DNAJC25-GNG10 readthrough protein (DNAJC25-GNG10)

The DNAJC25-GNG10 readthrough protein is a chimeric protein product formed by co-transcription of the adjacent human DNAJC25 and GNG10 genes[1][3][10]. The resulting mRNA transcript incorporates the first exon of DNAJC25—encoding a member of the Hsp40 (DnaJ) co-chaperone family—and the last two exons of GNG10, which codes for the gamma subunit 10 of heterotrimeric G-proteins[1][3][10]. The resulting protein thus contains the N-terminus derived from DNAJC25 and the C-terminus from GNG10[3]. This readthrough event is relatively rare and its biological significance, distinct from the individual parent proteins, is unclear; no established function or disease association is annotated for the chimeric protein[3][10]. The parental protein, DNAJC25, is primarily involved in protein folding and cellular proteostasis as a co-chaperone to Hsp70, with notable downregulation observed in hepatocellular carcinoma and possible tumor suppressor functions[2][5]. GNG10 is part of the G protein family involved in signal transduction, but its physiological and disease roles remain incompletely detailed and are not specifically attributed to the readthrough product[3][5]. No drugs are known to specifically interact with the DNAJC25-GNG10 readthrough protein, nor are there mechanisms of action, biomarker roles, or safety concerns specific to this fusion product[3][10]. This readthrough locus and the resulting protein are documented in gene annotation resources, but current evidence suggests no independent therapeutic, diagnostic, or biomarker status.

Other names

DNAJC25-GNG10 proteinDNAJC25-GNG10 readthrough transcript

None established