+ |
CyclinA2/CDK2 | up-regulates activity
phosphorylation
|
RBBP8 |
0.548 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263227 |
Ser327 |
ELPTRVSsPVFGATS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
15485915 |
Ser327 site is a Ser-Pro site, a preferred phosphorylation site by cyclin-dependent kinases|Unlike wild-type CtIP, the S327A mutant did not bind to BRCA1 BRCT domains in vitro (Fig. (Fig.1C)1C) and failed to associate with BRCA1 in vivo (Fig. (Fig.1D),1D), suggesting that residue Ser327 of CtIP is critical for the CtIP-BRCA1 interaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATM | down-regulates
phosphorylation
|
RBBP8 |
0.823 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-79872 |
Ser664 |
IDPGADLsQYKMDVT |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
10910365 |
Atm phosphorylates ctip at serine residues 664 and 745 our study suggests another dna damage-response pathway in which the signal is transmitted through phosphorylation of ctip by atm, leading to dissociation of the ctip_ctbp repressor complex from brca1, which in turn, activate transcription of gadd45 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-79876 |
Ser745 |
SCLADSFsQAADEEE |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
10910365 |
Atm phosphorylates ctip at serine residues 664 and 745 our study suggests another dna damage-response pathway in which the signal is transmitted through phosphorylation of ctip by atm, leading to dissociation of the ctip_ctbp repressor complex from brca1, which in turn, activate transcription of gadd45 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PKM | up-regulates activity
phosphorylation
|
RBBP8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277413 |
Thr126 |
ELMNERNtLQEENKK |
Homo sapiens |
U-87MG Cell |
pmid |
sentence |
30297868 |
Here, we uncover an unexpected mechanism through which pyruvate kinase M2 (PKM2), the highly expressed PK isoform in cancer cells and a master regulator of cancer metabolic reprogramming, integrates with the DDR to directly promote DNA double-strand break (DSB) repair. In response to ionizing radiation and oxidative stress, ATM phosphorylates PKM2 at T328 resulting in its nuclear accumulation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK2 | up-regulates
phosphorylation
|
RBBP8 |
0.603 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183840 |
Thr847 |
FRYIPPNtPENFWEV |
Homo sapiens |
|
pmid |
sentence |
19202191 |
Collectively, these findings thereby provided strong support for ctip thr-847 indeed being a cdk target. it is established that both cdk-dependent and checkpoint-dependent phosphorylations are required for activation of sae2/ctip in vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATR | up-regulates
phosphorylation
|
RBBP8 |
0.6 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200245 |
Thr859 |
WEVGFPStQTCMERG |
Homo sapiens |
|
pmid |
sentence |
23273981 |
Characterization of this site using phospho-specific antibodies and mutational analysis reveals that it is phosphorylated by atr and is required for binding of ctip to chromatin and subsequent processive resection. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAN2 | up-regulates activity
deubiquitination
|
RBBP8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273509 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
33097710 |
Here, we identify that USP52 directly interacts with and deubiquitinates CtIP, thereby promoting DNA end resection and HR. Mechanistically, USP52 removes the ubiquitination of CtIP to facilitate the phosphorylation and activation of CtIP at Thr-847. In addition, USP52 is phosphorylated by ATM at Ser-1003 after DNA damage, which enhances the catalytic activity of USP52. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP8 | down-regulates
binding
|
SPEN |
0.522 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-141616 |
|
|
Homo sapiens |
|
pmid |
sentence |
16287852 |
We identify the ctip and ctbp corepressors as novel components of the human rbp-jk/sharp-corepressor complex and show that ctip binds directly to the sharp repression domain. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BRCA1 | up-regulates
ubiquitination
|
RBBP8 |
0.836 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-147711 |
|
|
Homo sapiens |
|
pmid |
sentence |
16818604 |
In conclusion, our data show that ctip is a physiological substrate of the brca1 e3 ligase. Brca1 recruits ctip through its c-terminal brct domains and promotes ctip ubiquitination through its n-terminal ring domain. The ubiquitinated ctip is not targeted for degradation. Instead, ubiquitinated ctip binds to chromatin following dna damage and is likely to be involved in dna damage checkpoint control. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP8 | up-regulates quantity by expression
transcriptional regulation
|
ATM |
0.823 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198473 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
pmid |
sentence |
22832221 |
Brca1/e2f1/ctipbinding to atm promoter activates atm transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP8 | up-regulates activity
relocalization
|
BRCC ubiquitin ligase complex |
0.593 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263202 |
|
|
|
|
pmid |
sentence |
24832651 |
DNA damage activates ATM and CHK2 kinases, which mediate phosphorylation of CtIP and BRCA1. Phosphorylated CtIP associates with BRCA1 and with the MRN complex leading to the recruitment of the BRCC complex at the site of DNA damage where HR is initiated. |
|
Publications: |
1 |
+ |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
RBBP8 |
0.285 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272412 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27561354 |
Here, we identify the Cullin3 E3 ligase substrate adaptor Kelch-like protein 15 (KLHL15) as a new interaction partner of CtIP and show that KLHL15 promotes CtIP protein turnover via the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP8 | form complex
binding
|
BRCA1-C complex |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263220 |
|
|
|
|
pmid |
sentence |
25400280 |
The BRCA1–C complex consisting of BRCA1, Mre11:Rad50:Nbs1 (collectively known as the MRN complex) and CtIP plays a role in DSB end resection, a process that also involves EXO1 and DNA2|The interaction between BRCA1 and CtIP within this complex is mediated by CDK‐dependent phosphorylation of CtIP‐S327 |
|
Publications: |
1 |
+ |
KLHL15 | down-regulates quantity by destabilization
binding
|
RBBP8 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272410 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27561354 |
Here, we identify the Cullin3 E3 ligase substrate adaptor Kelch-like protein 15 (KLHL15) as a new interaction partner of CtIP and show that KLHL15 promotes CtIP protein turnover via the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP8 | up-regulates activity
relocalization
|
BRCA1 |
0.836 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263203 |
|
|
|
|
pmid |
sentence |
24832651 |
DNA damage activates ATM and CHK2 kinases, which mediate phosphorylation of CtIP and BRCA1. Phosphorylated CtIP associates with BRCA1 and with the MRN complex leading to the recruitment of the BRCC complex at the site of DNA damage where HR is initiated. |
|
Publications: |
1 |