EC Number |
General Information |
Reference |
---|
3.4.22.B79 | physiological function |
a serine that is close to the catalytical dyad is catalytically interchangeable with the dyad cysteine residue. The enzyme retains activity upon alanine replacement of either residue but a replacement of both cysteine and serine residues results in no detectable activity |
-, 755412 |
3.4.22.B79 | physiological function |
complete elimination of nonstructural proteins nsp1 and nsp2 does not abolish viral viability |
-, 754547 |
3.4.22.B79 | physiological function |
nsP2 inhibits cellular transcription by inducing rapid degradation of Rpb1, a catalytic subunit of the RNAPII complex. This degradation of Rpb1 is independent of the nsP2-associated protease activity, but, instead, it proceeds through nsP2-mediated Rpb1 ubiquitination. This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation |
732413 |
3.4.22.B79 | physiological function |
nsP2 is either directly or indirectly involved in the RNA encapsidation process |
732418 |
3.4.22.B79 | physiological function |
upon transfection of HeLa cells, 21 differentially regulated (six upregulated, 15 downregulated) spots are observed. Ubiquitin-conjugating enzyme UBE2L3 is downregulated. Transfection of full length UBE2L3 into HEK293T/17 cells prior to CHIKV infection reduces levels of infection but does not alter RNA genome levels |
755360 |