| http://purl.uniprot.org/citations/9244383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9244383 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein kinase C (PKC) is involved in cell-matrix and cell-cell adhesion, and the cytoplasmic domain of syndecan-2 contains two serines (residues 197 and 198) which lie in a consensus sequence for phosphorylation by PKC. Other serine and threonine residues are present but not in a consensus sequence. We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC, using purified GST-syndecan-2 fusion proteins and synthetic peptides corresponding to regions of the cytoplasmic domain. A synthetic peptide encompassing the entire cytoplasmic domain of syndecan-2 was phosphorylated by PKC with high affinity. Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. The efficiency of phosphorylation was concentration-dependent. At low concentrations, the cytoplasmic domain peptides were monomeric, with 2 mol/mol serine phosphorylation. At higher concentrations, however, the peptides formed dimers, with only 0.5 mol/mol phosphorylation. Concentration-dependent dimerization was not altered by phosphorylation. Phosphorylation is, therefore, dependent on the conformation of syndecan-2 cytoplasmic domain, but does not affect its oligomeric status."xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.1997.0180"xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/author | "Woods A."xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/author | "Couchman J.R."xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/author | "Oh E.S."xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/pages | "67-74"xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/title | "Serine phosphorylation of syndecan-2 proteoglycan cytoplasmic domain."xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://purl.uniprot.org/core/volume | "344"xsd:string |
| http://purl.uniprot.org/citations/9244383 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9244383 |
| http://purl.uniprot.org/citations/9244383 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9244383 |
| http://purl.uniprot.org/uniprot/#_P34900-mappedCitation-9244383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9244383 |
| http://purl.uniprot.org/uniprot/P34900 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/9244383 |