PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19041431-2	2009	We previously reported that, via their SH3 domains, several members of the PCH proteins interact with the proline-rich region of Fas ligand (FasL, CD95L), a key death factor in immune cells.	Proline	106-113	Fas ligand	Homo sapiens	129-139	
32905906-7	2020	A direct interaction between the proline-rich domain of FasL and the SH3 domain of PI(3)K-p85alpha initiates the first pathway.	Proline	33-40	Fas ligand	Homo sapiens	56-60	
32905906-10	2020	FasL can recruit Fyn via the proline-rich domain leading to the recruitment of ADAP.	Proline	29-36	Fas ligand	Homo sapiens	0-4	
24291222-4	2014	Previous work established that the proline-rich domain within the cytosolic N-terminus of FasL is required for protein-protein interactions with different Src homology 3 (SH3) or WW domain proteins.	Proline	35-42	Fas ligand	Homo sapiens	90-94	
19807924-7	2009	In addition to known SH3 domains mediating binding to the Fas ligand proline-rich domain, we were able to identify a number of additional SH3 domains that might also associate with FasL.	Proline	69-76	Fas ligand	Homo sapiens	58-68	
19807924-7	2009	In addition to known SH3 domains mediating binding to the Fas ligand proline-rich domain, we were able to identify a number of additional SH3 domains that might also associate with FasL.	Proline	69-76	Fas ligand	Homo sapiens	181-185	
19041431-2	2009	We previously reported that, via their SH3 domains, several members of the PCH proteins interact with the proline-rich region of Fas ligand (FasL, CD95L), a key death factor in immune cells.	Proline	106-113	Fas ligand	Homo sapiens	141-145	
19041431-2	2009	We previously reported that, via their SH3 domains, several members of the PCH proteins interact with the proline-rich region of Fas ligand (FasL, CD95L), a key death factor in immune cells.	Proline	106-113	Fas ligand	Homo sapiens	147-152	
18789888-2	2008	Here, we show that Grb2, an SH3 domain-containing adaptor protein, binds to the proline-rich domain of FasL and regulates its cell surface expression.	Proline	80-87	Fas ligand	Homo sapiens	103-107	
18673218-9	2008	Of interest, the intracellular portion of FasL contains a unique proline-rich domain, which plays a major role in the control of FasL transport and expression due to interactions with proteins containing SH3 or WW interaction domains.	Proline	65-72	Fas ligand	Homo sapiens	42-46	
18673218-9	2008	Of interest, the intracellular portion of FasL contains a unique proline-rich domain, which plays a major role in the control of FasL transport and expression due to interactions with proteins containing SH3 or WW interaction domains.	Proline	65-72	Fas ligand	Homo sapiens	129-133	
16318909-3	2006	It has been noted before that the proline-rich domain within the cytosolic part of FasL is required for its vesicular association.	Proline	34-41	Fas ligand	Homo sapiens	83-87	
17761170-3	2007	The intracellular domain of FasL contains consensus sequences for phosphorylation and an extended proline rich region, which regulate its surface expression through undetermined mechanism(s).	Proline	98-105	Fas ligand	Homo sapiens	28-32	
17505842-7	2007	RESULTS: We found that the level of endogenous FasL, but not Fas receptor, was increased at a permissive temperature with delayed kinetics when compared with p21WAF1 expression, but was coincident with p53-induced apoptosis, whereas an apoptosis-defective mutant p53, which lacks the PxxP region (P: Proline, x: any amino acid), failed to induce FasL expression and hence apoptosis.	Proline	300-307	Fas ligand	Homo sapiens	47-51	
17164290-2	2007	Previous studies identified a proline-rich domain in the cytoplasmic tail required for sorting FasL to secretory lysosomes, but the mechanisms by which this occurs have not been identified.	Proline	30-37	Fas ligand	Homo sapiens	95-99	
17947633-2	2007	We now show that Fas ligand molecules lacking amino acids 45-54 in the proline-rich region of the cytoplasmic domain fail to costimulate but serve as effective death inducers.	Proline	71-78	Fas ligand	Homo sapiens	17-27	
16595635-5	2006	Nck binds to the proline-rich portion of FasL and alters its subcellular distribution when coexpressed in 293T cells.	Proline	17-24	Fas ligand	Homo sapiens	41-45	
16849454-5	2006	We further show that the proline-rich intracellular domain of FasL is sufficient to costimulate by enhancing the phosphorylation of Akt, ERK1/2, JNK, and FasL itself, by activating the transcription factors NFAT and AP-1, and by enhancing IFN-gamma production.	Proline	25-32	Fas ligand	Homo sapiens	62-66	
16849454-5	2006	We further show that the proline-rich intracellular domain of FasL is sufficient to costimulate by enhancing the phosphorylation of Akt, ERK1/2, JNK, and FasL itself, by activating the transcription factors NFAT and AP-1, and by enhancing IFN-gamma production.	Proline	25-32	Fas ligand	Homo sapiens	154-158	
16332972-7	2006	Localization to lipid rafts appears to be predominantly mediated by the characteristic cytoplasmic proline-rich domain of Fas ligand because mutations of this domain result in reduced recruitment to lipid rafts and attenuated Fas ligand killing activity.	Proline	99-106	Fas ligand	Homo sapiens	122-132	
16332972-7	2006	Localization to lipid rafts appears to be predominantly mediated by the characteristic cytoplasmic proline-rich domain of Fas ligand because mutations of this domain result in reduced recruitment to lipid rafts and attenuated Fas ligand killing activity.	Proline	99-106	Fas ligand	Homo sapiens	226-236	
15470053-4	2004	Previous studies suggest that the proline-rich domain (aa 43-70) in FasLCyt (FasLPRD) inhibits FasL membrane expression by retaining FasL in the secretory lysosomes.	Proline	34-41	Fas ligand	Homo sapiens	68-72	
16282344-3	2006	In addition to its receptor-interacting and cell death-inducing extracellular domain, FasL has a well-conserved intracellular portion with a proline-rich SH3 domain-binding site probably involved in non-apoptotic functions.	Proline	141-148	Fas ligand	Homo sapiens	86-90	
16204241-3	2005	FasL contains an 80-amino acid-long cytoplasmic tail, which includes a proline-rich domain as a bona fide Src homology 3 domain-binding site.	Proline	71-78	Fas ligand	Homo sapiens	0-4	
16204241-4	2005	This proline-rich domain has been implicated in FasL sorting to secretory lysosomes, and it may also be important for reverse signaling via FasL, which has been described to influence T-cell activation.	Proline	5-12	Fas ligand	Homo sapiens	48-52	
16204241-4	2005	This proline-rich domain has been implicated in FasL sorting to secretory lysosomes, and it may also be important for reverse signaling via FasL, which has been described to influence T-cell activation.	Proline	5-12	Fas ligand	Homo sapiens	140-144	
16204241-5	2005	Here we report the identification of the Src homology 3 domain-containing adaptor protein PSTPIP as a FasL-interacting partner, which binds to the proline-rich domain.	Proline	147-154	Fas ligand	Homo sapiens	102-106	
15470053-4	2004	Previous studies suggest that the proline-rich domain (aa 43-70) in FasLCyt (FasLPRD) inhibits FasL membrane expression by retaining FasL in the secretory lysosomes.	Proline	34-41	Fas ligand	Homo sapiens	77-81	
15470053-7	2004	In addition, retention of proline-rich domain-containing FasL in the cytoplasm was not observed.	Proline	26-33	Fas ligand	Homo sapiens	57-61	
9920849-7	1999	Lastly, mutation of a proline motif in the core region of the nef gene, which disrupts its ability to interact with cellular kinases and reduces HIV-1 replication in vitro, completely abrogated the Nef-mediated induction of apoptosis as well as its ability to upregulate surface CD95 and CD95L.	Proline	22-29	Fas ligand	Homo sapiens	288-293	
15039212-7	2004	In cases of LOH, there was a preferential loss of the proline allele, which was associated with an up-regulation of Bcl2 and lack of co-expression of Fas/FasL and, thus, impaired apoptosis (P < 0.001).	Proline	54-61	Fas ligand	Homo sapiens	154-158	
15039212-13	2004	Homozygous proline 72 appears to be an important regulator of apoptosis via the Fas/FasL pathway in SCCHN.	Proline	11-18	Fas ligand	Homo sapiens	84-88	
11559749-0	2001	Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail.	Proline	52-59	Fas ligand	Homo sapiens	0-10	
11559749-3	2001	Here, we define a proline-rich domain (PRD) in the cytoplasmic tail of FasL that is responsible for sorting FasL to secretory lysosomes.	Proline	18-25	Fas ligand	Homo sapiens	71-75	
11559749-3	2001	Here, we define a proline-rich domain (PRD) in the cytoplasmic tail of FasL that is responsible for sorting FasL to secretory lysosomes.	Proline	18-25	Fas ligand	Homo sapiens	108-112	
7589480-3	1995	Here, we report that the Src homology 3 (SH3) domain of Fyn binds to the proline-rich cytoplasmic region of FasL.	Proline	73-80	Fas ligand	Homo sapiens	108-112