| + |
ATM | up-regulates 
phosphorylation
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73366 |
Ser264 |
EQQLFYIsQPGSSVV |
Homo sapiens |
|
| pmid |
sentence |
| 10608806 |
In this report, we showed that atm phosphorylates a p95 peptide (ser-343) and a mre11 peptide (ser-264) in vitro, suggesting that atm may regulate the function of p95?Mre11? Rad50 repair complex in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265896 |
Ser558 |
AEQMANDsDDSISAA |
in vitro |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265894 |
Ser561 |
MANDSDDsISAATNK |
in vitro |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265893 |
Ser688 |
SKGVDFEsSEDDDDD |
in vitro |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265895 |
Ser689 |
KGVDFESsEDDDDDP |
in vitro |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PLK1 | down-regulates activity 
phosphorylation
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265943 |
Ser649 |
EVIEVDEsDVEEDIF |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 28512243 |
Plk1 phosphorylates Mre11 at S649.Mre11 phosphorylation at S649/S688 inhibits its binding to dsDNA and antagonizes the ATM signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KB1 | down-regulates quantity by destabilization
phosphorylation
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265944 |
Thr597 |
SQRGRADtGLETSTR |
in vitro |
|
| pmid |
sentence |
| 28967905 |
MRE11 is highly unstable in PTEN-deficient cells but stability can be significantly restored by inhibiting mTORC1 or p70S6 kinase (p70S6K), downstream kinases whose activities are stimulated by AKT, or by mutating a residue in MRE11 that we show is phosphorylated by p70S6K in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBQLN4 | up-regulates activity
binding
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265077 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 30612738 |
These data suggest that MRE11 is one of probably many UBQLN4 interaction partners. >Particularly HRR is dependent on ATM activity (Dietlein et al., 2014). Here, we showed that UBQLN4 is an ATM substrate and that DSB sealing is markedly impaired in UBQLN4-depleted cells. HRR depends on a 5′-3′ DSB end resection, which is initiated by the MRE11 nuclease |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD50 | up-regulates
binding
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17713585 |
To organize the mrn complex, the mre11 exonuclease directly binds nbs1, dna, and rad50. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
MRE11 | up-regulates activity
binding
|
PIH1D1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WDCP | up-regulates activity
binding
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273733 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30297404 |
PLK1 Phosphorylates MMAP to Promote Its Interaction with KIF2A and MRE11. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MRE11 | up-regulates
binding
|
ATM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175006 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21763684 |
One of the earliest events is recruitment and activation of the atm at the damaged dna sites through the mre11rad50nbs1 (mrn) sensor complex. the mre11/rad50/nbs1 (mrn) complex maintains genomic stability by bridging dna ends and initiating dna damage signaling through activation of the atm kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181628 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18854157 |
One of the earliest events is recruitment and activation of the atm at the damaged dna sites through the mre11rad50nbs1 (mrn) sensor complex. the mre11/rad50/nbs1 (mrn) complex maintains genomic stability by bridging dna ends and initiating dna damage signaling through activation of the atm kinase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
MRE11 | form complex 
binding
|
MRE11/RAD50/NBS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251504 |
|
|
|
|
| pmid |
sentence |
| 17713585 |
The mre11_rad50_nbs1 (mrn) complex is among the earliest respondents to dna double-strand breaks (dsbs). To organize the mrn complex, the mre11 exonuclease directly binds nbs1, dna, and rad50. |
|
| Publications: |
1 |
| Pathways: | DNA repair in cancer |
| + |
PARP1 | up-regulates activity
relocalization
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19629035 |
PARP1 collaborates with Mre11 to promote replication fork restart after release from replication blocks, most likely by recruiting Mre11 to the replication fork to promote resection of DNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPA2 | up-regulates
binding
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186648 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19586055 |
The response to replication stress requires the recruitment of rpa and the mre11-rad50-nbs1 (mrn) complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MRE11 | up-regulates
binding
|
NBN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157475 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17713585 |
The mre11_rad50_nbs1 (mrn) complex is among the earliest respondents to dna double-strand breaks (dsbs). To organize the mrn complex, the mre11 exonuclease directly binds nbs1, dna, and rad50. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MRE11
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- 