Anti-NEDD4 antibody

Target data

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed : 19920177, PubMed : 21399620, PubMed : 23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes (By similarity). Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes (PubMed : 21765395). Promotes ubiquitination of RAPGEF2 (PubMed : 11598133). According to PubMed : 18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed : 17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD (By similarity). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (By similarity). Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (PubMed : 20086093). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed : 25631046). Ubiquitinates DAZAP2, leading to its proteasomal degradation (PubMed : 11342538). Ubiquitinates POLR2A (PubMed : 19920177). Functions as a platform to recruit USP13 to form an NEDD4-USP13 deubiquitination complex that plays a critical role in cleaving the 'Lys-48'-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes (PubMed : 32101753).. (Microbial infection) Involved in the ubiquitination of Ebola virus protein VP40 which plays a role in viral budding.