| http://purl.uniprot.org/citations/15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15777842 | http://www.w3.org/2000/01/rdf-schema#comment | "Iron regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, is subjected to iron-dependent degradation by the proteasome. Recent experiments proposed a mechanism involving 2-oxoglutarate-dependent oxygenases. Enzymes of this class, such as prolyl-4-hydroxylases, mediate the oxygen and iron-dependent degradation of the hypoxia inducible factor HIF-1alpha, which requires the E3 ubiquitin ligase activity of pVHL. Considering that the pathways for IRP2 and HIF-1alpha degradation share remarkable similarities, we investigated whether pVHL may also be involved in the degradation of IRP2. We show here that IRP2 can interact with pVHL in co-transfection/co-immunoprecipitation assays. Furthermore, pVHL is able to promote the ubiquitination and the decay of transfected IRP2. However, the iron-dependent degradation of endogenous IRP2 is not impaired in VHL-deficient cell lines, suggesting that pVHL is not a necessary component of this pathway."xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamcr.2004.08.011"xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/author | "Wang J."xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/author | "Pantopoulos K."xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/pages | "79-85"xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/title | "The pathway for IRP2 degradation involving 2-oxoglutarate-dependent oxygenase(s) does not require the E3 ubiquitin ligase activity of pVHL."xsd:string |
| http://purl.uniprot.org/citations/15777842 | http://purl.uniprot.org/core/volume | "1743"xsd:string |
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| http://purl.uniprot.org/uniprot/#_A4ZYX2-mappedCitation-15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15777842 |
| http://purl.uniprot.org/uniprot/#_A0A0S2Z4K1-mappedCitation-15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15777842 |
| http://purl.uniprot.org/uniprot/#_B4E1V7-mappedCitation-15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15777842 |
| http://purl.uniprot.org/uniprot/#_A0PJF6-mappedCitation-15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15777842 |
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| http://purl.uniprot.org/uniprot/#_P48200-mappedCitation-15777842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15777842 |
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| http://purl.uniprot.org/uniprot/A0A0S2Z4K1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15777842 |