CDD Conserved Protein Domain Family: mRING-HC-C3HC3D_TRAF7 TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF
Role of RING‐Type E3 Ubiquitin Ligases in . . . - Wiley Online Library RING-type E3 ligases catalyse monoubiquitination or multiple monoubiquitination by transferring a single ubiquitin to one or several residues of the substrate For polyubiquitination, ubiquitins form eight different linkage types including Met1, Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63
The RING finger protein family in health and disease The RING (really interesting new gene) finger (RNF) protein, containing the RING domain, exerts E3 ubiquitin ligase that mediates the covalent attachment of ubiquitin (Ub) to target proteins
TRAF7 protein expression summary - The Human Protein Atlas E3 ubiquitin and SUMO-protein ligase that plays a role in different biological processes such as innate immunity, inflam mation or apoptosis 1, 2 Potentiates MAP3K3-mediated activation of JUN AP1 and DDIT3 transcriptional regulators 3
E3 ubiquitin ligases: styles, structures and functions - PMC E3 ligases FBXO38, KLHL22, TRIM25, RNF2 regulate cancer cell immune response through promoting ubiquitination of specific substrates And E3 ligases PPARγ, SKP2, CHIP, VHL, TRAF6, HUEW1,MuRF1 are capable of mediating cancer cell metabolism by targeting related substrates for ubiquitination
Multifaceted Roles of the E3 Ubiquitin Ligase RING Finger . . . - PubMed Ubiquitination is a post-translational modification that plays essential roles in various physiological and pathological processes Protein ubiquitination depends on E3 ubiquitin ligases that catalyze the conjugation of ubiquitin molecules on lysine residues of targeted substrates
What Is Ubiquitin Tagging and How Does It Work? The final step is ligation, carried out by a ubiquitin ligase (E3) The E3 ligase recognizes both the E2-ubiquitin complex and the specific protein substrate With hundreds of E3 ligases, this family provides immense specificity, facilitating the transfer of ubiquitin from the E2 to the target protein Diverse Cellular Fates Dictated by
The E3 ubiquitin ligase RNF115 regulates phagosome maturation and host . . . Here, a phagosome‐localised E3 ubiquitin ligase, RNF115, is shown to control phagosomal maturation and cytokine responses to bacterial infection in vitro and in vivo Quantitative proteomics reveal high levels of typical and atypical ubiquitin chain types on phagosomal proteins
The E3 ubiquitin ligase RNF114 and TAB1 degradation are required for . . . Here we show that the E3 ubiquitin ligase, Rnf114, is highly expressed in mouse oocytes and that knockdown of Rnf114 inhibits development beyond the two‐cell stage To study the underlying mechanism, we identify its candidate substrates using a 9,000‐protein microarray and validate them using an in vitro ubiquitination system