UniProt Summary: Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin- protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833}.
Pfam DomainsGO Terms
Pfam Domains
zf-C3HC4
GO Terms
K63-linked polyubiquitin modification-dependent protein binding
nucleosome binding
negative regulation of double-strand break repair
negative regulation of DNA repair
site of double-strand break
transferase activity
regulation of double-strand break repair
negative regulation of response to DNA damage stimulus
negative regulation of DNA metabolic process
regulation of DNA repair
regulation of response to DNA damage stimulus
regulation of DNA metabolic process
nuclear speck
protein ubiquitination
regulation of cellular response to stress
protein modification by small protein conjugation
cellular response to DNA damage stimulus
protein modification by small protein conjugation or removal
negative regulation of nucleobase-containing compound metabolic process
regulation of response to stress
negative regulation of response to stimulus
cellular response to stress
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)