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	
3.4.22.B79	physiological function	nsP2 is either directly or indirectly involved in the RNA encapsidation process	
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	
3.4.22.B79	physiological function	complete elimination of nonstructural proteins nsp1 and nsp2 does not abolish viral viability	
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