MCM4DNA replication licensing factor MCM4
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.
UniProt locations Nucleus · Chromosome
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]
Evidence & references
- ECO:0000269 PubMed:16899510 ↗
- ECO:0000269 PubMed:25661590 ↗
- ECO:0000269 PubMed:32453425 ↗
- ECO:0000269 PubMed:34694004 ↗
- ECO:0000269 PubMed:34700328 ↗
- ECO:0000269 PubMed:35585232 ↗
- ECO:0000269 PubMed:9305914 ↗
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
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
- ECO:0000269 PubMed:25661590 ↗
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
GO:0003678 · evidence & context
- ECO:0000314 PMID:25661590 ↗ IDA · UniProt · 20220204qualifier: contributes_to
- ECO:0000314 PMID:9305914 ↗ IDA · UniProt · 20110207qualifier: contributes_to
GO:0003697 · evidence & context
- ECO:0000250 GO_REF:0000024 ISS · UniProt · 20220203qualifier: contributes_towithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49717"}]}]
- ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724qualifier: contributes_towithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49717"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000023353"}]}]
- ECO:0000314 PMID:25661590 ↗ IDA · UniProt · 20220204qualifier: contributes_to
GO:0017116 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210414qualifier: contributes_towithFrom: [{"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"}]}]
GO:0003677 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001208"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
GO:0003678 · evidence & context
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727qualifier: enableswithFrom: [{"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)
GO:0005515 · evidence & context
- ECO:0000353 PMID:12364596 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:15232106 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:23764002 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:33654309 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P33993"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:16902406 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
- ECO:0000353 PMID:16902406 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y5B9"}]}]
- ECO:0000353 PMID:17296731 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
- ECO:0000353 PMID:22190034 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Q2G4"}]}]
- ECO:0000353 PMID:22540012 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
- ECO:0000353 PMID:24299456 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
- ECO:0000353 PMID:24407287 ↗ IPI · AgBase · 20150317qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9ULZ3"}]}]
- ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BTE3"}]}]
- ECO:0000353 PMID:28514442 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
- ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
- ECO:0000353 PMID:35271311 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08945"}]}]
GO:0005524 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001208"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR031327"}]}]
GO:0016887 · evidence & context
- ECO:0007322 GO_REF:0000116 IEA · RHEA · 20260727qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "RHEA", "id": "13065"}]}]
- ECO:0000269 PMID:25661590 ↗ EXP · UniProt · 20251027qualifier: enables
GO:0000727 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190209qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
GO:0006259 · evidence & context
- ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00028839"}]}]
GO:0006260 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR018525"}]}]
- ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015qualifier: involved_in
- ECO:0000303 PMID:9465298 ↗ NAS · UniProt · 20021218qualifier: involved_in
GO:0006270 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR008047"}]}]
GO:0006271 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "SGD", "id": "S000006223"}]}]
GO:0030174 · evidence & context
- ECO:0005547 PMID:30069701 ↗ NAS · ComplexPortal · 20251229qualifier: involved_in
GO:1902975 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190210qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000179968"}]}, {"connectedXrefs": [{"db": "PomBase", "id": "SPCC16A11.17"}]}]
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"
}
]
}
]
}Subcellular Location
UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.
Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses
Evidence & references
- ECO:0000305 PubMed:35585232 ↗
Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses
Evidence & references
- ECO:0000305 PubMed:35585232 ↗
Evidence & references
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260528qualifier: is_active_inwithFrom: [{"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"}]}]
Evidence & references
- ECO:0007005 PMID:19135898 ↗ HDA · BHF-UCL · 20150720qualifier: located_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
- ECO:0000314 PMID:22474384 ↗ IDA · ComplexPortal · 20251015qualifier: located_in
- ECO:0000303 PMID:8265339 ↗ NAS · UniProt · 20021218qualifier: located_in
Evidence & references
- ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115qualifier: located_in
- ECO:0000304 Reactome:R-HSA-176298 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-176318 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68916 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68917 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68918 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68919 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68940 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68944 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-68954 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-69019 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9749253 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9757257 TAS · Reactome · 20130731qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9757258 TAS · Reactome · 20130731qualifier: located_in
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00026361"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0468"}]}]
Evidence & references
- ECO:0007005 PMID:19946888 ↗ HDA · UniProt · 20140627qualifier: located_in
All recorded location assertions (10)
Evidence & references
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250902qualifier: part_ofwithFrom: [{"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 · 20260727qualifier: part_ofwithFrom: [{"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 · 20110124qualifier: part_of
- ECO:0000353 PMID:22540012 ↗ IPI · ComplexPortal · 20251229qualifier: part_of
- ECO:0000314 PMID:25661590 ↗ IDA · UniProt · 20220204qualifier: part_of
Evidence & references
- ECO:0000250 GO_REF:0000024 ISS · UniProt · 20200807qualifier: part_ofwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q5XK83"}]}]
- ECO:0000353 PMID:22474384 ↗ IPI · ComplexPortal · 20251015qualifier: part_of
Membrane topology 0
No annotation is recorded in this UniProt entry.
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.
Evidence & references
- ECO:0000269 PubMed:22354167 ↗
- ECO:0000269 PubMed:22354170 ↗
- ECO:0000269 PubMed:22499342 ↗
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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| E460GVAR_020500 | 460 | in dbSNP:rs17287663 E → G | Experimental evidence Evidence & references
| No verified residues in this structure |
| L650MVAR_020501 | 650 | in 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| G364R | 364 | Reduced 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 |
PTM/Processing
Sumoylated; SUMO2 modified in response to stress caused by inhibition of proteasome activity (in vitro)
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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Initiator methionine | 1 | Removed | 3 publications Evidence & references
| No verified residues in this structure |
| ChainPRO_0000194101 | 2–863 | DNA replication licensing factor MCM4 | Evidence & referencesNo 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Modified residue | 2 | N-acetylserine | 3 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 6 | Phosphoserine; by CDC7 | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 7 | Phosphothreonine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 19 | Phosphothreonine | By similarity Evidence & references
| No verified residues in this structure |
| Modified residue | 26 | Phosphoserine | 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 31 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 32 | Phosphoserine | 3 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 34 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 102 | Phosphothreonine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 105 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 110 | Phosphothreonine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 120 | Phosphoserine | 5 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 131 | Phosphoserine | 4 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 142 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 145 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 220 | N6-acetyllysine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 450 | N6-acetyllysine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 858 | N6-acetyllysine | By similarity Evidence & references
| No verified residues in this structure |
| Cross-link | 439 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | 1 publication Evidence & references
| No verified residues in this structure |
| Cross-link | 798 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | 1 publication Evidence & references
| No verified residues in this structure |
Expression
No annotation is recorded in this UniProt entry.
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.
| Partner / product | Species | Experiments | Evidence & actions |
|---|---|---|---|
| MCM7P33993With P33991 | Homo sapiens | 16 | IntAct evidenceSource product: P33991. Partner: P33993. Reported experiment count: 16. |
| MCMBPQ9BTE3With P33991 | Homo sapiens | 14 | IntAct evidenceSource product: P33991. Partner: Q9BTE3. Reported experiment count: 14. |
| SSRP1Q08945With P33991 | Homo sapiens | 8 | IntAct evidenceSource product: P33991. Partner: Q08945. Reported experiment count: 8. |
| SUPT16HQ9Y5B9With P33991 | Homo sapiens | 3 | IntAct evidenceSource product: P33991. Partner: Q9Y5B9. Reported experiment count: 3. |
| ORFQ9Q2G4With P33991 | Human immunodeficiency virus type 1Cross-species | 3 | IntAct evidenceSource product: P33991. Partner: Q9Q2G4. Reported experiment count: 3. |
No partners match this filter.
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]
Evidence & references
- ECO:0000269 PubMed:16899510 ↗
- ECO:0000269 PubMed:17296731 ↗
- ECO:0000269 PubMed:32453425 ↗
- ECO:0000269 PubMed:34694004 ↗
- ECO:0000269 PubMed:34700328 ↗
- ECO:0000269 PubMed:9305914 ↗
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.
Structure
7W1Y · Human MCM double hexamer bound to natural DNA duplex (polyAT/polyTA)
ELECTRON MICROSCOPY · 2.59 Å
Recorded components
| Component | Species | Chains | Protein identities |
|---|---|---|---|
| DNA replication licensing factor MCM2protein · Entity 1 | Homo sapiens | A, G | P49736 |
| Isoform 2 of DNA replication licensing factor MCM3protein · Entity 2 | Homo sapiens | B, H | P25205 |
| DNA replication licensing factor MCM4protein · Entity 3 | Homo sapiens | C, I | P33991 |
| DNA replication licensing factor MCM5protein · Entity 4 | Homo sapiens | D, J | P33992 |
| DNA replication licensing factor MCM6protein · Entity 5 | Homo sapiens | E, K | Q14566 |
| DNA replication licensing factor MCM7protein · Entity 6 | Homo sapiens | F, L | P33993 |
| DNA (49-MER)dna · Entity 7 | Homo sapiens | M | No verified protein mapping |
| DNA (49-MER)dna · Entity 8 | Homo sapiens | N | No verified protein mapping |
| ZINC IONligand · Entity 9 | CA, FA, KA, NA, O, QA, T, TA, W, Z | No verified protein mapping | |
| MAGNESIUM IONligand · Entity 10 | AA, DA, GA, IA, LA, OA, P, R, RA, U, UA, X | No verified protein mapping | |
| ADENOSINE-5'-TRIPHOSPHATEligand · Entity 11 | EA, HA, JA, MA, Q, S, V, VA | No verified protein mapping | |
| ADENOSINE-5'-DIPHOSPHATEligand · Entity 12 | BA, PA, SA, Y | No 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
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29 recorded rows
| Record | Evidence type | Method | Resolution | Open |
|---|---|---|---|---|
| 7W1Y | experimental | EM | 2.59 A | Open in Atlas ↗ |
| 9E2Z | experimental | EM | 2.60 A | Open in Atlas ↗ |
| 7PLO | experimental | EM | 2.80 A | Open in Atlas ↗ |
| 8W0F | experimental | EM | 2.80 A | Open in Atlas ↗ |
| 8S09 | experimental | EM | 3.10 A | Open in Atlas ↗ |
| 7PFO | experimental | EM | 3.20 A | Open in Atlas ↗ |
| 8S0A | experimental | EM | 3.20 A | Open in Atlas ↗ |
| 9CAQ | experimental | EM | 3.20 A | Open in Atlas ↗ |
| 9LXD | experimental | EM | 3.27 A | Open in Atlas ↗ |
| 6XTX | experimental | EM | 3.29 A | Open in Atlas ↗ |
| 22VT | experimental | EM | 3.30 A | Open in Atlas ↗ |
| 8B9D | experimental | EM | 3.40 A | Open in Atlas ↗ |
| 8W0E | experimental | EM | 3.40 A | Open in Atlas ↗ |
| 9VLN | experimental | EM | 3.42 A | Open in Atlas ↗ |
| 9UQ0 | experimental | EM | 3.47 A | Open in Atlas ↗ |
| 8W0I | experimental | EM | 3.50 A | Open in Atlas ↗ |
| 8S0B | experimental | EM | 3.60 A | Open in Atlas ↗ |
| 8S0D | experimental | EM | 3.60 A | Open in Atlas ↗ |
| 8S0E | experimental | EM | 3.80 A | Open in Atlas ↗ |
| 8W0G | experimental | EM | 3.80 A | Open in Atlas ↗ |
| 9LXF | experimental | EM | 3.86 A | Open in Atlas ↗ |
| 9LXE | experimental | EM | 3.96 A | Open in Atlas ↗ |
| 9VLW | experimental | EM | 4.06 A | Open in Atlas ↗ |
| 8S0F | experimental | EM | 4.10 A | Open in Atlas ↗ |
| 9C6G | experimental | EM | 4.26 A | Open in Atlas ↗ |
| 7W68 | experimental | EM | 4.40 A | Open in Atlas ↗ |
| 8RWV | experimental | EM | 6.68 A | Open in Atlas ↗ |
| 6XTY | experimental | EM | 6.77 A | Open in Atlas ↗ |
| AF-P33991-F1 | predicted | AlphaFold | Not applicable | Open in Atlas ↗ |
Family & Domains
Belongs to the MCM family
Evidence & references
- ECO:0000305
Complete source annotation
{
"texts": [
{
"evidences": [
{
"evidenceCode": "ECO:0000305"
}
],
"value": "Belongs to the MCM family"
}
],
"commentType": "SIMILARITY"
}Domain architecture
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
| Annotation | Position | Source & interpretation | Inspect |
|---|---|---|---|
| MCM, N-terminal domainIPR027925 | 163–264 | INTERPROdomain This entry represents the N-terminal region of MCM proteins. This region is composed of three structural domains. Full source descriptionThis 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. | No verified residues in this structure |
| MCM OB domainIPR033762 | 270–398 | INTERPROdomain 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 domainIPR001208 | 441–775 | INTERPROdomain 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 descriptionProteins 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. | No verified residues in this structure |
| MCM, AAA-lid domainIPR041562 | 686–768 | INTERPROdomain 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 descriptionThis 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. | No verified residues in this structure |
| MCM4, winged helix domainPF21128 | 793–861 | PFAMdomain 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 descriptionDNA 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. | No verified residues in this structure |
UniProt domains, repeats & motifs 3
Scroll across the table for evidence and actions.
3 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Domain | 441–775 | MCM C-terminal AAA(+) ATPase | Sequence analysis Evidence & references
| No verified residues in this structure |
| Motif | 510–517 | Walker A | Sequence analysis Evidence & references
| No verified residues in this structure |
| Motif | 574–577 | Walker B | Sequence analysis Evidence & references
| No verified residues in this structure |
Functional sites 9
Scroll across the table for evidence and actions.
9 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Binding site | 471 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 497 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 516 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 517 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 618 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 643 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 732 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 735 | Binding site | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Site | 643 | Arginine finger | Sequence analysis Evidence & references
| No verified residues in this structure |
Sequence regions 3
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3 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Region | 1–60 | Disordered | Evidence & references
| No verified residues in this structure |
| Region | 91–126 | Disordered | Evidence & references
| No verified residues in this structure |
| Compositional bias | 1–10 | Low complexity | Evidence & references
| No verified residues in this structure |
Sequence & Isoforms
Sequence & isoforms
UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.
The mass describes this unmodified source sequence, not every mature or modified product.
MSSPASTPSRRGSRRGRATPAQTPRSEDARSSPSQRRRGEDSTSTGELQPMPTSPGVDLQSPAAQDVLFSSPPQMHSSAIPLDFDVSSPLTYGTPSSRVEGTPRSGVRGTPVRQRPDLGSAQKGLQVDLQSDGAAAEDIVASEQSLGQKLVIWGTDVNVAACKENFQRFLQRFIDPLAKEEENVGIDITEPLYMQRLGEINVIGEPFLNVNCEHIKSFDKNLYRQLISYPQEVIPTFDMAVNEIFFDRYPDSILEHQIQVRPFNALKTKNMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFQCQVCAHTTRVEMDRGRIAEPSVCGRCHTTHSMALIHNRSLFSDKQMIKLQESPEDMPAGQTPHTVILFAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVSNVKSVYKTHIDVIHYRKTDAKRLHGLDEEAEQKLFSEKRVELLKELSRKPDIYERLASALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEINILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPIESQWNPKKTTIENIQLPHTLLSRFDLIFLLLDPQDEAYDRRLAHHLVALYYQSEEQAEEELLDMAVLKDYIAYAHSTIMPRLSEEASQALIEAYVDMRKIGSSRGMVSAYPRQLESLIRLAEAHAKVRLSNKVEAIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATSRKRKEELAEALKKLILSKGKTPALKYQQLFEDIRGQSDIAITKDMFEEALRALADDDFLTVTGKTVRLLSource 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Sequence conflict | 62 | in Ref. 1; CAA52801 P → T | Curator inference Evidence & references
| No verified residues in this structure |
| Sequence conflict | 206 | in Ref. 1; CAA52801 P → Q | Curator inference Evidence & references
| No verified residues in this structure |
Recorded secondary structure 81
Scroll across the table for evidence and actions.
81 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Helix | 110–114 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 116–118 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 126–129 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 147–149 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 150–152 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 153–155 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 159–171 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 182–184 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 188–190 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 192–203 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 207–211 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 212–218 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 220–228 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 230–247 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 259–263 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 271–273 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 276–278 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 281–292 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 296–306 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 307–309 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 312–316 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 318–324 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 329–331 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 337–356 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 358–360 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 365–368 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 369–375 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 376–378 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 387–397 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 400–402 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 408–411 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 413–422 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 426–428 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 432–436 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 438–440 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 443–453 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 458–464 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 468–470 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 474–485 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 493–496 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 506–515 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 516–524 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 527–534 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 535–537 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 540–544 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 545–549 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 551–553 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 556–560 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 562–565 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 566–568 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 569–579 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 581–584 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 586–593 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 594–599 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 600–602 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 604–608 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 612–617 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 620–622 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 626–628 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 630–634 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 638–642 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 647–650 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 656–668 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 669–671 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 684–697 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 704–721 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 723–726 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 731–747 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 751–753 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 755–767 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 768–770 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 773–775 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 776–778 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 784–788 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 792–806 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 812–814 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 815–819 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 820–830 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 837–849 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 854–856 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 859–861 | Beta strand | Evidence & references
| No verified residues in this structure |
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.
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
- UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:10.782723+00:00
- InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:10.793165+00:00
- AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:17.838169+00:00
- UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:10.782723+00:00
- InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:10.793165+00:00
- AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:17.838169+00:00
- UniProt overview ↗ · 2026-11-10T20:42:46.255275+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:56.767058+00:00
- omabrowser.org ↗ · 2026-11-10T21:11:56.774611+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:56.782743+00:00
- omabrowser.org ↗ · 2026-11-10T21:11:56.842527+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:56.843917+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:56.858523+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:56.871862+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:56.985815+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:57.103567+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:57.185420+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:57.284924+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:57.387155+00:00
Recorded 2026-11-10. Source dates and identifiers are retained below.
Publications in this UniProt entry
1995 · Eur. J. Biochem.
PubMed 7601140 ↗Scope & authors
NUCLEOTIDE SEQUENCE [MRNA]; VARIANT MET-650
Musahl C., Schulte D., Burkhart R., Knippers R.
APR-2004 ·
Scope & authors
NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT GLY-460
2004 · Genome Res.
PubMed 15489334 ↗Scope & authors
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT MET-650
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)
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.
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.
1997 · J. Biol. Chem.
PubMed 9305914 ↗Scope & authors
IDENTIFICATION IN THE MCM2-7 COMPLEX; FUNCTION
Ishimi Y.
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.
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.
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.
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
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.
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.
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.
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.
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.
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.
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.
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.
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.
2012 · J. Med. Genet.
PubMed 22499342 ↗Scope & authors
INVOLVEMENT IN IMD54
Casey J.P., Nobbs M., McGettigan P., Lynch S., Ennis S.
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.
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.
2015 · J. Biochem.
PubMed 25661590 ↗Scope & authors
FUNCTION; MUTAGENESIS OF GLY-364; CATALYTIC ACTIVITY
Ishimi Y., Irie D.
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.
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.
2022 · Nature
PubMed 35585232 ↗Scope & authors
FUNCTION; SUBCELLULAR LOCATION
Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.
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.
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.
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 record | Type | Section |
|---|---|---|
| FUNCTION:0 | FUNCTION | function |
| CATALYTIC ACTIVITY:0 | CATALYTIC ACTIVITY | function |
| SUBUNIT:0 | SUBUNIT | interactions |
| INTERACTION:0 | INTERACTION | interactions |
| SUBCELLULAR LOCATION:0 | SUBCELLULAR LOCATION | location |
| PTM:0 | PTM | processing |
| DISEASE:0 | DISEASE | disease |
| MISCELLANEOUS:0 | MISCELLANEOUS | function |
| SIMILARITY:0 | SIMILARITY | domains |
| feature-0 | Initiator methionine | processing |
| feature-1 | Chain | processing |
| feature-2 | Domain | domains |
| feature-3 | Region | domains |
| feature-4 | Region | domains |
| feature-5 | Motif | domains |
| feature-6 | Motif | domains |
| feature-7 | Compositional bias | domains |
| feature-8 | Binding site | domains |
| feature-9 | Binding site | domains |
| feature-10 | Binding site | domains |
| feature-11 | Binding site | domains |
| feature-12 | Binding site | domains |
| feature-13 | Binding site | domains |
| feature-14 | Binding site | domains |
| feature-15 | Binding site | domains |
| feature-16 | Site | domains |
| feature-17 | Modified residue | processing |
| feature-18 | Modified residue | processing |
| feature-19 | Modified residue | processing |
| feature-20 | Modified residue | processing |
| feature-21 | Modified residue | processing |
| feature-22 | Modified residue | processing |
| feature-23 | Modified residue | processing |
| feature-24 | Modified residue | processing |
| feature-25 | Modified residue | processing |
| feature-26 | Modified residue | processing |
| feature-27 | Modified residue | processing |
| feature-28 | Modified residue | processing |
| feature-29 | Modified residue | processing |
| feature-30 | Modified residue | processing |
| feature-31 | Modified residue | processing |
| feature-32 | Modified residue | processing |
| feature-33 | Modified residue | processing |
| feature-34 | Modified residue | processing |
| feature-35 | Cross-link | processing |
| feature-36 | Cross-link | processing |
| feature-37 | Natural variant | disease |
| feature-38 | Natural variant | disease |
| feature-39 | Mutagenesis | disease |
| feature-40 | Sequence conflict | sequence |
| feature-41 | Sequence conflict | sequence |
| feature-42 | Helix | sequence |
| feature-43 | Helix | sequence |
| feature-44 | Beta strand | sequence |
| feature-45 | Helix | sequence |
| feature-46 | Beta strand | sequence |
| feature-47 | Turn | sequence |
| feature-48 | Helix | sequence |
| feature-49 | Beta strand | sequence |
| feature-50 | Beta strand | sequence |
| feature-51 | Helix | sequence |
| feature-52 | Beta strand | sequence |
| feature-53 | Helix | sequence |
| feature-54 | Helix | sequence |
| feature-55 | Helix | sequence |
| feature-56 | Beta strand | sequence |
| feature-57 | Helix | sequence |
| feature-58 | Helix | sequence |
| feature-59 | Beta strand | sequence |
| feature-60 | Beta strand | sequence |
| feature-61 | Turn | sequence |
| feature-62 | Beta strand | sequence |
| feature-63 | Beta strand | sequence |
| feature-64 | Turn | sequence |
| feature-65 | Beta strand | sequence |
| feature-66 | Turn | sequence |
| feature-67 | Helix | sequence |
| feature-68 | Beta strand | sequence |
| feature-69 | Helix | sequence |
| feature-70 | Beta strand | sequence |
| feature-71 | Beta strand | sequence |
| feature-72 | Beta strand | sequence |
| feature-73 | Beta strand | sequence |
| feature-74 | Beta strand | sequence |
| feature-75 | Helix | sequence |
| feature-76 | Beta strand | sequence |
| feature-77 | Helix | sequence |
| feature-78 | Helix | sequence |
| feature-79 | Beta strand | sequence |
| feature-80 | Helix | sequence |
| feature-81 | Turn | sequence |
| feature-82 | Beta strand | sequence |
| feature-83 | Helix | sequence |
| feature-84 | Beta strand | sequence |
| feature-85 | Helix | sequence |
| feature-86 | Helix | sequence |
| feature-87 | Beta strand | sequence |
| feature-88 | Turn | sequence |
| feature-89 | Beta strand | sequence |
| feature-90 | Helix | sequence |
| feature-91 | Turn | sequence |
| feature-92 | Beta strand | sequence |
| feature-93 | Helix | sequence |
| feature-94 | Helix | sequence |
| feature-95 | Beta strand | sequence |
| feature-96 | Beta strand | sequence |
| feature-97 | Beta strand | sequence |
| feature-98 | Beta strand | sequence |
| feature-99 | Helix | sequence |
| feature-100 | Beta strand | sequence |
| feature-101 | Helix | sequence |
| feature-102 | Helix | sequence |
| feature-103 | Beta strand | sequence |
| feature-104 | Helix | sequence |
| feature-105 | Turn | sequence |
| feature-106 | Helix | sequence |
| feature-107 | Helix | sequence |
| feature-108 | Beta strand | sequence |
| feature-109 | Helix | sequence |
| feature-110 | Beta strand | sequence |
| feature-111 | Helix | sequence |
| feature-112 | Turn | sequence |
| feature-113 | Beta strand | sequence |
| feature-114 | Beta strand | sequence |
| feature-115 | Helix | sequence |
| feature-116 | Helix | sequence |
| feature-117 | Turn | sequence |
| feature-118 | Beta strand | sequence |
| feature-119 | Helix | sequence |
| feature-120 | Helix | sequence |
| feature-121 | Beta strand | sequence |
| feature-122 | Beta strand | sequence |