SHARPIN report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0097039Biological processprotein linear polyubiquitination
GO_0031424Biological processkeratinization
GO_0030262Biological processapoptotic nuclear changes
GO_0010803Biological processregulation of tumor necrosis factor-mediated signaling pathway
GO_0007005Biological processmitochondrion organization
GO_0050728Biological processnegative regulation of inflammatory response
GO_0043123Biological processpositive regulation of canonical NF-kappaB signal transduction
GO_0042742Biological processdefense response to bacterium
GO_2000348Biological processregulation of CD40 signaling pathway
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0071797Cellular componentLUBAC complex
GO_0030425Cellular componentdendrite
GO_0005829Cellular componentcytosol
GO_0045202Cellular componentsynapse
GO_0044877Molecular functionprotein-containing complex binding
GO_0042802Molecular functionidentical protein binding
GO_0030674Molecular functionprotein-macromolecule adaptor activity
GO_0046872Molecular functionmetal ion binding
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0031593Molecular functionpolyubiquitin modification-dependent protein binding
GO_0005515Molecular functionprotein binding
GO_0043130Molecular functionubiquitin binding

IV. Literature review

[source]
Gene nameSHARPIN
Protein nameSHARPIN protein
SHANK associated RH domain interactor
Sharpin (Shank-associated RH domain-interacting protein) (Shank-interacting protein-like 1) (hSIPL1)
SynonymsSIPL1
PSEC0216
DescriptionFUNCTION: 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 . .

AccessionsENST00000359551.6 [Q9H0F6-2]
Q6PJD5
H0YCU2
ENST00000398712.7 [Q9H0F6-1]
ENST00000532536.5
Q9H0F6