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IID00806
 UniprotP49959
ProteinDouble-strand break repair protein MRE11
GeneMRE11
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
708
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-411 Homo dimer :
 Evidence X-RAY 3t1i D Reference
       Region 3t1i D 1-7 disorder
       Region 3t1i D 8-107 order
       Region 3t1i D 108-114 disorder
       Region 3t1i D 115-400 order
       Region 3t1i D 401-411 disorder
 Evidence X-RAY 3t1i C Reference
       Region 3t1i C 1-7 disorder
       Region 3t1i C 8-98 order
       Region 3t1i C 99-114 disorder
       Region 3t1i C 115-400 order
       Region 3t1i C 401-411 disorder
 Evidence X-RAY 3t1i B Reference
       Region 3t1i B 1-6 disorder
       Region 3t1i B 7-99 order
       Region 3t1i B 100-115 disorder
       Region 3t1i B 116-400 order
       Region 3t1i B 401-411 disorder
 Evidence X-RAY 3t1i A Reference
       Region 3t1i A 1-6 disorder
       Region 3t1i A 7-97 order
       Region 3t1i A 98-115 disorder
       Region 3t1i A 116-400 order
       Region 3t1i A 401-411 disorder
Seq 538-563 Hetero dimer : IID00036Complex
 Evidence X-RAY 8k00 B Reference
       Region 8k00 B 538-563 order
SeqProS predicted 538-563 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00036Complex
       Region 8k00 B 538-563 order
Seqphosphorylation
    641-641 Phosphoserine
    275-275 Phosphoserine
    2-2 Phosphoserine
    649-649 Phosphoserine
    619-619 Phosphoserine
    678-678 Phosphoserine
    689-689 Phosphoserine
    688-688 Phosphoserine
    701-701 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
 
Prediction
NeProc
Disorder 1-7,404-423,518-708
Order 8-403,424-517
ProS 412-419,537-544,641-645,683-687,694-698
AlphaFold
Disorder 1-7,402-428,430-430,439-445,490-492,530-708
Order 8-401,429-429,431-438,446-489,493-529
Pfam Hmmer
PF00149 13-249 2.3e-23
PF04152 250-461 1.1e-137
SEG 531-542 ,569-595 ,641-655 ,667-681 ,685-695
Function
Function in SwissProt
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547, PubMed:29670289). The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11 (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547, PubMed:29670289). RAD50 may be required to bind DNA ends and hold them in close proximity (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547, PubMed:29670289). This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547, PubMed:29670289, PubMed:30612738). The complex may also be required for DNA damage signaling via activation of the ATM kinase (PubMed:15064416). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888).
Biological Process
See also
Diagram with PDB data
H2AX/MDC1Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX