Редактирование: EPS15 (раздел)

==Publications==

{{medline-entry
|title=[[WWP1]]: a versatile ubiquitin E3 ligase in signaling and diseases.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/22051607
|abstract=WW domain-containing E3 ubiquitin protein ligase 1 ([[WWP1]]) is a multifunction protein containing an N-terminal [[C2]] domain, four tandem WW domains for substrate binding, and a C-terminal catalytic HECT domain for ubiquitin transferring. [[WWP1]] has been suggested to function as the E3 ligase for several PY motif-containing proteins, such as Smad2, [[KLF5]], p63, ErbB4/HER4, [[RUNX2]], JunB, [[RNF11]], SPG20, and Gag, as well as several non-PY motif containing proteins, such as TβR1, Smad4, [[KLF2]], and [[EPS15]]. [[WWP1]] regulates a variety of cellular biological processes including protein trafficking and degradation, signaling, transcription, and viral budding. [[WWP1]] has been implicated in several diseases, such as cancers, infectious diseases, neurological diseases, and aging. In this review article, we extensively summarize the current knowledge of [[WWP1]] with special emphasis on the roles and action of mechanism of [[WWP1]] in signaling and human diseases.
|mesh-terms=* Aging
* ErbB Receptors
* Gene Expression
* Humans
* Infections
* Kruppel-Like Transcription Factors
* Neoplasms
* Nervous System Diseases
* Protein Structure, Tertiary
* Signal Transduction
* Transforming Growth Factor beta
* Tumor Suppressor Protein p53
* Ubiquitin-Protein Ligases
* Ubiquitination

|full-text-url=https://sci-hub.do/10.1007/s00018-011-0871-7
}}