:25618846 ↗ EXP · DisProt · 20240220
    qualifier: enables
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P02299", "relation": "has_input"}, {"db": "UniProtKB", "id": "P84040", "relation": "has_input"}]}]
double-strand break repair via break-induced replicationinvolved inUniProtKB:P49736
GO
GO:0000727 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190209
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179907"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}]
DNA replicationinvolved inUniProtKB:P49736
GO
GO:0006260 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028858"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}]
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: involved_in
  • ECO:0000304 PMID:8175912 ↗ TAS · PINC · 20030904
    qualifier: involved_in
DNA replication initiationinvolved inUniProtKB:P49736
GO
GO:0006270 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR008045"}]}]
  • ECO:0000315 PMID:16899510 ↗ IMP · UniProt · 20110207
    qualifier: involved_in
apoptotic processinvolved inUniProtKB:P49736
GO
GO:0006915 · evidence & context
regulation of DNA-templated DNA replication initiationinvolved inUniProtKB:P49736
GO
GO:0030174 · evidence & context
cochlea developmentinvolved inUniProtKB:P49736
GO
GO:0090102 · evidence & context
mitotic DNA replication initiationinvolved inUniProtKB:P49736
GO
GO:1902975 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179907"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}]
02

Names & Taxonomy

Recommended name
DNA replication licensing factor MCM2
Gene
MCM2
Accession / entry
P49736 · MCM2_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
BM28 · CCNL1 · CDCL1 · KIAA0030 · Minichromosome maintenance protein 2 homolog · Nuclear protein BM28
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 MCM2"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "32453425"
            }
          ],
          "value": "3.6.4.12"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "Minichromosome maintenance protein 2 homolog"
        }
      },
      {
        "fullName": {
          "value": "Nuclear protein BM28"
        }
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:6944"
          }
        ],
        "value": "MCM2"
      },
      "synonyms": [
        {
          "value": "BM28"
        },
        {
          "value": "CCNL1"
        },
        {
          "value": "CDCL1"
        },
        {
          "value": "KIAA0030"
        }
      ]
    }
  ]
}
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
Experimental evidence 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"}]}]
nuclear chromosomelocated in
GO
Evidence & references
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028418"}]}]
chromosome, telomeric regionlocated in
GO
1 publication
Evidence & references
chromatinlocated in
GO
2 publications
Evidence & references
nucleuslocated in
GO
4 publications
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008045"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
  • ECO:0000314 PMID:16899510 ↗ IDA · UniProt · 20110207
    qualifier: located_in
  • ECO:0000314 PMID:21383955 ↗ IDA · UniProt · 20170426
    qualifier: located_in
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: located_in
  • ECO:0000304 PMID:8175912 ↗ TAS · PINC · 20030904
    qualifier: located_in
All recorded location assertions (14)
nucleoplasmlocated in
GO
Evidence & references
  • ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
    qualifier: located_in
  • 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-9757258 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9926522 TAS · Reactome · 20130528
    qualifier: located_in
chromosomelocated in
GO
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0468"}]}]
cytoplasmlocated in
GO
1 publication
Evidence & references
nuclear origin of replication recognition complexpart of
GO
Evidence & references
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}]
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": "UniProtKB", "id": "P97310"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000061923"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008045"}]}]
  • 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": "P55861"}]}]
  • 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.

Deafness, autosomal dominant, 70 DFNA70

A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA70 is characterized by slowly progressive, postlingual hearing impairment.

Experimental evidence 1 publication
Evidence & references

The disease is caused by variants affecting the gene represented in this entry

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Deafness, autosomal dominant, 70",
    "diseaseAccession": "DI-04728",
    "acronym": "DFNA70",
    "description": "A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA70 is characterized by slowly progressive, postlingual hearing impairment.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "616968"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "26196677"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

Natural variants 8

Scroll across the table for evidence and actions.

8 recorded rows

FeaturePositionDescriptionEvidenceInspect
R44CVAR_07704944in DFNA70; increases the apoptotic process; no effect on cell proliferation and cell cycle phase; dbSNP:rs375851208
R → C
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
D68EVAR_02111168in dbSNP:rs3087452
D → E
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.3
No verified residues in this structure
L135FVAR_021112135in dbSNP:rs2307314
L → F
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.3
No verified residues in this structure
E166QVAR_033298166in dbSNP:rs1048225
E → Q
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
A396TVAR_016137396in dbSNP:rs3087450
A → T
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.3
No verified residues in this structure
G501RVAR_033299501in dbSNP:rs13087457
G → R
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
V667MVAR_016138667in dbSNP:rs2307311
V → M
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.3
No verified residues in this structure
A727TVAR_016139727in dbSNP:rs2307313
A → T
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure

Laboratory mutagenesis 5

Scroll across the table for evidence and actions.

5 recorded rows

FeaturePositionDescriptionEvidenceInspect
S27A27Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139.
S → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
S41A41Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139.
S → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
YRAIPELDAY81ARAIPELDAA81–90Loss of interaction with DNAJC9.
YRAIPELDAY → ARAIPELDAA
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
S108A108Reduces phosphorylation by ATR.
S → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
S139A139Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41.
S → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
05

PTM/Processing

Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex.

Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication

Experimental evidence 3 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15210935"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17062569"
        }
      ],
      "value": "Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Initiator methionine1Removed
5 publications
Evidence & references
No verified residues in this structure
ChainPRO_00001940872–904DNA replication licensing factor MCM2
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure

Modifications 19

Scroll across the table for evidence and actions.

19 recorded rows

FeaturePositionDescriptionEvidenceInspect
Modified residue2N-acetylalanine
5 publications
Evidence & references
No verified residues in this structure
Modified residue12Phosphoserine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P97310
No verified residues in this structure
Modified residue13Phosphoserine
4 publications
Evidence & references
No verified residues in this structure
Modified residue25Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue26Phosphoserine
3 publications
Evidence & references
No verified residues in this structure
Modified residue27Phosphoserine
Experimental evidence 7 publications
Evidence & references
No verified residues in this structure
Modified residue32Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue39Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue40Phosphoserine; by CDC7
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Modified residue41Phosphoserine
Experimental evidence 6 publications
Evidence & references
No verified residues in this structure
Modified residue53Phosphoserine; by CDC7
Experimental evidence 4 publications
Evidence & references
No verified residues in this structure
Modified residue59Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue108Phosphoserine; by ATR
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Modified residue137Phosphotyrosine
1 publication
Evidence & references
No verified residues in this structure
Modified residue139Phosphoserine
Experimental evidence 7 publications
Evidence & references
No verified residues in this structure
Modified residue216N6-acetyllysine
1 publication
Evidence & references
No verified residues in this structure
Modified residue381Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue484Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Cross-link178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
1 publication
Evidence & references
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.

19 records
Partner / productSpeciesExperimentsEvidence & actions
AKAP8O43823With P49736Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: O43823. Reported experiment count: 7.

Open protein ↗
ASF1AQ9Y294With P49736Homo sapiens12
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9Y294. Reported experiment count: 12.

Open protein ↗
CDC45O75419With P49736Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: O75419. Reported experiment count: 2.

Open protein ↗
CENPAP49450With P49736Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P49450. Reported experiment count: 3.

Open protein ↗
DONSONQ9NYP3With P49736Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9NYP3. Reported experiment count: 10.

Open protein ↗
FANCMQ8IYD8With P49736Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q8IYD8. Reported experiment count: 5.

Open protein ↗
GINS3Q9BRX5With P49736Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9BRX5. Reported experiment count: 2.

Open protein ↗
H3C12P68431With P49736Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P68431. Reported experiment count: 8.

Open protein ↗
H4C9P62805With P49736Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P62805. Reported experiment count: 9.

Open protein ↗
L3MBTL1Q9Y468With P49736Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9Y468. Reported experiment count: 3.

Open protein ↗
MCM3P25205With P49736Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

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

Open protein ↗
MCM5P33992With P49736Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P33992. Reported experiment count: 5.

Open protein ↗
MCM6Q14566With P49736Homo sapiens18
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q14566. Reported experiment count: 18.

Open protein ↗
MCM7P33993With P49736Homo sapiens24
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P33993. Reported experiment count: 24.

Open protein ↗
MCMBPQ9BTE3With P49736Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9BTE3. Reported experiment count: 5.

Open protein ↗
PLK1P53350With P49736Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: P53350. Reported experiment count: 2.

Open protein ↗
SNF8Q96H20With P49736Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q96H20. Reported experiment count: 8.

Open protein ↗
SSRP1Q08945With P49736Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q08945. Reported experiment count: 7.

Open protein ↗
TERF2IPQ9NYB0With P49736Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P49736. Partner: Q9NYB0. 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 [12, 17, 8]. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 [12, 17, 38, 40, 41, 8]. Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex [38, 40, 41].

Interacts with DBF4 (By similarity). Interacts with KAT7 [13]. May interact with MCM10 [9].

Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR [34]. Forms a co-chaperone complex with DNAJC9 and histone H3.3-H4 heterodimers [39]. Within the complex, interacts (via N-terminus) with DNAJC9 (via C-terminus); the interaction is histone-dependent [39].

Interacts with histones H3.1 and H3.3 [39]. Interacts with AGER/RAGE; the interaction is increased following DNA replication stress and stabilizes the MCM2-7 complex at replication forks [37]

By similarityExperimental evidence 11 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P55861"
        },
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P97310"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11095689"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16387653"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17296731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "28191891"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "33857403"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "36807739"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9305914"
        }
      ],
      "value": "Component of the MCM2-7 complex (PubMed:16899510, PubMed:17296731, PubMed:9305914). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:17296731, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:9305914). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex (PubMed:32453425, PubMed:34694004, PubMed:34700328). Interacts with DBF4 (By similarity). Interacts with KAT7 (PubMed:16387653). May interact with MCM10 (PubMed:11095689). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (PubMed:28191891). Forms a co-chaperone complex with DNAJC9 and histone H3.3-H4 heterodimers (PubMed:33857403). Within the complex, interacts (via N-terminus) with DNAJC9 (via C-terminus); the interaction is histone-dependent (PubMed:33857403). Interacts with histones H3.1 and H3.3 (PubMed:33857403). Interacts with AGER/RAGE; the interaction is increased following DNA replication stress and stabilizes the MCM2-7 complex at replication forks (PubMed:36807739)"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

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

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 40

Scroll across the table for evidence and actions.

40 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 ↗
9VLNexperimentalEM3.42 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 ↗
9VLWexperimentalEM4.06 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 ↗
7CIZexperimentalX-ray1.80 AOpen in Atlas ↗
5BNXexperimentalX-ray2.31 AOpen in Atlas ↗
5JA4experimentalX-ray2.42 AOpen in Atlas ↗
7CJ0experimentalX-ray2.50 AOpen in Atlas ↗
6YA7experimentalX-ray1.67 AOpen in Atlas ↗
5BNVexperimentalX-ray2.79 AOpen in Atlas ↗
4UUZexperimentalX-ray2.90 AOpen in Atlas ↗
5BO0experimentalX-ray2.91 AOpen in Atlas ↗
8YJMexperimentalX-ray4.15 AOpen in Atlas ↗
8YJFexperimentalX-ray4.40 AOpen in Atlas ↗
5C3IexperimentalX-ray3.50 AOpen in Atlas ↗
AF-P49736-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 sequence1904 aa

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
MCM2, N-terminalIPR06150662–181INTERPROdomain

This entry represents the N-terminal region of MCM2 which acts a component of the MCM2-7 complex (MCM complex), the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. It is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.

Full source description

This entry represents the N-terminal region of MCM2 which acts a component of the MCM2-7 complex (MCM complex), the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. It is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. This region is responsible for histone binding.

Source entry ↗
No verified residues in this structure
MCM, N-terminal domainIPR027925197–286INTERPROdomain

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 domainIPR033762294–420INTERPROdomain

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 domainIPR001208456–808INTERPROdomain

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
MCM, AAA-lid domainIPR041562718–802INTERPROdomain

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
DNA replication licensing factor MCM2-like, winged-helix domainIPR059098826–900INTERPROdomain

This is the winged-helix (WH) domain found at the C-terminal end of human DNA replication licensing factor MCM2 and similar eukaryotic proteins. MCM2 is a component of the MCM2-7 complex, the replicative helicase essential for DNA replication initiation and elongation in eukaryotic cells, and a core component of the CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.

Source entry ↗
No verified residues in this structure

UniProt domains, repeats & motifs 3

Scroll across the table for evidence and actions.

3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Domain456–808MCM C-terminal AAA(+) ATPase
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif523–530Walker A
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif587–590Walker B
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Functional sites 4

Scroll across the table for evidence and actions.

4 recorded rows

FeaturePositionDescriptionEvidenceInspect
Zinc finger329–355C4-type
Sequence analysis
Evidence & references
  • ECO:0000255
No verified residues in this structure
Binding site530Binding site
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Binding site531Binding site
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Site656Arginine finger
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Sequence regions 8

Scroll across the table for evidence and actions.

8 recorded rows

FeaturePositionDescriptionEvidenceInspect
Region1–80Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Region2–257Interaction with KAT7
By similarity
Evidence & references
  • ECO:0000250
No verified residues in this structure
Region61–130Interaction with DNJC9
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Region109–167Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Region686–705Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias1–15Polar residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias62–73Acidic residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias111–125Basic 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 · P49736904 aa101,896 Da · source sequence mass

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

MAESSESFTMASSPAQRRRGNDPLTSSPGRSSRRTDALTSSPGRDLPPFEDESEGLLGTEGPLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRQVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCNKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEVNMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHVAKKDNKVAVGELTDEDVKMITSLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDILCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKEEEGLANGSAAEPAMPNTYGVEPLPQEVLKKYIIYAKERVHPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARIHLRDYVIEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLSFRRDNNELLLFILKQLVAEQVTYQRNRFGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSELFRMNKFSHDLKRKMILQQF

Source isoform notes & selection

Isoform sequence differences 0

No annotation is recorded in this UniProt entry.

Sequence conflicts & cautions 6

Scroll across the table for evidence and actions.

6 recorded rows

FeaturePositionDescriptionEvidenceInspect
Sequence conflict1in Ref. 1; CAA47749
M → S
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict109in Ref. 1; CAA47749
Q → R
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict388in Ref. 1; CAA47749
G → R
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict407–408in Ref. 1; CAA47749 and 5; BAA12177
KP → NA
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict495in Ref. 1; CAA47749
L → P
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict555–556in Ref. 1; CAA47749
GL → AV
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Erroneous initiation

Source sequence: BAA04642.1

Extended N-terminus.

Curator inference
Evidence & references
  • ECO:0000305
Erroneous initiation

Source sequence: BAA12177.1

Truncated N-terminus.

Curator inference
Evidence & references
  • ECO:0000305
Erroneous initiation

Source sequence: CAA47749.1

Extended N-terminus.

Curator inference
Evidence & references
  • ECO:0000305
Frameshift

Source sequence: CAA47749.1

Curator inference
Evidence & references
  • ECO:0000305

Recorded secondary structure 88

Scroll across the table for evidence and actions.

88 recorded rows

FeaturePositionDescriptionEvidenceInspect
Beta strand69–74Beta strand
Evidence & references
  • ECO:0007829 PDB:7CIZ
No verified residues in this structure
Helix77–81Helix
Evidence & references
  • ECO:0007829 PDB:7CIZ
No verified residues in this structure
Turn85–87Turn
Evidence & references
  • ECO:0007829 PDB:7CIZ
No verified residues in this structure
Beta strand98–100Beta strand
Evidence & references
  • ECO:0007829 PDB:5BO0
No verified residues in this structure
Helix103–106Helix
Evidence & references
  • ECO:0007829 PDB:7CIZ
No verified residues in this structure
Helix107–124Helix
Evidence & references
  • ECO:0007829 PDB:7CIZ
No verified residues in this structure
Helix182–187Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix189–205Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand209–211Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix214–224Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand229–233Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix234–240Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix242–250Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix252–270Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix272–276Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn277–279Turn
Evidence & references
  • ECO:0007829 PDB:8W0F
No verified residues in this structure
Beta strand282–286Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix289–292Helix
Evidence & references
  • ECO:0007829 PDB:8S09
No verified residues in this structure
Helix294–296Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix299–301Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand304–315Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand319–329Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn330–332Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand335–340Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand343–345Beta strand
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Turn353–355Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand361–379Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix382–384Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand387–389Beta strand
Evidence & references
  • ECO:0007829 PDB:7PFO
No verified residues in this structure
Beta strand393–399Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix400–402Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Beta strand403–405Beta strand
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Beta strand411–419Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand428–432Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand438–446Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix448–450Helix
Evidence & references
  • ECO:0007829 PDB:8W0I
No verified residues in this structure
Turn453–455Turn
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix461–468Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix473–479Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand481–485Beta strand
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Helix489–500Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix507–509Helix
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Beta strand519–523Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand525–528Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix529–539Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand540–550Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand552–554Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand559–562Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn564–566Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand569–572Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix575–578Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn579–581Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand582–588Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix589–591Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix594–606Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand607–615Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand617–621Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand625–630Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix633–635Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand639–641Beta strand
Evidence & references
  • ECO:0007829 PDB:9CAQ
No verified residues in this structure
Helix643–645Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand646–648Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix651–654Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand658–663Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix669–685Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix688–690Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand709–712Beta strand
Evidence & references
  • ECO:0007829 PDB:8S0A
No verified residues in this structure
Beta strand713–715Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix720–728Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand734–736Beta strand
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Beta strand737–739Beta strand
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Helix741–756Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand757–759Beta strand
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Helix764–780Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand784–786Beta strand
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Helix788–804Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix808–817Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix819–822Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn823–825Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix828–850Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand851–853Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand856–861Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix862–871Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix878–882Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix884–888Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand891–894Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn895–898Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand899–902Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
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.

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.

Source dates & provenance

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

Publications in this UniProt entry

1 · A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division.

1994 · J. Cell Sci.

PubMed 8175912 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; SUBCELLULAR LOCATION; VARIANT GLN-166

Todorov I.T., Pepperkok R., Philipova R.N., Kearsey S.E., Ansorge W., Werner D.

2 · Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1.

1994 · DNA Res.

PubMed 7584026 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]

Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.

· Reference

JUL-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS GLU-68; PHE-135; THR-396; MET-667 AND THR-727

4 · 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]; VARIANTS ARG-501 AND THR-727

All source publications (42)
· Homo sapiens DNA replication licensing factor (huMCM2).

MAR-1996 ·

Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 2-904

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

· Cloning of human full-length CDSs in BD Creator(TM) system donor vector.

AUG-2003 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-904

Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.

7 · The human gene for nuclear protein BM28 (CDCL1), a new member of the early S-phase family of proteins, maps to chromosome band 3q21.

1994 · Cytogenet. Cell Genet.

PubMed 8258304 ↗
Scope & authors

CHROMOSOMAL LOCATION

Mincheva A., Todorov I.T., Werner D., Fink T.M., Lichter P.

8 · A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex.

1997 · J. Biol. Chem.

PubMed 9305914 ↗
Scope & authors

IDENTIFICATION IN THE MCM2-7 COMPLEX

Ishimi Y.

9 · The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase.

2000 · Nucleic Acids Res.

PubMed 11095689 ↗
Scope & authors

INTERACTION WITH MCM10

Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., Hurwitz J., Yatagai F., Hanaoka F.

10 · 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-108; MUTAGENESIS OF SER-108

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

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

2006 · Cell

PubMed 17081983 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

12 · 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

PHOSPHORYLATION AT SER-27; SER-41; SER-53; SER-108 AND SER-139; MUTAGENESIS OF SER-27; SER-41 AND SER-139; IDENTIFICATION IN THE MCM2-7 COMPLEX; ATPASE ACTIVITY OF THE MCM2-7 COMPLEX

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

13 · ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation.

2006 · Mol. Cell

PubMed 16387653 ↗
Scope & authors

INTERACTION WITH KAT7

Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.

14 · 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-27 AND SER-41; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

15 · 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

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

16 · Cdc7 is an active kinase in human cancer cells undergoing replication stress.

2007 · J. Biol. Chem.

PubMed 17062569 ↗
Scope & authors

PHOSPHORYLATION AT SER-40 AND SER-53

Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.

17 · 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; IDENTIFICATION BY MASS SPECTROMETRY

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

18 · ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

2007 · Science

PubMed 17525332 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.

19 · Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

2008 · J. Proteome Res.

PubMed 18220336 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III

20 · Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

2008 · J. Proteome Res.

PubMed 19367720 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.

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

2008 · Mol. Cell

PubMed 18691976 ↗
Scope & authors

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.

22 · A quantitative atlas of mitotic phosphorylation.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18669648 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-39; SER-40; SER-41; SER-53 AND SER-139; 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.

23 · 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.

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-27; THR-59; SER-108 AND SER-139; 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 · Lysine acetylation targets protein complexes and co-regulates major cellular functions.

2009 · Science

PubMed 19608861 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.

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

2010 · Sci. Signal.

PubMed 20068231 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; SER-41; SER-108 AND SER-139; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; 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.

27 · 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.

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

2011 · Sci. Signal.

PubMed 21406692 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-26; SER-27; SER-41; SER-139 AND SER-381; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; 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.

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

2013 · J. Proteome Res.

PubMed 23186163 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-25; SER-26; SER-27; SER-32; SER-40; SER-41; SER-139 AND SER-484; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

32 · An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

2014 · J. Proteomics

PubMed 24275569 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; TYR-137 AND SER-139; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.

33 · Claspin recruits Cdc7 kinase for initiation of DNA replication in human cells.

2016 · Nat. Commun.

PubMed 27401717 ↗
Scope & authors

PHOSPHORYLATION AT SER-53

Yang C.C., Suzuki M., Yamakawa S., Uno S., Ishii A., Yamazaki S., Fukatsu R., Fujisawa R., Sakimura K., Tsurimoto T., Masai H.

34 · Mutations in DONSON disrupt replication fork stability and cause microcephalic dwarfism.

2017 · Nat. Genet.

PubMed 28191891 ↗
Scope & authors

INTERACTION WITH DONSON

Reynolds J.J., Bicknell L.S., Carroll P., Higgs M.R., Shaheen R., Murray J.E., Papadopoulos D.K., Leitch A., Murina O., Tarnauskaite Z., Wessel S.R., Zlatanou A., Vernet A., von Kriegsheim A., Mottram R.M., Logan C.V., Bye H., Li Y., Brean A., Maddirevula S., Challis R.C., Skouloudaki K., Almoisheer A., Alsaif H.S., Amar A., Prescott N.J., Bober M.B., Duker A., Faqeih E., Seidahmed M.Z., Al Tala S., Alswaid A., Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M., Brady A.F., Chessa L., Cox H., Fischetto R., Heller R., Henderson B.D., Hobson E., Nuernberg P., Percin E.F., Peron A., Spaccini L., Quigley A.J., Thakur S., Wise C.A., Yoon G., Alnemer M., Tomancak P., Yigit G., Taylor A.M., Reijns M.A., Simpson M.A., Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P., Stewart G.S.

35 · Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

2017 · Nat. Struct. Mol. Biol.

PubMed 28112733 ↗
Scope & authors

SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., Nielsen M.L.

36 · 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.

37 · The importance of nuclear RAGE-Mcm2 axis in diabetes or cancer-associated replication stress.

2023 · Nucleic Acids Res.

PubMed 36807739 ↗
Scope & authors

INTERACTION WITH AGER

Han Z., Andrs M., Madhavan B.K., Kaymak S., Sulaj A., Kender Z., Kopf S., Kihm L., Pepperkok R., Janscak P., Nawroth P., Kumar V.

38 · 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 IN CMG COMPLEX; SUBUNIT; CATALYTIC ACTIVITY; FUNCTION

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

39 · DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.

2021 · Mol. Cell

PubMed 33857403 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DNJC9 171-249 MUTANT CYS-243 AND HISTONES H3.3 58-136 AND H4; IDENTIFICATION IN A CO-CHAPERONE COMPLEX WITH DNJC9 AND HISTONES H3.3 AND H4; INTERACTION WITH DNJC9; H3.1 AND H3.3; MUTAGENESIS OF 81-TYR--TYR-90

Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y., Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L., Patel D.J., Huang H., Groth A.

40 · 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.

41 · 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.

42 · Whole exome sequencing identified MCM2 as a novel causative gene for autosomal dominant nonsyndromic deafness in a chinese family.

2015 · PLoS ONE

PubMed 26196677 ↗
Scope & authors

INVOLVEMENT IN DFNA70; VARIANT DFNA70 CYS-44; CHARACTERIZATION OF VARIANT DFNA70 CYS-44; FUNCTION

Gao J., Wang Q., Dong C., Chen S., Qi Y., Liu Y.

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.

156 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
PTM:0PTMprocessing
DISEASE:0DISEASEdisease
MISCELLANEOUS:0MISCELLANEOUSfunction
SIMILARITY:0SIMILARITYdomains
SEQUENCE CAUTION:0SEQUENCE CAUTIONsequence
SEQUENCE CAUTION:1SEQUENCE CAUTIONsequence
SEQUENCE CAUTION:2SEQUENCE CAUTIONsequence
SEQUENCE CAUTION:3SEQUENCE CAUTIONsequence
feature-0Initiator methionineprocessing
feature-1Chainprocessing
feature-2Domaindomains
feature-3Zinc fingerdomains
feature-4Regiondomains
feature-5Regiondomains
feature-6Regiondomains
feature-7Regiondomains
feature-8Regiondomains
feature-9Motifdomains
feature-10Motifdomains
feature-11Compositional biasdomains
feature-12Compositional biasdomains
feature-13Compositional biasdomains
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-35Cross-linkprocessing
feature-36Natural variantdisease
feature-37Natural variantdisease
feature-38Natural variantdisease
feature-39Natural variantdisease
feature-40Natural variantdisease
feature-41Natural variantdisease
feature-42Natural variantdisease
feature-43Natural variantdisease
feature-44Mutagenesisdisease
feature-45Mutagenesisdisease
feature-46Mutagenesisdisease
feature-47Mutagenesisdisease
feature-48Mutagenesisdisease
feature-49Sequence conflictsequence
feature-50Sequence conflictsequence
feature-51Sequence conflictsequence
feature-52Sequence conflictsequence
feature-53Sequence conflictsequence
feature-54Sequence conflictsequence
feature-55Beta strandsequence
feature-56Helixsequence
feature-57Turnsequence
feature-58Beta strandsequence
feature-59Helixsequence
feature-60Helixsequence
feature-61Helixsequence
feature-62Helixsequence
feature-63Beta strandsequence
feature-64Helixsequence
feature-65Beta strandsequence
feature-66Helixsequence
feature-67Helixsequence
feature-68Helixsequence
feature-69Helixsequence
feature-70Turnsequence
feature-71Beta strandsequence
feature-72Helixsequence
feature-73Helixsequence
feature-74Helixsequence
feature-75Beta strandsequence
feature-76Beta strandsequence
feature-77Turnsequence
feature-78Beta strandsequence
feature-79Beta strandsequence
feature-80Turnsequence
feature-81Beta strandsequence
feature-82Helixsequence
feature-83Beta strandsequence
feature-84Beta strandsequence
feature-85Helixsequence
feature-86Beta strandsequence
feature-87Beta strandsequence
feature-88Beta strandsequence
feature-89Beta strandsequence
feature-90Helixsequence
feature-91Turnsequence
feature-92Helixsequence
feature-93Helixsequence
feature-94Beta strandsequence
feature-95Helixsequence
feature-96Helixsequence
feature-97Beta strandsequence
feature-98Beta strandsequence
feature-99Helixsequence
feature-100Beta strandsequence
feature-101Beta strandsequence
feature-102Beta strandsequence
feature-103Turnsequence
feature-104Beta strandsequence
feature-105Helixsequence
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feature-107Beta strandsequence
feature-108Helixsequence
feature-109Helixsequence
feature-110Beta strandsequence
feature-111Beta strandsequence
feature-112Beta strandsequence
feature-113Helixsequence
feature-114Beta strandsequence
feature-115Helixsequence
feature-116Beta strandsequence
feature-117Helixsequence
feature-118Beta strandsequence
feature-119Helixsequence
feature-120Helixsequence
feature-121Beta strandsequence
feature-122Beta strandsequence
feature-123Helixsequence
feature-124Beta strandsequence
feature-125Beta strandsequence
feature-126Helixsequence
feature-127Beta strandsequence
feature-128Helixsequence
feature-129Beta strandsequence
feature-130Helixsequence
feature-131Helixsequence
feature-132Helixsequence
feature-133Turnsequence
feature-134Helixsequence
feature-135Beta strandsequence
feature-136Beta strandsequence
feature-137Helixsequence
feature-138Helixsequence
feature-139Helixsequence
feature-140Beta strandsequence
feature-141Turnsequence
feature-142Beta strandsequence