Aliases for TRIP12 Gene
External Ids for TRIP12 Gene
Previous GeneCards Identifiers for TRIP12 Gene
The protein encoded by this gene is an E3 ubiquitin-protein ligase involved in the degradation of the p19ARF/ARF isoform of CDKN2A, a tumor suppressor. The encoded protein also plays a role in the DNA damage response by regulating the stability of USP7, which regulates tumor suppressor p53. [provided by RefSeq, Jan 2017]
GeneCards Summary for TRIP12 Gene
TRIP12 (Thyroid Hormone Receptor Interactor 12) is a Protein Coding gene. Diseases associated with TRIP12 include Chronic Inflammation Of Lacrimal Passage and Acute Inflammation Of Lacrimal Passage. Among its related pathways are Innate Immune System and Class I MHC mediated antigen processing and presentation. GO annotations related to this gene include binding and ubiquitin-protein transferase activity. An important paralog of this gene is HECTD1.
UniProtKB/Swiss-Prot for TRIP12 Gene
E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of Lys-63-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.