PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 26-29 OCA2 melanosomal transmembrane protein Homo sapiens 97-106 10704359-9 2000 Interestingly, the ability of the multiple site mutant of P (combo mutant has eight serine residues changed to alanine residues) to support efficient virus RNA synthesis suggests that the P protein has a high flexibility at least in its sequence and perhaps also in structure. Serine 84-90 OCA2 melanosomal transmembrane protein Homo sapiens 188-197 8551618-6 1996 However, sequence requirements for the P protein C-terminal end were not absolute, and mutants with the substitution Ser-237-->Ala or Ser-237-->Thr were as efficient as the wild type in interacting with N. In addition, P and N proteins from strains of different HRSV antigenic groups, with sequence differences in the P protein C-terminal end, were able to coimmunoprecipitate and formed cytoplasmic inclusions. Serine 117-120 OCA2 melanosomal transmembrane protein Homo sapiens 39-48 8551618-6 1996 However, sequence requirements for the P protein C-terminal end were not absolute, and mutants with the substitution Ser-237-->Ala or Ser-237-->Thr were as efficient as the wild type in interacting with N. In addition, P and N proteins from strains of different HRSV antigenic groups, with sequence differences in the P protein C-terminal end, were able to coimmunoprecipitate and formed cytoplasmic inclusions. Serine 137-140 OCA2 melanosomal transmembrane protein Homo sapiens 39-48 8614993-1 1996 Previously we showed that the Sendai virus P protein (568 aa) in virus-infected cells and in virions was primarily and constitutively phosphorylated on serine(s) in a single tryptic phosphopeptide TP1. Serine 152-158 OCA2 melanosomal transmembrane protein Homo sapiens 43-52 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 26-29 OCA2 melanosomal transmembrane protein Homo sapiens 164-173 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 34-37 OCA2 melanosomal transmembrane protein Homo sapiens 97-106 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 34-37 OCA2 melanosomal transmembrane protein Homo sapiens 164-173 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 34-37 OCA2 melanosomal transmembrane protein Homo sapiens 97-106 7645214-6 1995 The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein. Serine 34-37 OCA2 melanosomal transmembrane protein Homo sapiens 164-173 11831729-3 1995 In contrast, cell-free phosphorylation of the P protein with virion-associated protein kinase (VAPK) occurred at both threonine and serine. Serine 132-138 OCA2 melanosomal transmembrane protein Homo sapiens 46-55 11831729-6 1995 Inhibition of cellular phosphatases (PP1 and PP2A) by okadaic acid (OA) in virus-infected cells caused a sixfold increase in the P protein phosphorylation, solely at serine residues. Serine 166-172 OCA2 melanosomal transmembrane protein Homo sapiens 129-138 24501400-0 2014 Roles of serine and threonine residues of mumps virus P protein in viral transcription and replication. Serine 9-15 OCA2 melanosomal transmembrane protein Homo sapiens 54-63 7975241-5 1994 Through deletions and site-directed mutagenesis, the site of CKII phosphorylation was mapped to a single serine residue (Ser237) near the C-terminal end of the P protein. Serine 105-111 OCA2 melanosomal transmembrane protein Homo sapiens 160-169 8126452-1 1994 P protein, the structural phosphoprotein of the Long strain of respiratory syncytial (RS) virus, is phosphorylated at serine residues. Serine 118-124 OCA2 melanosomal transmembrane protein Homo sapiens 0-9 8126452-5 1994 The P protein is modified in vitro by this activity mainly at serine residues located near the C terminus, which are also modified during virus infection. Serine 62-68 OCA2 melanosomal transmembrane protein Homo sapiens 4-13 19531639-4 2009 In particular, PKC phosphorylates PED/PEA-15 at Ser(104) and CAM kinase II or Akt at Ser(116), modifying its stability. Serine 48-51 OCA2 melanosomal transmembrane protein Homo sapiens 34-37 20956287-6 2010 SHEP1 association is required for the BCR or S1P receptor(s) to induce the conversion of CasL into its serine/threonine hyperphosphorylated form, which is important for lymphocyte adhesion and motility. Serine 103-109 OCA2 melanosomal transmembrane protein Homo sapiens 0-5 20072825-3 2010 Among these, six Ser sites and one Thr site were identified in the highly conserved C-terminal region of eight P-proteins of various P-protein subfamilies, including two P0, two P1, three P2 and one P3 protein. Serine 17-20 OCA2 melanosomal transmembrane protein Homo sapiens 111-120 21895963-8 2012 PED/PEA-15 overexpression significantly increased 67LR-mediated HEK-293 cell adhesion and migration to laminin that, in turn, determined PED/PEA-15 phosphorylation both in Ser-104 and Ser-116, thus enabling cell proliferation and resistance to apoptosis. Serine 172-175 OCA2 melanosomal transmembrane protein Homo sapiens 0-3 21895963-8 2012 PED/PEA-15 overexpression significantly increased 67LR-mediated HEK-293 cell adhesion and migration to laminin that, in turn, determined PED/PEA-15 phosphorylation both in Ser-104 and Ser-116, thus enabling cell proliferation and resistance to apoptosis. Serine 172-175 OCA2 melanosomal transmembrane protein Homo sapiens 137-140 21895963-8 2012 PED/PEA-15 overexpression significantly increased 67LR-mediated HEK-293 cell adhesion and migration to laminin that, in turn, determined PED/PEA-15 phosphorylation both in Ser-104 and Ser-116, thus enabling cell proliferation and resistance to apoptosis. Serine 184-187 OCA2 melanosomal transmembrane protein Homo sapiens 0-3 21895963-8 2012 PED/PEA-15 overexpression significantly increased 67LR-mediated HEK-293 cell adhesion and migration to laminin that, in turn, determined PED/PEA-15 phosphorylation both in Ser-104 and Ser-116, thus enabling cell proliferation and resistance to apoptosis. Serine 184-187 OCA2 melanosomal transmembrane protein Homo sapiens 137-140 18614634-8 2008 Furthermore, we found that a single amino acid residue change at position 157 of the P protein from Ser (the residue in the wild-type P protein) to Phe (the residue in Pcpi-) is sufficient for elevated viral gene expression. Serine 100-103 OCA2 melanosomal transmembrane protein Homo sapiens 85-94 18614634-8 2008 Furthermore, we found that a single amino acid residue change at position 157 of the P protein from Ser (the residue in the wild-type P protein) to Phe (the residue in Pcpi-) is sufficient for elevated viral gene expression. Serine 100-103 OCA2 melanosomal transmembrane protein Homo sapiens 134-143 17227770-12 2007 Taken together, our results indicate that TPA increases PED/PEA-15 expression at the post-translational level by inducing phosphorylation at serine 116 and preventing ubiquitinylation and proteosomal degradation. Serine 141-147 OCA2 melanosomal transmembrane protein Homo sapiens 56-59 12808093-1 2003 The antiapoptotic protein PED/PEA-15 features an Akt phosphorylation motif upstream from Ser(116). Serine 89-92 OCA2 melanosomal transmembrane protein Homo sapiens 26-29 12808093-3 2003 Based on Western blotting with specific phospho-Ser(116) PED/PEA-15 antibodies, Akt phosphorylation of PED/PEA-15 occurred mainly at Ser(116). Serine 48-51 OCA2 melanosomal transmembrane protein Homo sapiens 103-106 12808093-3 2003 Based on Western blotting with specific phospho-Ser(116) PED/PEA-15 antibodies, Akt phosphorylation of PED/PEA-15 occurred mainly at Ser(116). Serine 133-136 OCA2 melanosomal transmembrane protein Homo sapiens 103-106 12808093-4 2003 In addition, a mutant of PED/PEA-15 featuring the substitution of Ser(116)-->Gly (PED(S116-->G)) showed 10-fold-decreased phosphorylation by Akt. Serine 66-69 OCA2 melanosomal transmembrane protein Homo sapiens 25-28 12808093-4 2003 In addition, a mutant of PED/PEA-15 featuring the substitution of Ser(116)-->Gly (PED(S116-->G)) showed 10-fold-decreased phosphorylation by Akt. Serine 66-69 OCA2 melanosomal transmembrane protein Homo sapiens 85-88 12808093-5 2003 In intact 293 cells, Akt also induced phosphorylation of PED/PEA-15 at Ser(116). Serine 71-74 OCA2 melanosomal transmembrane protein Homo sapiens 57-60 17227770-2 2007 Exposure of untransfected C5N keratinocytes and transfected HEK293 cells to phorbol esters (12-O-tetradecanoylphorbol-13-acetate (TPA)) increased PED/PEA-15 cellular content and enhanced its phosphorylation at serine 116 in a time-dependent fashion. Serine 210-216 OCA2 melanosomal transmembrane protein Homo sapiens 146-149 17227770-3 2007 Ser-116 --> Gly (PED(S116G)) but not Ser-104 --> Gly (PED(S104G)) substitution almost completely abolished TPA regulation of PED/PEA-15 expression. Serine 0-3 OCA2 melanosomal transmembrane protein Homo sapiens 20-23