ALPHASUITEATLASTM
MCM4 · P33991Homo sapiens
PROTEIN OVERVIEW

MCM4DNA replication licensing factor MCM4

P33991Homo 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.

Sequence863 aa
Source mass96.56 kDa
Recorded PDB entries28
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 [9, 24, 28, 30, 29, 27, 7]. 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 [9, 24, 28, 7]

Experimental evidence 7 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25661590"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "35585232"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9305914"
        }
      ],
      "value": "Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:9305914). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:9305914)"
    }
  ],
  "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

By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P49717
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P49717"
        }
      ],
      "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": "25661590"
      }
    ]
  },
  "physiologicalReactions": [
    {
      "directionType": "left-to-right",
      "reactionCrossReference": {
        "database": "Rhea",
        "id": "RHEA:13066"
      },
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25661590"
        }
      ]
    }
  ]
}

GO functions & biological processes

DNA helicase activitycontributes toUniProtKB:P33991
GO
GO:0003678 · evidence & context
single-stranded DNA bindingcontributes toUniProtKB:P33991
GO
GO:0003697 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20220203
    qualifier: contributes_to
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49717"}]}]
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: contributes_to
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49717"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000023353"}]}]
  • ECO:0000314 PMID:25661590 ↗ IDA · UniProt · 20220204
    qualifier: contributes_to
single-stranded DNA helicase activitycontributes toUniProtKB:P33991
GO
GO:0017116 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210414
    qualifier: contributes_to
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179711"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC211.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC25D12.03c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000406"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000758"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000003169"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000004264"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
DNA bindingenablesUniProtKB:P33991
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": "IPR008047"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
DNA helicase activityenablesUniProtKB:P33991
GO
GO:0003678 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49717"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000023353"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}, {"connectedXrefs": [{"db": "EC", "id": "3.6.4.12"}]}]
All recorded function and process assertions (16)
protein bindingenablesUniProtKB:P33991 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:12364596 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:23764002 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:33654309 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P33991
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:16902406 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
  • ECO:0000353 PMID:16902406 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y5B9"}]}]
  • ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:22190034 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Q2G4"}]}]
  • ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:24407287 ↗ IPI · AgBase · 20150317
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9ULZ3"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
  • ECO:0000353 PMID:28514442 ↗ 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": "Q08945"}]}]
  • ECO:0000353 PMID:35271311 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
ATP bindingenablesUniProtKB:P33991
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": "IPR008047"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
ATP hydrolysis activityenablesUniProtKB:P33991
GO
GO:0016887 · evidence & context
  • ECO:0007322 GO_REF:0000116 IEA · RHEA · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "RHEA", "id": "13065"}]}]
  • ECO:0000269 PMID:25661590 ↗ EXP · UniProt · 20251027
    qualifier: enables
double-strand break repair via break-induced replicationinvolved inUniProtKB:P33991
GO
GO:0000727 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190209
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
DNA metabolic processinvolved inUniProtKB:P33991
GO
GO:0006259 · evidence & context
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028839"}]}]
DNA replicationinvolved inUniProtKB:P33991
GO
GO:0006260 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}]
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: involved_in
  • ECO:0000303 PMID:9465298 ↗ NAS · UniProt · 20021218
    qualifier: involved_in
DNA replication initiationinvolved inUniProtKB:P33991
GO
GO:0006270 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}]
DNA strand elongation involved in DNA replicationinvolved inUniProtKB:P33991
GO
GO:0006271 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
regulation of DNA-templated DNA replication initiationinvolved inUniProtKB:P33991
GO
GO:0030174 · evidence & context
mitotic DNA replication initiationinvolved inUniProtKB:P33991
GO
GO:1902975 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}]
02

Names & Taxonomy

Recommended name
DNA replication licensing factor MCM4
Gene
MCM4
Accession / entry
P33991 · MCM4_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
CDC21 · CDC21 homolog · P1-CDC21
Full taxonomy & recorded names

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

{
  "names": {
    "recommendedName": {
      "fullName": {
        "value": "DNA replication licensing factor MCM4"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000250",
              "source": "UniProtKB",
              "id": "P49717"
            }
          ],
          "value": "3.6.4.12"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "CDC21 homolog"
        }
      },
      {
        "fullName": {
          "value": "P1-CDC21"
        }
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:6947"
          }
        ],
        "value": "MCM4"
      },
      "synonyms": [
        {
          "value": "CDC21"
        }
      ]
    }
  ]
}
03

Subcellular Location

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

NucleusReported location

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

UniProt
Curator inference 1 publication
Evidence & references
ChromosomeReported location

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

UniProt
Curator inference 1 publication
Evidence & references
nucleusis active in
GO
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260528
    qualifier: is_active_in
    withFrom: [{"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT1G44900"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT2G07690"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT2G16440"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT4G02060"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT5G44635"}]}, {"connectedXrefs": [{"db": "AGI_LocusCode", "id": "AT5G46280"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003227"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0014861"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0015929"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0017577"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0020633"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0284442"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:101845"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:105380"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1298227"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1918817"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179712"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPAC1B2.05"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC25D12.03c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPBC4.04c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC1682.02c"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000119"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000000406"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000003169"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000004264"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP3"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "I0IUP4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P25205"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P30664"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33991"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33992"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49736"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P49739"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P55862"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q14566"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q24849"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q381H2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q382V6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q383B6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q384N2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q385L1"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q389T6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q38E36"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q586W7"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5F310"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5FWY4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q5XK83"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q6NRM6"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q8ILR7"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91876"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJA3"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003154"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003155"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003156"}]}]
chromosome, telomeric regionlocated in
GO
1 publication
Evidence & references
nucleuslocated in
GO
Published statement 2 publications
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
  • ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015
    qualifier: located_in
  • ECO:0000303 PMID:8265339 ↗ NAS · UniProt · 20021218
    qualifier: located_in
nucleoplasmlocated in
GO
Evidence & references
  • ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-176298 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-176318 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68916 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68917 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68918 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68919 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68940 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68944 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-68954 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-69019 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9749253 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9757257 TAS · Reactome · 20130731
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9757258 TAS · Reactome · 20130731
    qualifier: located_in
chromosomelocated in
GO
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00026361"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0468"}]}]
membranelocated in
GO
1 publication
Evidence & references
All recorded location assertions (10)
MCM complexpart of
GO
3 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": "P49717"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000023353"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}]
  • ECO:0000314 PMID:17296731 ↗ IDA · UniProt · 20110124
    qualifier: part_of
  • ECO:0000353 PMID:22540012 ↗ IPI · ComplexPortal · 20251229
    qualifier: part_of
  • ECO:0000314 PMID:25661590 ↗ IDA · UniProt · 20220204
    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": "Q5XK83"}]}]
  • 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.

Immunodeficiency 54 IMD54

An autosomal recessive disorder characterized by severe intra- and extrauterine growth retardation, microcephaly, decreased numbers of natural killer cells, and recurrent viral infections, most often affecting the respiratory tract and leading to respiratory failure. Affected individuals also have adrenal insufficiency requiring corticosteroid replacement therapy and may have an increased susceptibility to cancer.

Experimental evidence 3 publications
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": "Immunodeficiency 54",
    "diseaseAccession": "DI-03605",
    "acronym": "IMD54",
    "description": "An autosomal recessive disorder characterized by severe intra- and extrauterine growth retardation, microcephaly, decreased numbers of natural killer cells, and recurrent viral infections, most often affecting the respiratory tract and leading to respiratory failure. Affected individuals also have adrenal insufficiency requiring corticosteroid replacement therapy and may have an increased susceptibility to cancer.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "609981"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "22354167"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "22354170"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "22499342"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

Natural variants 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
E460GVAR_020500460in dbSNP:rs17287663
E → G
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.2
No verified residues in this structure
L650MVAR_020501650in dbSNP:rs762679
L → M
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure

Laboratory mutagenesis 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
G364R364Reduced MCM complex DNA helicase activity. No effect on MCM complex formation. No effect on MCM complex ssDNA binding and ATPase activity.
G → R
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
05

PTM/Processing

Sumoylated; SUMO2 modified in response to stress caused by inhibition of proteasome activity (in vitro)

By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P49717
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P49717"
        }
      ],
      "value": "Sumoylated; SUMO2 modified in response to stress caused by inhibition of proteasome activity (in vitro)"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Initiator methionine1Removed
3 publications
Evidence & references
No verified residues in this structure
ChainPRO_00001941012–863DNA replication licensing factor MCM4
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure

Modifications 20

Scroll across the table for evidence and actions.

20 recorded rows

FeaturePositionDescriptionEvidenceInspect
Modified residue2N-acetylserine
3 publications
Evidence & references
No verified residues in this structure
Modified residue6Phosphoserine; by CDC7
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue7Phosphothreonine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue19Phosphothreonine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P49717
No verified residues in this structure
Modified residue26Phosphoserine
2 publications
Evidence & references
No verified residues in this structure
Modified residue31Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue32Phosphoserine
3 publications
Evidence & references
No verified residues in this structure
Modified residue34Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue102Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue105Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue110Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue120Phosphoserine
5 publications
Evidence & references
No verified residues in this structure
Modified residue131Phosphoserine
4 publications
Evidence & references
No verified residues in this structure
Modified residue142Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue145Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue220N6-acetyllysine
1 publication
Evidence & references
No verified residues in this structure
Modified residue450N6-acetyllysine
1 publication
Evidence & references
No verified residues in this structure
Modified residue858N6-acetyllysine
By similarity
Evidence & references
  • ECO:0000250 UniProtKB:P49717
No verified residues in this structure
Cross-link439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
1 publication
Evidence & references
No verified residues in this structure
Cross-link798Glycyl 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.

5 records
Partner / productSpeciesExperimentsEvidence & actions
MCM7P33993With P33991Homo sapiens16
IntAct evidence

Pair evidence in IntAct ↗

Source product: P33991. Partner: P33993. Reported experiment count: 16.

Open protein ↗
MCMBPQ9BTE3With P33991Homo sapiens14
IntAct evidence

Pair evidence in IntAct ↗

Source product: P33991. Partner: Q9BTE3. Reported experiment count: 14.

Open protein ↗
SSRP1Q08945With P33991Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P33991. Partner: Q08945. Reported experiment count: 8.

Open protein ↗
SUPT16HQ9Y5B9With P33991Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P33991. Partner: Q9Y5B9. Reported experiment count: 3.

Open protein ↗
ORFQ9Q2G4With P33991Human immunodeficiency virus type 1Cross-species3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P33991. Partner: Q9Q2G4. Reported experiment count: 3.

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 [9, 7]. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 [9, 28, 7]. Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex [28, 30, 29].

Interacts with MCMBP [10]

Experimental evidence 6 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16899510"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17296731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32453425"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34694004"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34700328"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9305914"
        }
      ],
      "value": "Component of the MCM2-7 complex (PubMed:16899510, PubMed:9305914). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:32453425, PubMed:9305914). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex (PubMed:32453425, PubMed:34694004, PubMed:34700328). Interacts with MCMBP (PubMed:17296731)"
    }
  ],
  "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 29

Scroll across the table for evidence and actions.

29 recorded rows

RecordEvidence typeMethodResolutionOpen
7W1YexperimentalEM2.59 AOpen in Atlas ↗
9E2ZexperimentalEM2.60 AOpen in Atlas ↗
7PLOexperimentalEM2.80 AOpen in Atlas ↗
8W0FexperimentalEM2.80 AOpen in Atlas ↗
8S09experimentalEM3.10 AOpen in Atlas ↗
7PFOexperimentalEM3.20 AOpen in Atlas ↗
8S0AexperimentalEM3.20 AOpen in Atlas ↗
9CAQexperimentalEM3.20 AOpen in Atlas ↗
9LXDexperimentalEM3.27 AOpen in Atlas ↗
6XTXexperimentalEM3.29 AOpen in Atlas ↗
22VTexperimentalEM3.30 AOpen in Atlas ↗
8B9DexperimentalEM3.40 AOpen in Atlas ↗
8W0EexperimentalEM3.40 AOpen in Atlas ↗
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 ↗
AF-P33991-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 sequence1863 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 5

Scroll across the table for evidence and actions.

5 recorded rows

AnnotationPositionSource & interpretationInspect
MCM, N-terminal domainIPR027925163–264INTERPROdomain

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 domainIPR033762270–398INTERPROdomain

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 domainIPR001208441–775INTERPROdomain

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 domainIPR041562686–768INTERPROdomain

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
MCM4, winged helix domainPF21128793–861PFAMdomain

DNA replication licensing factor MCM4 is a component of the MCM2-MCM7 complex which consists of six sequence-related AAA+ type ATPases/helicases that form a heterohexameric ring essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. This is the winged helix domain (WHD) found at the C-terminal of MCM4.

Full source description

DNA replication licensing factor MCM4 is a component of the MCM2-MCM7 complex which consists of six sequence-related AAA+ type ATPases/helicases that form a heterohexameric ring essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. This is the winged helix domain (WHD) found at the C-terminal of MCM4. Upon ssDNA binding the MCM5-WHD moves out of the central channel and becomes disordered, the MCM6-WHD moves backward and away from the channel, and the MCM4-WHD now partially occludes the channel opening. These changes enable CMG (Cdc45, Mcm2-7, GINS, the eukaryotic replicative helicase) to encircle dsDNA, and is consistent with reports that showed the MCM2-7 matures into two fully assembled CMGs on dsDNA before origin DNA unwinding occurs.

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
Domain441–775MCM C-terminal AAA(+) ATPase
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif510–517Walker A
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure
Motif574–577Walker B
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Functional sites 9

Scroll across the table for evidence and actions.

9 recorded rows

FeaturePositionDescriptionEvidenceInspect
Binding site471Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site497Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site516Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site517Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site618Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site643Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site732Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Binding site735Binding site
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Site643Arginine finger
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU01410
No verified residues in this structure

Sequence regions 3

Scroll across the table for evidence and actions.

3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Region1–60Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Region91–126Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias1–10Low complexity
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 · P33991863 aa96,558 Da · source sequence mass

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

MSSPASTPSRRGSRRGRATPAQTPRSEDARSSPSQRRRGEDSTSTGELQPMPTSPGVDLQSPAAQDVLFSSPPQMHSSAIPLDFDVSSPLTYGTPSSRVEGTPRSGVRGTPVRQRPDLGSAQKGLQVDLQSDGAAAEDIVASEQSLGQKLVIWGTDVNVAACKENFQRFLQRFIDPLAKEEENVGIDITEPLYMQRLGEINVIGEPFLNVNCEHIKSFDKNLYRQLISYPQEVIPTFDMAVNEIFFDRYPDSILEHQIQVRPFNALKTKNMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFQCQVCAHTTRVEMDRGRIAEPSVCGRCHTTHSMALIHNRSLFSDKQMIKLQESPEDMPAGQTPHTVILFAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVSNVKSVYKTHIDVIHYRKTDAKRLHGLDEEAEQKLFSEKRVELLKELSRKPDIYERLASALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEINILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPIESQWNPKKTTIENIQLPHTLLSRFDLIFLLLDPQDEAYDRRLAHHLVALYYQSEEQAEEELLDMAVLKDYIAYAHSTIMPRLSEEASQALIEAYVDMRKIGSSRGMVSAYPRQLESLIRLAEAHAKVRLSNKVEAIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATSRKRKEELAEALKKLILSKGKTPALKYQQLFEDIRGQSDIAITKDMFEEALRALADDDFLTVTGKTVRLL

Source isoform notes & selection

Isoform sequence differences 0

No annotation is recorded in this UniProt entry.

Sequence conflicts & cautions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Sequence conflict62in Ref. 1; CAA52801
P → T
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure
Sequence conflict206in Ref. 1; CAA52801
P → Q
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure

Recorded secondary structure 81

Scroll across the table for evidence and actions.

81 recorded rows

FeaturePositionDescriptionEvidenceInspect
Helix110–114Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix116–118Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand126–129Beta strand
Evidence & references
  • ECO:0007829 PDB:8W0F
No verified residues in this structure
Helix147–149Helix
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Beta strand150–152Beta strand
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Turn153–155Turn
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Helix159–171Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand182–184Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand188–190Beta strand
Evidence & references
  • ECO:0007829 PDB:8W0F
No verified residues in this structure
Helix192–203Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand207–211Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix212–218Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix220–228Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix230–247Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand259–263Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix271–273Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix276–278Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand281–292Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand296–306Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn307–309Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand312–316Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand318–324Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn329–331Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand337–356Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn358–360Turn
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix365–368Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Beta strand369–375Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix376–378Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Beta strand387–397Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand400–402Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand408–411Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand413–422Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand426–428Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix432–436Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand438–440Beta strand
Evidence & references
  • ECO:0007829 PDB:8S0A
No verified residues in this structure
Helix443–453Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix458–464Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand468–470Beta strand
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix474–485Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn493–496Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand506–515Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix516–524Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand527–534Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix535–537Helix
Evidence & references
  • ECO:0007829 PDB:8S09
No verified residues in this structure
Helix540–544Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand545–549Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn551–553Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand556–560Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix562–565Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn566–568Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand569–579Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix581–584Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix586–593Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand594–599Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand600–602Beta strand
Evidence & references
  • ECO:0007829 PDB:7PFO
No verified residues in this structure
Beta strand604–608Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand612–617Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix620–622Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand626–628Beta strand
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Helix630–634Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix638–642Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand647–650Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix656–668Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn669–671Turn
Evidence & references
  • ECO:0007829 PDB:6XTX
No verified residues in this structure
Helix684–697Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix704–721Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand723–726Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix731–747Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand751–753Beta strand
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Helix755–767Helix
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Turn768–770Turn
Evidence & references
  • ECO:0007829 PDB:7W1Y
No verified residues in this structure
Beta strand773–775Beta strand
Evidence & references
  • ECO:0007829 PDB:7PLO
No verified residues in this structure
Beta strand776–778Beta strand
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix784–788Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Helix792–806Helix
Evidence & references
  • ECO:0007829 PDB:9E2Z
No verified residues in this structure
Turn812–814Turn
Evidence & references
  • ECO:0007829 PDB:8B9D
No verified residues in this structure
Beta strand815–819Beta strand
Evidence & references
  • ECO:0007829 PDB:8B9D
No verified residues in this structure
Helix820–830Helix
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Helix837–849Helix
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand854–856Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
Beta strand859–861Beta strand
Evidence & references
  • ECO:0007829 PDB:9LXD
No verified residues in this structure
12

Homologs

OMA orthologs

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

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

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 homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins.

1995 · Eur. J. Biochem.

PubMed 7601140 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA]; VARIANT MET-650

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

· Reference

APR-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT GLY-460

3 · 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]; VARIANT MET-650

4 · The promoters for human DNA-PKcs (PRKDC) and MCM4: divergently transcribed genes located at chromosome 8 band q11.

1998 · Genomics

PubMed 9465298 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-712

Connelly M.A., Zhang H., Kieleczawa J., Anderson C.W.

All source publications (30)
5 · MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close neighbours located on chromosome 8q12-->q13.

1997 · Cytogenet. Cell Genet.

PubMed 9284934 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-23

Ladenburger E.M., Fackelmayer F.O., Hameister H., Knippers R.

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

1993 · Nucleic Acids Res.

PubMed 8265339 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 440-863; VARIANT MET-650

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

7 · 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; FUNCTION

Ishimi Y.

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

2006 · Cell

PubMed 17081983 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

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

2006 · Mol. Biol. Cell

PubMed 16899510 ↗
Scope & authors

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

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

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

2007 · Mol. Cell. Biol.

PubMed 17296731 ↗
Scope & authors

HELICASE ACTIVITY OF THE MCM2-3 COMPLEX; INTERACTION WITH MCMBP; IDENTIFICATION IN THE MCM2-7 COMPLEX; IDENTIFICATION BY MASS SPECTROMETRY

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

11 · 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

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

2008 · Mol. Cell

PubMed 18691976 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; 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.

13 · 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; SER-31; SER-32 AND SER-34; 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.

14 · 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-131; 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.

15 · Lysine acetylation targets protein complexes and co-regulates major cellular functions.

2009 · Science

PubMed 19608861 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-450; 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.

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

2010 · Sci. Signal.

PubMed 20068231 ↗
Scope & authors

ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-120; SER-131; SER-142 AND SER-145; 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.

17 · 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.

18 · 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 SER-2; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-131; 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.

19 · MCM4 mutation causes adrenal failure, short stature, and natural killer cell deficiency in humans.

2012 · J. Clin. Invest.

PubMed 22354170 ↗
Scope & authors

INVOLVEMENT IN IMD54

Hughes C.R., Guasti L., Meimaridou E., Chuang C.H., Schimenti J.C., King P.J., Costigan C., Clark A.J., Metherell L.A.

20 · Partial MCM4 deficiency in patients with growth retardation, adrenal insufficiency, and natural killer cell deficiency.

2012 · J. Clin. Invest.

PubMed 22354167 ↗
Scope & authors

INVOLVEMENT IN IMD54

Gineau L., Cognet C., Kara N., Lach F.P., Dunne J., Veturi U., Picard C., Trouillet C., Eidenschenk C., Aoufouchi S., Alcais A., Smith O., Geissmann F., Feighery C., Abel L., Smogorzewska A., Stillman B., Vivier E., Casanova J.L., Jouanguy E.

21 · Recessive mutations in MCM4/PRKDC cause a novel syndrome involving a primary immunodeficiency and a disorder of DNA repair.

2012 · J. Med. Genet.

PubMed 22499342 ↗
Scope & authors

INVOLVEMENT IN IMD54

Casey J.P., Nobbs M., McGettigan P., Lynch S., Ennis S.

22 · 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 SER-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.

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

2013 · J. Proteome Res.

PubMed 23186163 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-32; THR-102; SER-105; THR-110; SER-120 AND SER-131; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

24 · G364R mutation of MCM4 detected in human skin cancer cells affects DNA helicase activity of MCM4/6/7 complex.

2015 · J. Biochem.

PubMed 25661590 ↗
Scope & authors

FUNCTION; MUTAGENESIS OF GLY-364; CATALYTIC ACTIVITY

Ishimi Y., Irie D.

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

2016 · Nat. Commun.

PubMed 27401717 ↗
Scope & authors

PHOSPHORYLATION AT SER-6 AND THR-7

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

26 · 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-439 AND LYS-798; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

27 · 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.

28 · 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 ATP ANALOG AND WDHD1 IN CMG COMPLEX; SUBUNIT; FUNCTION

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

29 · 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.

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

2021 · EMBO J.

PubMed 34694004 ↗
Scope & authors

STRUCTURE BY ELECTRON MICROSCOPY IN REPLISOME; SUBUNIT; FUNCTION

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

Annotation coverage audit

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

132 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
feature-0Initiator methionineprocessing
feature-1Chainprocessing
feature-2Domaindomains
feature-3Regiondomains
feature-4Regiondomains
feature-5Motifdomains
feature-6Motifdomains
feature-7Compositional biasdomains
feature-8Binding sitedomains
feature-9Binding sitedomains
feature-10Binding sitedomains
feature-11Binding sitedomains
feature-12Binding sitedomains
feature-13Binding sitedomains
feature-14Binding sitedomains
feature-15Binding sitedomains
feature-16Sitedomains
feature-17Modified residueprocessing
feature-18Modified residueprocessing
feature-19Modified residueprocessing
feature-20Modified residueprocessing
feature-21Modified residueprocessing
feature-22Modified residueprocessing
feature-23Modified residueprocessing
feature-24Modified residueprocessing
feature-25Modified residueprocessing
feature-26Modified residueprocessing
feature-27Modified residueprocessing
feature-28Modified residueprocessing
feature-29Modified residueprocessing
feature-30Modified residueprocessing
feature-31Modified residueprocessing
feature-32Modified residueprocessing
feature-33Modified residueprocessing
feature-34Modified residueprocessing
feature-35Cross-linkprocessing
feature-36Cross-linkprocessing
feature-37Natural variantdisease
feature-38Natural variantdisease
feature-39Mutagenesisdisease
feature-40Sequence conflictsequence
feature-41Sequence conflictsequence
feature-42Helixsequence
feature-43Helixsequence
feature-44Beta strandsequence
feature-45Helixsequence
feature-46Beta strandsequence
feature-47Turnsequence
feature-48Helixsequence
feature-49Beta strandsequence
feature-50Beta strandsequence
feature-51Helixsequence
feature-52Beta strandsequence
feature-53Helixsequence
feature-54Helixsequence
feature-55Helixsequence
feature-56Beta strandsequence
feature-57Helixsequence
feature-58Helixsequence
feature-59Beta strandsequence
feature-60Beta strandsequence
feature-61Turnsequence
feature-62Beta strandsequence
feature-63Beta strandsequence
feature-64Turnsequence
feature-65Beta strandsequence
feature-66Turnsequence
feature-67Helixsequence
feature-68Beta strandsequence
feature-69Helixsequence
feature-70Beta strandsequence
feature-71Beta strandsequence
feature-72Beta strandsequence
feature-73Beta strandsequence
feature-74Beta strandsequence
feature-75Helixsequence
feature-76Beta strandsequence
feature-77Helixsequence
feature-78Helixsequence
feature-79Beta strandsequence
feature-80Helixsequence
feature-81Turnsequence
feature-82Beta strandsequence
feature-83Helixsequence
feature-84Beta strandsequence
feature-85Helixsequence
feature-86Helixsequence
feature-87Beta strandsequence
feature-88Turnsequence
feature-89Beta strandsequence
feature-90Helixsequence
feature-91Turnsequence
feature-92Beta strandsequence
feature-93Helixsequence
feature-94Helixsequence
feature-95Beta strandsequence
feature-96Beta strandsequence
feature-97Beta strandsequence
feature-98Beta strandsequence
feature-99Helixsequence
feature-100Beta strandsequence
feature-101Helixsequence
feature-102Helixsequence
feature-103Beta strandsequence
feature-104Helixsequence
feature-105Turnsequence
feature-106Helixsequence
feature-107Helixsequence
feature-108Beta strandsequence
feature-109Helixsequence
feature-110Beta strandsequence
feature-111Helixsequence
feature-112Turnsequence
feature-113Beta strandsequence
feature-114Beta strandsequence
feature-115Helixsequence
feature-116Helixsequence
feature-117Turnsequence
feature-118Beta strandsequence
feature-119Helixsequence
feature-120Helixsequence
feature-121Beta strandsequence
feature-122Beta strandsequence