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Literature summary for 2.3.2.27 extracted from

  • Baranes-Bachar, K.; Levy-Barda, A.; Oehler, J.; Reid, D.A.; Soria-Bretones, I.; Voss, T.C.; Chung, D.; Park, Y.; Liu, C.; Yoon, J.B.; Li, W.; Dellaire, G.; Misteli, T.; Huertas, P.; Rothenberg, E.; Ramadan, K.; Ziv, Y.; Shiloh, Y.
    The ubiquitin E3/E4 ligase UBE4A adjusts protein ubiquitylation and accumulation at sites of DNA damage, facilitating double-strand break repair (2018), Mol. Cell, 69, 866-878.e7 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q14139 isoform Ube4A
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Synonyms

Synonyms Comment Organism
Ube4A
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function Ube4A is required for complete assembly of specific DNA damage repair factors at double-strand break sites and proper internal organization of double-strand break-associated protein foci. UBE4A's recruitment to sites of DNA damage is dependent on primary E3 ligases in the DNA damage repair and promotes enhancement and sustainment of K48- and K63-linked ubiquitin chains at these sites. This step is required for timely recruitment of the RAP80 and BRCA1 proteins and proper organization of RAP80- and BRCA1-associated protein complexes at double-strand break sites. The pathway is required for optimal end-resection at double-strand breaks, and its abrogation leads to up-regulation of the highly mutagenic alternative end-joining repair at the expense of error-free homologous recombination repair Homo sapiens