RGD Reference Report - HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized. - Rat Genome Database

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HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized.

Authors: Lee, HJ  Kim, MS  Kim, YK  Oh, YK  Baek, KH 
Citation: Lee HJ, etal., FEBS Lett. 2005 Aug 29;579(21):4867-72.
RGD ID: 2316134
Pubmed: PMID:16111684   (View Abstract at PubMed)
DOI: DOI:10.1016/j.febslet.2005.07.048   (Journal Full-text)

The tumor suppressor protein p53 is ubiquitinated and neddylated by MDM2 and then degraded by 26S proteasome. However, p53 is stabilized by the HAUSP (Herpes-virus-associated ubiquitin-specific protease) deubiquitinating enzyme. In this study, we discovered that rat HAUSP (rHAUSP) is polyubiquitinated, polyneddylated, and dimerized using co-immunoprecipitation assays. This suggests that rHAUSP may function as a dimer or multimer and is also degraded through the proteasome-mediated degradation. Transfection of rHAUSP into RGC-Lac-Z cell line with the integrated p53 response element revealed that rHAUSP contributed to p53 stabilization, and a rHAUSP (C224S) mutant contributed to p53 destabilization in a dose-dependent manner.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
regulation of protein stability  IDA 2316134 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding  IPIUsp7 (Rattus norvegicus)2316134homodimerizationRGD 

Objects Annotated

Genes (Rattus norvegicus)
Usp7  (ubiquitin specific peptidase 7)


Additional Information