PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33887136-4	2021	To investigate how site-specific S-palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes.	Cysteine	198-206	interferon induced transmembrane protein 3	Homo sapiens	59-65	
33887136-4	2021	To investigate how site-specific S-palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes.	Cysteine	198-206	interferon induced transmembrane protein 3	Homo sapiens	245-251	
29575903-6	2018	Notably, we directly identified the S-fatty-acylation sites of IFITM3, an important interferon-stimulated inhibitor of virus entry, and we further demonstrated that the highly conserved Cys residues are primarily modified by palmitic acid.	Cysteine	186-189	interferon induced transmembrane protein 3	Homo sapiens	63-69	
31826928-6	2020	This mutant shows altered subcellular localization and reduced S-palmitoylation, a phenotype copied by mutation of conserved cysteine residues in microbat IFITM3.	Cysteine	125-133	interferon induced transmembrane protein 3	Homo sapiens	155-161	
31826928-7	2020	Furthermore, we show that microbat IFITM3 is S-palmitoylated on cysteine residues C71, C72, and C105, mutation of each cysteine individually impairs virus restriction, and a triple C71A-C72A-C105A mutant loses all restriction activity, concomitant with subcellular re-localization of microbat IFITM3 to Golgi-associated sites.	Cysteine	64-72	interferon induced transmembrane protein 3	Homo sapiens	35-41	
31826928-7	2020	Furthermore, we show that microbat IFITM3 is S-palmitoylated on cysteine residues C71, C72, and C105, mutation of each cysteine individually impairs virus restriction, and a triple C71A-C72A-C105A mutant loses all restriction activity, concomitant with subcellular re-localization of microbat IFITM3 to Golgi-associated sites.	Cysteine	119-127	interferon induced transmembrane protein 3	Homo sapiens	35-41	
27044110-5	2016	Using APE, we show that endogenous interferon-induced transmembrane protein 3 is S-fatty acylated on three cysteine residues and site-specific modification of highly conserved cysteines are crucial for the antiviral activity of this IFN-stimulated immune effector.	Cysteine	107-115	interferon induced transmembrane protein 3	Homo sapiens	35-77	
27044110-5	2016	Using APE, we show that endogenous interferon-induced transmembrane protein 3 is S-fatty acylated on three cysteine residues and site-specific modification of highly conserved cysteines are crucial for the antiviral activity of this IFN-stimulated immune effector.	Cysteine	176-185	interferon induced transmembrane protein 3	Homo sapiens	35-77	
24058703-3	2013	IFITM3 possesses three cysteine residues for the S-palmitoylation in the first transmembrane (TM1) domain and in the cytoplasmic (CP) loop.	Cysteine	23-31	interferon induced transmembrane protein 3	Homo sapiens	0-6