Description
Tripartite motif containing protein 41 or E3 ubiquitin-protein ligase TRIM41 (human TRIM41 theoretical molecular weight 72 kDa) is a RING finger domain protein which catalyzes the degradation of protein kinase C (PKC). TRIM family members share N-terminal RING finger, one or two B box, and Coiled-Coil domains (CCD). The RING (Really Interesting New Gene) finger domain imparts TRIMs with E3 ubiquitin ligase activity and ability to regulate cell cycle, transcription factor, and signal transducing genes. TRIMs are involved in different cellular processes including cellular differentiation, senescence, stem cell pluripotency, and control of microbial infections (1). TRIM41 plays a role in the regulation of innate immunity to viral infections. Hepatitis B virus (HBV) replication is inhibited by TRIM41 in a process dependent on its E3 ligase activity (2, 3). TRIM41 is also involved in the inhibition of influenza A virus (IAV) by ubiquitinating and targeting the influenza nucleoprotein for proteasome degradation (4).
1. Kimura, T., Mandell, M., & Deretic, V. (2016). Precision autophagy directed by receptor regulators - emerging examples within the TRIM family. Journal of Cell Science.https://doi.org/10.1242/jcs.163758
2. Kong, F., You, H., Kong, D., Zheng, K., & Tang, R. (2019). The interaction of hepatitis B virus with the ubiquitin proteasome system in viral replication and associated pathogenesis. Virology Journal. https://doi.org/10.1186/s12985-019-1183-z
3. van Tol, S., Hage, A., Giraldo, M. I., Bharaj, P., & Rajsbaum, R. (2017). The TRIMendous role of TRIMs in virus-host interactions. Vaccines. https://doi.org/10.3390/vaccines5030023
Bioinformatics
| Product By Gene ID |
90933 |
| Alternate Names |
- tripartite motif containing 41
|
