Sharpin - SHANK-associated RH domain interactor (Norway rat)
Gene
Symbol
Taxonomy
Dates
- Create:2016-09-14
- Modify:2025-01-15
Description
Enables identical protein binding activity. Predicted to be involved in several processes, including proteasome-mediated ubiquitin-dependent protein catabolic process; protein linear polyubiquitination; and regulation of signal transduction. Predicted to act upstream of or within apoptotic nuclear changes; keratinization; and mitochondrion organization. Located in dendrite. Is active in glutamatergic synapse and postsynaptic density. Orthologous to human SHARPIN (SHANK associated RH domain interactor).
- Conneck1
- sharpin
- SHANK-associated RH domain interacting protein
- shank-associated RH domain-interacting protein
- shank-interacting protein
Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605
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