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Validated All-in-One™ qPCR Primer for WWP1(NM_007013.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. The encoded protein belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Alternative splicing of this gene generates at least 6 transcript variants; however, the full length nature of these transcripts has not been defined. [provided by RefSeq].
Gene References into function
- First demonstration of ubiquitin-protein ligase WWP1 from human lung cDNA library recruited by penton base proteins of human adenovirus serotypes Ad2 and Ad3 in vitro and in vivo.
- the interaction of nonenveloped viruses with ubiquitin-protein ligases of host cells.
- Data show that the crystal structure of the HECT domain of the human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP.
- WWP1 negatively regulates TGF-beta signaling in cooperation with Smad7.
- KLF5 is a target of the E3 ubiquitin ligase WWP1 for proteolysis in epithelial cells
- Full-length expressed WWP1 could interact in vitro with the cytoplasmic domain of human Notch1, which also regulate the nuclear localization of WWP1.
- these findings identify the first instance of a ubiquitin ligase that causes stabilization of p53 while inactivating its transcriptional activities.
- WWP1 overexpression is a common mechanism involved in the inactivation of TGFbeta function in human cancer.
- genomic aberrations of WWP1 may contribute to the pathogenesis of breast cancer
- the interaction between Gag and WWP1 is required for functions other than Gag ubiquitination
- WWP1 may promote cell proliferation and survival partially through suppressing RNF11-mediated ErbB2 and EGFR downregulation in human cancer cells.
- WWP1 may have a context-dependent role in regulating cell survival through targeting different p63 proteins for degradation.
- analysis of the interaction between ubiquitin ligase WWP1 and Nogo-A
- WWP1 ubiquitinated and caused the degradation of HER4 but not of EGFR, HER2, or HER3.
