Редактирование: RNF111

E3 ubiquitin-protein ligase Arkadia (EC 2.3.2.27) (RING finger protein 111) (hRNF111) (RING-type E3 ubiquitin transferase Arkadia)

==Publications==

{{medline-entry
|title=Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27200078
|abstract=Global-genome nucleotide excision repair (GG-NER) prevents genome instability by excising a wide range of different DNA base adducts and crosslinks induced by chemical carcinogens, ultraviolet (UV) light or intracellular side products of metabolism. As a versatile damage sensor, xeroderma pigmentosum group C ([[XPC]]) protein initiates this generic defense reaction by locating the damage and recruiting the subunits of a large lesion demarcation complex that, in turn, triggers the excision of aberrant DNA by endonucleases. In the very special case of a DNA repair response to UV radiation, the function of this [[XPC]] initiator is tightly controlled by the dual action of cullin-type CRL4(DDB2) and sumo-targeted [[RNF111]] ubiquitin ligases. This twofold protein ubiquitination system promotes GG-NER reactions by spatially and temporally regulating the interaction of [[XPC]] protein with damaged DNA across the nucleosome landscape of chromatin. In the absence of either CRL4(DDB2) or [[RNF111]], the DNA excision repair of UV lesions is inefficient, indicating that these two ubiquitin ligases play a critical role in mitigating the adverse biological effects of UV light in the exposed skin. 

|keywords=* DNA repair
* UV radiation
* aging
* cyclobutane pyrimidine dimer
* genomic instability
* photoproducts
* skin cancer
* sunburns
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4848295
}}
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