| http://purl.uniprot.org/citations/12876068 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12876068 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12876068 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutations that disrupt a PY motif in epithelial Na+ channel (ENaC) subunits increase surface expression of Na+ channels in the collecting duct, resulting in greater Na+ reabsorption. Recently, Nedd4 and Nedd4-2 have been identified as ubiquitin ligases that can interact with ENaC via its PY motifs to regulate channel activity. To further understand the role of human Nedd4-2 (hNedd4-2), we cloned its cDNAs and determined its genomic organization using a bioinformatic approach. The gene is present as a single copy, spans at least 400 kb, and contains >40 exons. Multiple 5'-exons were identified by 5'-rapid amplification of cDNA ends, and tissue-specific expression of these transcripts was noted by RT-PCR and RNase protection assay. Alternate polyadenylation signal sequences led to varying lengths of the 3'-untranslated region. Alternate splicing events within internal exons were also noted. Open reading frame analysis indicates that hNedd4-2 encode multiple protein variants with and without a C2 domain, and with a variable number of WW domains. Coexpression, in Fischer rat thyroid epithelia, of ENaC and Nedd4-2 cDNAs leads to a significant reduction in amiloride-sensitive currents, confirming a role in Na+ transport regulation. In vitro binding studies demonstrated that individual PY motifs of alpha-, beta-, and gamma-ENaC have strong affinity for WW domains 3 and 4 but not 1 and 2. These studies indicate that alternate transcripts of Nedd4-2 may interact with ENaC differently. Understanding the function of variant proteins will increase our knowledge of the role of hNedd4-2 in the regulation of ENaC and define protein domains important for Nedd4-2 function."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajprenal.00203.2003"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Herrero J."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Herrero J."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Campbell J.R."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Campbell J.R."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Snyder P.M."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Snyder P.M."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Thomas C.P."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Thomas C.P."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Itani O.A."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/author | "Itani O.A."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/name | "Am. J. Physiol. Renal Physiol."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/name | "Am J Physiol Renal Physiol"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/pages | "F916-F929"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/pages | "F916-29"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/title | "Alternate promoters and variable splicing lead to hNedd4-2 isoforms with a C2 domain and varying number of WW domains."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/title | "Alternate promoters and variable splicing lead to hNedd4-2 isoforms with a C2 domain and varying number of WW domains."xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/12876068 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12876068 |