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RAP80 is a critical gatekeeper in impeding epithelial-mesenchymal transition-induced metastasis and malignant phenotypes of cancer as well as preserving DNA integrity.
Data suggest that RAP80 SIM (show SIM2 ELISA Kits) (SUMO interacting motif) binds SUMO-2 (show SUMO2 ELISA Kits); both specificity and affinity are enhanced through phosphorylation of canonical CK2 (show CSNK2A1 ELISA Kits) (casein kinase 2) site within the SIM (show SIM2 ELISA Kits).
Impaired TIP60 (show KAT5 ELISA Kits)-mediated H4K16 acetylation accounts for the aberrant chromatin accumulation of 53BP1 (show TP53BP1 ELISA Kits) and RAP80 in Fanconi anemia (show PALB2 ELISA Kits) pathway-deficient cells.
TRAIP/RNF206 (show TRAIP ELISA Kits) is required for recruitment of RAP80 to sites of DNA damage.(
A new role of FANCG in Homologous recombination repair of interstrand crosslinks through K63Ub-mediated interaction with the Rap80-BRCA1 complex.
patients with low RAP80 expression received gemcitabine/cisplatin, those with intermediate/high RAP80 expression and low/intermediate BRCA1 expression received docetaxel/cisplatin
Data indicate that a single point deletion (DeltaE81) in RAP80 abrogates multivalent interactions with polyubiquitin (show UBB ELISA Kits).
connect ubiquitin- and SUMO-dependent DSB recognition, revealing that RNF4-synthesized hybrid SUMO-ubiquitin chains are recognized by RAP80 to promote BRCA1 recruitment and DNA repair.
post-translational phosphorylation of RAP80 by the Cdk1 (show CDK1 ELISA Kits)-cyclin B(1) complex is important for RAP80 functional sensitivity to IR and G(2)/M checkpoint control.
Loss of RAP80 abolishes the recruitment of the BRCA1-A complex to DNA lesions in response to DNA damage.
Data indicate that RAP80-deficiency promotes genomic instability and causes an increase in cancer risk consistent with the concept that RAP80 exhibits a tumor suppressor function.
a model in which SUMO and Ub modification is coordinated to recruit Rap80 and BRCA1 to DNA damage sites.
Mechanistically, loss of RAP80 suppresses recruitment of the BRCA1-A complex to DNA damage sites and abrogates the DNA damage repair process at DNA damage sites.
Both ubiquitin-interacting motif 1(UIM1) and UIM2 of RAP80 recognize an Ile 44-centered hydrophobic patch on ubiquitin but neither UIM interacts with the Lys (show LYZ ELISA Kits) 63-linked isopeptide bond. [RAP80]
Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B\; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly Act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1 (By similarity).
ubiquitin interaction motif containing 1
, BRCA1-A complex subunit RAP80-like
, BRCA1-A complex subunit RAP80
, receptor-associated protein 80
, ubiquitin interaction motif-containing protein 1
, receptor associated protein 80
, retinoid X receptor-interacting protein 110
, retinoid x receptor interacting protein
, retinoid X receptor interacting protein 110