PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7683646-9	1993	Although substitution of residues 54 and 55 with the analogous residues from IGF-I (Arg-Arg) abolished binding to the IGF-II/mannose 6-phosphate receptor, binding to IGFBPs was not substantially affected.	Arginine	84-87	insulin like growth factor 2	Homo sapiens	118-124	
11811790-2	2001	We have mutated residues A54 and L55 of IGF-II in the second A domain helix to arginine (found in the corresponding positions of IGF-I) and measured IGF2R binding.	Arginine	79-87	insulin like growth factor 2	Homo sapiens	40-46	
7633596-4	1995	N-Terminal sequencing revealed IGF II and an IGF II variant in which Ser29 was replaced by the tetrapeptide Arg-Leu-Pro-Gly.	Arginine	108-111	insulin like growth factor 2	Homo sapiens	45-51	
9712856-1	1998	The two mannose 6-phosphate (Man-6-P) binding sites of the insulin-like growth factor-II/mannose 6-phosphate receptor (IGF-II/MPR) have been localized to domains 1-3 and 7-9, and studies have shown that Arg435 in domain 3 and Arg 1334 in domain 9 are essential for Man-6-P binding.	Arginine	203-206	insulin like growth factor 2	Homo sapiens	119-125	
7957246-8	1994	Determination of the N-terminal amino acid sequence of human IGF-II before and after digestion with DAP-I showed that DAP-I cleaved Ala-Tyr, terminating at Arg-Pro-; the rat IGF-II species beginning with Tyr-Arg-Pro-Ser- was resistant to digestion.	Arginine	156-159	insulin like growth factor 2	Homo sapiens	61-67	
7957246-8	1994	Determination of the N-terminal amino acid sequence of human IGF-II before and after digestion with DAP-I showed that DAP-I cleaved Ala-Tyr, terminating at Arg-Pro-; the rat IGF-II species beginning with Tyr-Arg-Pro-Ser- was resistant to digestion.	Arginine	208-211	insulin like growth factor 2	Homo sapiens	61-67	
7683646-9	1993	Although substitution of residues 54 and 55 with the analogous residues from IGF-I (Arg-Arg) abolished binding to the IGF-II/mannose 6-phosphate receptor, binding to IGFBPs was not substantially affected.	Arginine	88-91	insulin like growth factor 2	Homo sapiens	118-124	
1282887-2	1992	A mutant of human insulin-like growth factor II (IGF II) was constructed by site-directed mutagenesis: the nucleotides coding for Ser33 and Ser39 were changed to yield Arg and Lys, respectively, thus creating two pairs of basic residues, Arg-Arg and Lys-Arg, as flanking sequences of the remaining C domain.	Arginine	168-171	insulin like growth factor 2	Homo sapiens	18-55	
1282887-2	1992	A mutant of human insulin-like growth factor II (IGF II) was constructed by site-directed mutagenesis: the nucleotides coding for Ser33 and Ser39 were changed to yield Arg and Lys, respectively, thus creating two pairs of basic residues, Arg-Arg and Lys-Arg, as flanking sequences of the remaining C domain.	Arginine	238-241	insulin like growth factor 2	Homo sapiens	18-55	
1282887-2	1992	A mutant of human insulin-like growth factor II (IGF II) was constructed by site-directed mutagenesis: the nucleotides coding for Ser33 and Ser39 were changed to yield Arg and Lys, respectively, thus creating two pairs of basic residues, Arg-Arg and Lys-Arg, as flanking sequences of the remaining C domain.	Arginine	238-241	insulin like growth factor 2	Homo sapiens	18-55	
1282887-2	1992	A mutant of human insulin-like growth factor II (IGF II) was constructed by site-directed mutagenesis: the nucleotides coding for Ser33 and Ser39 were changed to yield Arg and Lys, respectively, thus creating two pairs of basic residues, Arg-Arg and Lys-Arg, as flanking sequences of the remaining C domain.	Arginine	238-241	insulin like growth factor 2	Homo sapiens	18-55	
6172444-3	1982	The synthetic 8-amino acid C-peptide segment of IGF-II (Ser-Arg-Val-Ser-Arg-Arg-Ser-Arg) was covalently linked to thyroglobulin to render it more antigenic.	Arginine	60-63	insulin like growth factor 2	Homo sapiens	48-54	
34944251-3	2021	Skeletal muscle from piglets born from sows from ARG group had greater mRNA expression of MYOD (p = 0.043) and MYOG (p <= 0.01), and tended to present greater mRNA expression (p = 0.06) of IGF-2 gene compared to those born from CON sows.	Arginine	49-52	insulin like growth factor 2	Homo sapiens	189-194	
2553732-2	1989	The amino-terminal sequence of the first 35 amino acid residues showed a replacement of Ser-29 of IGF-II with the tetrapeptide Arg-Leu-Pro-Gly of IGF-II variant.	Arginine	127-130	insulin like growth factor 2	Homo sapiens	98-104	
2553732-2	1989	The amino-terminal sequence of the first 35 amino acid residues showed a replacement of Ser-29 of IGF-II with the tetrapeptide Arg-Leu-Pro-Gly of IGF-II variant.	Arginine	127-130	insulin like growth factor 2	Homo sapiens	146-152	
2536701-6	1989	Residues 49, 50, and 51 in IGF I are Phe-Arg-Ser and are strictly conserved in IGF II.	Arginine	41-44	insulin like growth factor 2	Homo sapiens	79-85	
2536701-7	1989	Residues 55 and 56 of IGF I and the corresponding residues in IGF II are Arg-Arg and Ala-Leu, respectively.	Arginine	73-76	insulin like growth factor 2	Homo sapiens	62-68	
2536701-7	1989	Residues 55 and 56 of IGF I and the corresponding residues in IGF II are Arg-Arg and Ala-Leu, respectively.	Arginine	77-80	insulin like growth factor 2	Homo sapiens	62-68	
3881277-4	1985	In the amino acid sequence predicted by the IGF-II variant cDNA, the Ser residue 29 in the B-domain has been replaced by an Arg-Leu-Pro-Gly sequence.	Arginine	124-127	insulin like growth factor 2	Homo sapiens	44-50	
6172444-3	1982	The synthetic 8-amino acid C-peptide segment of IGF-II (Ser-Arg-Val-Ser-Arg-Arg-Ser-Arg) was covalently linked to thyroglobulin to render it more antigenic.	Arginine	72-75	insulin like growth factor 2	Homo sapiens	48-54