Description
Product Characteristics:
WWP1 is an E3 ubiquitin ligase and belongs to a family of NEDD4-like proteins. WWP1 contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. The HECT domain of WWP1 has been implicated in regulating the localization and stability of p53 inhibition of WWP1 results in a decrease in p53 expression, whilst WWP1 mediated stabilization of p53 appears to be associated with an accumulation of cytoplasmic p53. WWP1 also negatively regulates the TGF beta tumor suppressor pathway by inactivating its molecular components (SMAD2, SMAD4 and TGFbetaR1). WWP1 has been implicated in both breast and prostate cancers.
Subcellular location: Cytoplasm, Nucleus, Cell membrane
Synonyms: AIP 5, AIP5, Atropin-1-interacting protein 5, hSDRP1, nedd4 like, NEDD4-like E3 ubiquitin-protein ligase WWP1, Tiul1, WW domain containing E3 ubiquitin protein ligase 1, WW domain-containing protein 1, WWP 1, WWP1_HUMAN.
Target Information: 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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1\, the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF