ITCH

E3 ubiquitin-protein ligase Itchy homolog ;
Itch ;
Atrophin-1-interacting protein 4 ;
AIP4 ;
NFE2-associated polypeptide 1 ;
NAPP1 ;

function: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. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response.,pathway:Protein modification; protein ubiquitination.,PTM:Phosphorylated on tyrosine residues.,similarity:Contains 1 C2 domain.,similarity:Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.,similarity:Contains 4 WW domains.,subunit:Interacts via its WW domains with DRPLA, NFE2 and CBLC. Interacts with Epstein-Barr virus LMP2A. Interacts with NOTCH1, OCLN, JUN and JUNB. Interacts with NDFIP1 in vitro (By similarity). Interacts with ARHGEF7.,tissue specificity:Widely expressed.,

protein polyubiquitination, regulation of cell growth, regulation of tolerance induction, positive regulation of tolerance induction, regulation of T cell tolerance induction, positive regulation of T cell tolerance induction, regulation of T cell anergy, positive regulation of T cell anergy, negative regulation of immune system process, positive regulation of immune system process, regulation of leukocyte activation, negative regulation of leukocyte activation, regulation of lymphocyte anergy, positive regulation of lymphocyte anergy, proteolysis, ubiquitin-dependent protein catabolic process, ubiquitin cycle, defense response, inflammatory response, negative regulation of cell proliferation,macromolecule catabolic process, response to wounding, regulation of catabolic process, positive regulation of catabolic process, positive regulation of macromolecule metabolic process, viral reproduction, protein ubiquitination,viral infectious cycle, initiation of viral infection, modification-dependent protein catabolic process, viral reproductive process, protein catabolic process, entry into host cell, protein modification by small protein conjugation, regulation of mononuclear cell proliferation, negative regulation of mononuclear cell proliferation, regulation of growth, regulation of cell proliferation, regulation of T cell proliferation, negative regulation of T cell proliferation, regulation of protein catabolic process, protein ubiquitination during ubiquitin-dependent protein catabolic process, modification-dependent macromolecule catabolic process, cellular protein catabolic process, cellular macromolecule catabolic process, entry into host, positive regulation of protein catabolic process, regulation of alpha-beta T cell activation, negative regulation of alpha-beta T cell activation, regulation of alpha-beta T cell proliferation, negative regulation of alpha-beta T cell proliferation, entry of virus into host cell, regulation of lymphocyte proliferation, negative regulation of lymphocyte proliferation, regulation of T cell activation, regulation of cell activation, negative regulation of cell activation, negative regulation of T cell activation, positive regulation of protein metabolic process, regulation of lymphocyte activation,negative regulation of lymphocyte activation, proteolysis involved in cellular protein catabolic process, entry into cell of other organism during symbiotic interaction, entry into other organism during symbiotic interaction, movement in host environment, movement in environment of other organism during symbiotic interaction, protein modification by small protein conjugation or removal, regulation of leukocyte proliferation, negative regulation of leukocyte proliferation,

Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm . Nucleus . Early endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . May be recruited to exosomes by NDFIP1 (PubMed:18819914). Localizes to plasma membrane upon CXCL12 stimulation where it co-localizes with CXCL4 (PubMed:14602072). Localization to early endosomes is increased upon CXCL12 stimulation where it co-localizes with DTX3L and CXCL4 (PubMed:24790097). .

Widely expressed.