RNF138

The protein encoded by this gene contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]

Ring Finger Protein 138

E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination (PubMed:26502055, PubMed:26502057).
Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination (PubMed:26502055, PubMed:26502057).
Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination (PubMed:26502055).
According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP (PubMed:26502057).
Together with NLK, involved in the ubiquitination and degradation of TCF/LEF (PubMed:16714285).
Also exhibits auto-ubiquitination activity in combination with UBE2K (PubMed:16714285).
May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway (PubMed:16714285).

Biological Process DNA double-strand break processing involved in repair via single-strand annealingManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process protein ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process Wnt signaling pathwayIEA:UniProtKB-KW

Chromosome
Recruited at DNA damage sites (PubMed:26502055).
Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers (PubMed:26502055, PubMed:26502057).

Auto-ubiquitinated.