| http://purl.uniprot.org/citations/10212274 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10212274 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10212274 | http://www.w3.org/2000/01/rdf-schema#comment | "Keratin polypeptide 19 (K19) is a type I intermediate filament protein that is expressed in stratified and simple-type epithelia. Little is known regarding K19 regulation or function, and the only other type I keratin that has been studied in terms of regulation is keratin 18 (K18). We characterized K19 phosphorylation as a handle to study its function. In vivo, serine is the major phosphorylated residue, and phosphopeptide mapping of 32PO4-labeled K19 generates one major phosphopeptide. Edman degradation suggested that the radiolabeled phosphopeptide represents K19 Ser-10 and/or Ser-35 phosphorylation. Mutation of Ser-10 or Ser-35 followed by transfection confirmed that Ser-35 is the major K19 phosphorylation site. Transfection of Ser-35 --> Ala K19 showed a filament assembly defect as compared with normal or with Ser-10 --> Ala K19. Comparison of K18 and K19 phosphorylation features in interphase cells showed that both are phosphorylated primarily at a single site, preferentially in the soluble versus the insoluble keratin fractions. K19 has higher basal phosphorylation, whereas K18 phosphorylation is far more sensitive to phosphatase type I and IIA inhibition. Our results demonstrate that Ser-35 is the major K19 interphase phosphorylation site and that it plays a role in keratin filament assembly. K19 and K18 phosphorylations share some features but also have distinct properties that suggest different regulation of type I keratins within the same cells."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.18.12861"xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.18.12861"xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Feng L."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Feng L."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Zhou X."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Zhou X."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Hu L."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Hu L."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Liao J."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Liao J."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Omary M.B."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/author | "Omary M.B."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/pages | "12861-12866"xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/pages | "12861-12866"xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/title | "Characterization of the major physiologic phosphorylation site of human keratin 19 and its role in filament organization."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/title | "Characterization of the major physiologic phosphorylation site of human keratin 19 and its role in filament organization."xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10212274 | http://purl.uniprot.org/core/volume | "274"xsd:string |