Mouse Anti-RNF168 Recombinant Antibody (3E1) (CBMAB-R2960-CN)

Ring Finger Protein 168

This gene encodes an E3 ubiquitin ligase protein that 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. The protein is involved in DNA double-strand break (DSB) repair. Mutations in this gene result in Riddle syndrome. [provided by RefSeq, Sep 2011]

Ring Finger Protein 168; Ring Finger Protein 168, E3 Ubiquitin Protein Ligase; RING-Type E3 Ubiquitin Transferase RNF168; RING Finger Protein 168; HRNF168; E3 Ubiquitin-Protein Ligase RNF168; EC 2.3.2.27; EC 6.3.2;

E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively).

Biological Process cellular response to DNA damage stimulusManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process chromatin organizationIEA:UniProtKB-KW
Biological Process double-strand break repairManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H2A K63-linked ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H2A monoubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H2A-K13 ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H2A-K15 ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process interstrand cross-link repairManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process isotype switchingISS:UniProtKB
Biological Process negative regulation of transcription elongation from RNA polymerase II promoterManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of DNA repairManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein K63-linked ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process response to ionizing radiationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB

Nucleus
Localizes to double-strand breaks (DSBs) sites of DNA damage.

Riddle syndrome (RIDL):
An autosomal recessive disorder characterized by increased radiosensitivity, immunodeficiency, mild motor control and learning difficulties, facial dysmorphism, and short stature.

Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs).
Ubiquitinated.