PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30488434-0	2019	HNRNP Q suppresses polyglutamine huntingtin aggregation by post-transcriptional regulation of vaccinia-related kinase 2.	polyglutamine	19-32	VRK serine/threonine kinase 2	Homo sapiens	94-119	
30488434-2	2019	Recently, it was found that polyQ aggregates accumulate as a result of vaccinia-related kinase 2 (VRK2)-mediated degradation of TCP-1 ring complex (TRiC)/chaperonin-containing TCP-1 (CCT), which has an essential role in the prevention of polyQ protein aggregation and cytotoxicity.	polyglutamine	28-33	VRK serine/threonine kinase 2	Homo sapiens	71-96	
30488434-2	2019	Recently, it was found that polyQ aggregates accumulate as a result of vaccinia-related kinase 2 (VRK2)-mediated degradation of TCP-1 ring complex (TRiC)/chaperonin-containing TCP-1 (CCT), which has an essential role in the prevention of polyQ protein aggregation and cytotoxicity.	polyglutamine	28-33	VRK serine/threonine kinase 2	Homo sapiens	98-102	
27377031-0	2016	Glycogen synthase kinase 3beta suppresses polyglutamine aggregation by inhibiting Vaccinia-related kinase 2 activity.	polyglutamine	42-55	VRK serine/threonine kinase 2	Homo sapiens	82-107	
24298020-0	2014	Vaccinia-related kinase 2 mediates accumulation of polyglutamine aggregates via negative regulation of the chaperonin TRiC.	polyglutamine	51-64	VRK serine/threonine kinase 2	Homo sapiens	0-25	
24298020-6	2014	Interestingly, VRK2-mediated downregulation of TRiC increased aggregate formation of a polyQ-expanded huntingtin fragment.	polyglutamine	87-92	VRK serine/threonine kinase 2	Homo sapiens	15-19	
24298020-11	2014	Taken together, these results demonstrate that VRK2 is crucial to regulate the ubiquitination-proteosomal degradation of TRiC, which controls folding of polyglutamine proteins involved in Huntington"s disease.	polyglutamine	153-166	VRK serine/threonine kinase 2	Homo sapiens	47-51