Recombinant Human RNF146 protein
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Recombinant Human RNF146 protein is a Human Full Length protein, in the 1 to 358 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
E3 ubiquitin-protein ligase RNF146, Dactylidin, Iduna, RING finger protein 146, RING-type E3 ubiquitin transferase RNF146, RNF146
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human RNF146 protein (AB153534)
ab153534 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
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
RNF146 exhibits significant functions that influence cell survival and DNA repair. It interacts with PARP1 an important protein in the DNA damage response. As part of a larger protein complex RNF146 identifies and ubiquitinates proteins modified by PAR facilitating their recognition and subsequent degradation by the proteasome. Through these interactions RNF146 controls levels of damaged proteins and modulates the cellular response to stress contributing to genomic stability.
Pathways
RNF146 plays a part in the Wnt/β-catenin signaling pathway and the DNA damage response pathway. Within the Wnt signaling pathway RNF146 regulates Axin1 and other components influencing cell proliferation and differentiation. Additionally in the DNA damage pathway RNF146 aids in the fine-tuning of protein levels necessary for efficient repair by controlling PAR-modified proteins. Its interactions with proteins such as PARP1 and Tankyrase position RNF146 as a significant player in these pathways.
Specifications
Form
Liquid
General info
Function
E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation (PubMed : 21478859, PubMed : 21799911, PubMed : 22267412). May regulate many important biological processes, such as cell survival and DNA damage response (PubMed : 21825151, PubMed : 22267412). Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex (PubMed : 21478859, PubMed : 21799911). Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2 (PubMed : 21799911). Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation (PubMed : 21799911). Different ubiquitin linkage types have been observed : TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48' (PubMed : 21799911). May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location (PubMed : 21799911). Neuroprotective protein (PubMed : 21602803). Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos (By similarity). Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner (By similarity). Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest (By similarity). Promotes cell survival after gamma-irradiation (PubMed : 21825151). Facilitates DNA repair (PubMed : 21825151).
Post-translational modifications
Ubiquitinated; autoubiquitinated. Polyubiquitinated in the presence of UBE2D1, UBE2D2 and UBE2D3. Multimonoubiquitinated in the presence of UBE2E1. Not ubiquitinated in the presence of UBE2H, CDC34, UBE2L3, UBE2L6, nor UBE2C. In the absence of PAR, autoubiquitination occurs on Lys-85, Lys-95 and Lys-176 via 'Lys-11' and 'Lys-48' ubiquitin linkages. In the presence of PAR, Lys-131 and Lys-176 are ubiquitinated via 'Lys-6', 'Lys-33' and 'Lys-48' ubiquitin linkages. Autoubiquitination is enhanced upon PAR-binding.
Subcellular localisation
Nucleus
Target data
Product promise
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