PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24824036-2	2014	TIA-1 possesses three RNA recognition motifs (RRM) along with a glutamine-rich domain, with the central domains (RRM2 and RRM3) acting as RNA binding platforms.	Glutamine	64-73	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	0-5	
1934064-3	1991	Sequence analysis reveals that the 40 kd TIA-1 isoform (rp40-TIA-1) is structurally related to the poly(A)-binding proteins, possessing three RNA-binding domains and a carboxy-terminal, glutamine-rich auxiliary domain.	Glutamine	186-195	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	41-46	
21189287-4	2011	TIA1 and TIAR are modular proteins with three N-terminal RNA recognition motifs (RRMs) and a C-terminal glutamine-rich (Q-rich) domain.	Glutamine	104-113	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	0-4	
23902765-2	2013	TIA-1 is composed of three RNA recognition motifs (RRMs) and a glutamine-rich domain and binds to uridine-rich RNA sequences through its C-terminal RRM2 and RRM3 domains.	Glutamine	63-72	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	0-5	
16775137-9	2006	This glutamine-rich region behaves in a similar manner as TIA-1 and prion protein, two molecules with known roles in protein aggregation.	Glutamine	5-14	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	58-63	
1934064-3	1991	Sequence analysis reveals that the 40 kd TIA-1 isoform (rp40-TIA-1) is structurally related to the poly(A)-binding proteins, possessing three RNA-binding domains and a carboxy-terminal, glutamine-rich auxiliary domain.	Glutamine	186-195	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	61-66