+ |
ATM | up-regulates
phosphorylation
|
NBN |
0.852 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78025 |
Ser278 |
VDTGITNsQTLIPDC |
Homo sapiens |
|
pmid |
sentence |
10839544 |
We have identified two residues of nbs1, ser 278 and ser 343 that are phosphorylated in vitro by atm and whose modification in vivo is essential for the cellular response to dna damage. This response includes s-phase checkpoint activation, formation of the nbs1/mrel1/rad50 nuclear foci and rescue of hypersensitivity to ionizing radiation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-73432 |
Ser343 |
TTPGPSLsQGVSVDE |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77149 |
Ser343 |
TTPGPSLsQGVSVDE |
Homo sapiens |
|
pmid |
sentence |
10802669 |
We show that atm physically interacts with and phosphorylates nibrin on serine 343 both in vivo and in vitro. Phosphorylation of this site appears to be functionally important because mutated nibrin (s343a) does not completely complement radiosensitivity in nbs cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78030 |
Ser397 |
EQKFRMLsQDAPTVK |
Homo sapiens |
|
pmid |
sentence |
10839545 |
We have identified two residues of nbs1, ser 278 and ser 343 that are phosphorylated in vitro by atm and whose modification in vivo is essential for the cellular response to dna damage. This response includes s-phase checkpoint activation, formation of the nbs1/mrel1/rad50 nuclear foci and rescue of hypersensitivity to ionizing radiation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78034 |
Ser615 |
VPESSKIsQENEIGK |
Homo sapiens |
|
pmid |
sentence |
10839545 |
In vivo, nbs was phosphorylated on many serine residues, of which s343, s397 and s615 were phosphorylated by atm in vitro. Reconstituting nbs cells with a mutant form of nbs that cannot be phosphorylated at selected, atm-dependent serine residues led to a specific reduction in clonogenic survival after gamma-radiation. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
ATR | up-regulates
phosphorylation
|
NBN |
0.777 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155214 |
Ser343 |
TTPGPSLsQGVSVDE |
Homo sapiens |
|
pmid |
sentence |
17526493 |
We demonstrate that mrn and atr/atr-interacting protein (trip) interact with each other, and the forkhead-associated/breast cancer c-terminal domains (fha/brct) of nbs1 play a significant role in mediating this interaction. Mutations in the fha/brct domains do not prevent atr activation but specifically impair atr-mediated nbs1 phosphorylation at ser-343, which results in a defect in the s-phase checkpoint. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NBN | form complex
binding
|
MRE11/RAD50/NBS1 |
0.911 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251505 |
|
|
|
|
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 |
+ |
NBN | up-regulates
binding
|
ATM |
0.852 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134508 |
|
|
Homo sapiens |
|
pmid |
sentence |
15758953 |
Nbs1 can also immobilize atm at the site of the dsb via direct binding of atm to a c-terminal atm interaction motif on nbs1 . the mre11/rad50/nbs1 (mrn) complex maintains genomic stability by bridging dna ends and initiating dna damage signaling through activation of the atm |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-181631 |
|
|
Homo sapiens |
|
pmid |
sentence |
18854157 |
Nbs1 can also immobilize atm at the site of the dsb via direct binding of atm to a c-terminal atm interaction motif on nbs1 . the mre11/rad50/nbs1 (mrn) complex maintains genomic stability by bridging dna ends and initiating dna damage signaling through activation of the atm |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TCOF1 | up-regulates activity
relocalization
|
NBN |
0.324 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265085 |
|
|
Homo sapiens |
|
pmid |
sentence |
25064736 |
We further identify TCOF1 (also known as Treacle), a nucleolar factor implicated in ribosome biogenesis and mutated in Treacher Collins syndrome, as an interaction partner of NBS1, and demonstrate that NBS1 translocation and accumulation in the nucleoli is Treacle dependent. |
|
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 |
+ |
H2AX | up-regulates
binding
|
NBN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133020 |
|
|
Homo sapiens |
|
pmid |
sentence |
15635255 |
Nbs1 physically interacts with ?-H2ax to form nuclear foci at dna damage sites. The inhibition of this interaction by introduction of anti-?-H2ax antibody into cells abolishes nbs1 foci formation in response to dna damage. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MDC1 | up-regulates
binding
|
NBN |
0.829 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184141 |
|
|
Homo sapiens |
|
pmid |
sentence |
19230643 |
Mdc1 also undergoes phosphorylation by ck2 after dna damage to generate a phospho-motif on mdc1, which binds directly to nbs1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPA2 | up-regulates
binding
|
NBN |
0.53 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-186651 |
|
|
Homo sapiens |
|
pmid |
sentence |
19586055 |
The response to replication stress requires the recruitment of rpa and the mre11-rad50-nbs1 (mrn) complex. We observe a direct interaction between rpa with both nbs1 and mre11. By utilizing rpa bound to ssdna, we demonstrate that substituting rpa with phosphorylated rpa or a phosphomimetic weakens the interaction with the mrn complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |