|Other Names||E3 ubiquitin-protein ligase Itchy homolog, Itch, 632-, Atrophin-1-interacting protein 4, AIP4, NFE2-associated polypeptide 1, NAPP1, ITCH|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13626c was selected from the Center region of ITCH. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Acts as an 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. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.|
|Cellular Location||Cell membrane. Cytoplasm. Nucleus. Note=Associates with endocytic vesicles. May be recruited to exosomes by NDFIP1|
|Tissue Location||Widely expressed.|
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Atrophin-1 contains a polyglutamine repeat, expansion ofwhich is responsible for dentatorubral and pallidoluysian atrophy.The protein encoded by this gene interacts with atrophin-1. Thisencoded protein is a closely related member of the NEDD4-likeprotein family. This family of proteins are E3 ubiquitin-ligasemolecules and regulate key trafficking decisions, includingtargeting of proteins to proteosomes or lysosomes. This encodedprotein contains four tandem WW domains and a HECT (homologous tothe E6-associated protein carboxyl terminus) domain. It can act asa transcriptional corepressor of p45/NFE2 and may participate inthe regulation of immune responses by modifying Notch-mediatedsignaling. It is highly similar to the mouse Itch protein, whichhas been implicated in the regulation and differentiation oferythroid and lymphoid cells.
Yang, F., et al. Cell Death Differ. 17(8):1354-1367(2010)Baumann, C., et al. FEBS J. 277(13):2803-2814(2010)Venuprasad, K. Cancer Res. 70(8):3009-3012(2010)Lohr, N.J., et al. Am. J. Hum. Genet. 86(3):447-453(2010)Ushijima, Y., et al. Virol. J. 7, 179 (2010) :
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