P32829 · MRE11_YEAST
- ProteinDouble-strand break repair protein MRE11
- GeneMRE11
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids692 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Core 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:14522986, PubMed:22002605, PubMed:22705791, PubMed:23080121, PubMed:7625279, PubMed:9651580).
The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:22002605, PubMed:22705791, PubMed:23080121).
The complex 1 mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is 2 required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:22002605, PubMed:23080121).
Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:14522986, PubMed:22002605).
MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:23080121).
It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination (PubMed:22002605).
The MRN complex is also required for the processing of R-loops (PubMed:31537797).
The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:22002605, PubMed:22705791, PubMed:23080121).
The complex 1 mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is 2 required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:22002605, PubMed:23080121).
Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:14522986, PubMed:22002605).
MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:23080121).
It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination (PubMed:22002605).
The MRN complex is also required for the processing of R-loops (PubMed:31537797).
Miscellaneous
Present with 432 molecules/cell in log phase SD medium.
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 18 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 56 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 56 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 125 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 213 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 241 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 243 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDouble-strand break repair protein MRE11
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32829
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to discrete nuclear foci after treatment with genotoxic agents.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 59 | Reduced but not abolished 3'-5' exonuclease activity. | ||||
Sequence: H → S | ||||||
Mutagenesis | 76 | Does not affect ability to mediate DNA repair. | ||||
Sequence: R → K | ||||||
Mutagenesis | 109 | Does not affect ability to mediate DNA repair. | ||||
Sequence: D → G | ||||||
Mutagenesis | 113 | Abolished ability to mediate DNA repair. | ||||
Sequence: N → S | ||||||
Mutagenesis | 239 | Meiotic defects due to inability to DNA double-strand break repair. Decreased interaction with RAD50. | ||||
Sequence: W → R | ||||||
Natural variant | 380 | in strain: SK1 | ||||
Sequence: P → S | ||||||
Natural variant | 659 | in strain: SK1 | ||||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000138680 | 1-692 | Double-strand break repair protein MRE11 | |||
Sequence: MDYPDPDTIRILITTDNHVGYNENDPITGDDSWKTFHEVMMLAKNNNVDMVVQSGDLFHVNKPSKKSLYQVLKTLRLCCMGDKPCELELLSDPSQVFHYDEFTNVNYEDPNFNISIPVFGISGNHDDASGDSLLCPMDILHATGLINHFGKVIESDKIKVVPLLFQKGSTKLALYGLAAVRDERLFRTFKDGGVTFEVPTMREGEWFNLMCVHQNHTGHTNTAFLPEQFLPDFLDMVIWGHEHECIPNLVHNPIKNFDVLQPGSSVATSLCEAEAQPKYVFILDIKYGEAPKMTPIPLETIRTFKMKSISLQDVPHLRPHDKDATSKYLIEQVEEMIRDANEETKQKLADDGEGDMVAELPKPLIRLRVDYSAPSNTQSPIDYQVENPRRFSNRFVGRVANGNNVVQFYKKRSPVTRSKKSGINGTSISDRDVEKLFSESGGELEVQTLVNDLLNKMQLSLLPEVGLNEAVKKFVDKDEKTALKEFISHEISNEVGILSTNEEFLRTDDAEEMKALIKQVKRANSVRPTPPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKPTSKPKRVRTATKKKIPAFSDSTVISDAENELGDNNDAQDDVDIDENDIIMVSTDEEDASYGLLNGRKTKTKTRPAASTKTASRRGKGRASRTPKTDILGSLLAKKRK |
Proteomic databases
PTM databases
Interaction
Subunit
Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single XRS2 (PubMed:23080121, PubMed:35501303, PubMed:9845372).
The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:35501303).
The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:35501303).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32829 | RAD50 P12753 | 21 | EBI-11255, EBI-14700 | |
BINARY | P32829 | SAE2 P46946 | 2 | EBI-11255, EBI-16440 | |
BINARY | P32829 | XRS2 P33301 | 20 | EBI-11255, EBI-20599 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 522-597 | Disordered | ||||
Sequence: RANSVRPTPPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKPTSKPKRVRTATK | ||||||
Compositional bias | 530-585 | Polar residues | ||||
Sequence: PPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKP | ||||||
Region | 610-629 | Disordered | ||||
Sequence: SDAENELGDNNDAQDDVDID | ||||||
Region | 644-692 | Disordered | ||||
Sequence: SYGLLNGRKTKTKTRPAASTKTASRRGKGRASRTPKTDILGSLLAKKRK |
Sequence similarities
Belongs to the MRE11/RAD32 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length692
- Mass (Da)77,650
- Last updated1996-10-01 v2
- ChecksumD58433E32E852B73
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 530-585 | Polar residues | ||||
Sequence: PPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D11463 EMBL· GenBank· DDBJ | BAA02017.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49939 EMBL· GenBank· DDBJ | CAA90195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U60829 EMBL· GenBank· DDBJ | AAB61454.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA10123.1 EMBL· GenBank· DDBJ | Genomic DNA |