WWP1

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. This gene encodes a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. The encoded protein belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Alternative splicing of this gene generates at least 6 transcript variants; however, the full length nature of these transcripts has not been defined. [provided by RefSeq]

WW domain containing E3 ubiquitin protein ligase 1

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.

Biological Process central nervous system development Source:UniProtKB1 Publication
Biological Process ion transmembrane transport Source:Reactome
Biological Process negative regulation of DNA-templated transcription Source:UniProtKB
Biological Process proteasome-mediated ubiquitin-dependent protein catabolic process Source:GO_Central1 Publication
Biological Process protein polyubiquitination Source:GO_Central1 Publication
Biological Process protein ubiquitination Source:GO_Central1 Publication
Biological Process signal transduction Source:UniProtKB1 Publication
Biological Process viral entry into host cell Source:UniProtKB1 Publication

Cytoplasm
Cell membrane
Nucleus

Auto-ubiquitinated and ubiquitinated by RNF11.