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IID00715
 UniprotP49736
ProteinDNA replication licensing factor MCM2
GeneMCM2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
904
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 1-160
 Evidence NMR This fragment is mainly disordered in solution (PubMed: 25618846) Reference
       Region 1-160 disorder
Seq 33-47 Hetero tetramer : O00311,Q9UBU7
 Evidence X-RAY 6ya7 C Reference
       Region 6ya7 C 33-37 disorder
       Region 6ya7 C 38-46 order
       Region 6ya7 C 47-47 disorder
Seq 61-130 Hetero dodecamer : IID00058Complex,IID00239Complex,Q8WXX5
 Evidence X-RAY 7ciz K Reference
       Region 7ciz K 61-62 disorder
       Region 7ciz K 63-125 order
       Region 7ciz K 126-130 disorder
 Evidence X-RAY 7ciz G Reference
       Region 7ciz G 61-61 disorder
       Region 7ciz G 62-125 order
       Region 7ciz G 126-130 disorder
 Evidence X-RAY 7ciz C Reference
       Region 7ciz C 61-67 disorder
       Region 7ciz C 68-125 order
       Region 7ciz C 126-130 disorder
Seq 61-130 Hetero tetramer : IID00058Complex,IID00239Complex
 Evidence X-RAY 5bnx C Reference
       Region 5bnx C 61-67 disorder
       Region 5bnx C 68-124 order
       Region 5bnx C 125-130 disorder
Seq 61-130 Hetero tetramer : IID00058Complex,IID00088Complex
 Evidence X-RAY 5bo0 C Reference
       Region 5bo0 C 61-67 disorder
       Region 5bo0 C 68-124 order
       Region 5bo0 C 125-130 disorder
Seq 61-130 Hetero octamer : IID00058Complex,IID00239Complex
 Evidence X-RAY 5ja4 C Reference
       Region 5ja4 C 61-67 disorder
       Region 5ja4 C 68-124 order
       Region 5ja4 C 125-130 disorder
Seq 61-130 Hetero hexamer : IID00058Complex,IID00239Complex
 Evidence X-RAY 5bnv F Reference
       Region 5bnv F 61-67 disorder
       Region 5bnv F 68-125 order
       Region 5bnv F 126-130 disorder
 Evidence X-RAY 5bnv C Reference
       Region 5bnv C 61-67 disorder
       Region 5bnv C 68-124 order
       Region 5bnv C 125-130 disorder
Seq 61-130 Hetero octamer : IID00058Complex,IID00239Complex,Q8WXX5
 Evidence X-RAY 7cj0 H Reference
       Region 7cj0 H 61-66 disorder
       Region 7cj0 H 67-125 order
       Region 7cj0 H 126-130 disorder
 Evidence X-RAY 7cj0 G Reference
       Region 7cj0 G 61-64 disorder
       Region 7cj0 G 65-124 order
       Region 7cj0 G 125-130 disorder
Seq 63-124 Hetero tetramer : IID00058Complex,IID00062Complex,IID00182Complex
 Evidence X-RAY 5c3i D Reference
       Region 5c3i D 63-67 disorder
       Region 5c3i D 68-123 order
       Region 5c3i D 124-124 disorder
Seq 63-124 Hetero tetramer : IID00058Complex,IID00062Complex
 Evidence X-RAY 5c3i L Reference
       Region 5c3i L 63-67 disorder
       Region 5c3i L 68-123 order
       Region 5c3i L 124-124 disorder
 Evidence X-RAY 5c3i H Reference
       Region 5c3i H 63-67 disorder
       Region 5c3i H 68-123 order
       Region 5c3i H 124-124 disorder
 Evidence X-RAY 5c3i P Reference
       Region 5c3i P 63-68 disorder
       Region 5c3i P 69-116 order
       Region 5c3i P 117-124 disorder
 Evidence X-RAY 5c3i T Reference
       Region 5c3i T 63-68 disorder
       Region 5c3i T 69-124 order
 Evidence X-RAY 5c3i X Reference
       Region 5c3i X 63-67 disorder
       Region 5c3i X 68-123 order
       Region 5c3i X 124-124 disorder
Seqdisorder 63-153
 Evidence NMR This region is largely unfolded in solution with a residual helix (107-122) (PubMed: 25618846) Reference
       Region 63-153 disorder
Seq 69-138 Hetero trimer : P02299,P84040
 Evidence X-RAY 4uuz C Reference
       Region 4uuz C 69-121 order
       Region 4uuz C 122-138 disorder
SeqProS verified 38-46 Hetero tetramer : O00311,Q9UBU7
       Region 6ya7 C 38-46 order
       Region 1-160 disorder
SeqProS verified 62-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero octamer : IID00058Complex,IID00239Complex,Q8WXX5
       Region 7cj0 G 65-124 order
       Region 7cj0 H 67-125 order
       Region 1-160 disorder
SeqProS verified 62-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero dodecamer : IID00058Complex,IID00239Complex,Q8WXX5
       Region 7ciz C 68-125 order
       Region 7ciz G 62-125 order
       Region 7ciz K 63-125 order
       Region 1-160 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero tetramer : IID00058Complex,IID00062Complex,IID00182Complex
       Region 5c3i D 68-123 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero trimer : P02299,P84040
       Region 4uuz C 69-121 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero tetramer : IID00058Complex,IID00239Complex
       Region 5bnx C 68-124 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero tetramer : IID00058Complex,IID00062Complex
       Region 5c3i H 68-123 order
       Region 5c3i L 68-123 order
       Region 5c3i P 69-116 order
       Region 5c3i T 69-124 order
       Region 5c3i X 68-123 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero octamer : IID00058Complex,IID00239Complex
       Region 5ja4 C 68-124 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero hexamer : IID00058Complex,IID00239Complex
       Region 5bnv C 68-124 order
       Region 5bnv F 68-125 order
       Region 63-153 disorder
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed: 25618846) Hetero tetramer : IID00058Complex,IID00088Complex
       Region 5bo0 C 68-124 order
       Region 63-153 disorder
Seqphosphorylation
    25-25 Phosphothreonine
    26-26 Phosphoserine
    27-27 Phosphoserine
    32-32 Phosphoserine
    39-39 Phosphothreonine
    40-40 Phosphoserine; by CDC7
    13-13 Phosphoserine
    12-12 Phosphoserine
    41-41 Phosphoserine
    484-484 Phosphoserine
    381-381 Phosphoserine
    139-139 Phosphoserine
    137-137 Phosphotyrosine
    108-108 Phosphoserine; by ATR
    59-59 Phosphothreonine
    53-53 Phosphoserine; by CDC7
Seqacetylation
    2-2 N-acetylalanine
    216-216 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-177,687-711
Order 178-686,712-904
ProS 56-59,70-99,104-138,150-157,174-177
AlphaFold
Disorder 1-73,76-83,85-105,123-172,210-210,343-344,448-455,565-565,690-713,823-831,852-855,872-873,875-875,884-885,904-904
Order 74-75,84-84,106-122,173-209,211-342,345-447,456-564,566-689,714-822,832-851,856-871,874-874,876-883,886-903
Pfam Hmmer
PF00493 460-803 7.4e-218
SEG 52-78 ,107-136 ,155-176
Function
Function in SwissProt
Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677).