PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23558684-6	2013	Although a fraction of RRM1 aggregates comprised disulfide-bonded oligomers, the substitution of cysteine(s) to serine(s) (C/S) resulted in unexpected acceleration of amyloid fibrils of RRM1 and disulfide-independent aggregate formation of full-length TDP-43.	Serine	112-118	ribonucleotide reductase catalytic subunit M1	Homo sapiens	186-190	
2172449-3	1990	Here, it is shown that the ts mutant phenotype is due to the substitution of an asparagine for the wild-type (wt) serine at RR1 position 961, which is located within a region highly conserved between herpesviral and cellular RR1 subunit polypeptides.	Serine	114-120	ribonucleotide reductase catalytic subunit M1	Homo sapiens	124-127	
34126361-5	2021	Mechanistically, mTORC2 directly interacted and phosphorylated RNR large subunit RRM1 at Ser 631.	Serine	89-92	ribonucleotide reductase catalytic subunit M1	Homo sapiens	81-85	
32712628-5	2020	Here, we report that RRM1 is phosphorylated at Ser 559 by CDK2/cyclin A during S/G2 phase.	Serine	47-50	ribonucleotide reductase catalytic subunit M1	Homo sapiens	21-25	
19886675-1	2009	ASF/SF2, a member of the serine-arginine (SR) protein family, has two RRM domains (RRM1 and RRM2) and a C-terminal domain rich in RS dipeptides.	Serine	25-31	ribonucleotide reductase catalytic subunit M1	Homo sapiens	83-87	
18687337-1	2008	The SR (arginine-serine rich) protein ASF/SF2 (also called human alternative splicing factor), an essential splicing factor, contains two functional modules consisting of tandem RNA recognition motifs (RRMs; RRM1-RRM2) and a C-terminal arginine-serine repeat region (RS domain, a domain rich in arginine-serine repeats).	Serine	17-23	ribonucleotide reductase catalytic subunit M1	Homo sapiens	208-212	
18687337-1	2008	The SR (arginine-serine rich) protein ASF/SF2 (also called human alternative splicing factor), an essential splicing factor, contains two functional modules consisting of tandem RNA recognition motifs (RRMs; RRM1-RRM2) and a C-terminal arginine-serine repeat region (RS domain, a domain rich in arginine-serine repeats).	Serine	245-251	ribonucleotide reductase catalytic subunit M1	Homo sapiens	208-212	
18687337-1	2008	The SR (arginine-serine rich) protein ASF/SF2 (also called human alternative splicing factor), an essential splicing factor, contains two functional modules consisting of tandem RNA recognition motifs (RRMs; RRM1-RRM2) and a C-terminal arginine-serine repeat region (RS domain, a domain rich in arginine-serine repeats).	Serine	245-251	ribonucleotide reductase catalytic subunit M1	Homo sapiens	208-212