Recombinant Human RNF115 protein (GST tag N-Terminus)
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Recombinant Human RNF115 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 304 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
ZNF364, RNF115, E3 ubiquitin-protein ligase RNF115, RING finger protein 115, RING-type E3 ubiquitin transferase RNF115, Rab7-interacting RING finger protein, Zinc finger protein 364, Rabring 7
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human RNF115 protein (GST tag N-Terminus) (AB162124)
ab162124 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RNF115 affects protein regulation through its involvement in ubiquitin-mediated processes. It interacts with different substrates and has been identified as part of the BRCA1-A complex which is important in DNA repair mechanisms. It helps regulate cellular levels and stability of proteins impacting cell cycle progression and response to DNA damage. Its activity ensures proper cellular development and homeostasis by maintaining protein turnover.
Pathways
RNF115 engages in the ubiquitin-proteasome system and is implicated in the DNA damage response pathways. It acts within the ubiquitination pathways collaborating with other proteins like BRCA1 and UBE2D1 to influence protein degradation and DNA repair processes. RNF115's role in the regulation of the DNA damage response highlights its connection to cellular stress resilience linking it to cellular pathways that maintain genetic stability.
Specifications
Form
Liquid
General info
Function
E3 ubiquitin-protein ligase that catalyzes the 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of various substrates and thereby plays a role in a number of signaling pathways including autophagy, innate immunity, cell proliferation and cell death (PubMed : 20019814, PubMed : 30689267). Plays a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4 through their polyubiquitination. Participates together with BST2 in antiviral immunity by facilitating the internalization of HIV-1 virions into intracellular vesicles leading to their lysosomal degradation (PubMed : 20019814). Also possesses an antiviral activity independently of BST2 by promoting retroviral GAG proteins ubiquitination, redistribution to endo-lysosomal compartments and, ultimately, lysosomal degradation (PubMed : 24852021). Catalyzes distinct types of ubiquitination on MAVS and STING1 at different phases of viral infection to promote innate antiviral response (PubMed : 33139700). Mediates the 'Lys-48'-linked ubiquitination of MAVS leading to its proteasomal degradation and ubiquitinates STING1 via 'Lys-63'-linked polyubiquitination, critical for its oligomerization and the subsequent recruitment of TBK1 (PubMed : 33139700). Plays a positive role in the autophagosome-lysosome fusion by interacting with STX17 and enhancing its stability without affecting 'Lys-48'- or 'Lys-63'-linked polyubiquitination levels, which in turn promotes autophagosome maturation (PubMed : 32980859). Negatively regulates TLR-induced expression of proinflammatory cytokines by catalyzing 'Lys-11'-linked ubiquitination of RAB1A and RAB13 to inhibit post-ER trafficking of TLRs to the Golgi by RAB1A and subsequently from the Golgi apparatus to the cell surface by RAB13 (PubMed : 35343654).
Post-translational modifications
Phosphorylated by AKT1, allowing association with the 14-3-3 chaperones that facilitates associating with TLRs.. RING-type zinc finger-dependent and E2-dependent autoubiquitination.. Deubiquitinated by USP9X; antogonizing its autoubiquitination and subsequent proteasomal degradation.
Subcellular localisation
Nucleus
Target data
Product promise
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