| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/2000/01/rdf-schema#comment | "Hydroxyproline (Hyp) O-arabinosylation is a post-translational modification that is prominent in extracellular glycoproteins in plants. Hyp O-arabinosylation is generally found in these glycoproteins in the form of linear oligoarabinoside chains and has a key role in their function by contributing to conformational stability. However, Hyp O-arabinosyltransferase (HPAT), a key enzyme that catalyzes the transfer of the L-arabinose to the hydroxyl group of Hyp residues, has remained undiscovered. Here, we purified and identified Arabidopsis HPAT as a Golgi-localized transmembrane protein that is structurally similar to the glycosyltransferase GT8 family. Loss-of-function mutations in HPAT-encoding genes cause pleiotropic phenotypes that include enhanced hypocotyl elongation, defects in cell wall thickening, early flowering, early senescence and impaired pollen tube growth. Our results indicate essential roles of Hyp O-arabinosylation in both vegetative and reproductive growth in plants."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.org/dc/terms/identifier | "doi:10.1038/nchembio.1351"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.org/dc/terms/identifier | "doi:10.1038/nchembio.1351"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Matsubayashi Y."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Matsubayashi Y."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Ogawa-Ohnishi M."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Ogawa-Ohnishi M."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Matsushita W."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/author | "Matsushita W."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/name | "Nat. Chem. Biol."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/name | "Nat. Chem. Biol."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/pages | "726-730"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/pages | "726-730"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/title | "Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/title | "Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/volume | "9"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://purl.uniprot.org/core/volume | "9"xsd:string |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24036508 |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24036508 |
| http://purl.uniprot.org/citations/24036508 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24036508 |