Relation Results

Summary

Name RBBP8
Full Name DNA endonuclease RBBP8
Synonyms CtBP-interacting protein, CtIP, Retinoblastoma-binding protein 8, RBBP-8, Retinoblastoma-interacting protein and myosin-like, RIM, Sporulation in the absence of SPO11 protein 2 homolog, SAE2 | CTIP
Primary ID Q99708
Links - -
Type protein
Relations 15
Function Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through t ...
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Type: Score: Layout: SPV 
0.5640.8290.20.6160.6140.4770.2820.8290.8420.8420.6070.20.5390.2CyclinA2/CDK2RBBP8ATMPKMCDK2ATRKLHL15Cullin 3-RBX1-Skp1BRCA1BRCC ubiquitin ligase complexBRCA1-C complexSPENPAN2

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ up-regulates activity img/direct-activation.png phosphorylation RBBP8 0.564
Identifier Residue Sequence Organism Cell Line
SIGNOR-263227 Ser327 ELPTRVSsPVFGATS Homo sapiens HeLa Cell
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation RBBP8 0.829
Identifier Residue Sequence Organism Cell Line
SIGNOR-79872 Ser664 IDPGADLsQYKMDVT Homo sapiens Breast Cancer Cell
pmid sentence
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
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
+ up-regulates activity img/direct-activation.png phosphorylation RBBP8 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277413 Thr126 ELMNERNtLQEENKK Homo sapiens U-87MG Cell
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation RBBP8 0.616
Identifier Residue Sequence Organism Cell Line
SIGNOR-183840 Thr847 FRYIPPNtPENFWEV Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation RBBP8 0.614
Identifier Residue Sequence Organism Cell Line
SIGNOR-200245 Thr859 WEVGFPStQTCMERG Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png binding RBBP8 0.477
Identifier Residue Sequence Organism Cell Line
SIGNOR-272410 Homo sapiens U2-OS Cell
pmid sentence
 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
+ down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination RBBP8 0.282
Identifier Residue Sequence Organism Cell Line
SIGNOR-272412 Homo sapiens U2-OS Cell
pmid sentence
 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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation ATM 0.829
Identifier Residue Sequence Organism Cell Line
SIGNOR-198473 Homo sapiens Prostate Gland Cancer Cell
pmid sentence
Brca1/e2f1/ctipbinding to atm promoter activates atm transcription.
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png relocalization BRCA1 0.842
Identifier Residue Sequence Organism Cell Line
SIGNOR-263203
pmid sentence
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
+ up-regulates img/direct-activation.png ubiquitination RBBP8 0.842
Identifier Residue Sequence Organism Cell Line
SIGNOR-147711 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png relocalization BRCC ubiquitin ligase complex 0.607
Identifier Residue Sequence Organism Cell Line
SIGNOR-263202
pmid sentence
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
+ form complex img/form-complex.png binding BRCA1-C complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263220
pmid sentence
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
+ down-regulates img/direct_inhibition.png binding SPEN 0.539
Identifier Residue Sequence Organism Cell Line
SIGNOR-141616 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png deubiquitination RBBP8 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273509 Homo sapiens HEK-293 Cell
pmid sentence
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
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