ribonuclease P/MRP subunit p25 (Ensembl:ribonuclease P and MRP subunit p25)
RGD ID:
1305290
Description:
Predicted to enable ribonuclease P RNA binding activity. Predicted to contribute to ribonuclease P activity. Predicted to be involved in tRNA 5'-leader removal. Predicted to be located in centriolar satellite; nucleolus; and nucleoplasm. Predicted to be part of multimeric ribonuclease P complex and ribonuclease MRP complex. Orthologous to human RPP25 (ribonuclease P and MRP subunit p25); PARTICIPATES IN tRNA maturation pathway; ribosome biogenesis pathway; RNA transport pathway; INTERACTS WITH 2,3,7,8-tetrachlorodibenzodioxine; 6-propyl-2-thiouracil; alpha-Zearalanol.
LOC315705; ribonuclease P 25 subunit; ribonuclease P 25 subunit (human); ribonuclease P and MRP subunit p25; ribonuclease P protein subunit p25; ribonuclease P/MRP 25 subunit; RNase P protein subunit p25
[NOG protein co-treated with entinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression more ...
[NOG protein co-treated with entinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression more ...
[NOG protein co-treated with Panobinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression more ...
[NOG protein co-treated with Phenylmercuric Acetate co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in decreased more ...
[NOG protein co-treated with entinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression more ...
[NOG protein co-treated with Valproic Acid co-treated with dorsomorphin co-treated with 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased more ...