Target intelligence / Profile preview

Ring finger protein 113B (RNF113B)

Target
RNF113B
Molecular classification
Other (RING finger protein, E3 ubiquitin ligase family; zinc finger protein; not a classical receptor, enzyme, or transporter)
01

Overview

Ring finger protein 113B (RNF113B) is a primate-specific paralog of RNF113A, encoded on human chromosome 13[1][5]. It features both a RING finger domain and a zinc finger motif—structural elements characteristic of proteins with E3 ubiquitin ligase activity, though its specific biochemical function remains incompletely defined[1][3]. Preliminary evidence predicts a role in snoRNA splicing and possible involvement in the U2-type spliceosomal complex, as well as metal ion binding[3][4]. While its paralog, RNF113A, is implicated in disease and spliceosome biology, RNF113B itself has no confirmed human disease associations or established physiological or disease roles as of the latest genetic databases[1][3][5][6]. Its function may overlap with RNF113A in aspects of DNA repair and RNA processing, particularly under genotoxic stress, but the precise relevance to human biology and pathology requires further study[1]. Key points: - Ring finger protein 113B is not a recognized therapeutic target; it is not classified as a receptor, enzyme, transporter, or transcription factor according to available resources[3][5]. - It is a protein coding gene with predicted molecular functions, but with no established interacting drugs, biomarker status, or safety profile for clinical targeting[3][4]. - Aliases include RNF161 and ZNF183L1; these should not be confused with RNF113A, which has distinct genetic disease implications[3][5][1].

Other names
RNF161ZNF183L1bA10G5.1Zinc finger protein 183-like 1
02

Mechanism of action

Not established for therapeutic modulation; predicted function as E3 ubiquitin ligase and involvement in RNA splicing or DNA repair

03

Biological functions

Likely involved in DNA repairmay act in RNA splicing (snoRNA splicing, potential role in spliceosomal complex)metal ion binding
04

Disease associations

No direct association with human disease currently establishedpreliminary research suggests possible roles in development and DNA repair mechanisms, especially in relation to cisplatin-induced DNA crosslinks

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