PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24311590-2	2013	The nuclear isoform of human dUTPase, an enzyme that is essential for genomic integrity, has been shown to be phosphorylated on a serine residue (Ser11) in the vicinity of its nuclear localization signal; however, the effect of this phosphorylation is not yet known.	Serine	130-136	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36	
30902068-8	2019	The resulting Dr-dUTPase had the leading peptide Gly-Ser-His- originating from the vector at the amino terminus, and a mutation, Arg66Lys, to remove the internal thrombin site.	Serine	53-56	Deoxyuridine triphosphatase	Drosophila melanogaster	17-24	
24760895-1	2014	We recently reported that herpes simplex virus 1 (HSV-1) protein kinase Us3 phosphorylated viral dUTPase (vdUTPase) at serine 187 (Ser-187) to upregulate its enzymatic activity, which promoted HSV-1 replication in human neuroblastoma SK-N-SH cells but not in human carcinoma HEp-2 cells.	Serine	119-125	Deoxyuridine triphosphatase	Drosophila melanogaster	97-104	
24760895-1	2014	We recently reported that herpes simplex virus 1 (HSV-1) protein kinase Us3 phosphorylated viral dUTPase (vdUTPase) at serine 187 (Ser-187) to upregulate its enzymatic activity, which promoted HSV-1 replication in human neuroblastoma SK-N-SH cells but not in human carcinoma HEp-2 cells.	Serine	131-134	Deoxyuridine triphosphatase	Drosophila melanogaster	97-104	
24760895-4	2014	Furthermore, the replacement of Ser-187 in vdUTPase with aspartic acid, which mimics constitutive phosphorylation, and overexpression of cellular dUTPase restored viral replication to the wild-type level in cellular dUTPase knockdown HEp-2 cells.	Serine	32-35	Deoxyuridine triphosphatase	Drosophila melanogaster	44-51	
24760895-5	2014	These results indicated that sufficient dUTPase activity was required for efficient HSV-1 replication and supported the hypothesis that Us3 phosphorylation of vdUTPase Ser-187 upregulated vdUTPase activity in host cells with low cellular dUTPase activity to produce efficient viral replication.virus.	Serine	168-171	Deoxyuridine triphosphatase	Drosophila melanogaster	40-47	
24760895-5	2014	These results indicated that sufficient dUTPase activity was required for efficient HSV-1 replication and supported the hypothesis that Us3 phosphorylation of vdUTPase Ser-187 upregulated vdUTPase activity in host cells with low cellular dUTPase activity to produce efficient viral replication.virus.	Serine	168-171	Deoxyuridine triphosphatase	Drosophila melanogaster	160-167	
2168898-4	1990	Further characterization of the cellular dUTPase, in uninfected cells, reveals that the protein is post-translationally phosphorylated at serine residues.	Serine	138-144	Deoxyuridine triphosphatase	Drosophila melanogaster	41-48	
18597482-0	2008	A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism.	Serine	39-45	Deoxyuridine triphosphatase	Drosophila melanogaster	73-80	
18597482-4	2008	However, in the complex of the Asp90 --> Asn mutant dUTPase with the true substrate dUTP.Mg, the serine beta-OH points in the opposite direction and may form a hydrogen bond to Asn84 at the bottom of the pyrimidine pocket.	Serine	100-106	Deoxyuridine triphosphatase	Drosophila melanogaster	55-62	
18597482-9	2008	We find that the E. coli dUTPase does not catalyze the hydrolysis of the alpha,beta-imido-dUTP.Mg, suggesting that the analogue provides the hydrogen in the bond to the serine beta-OH.	Serine	169-175	Deoxyuridine triphosphatase	Drosophila melanogaster	25-32	
7950368-4	1994	The purified dUTPase has two additional vector-encoded residues at the amino terminus (gly-ser), but they have no apparent effect on the activity of the enzyme since the recombinant dUTPase has catalytic properties similar to those reported for dUTPase purified from human cells (32.3 U/mg, kcat = 25 s-1, Km = 2.6 microM).	Serine	91-94	Deoxyuridine triphosphatase	Drosophila melanogaster	13-20	
8631817-8	1996	In previous work, this laboratory demonstrated that dUTPase is posttranslationally phosphorylated on serine residue(s) (Lirette, R., and Caradonna, S. (1990) J.	Serine	101-107	Deoxyuridine triphosphatase	Drosophila melanogaster	52-59	
8631817-15	1996	Mutation of Ser-11 by replacement with Ala blocks phosphorylation of dUTPase in vivo.	Serine	12-15	Deoxyuridine triphosphatase	Drosophila melanogaster	69-76