PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	49-63	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	109-113	
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	65-67	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	109-113	
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	77-81	
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	77-81