Disease Score gda Association Type Type Original DB Sentence supporting the association PMID PMID Year
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE We now report that the chromatin-targeting E3 ubiquitin ligase RNF20/RNF40, driving histone H2B monoubiquitylation (H2Bub1), modulates inflammation and inflammation-associated cancer in mice and humans. 26854224 2016
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 AlteredExpression group BEFREE Moreover, many mutant p53 proteins, termed 'gain-of-function' (GOF), acquire new activities that help drive cancer aggression. p53 is regulated mainly through protein turnover and operates within a negative-feedback loop with its transcriptional target, MDM2 (murine double minute 2), an E3 ubiquitin ligase which mediates the ubiquitylation and proteasomal degradation of p53. 26205489 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 GeneticVariation group BEFREE The SPOP gene, which encodes an E3 ubiquitin ligase adaptor, is frequently mutated in a number of cancer types. 26527005 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE The hypoxia-inducible factor (Hif)-1α (Hif-1α) and Hif-2α (Epas1) have a critical role in both normal development and cancer. von Hippel Lindau (Vhl) protein, encoded by a tumor suppressor gene, is an E3 ubiquitin ligase that targets Hif-1α and Epas1 to the proteasome for degradation. 26348575 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Elucidating its mechanism of action has become crucial for cancer therapy; however, it is also complicated by the fact that FBXW7 can influence many pathways due to its role as an E3-ubiquitin ligase in proteasome degradation. 25860929 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Together, our findings uncover novel cancer-associated functions of PARK2 and provide a potential therapeutic approach to treat glioma. 25877876 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE We further highlight future efforts for the study of PARK2 in cancer. 24297497 2014
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Parkin, an E3 ubiquitin ligase well known for its role in the pathogenesis of juvenile Parkinson disease, has been considered as a candidate tumor suppressor in certain types of cancer. 23470638 2013
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 GeneticVariation group BEFREE We have asked whether PARKIN mutations are associated with history of cancer in humans. 22927236 2012
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Furthermore, three independent laboratories including our own have demonstrated that the stability of DEPTOR is controlled by the SCF(β-TrCP) E3 ubiquitin ligase and deregulated DEPTOR destruction might contribute to hyperactivation of mTOR in pathologic conditions including cancer. 22745583 2012
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 AlteredExpression group BEFREE Here, we summarize our current knowledge about the various roles of the CRL4Cdt2 E3 ubiquitin ligase, and how its activity contributes both to the preservation of genome integrity and to normal cell cycle progression, and how its deregulation may contribute to human cancer. 21212733 2011
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 AlteredExpression group BEFREE Six of the eight IPMNs and three of the eight MCNs harbored mutations of RNF43, a gene coding for a protein with intrinsic E3 ubiquitin ligase activity that has not previously been found to be genetically altered in any human cancer. 22158988 2011
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Taking these data together, our study identifies E3 ubiquitin ligase Itch as a unique negative regulator of LATS1 and presents a possibility of targeting LATS1/Itch interaction as a therapeutic strategy in cancer. 21383157 2011
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE As PARK2 lies within FRA6E, a large common fragile site, it has been argued that the observed DCN losses in PARK2 in cancer may represent merely the result of enforced replication of locally vulnerable DNA. 20696900 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE The findings showed that SAG E3 ubiquitin ligase plays an essential role in cancer cell proliferation and tumor growth and may serve as a promising anticancer and radiosensitizing target. 20103673 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Pathways that have emerged as having critical roles in both cancer and neurodegenerative disease include those involving genes such as PARK2, ATM, PTEN, PTPRD, and mTOR. 20418918 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Non-small cell lung cancer (NSCLC) is a heterogeneous group of disorders with a number of genetic and proteomic alterations. c-CBL is an E3 ubiquitin ligase and adaptor molecule important in normal homeostasis and cancer. 20126411 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 GeneticVariation group BEFREE PARK2 mutations in cancer decrease PARK2's E3 ligase activity, compromising its ability to ubiquitinate cyclin E and resulting in mitotic instability. 19946270 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE To elucidate the molecular mechanisms underlying this fragility, we performed a custom-designed high-density comparative genomic hybridization analysis to determine the junction sequences of approximately 500 breakpoints in germ cell lines and cancer cell lines involving PARK2 or DMD. 20598272 2010
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Parkin is an E3 ubiquitin ligase encoded by the Parkin gene (also called PARK2, located at 6q25.2-q27) and is involved in the pathogenesis of Parkinson's disease and the development of cancer. 19214989 2009
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 GeneticVariation group BEFREE Mutations in parkin gene, for example, have been reported in several types of cancer. 17699801 2007
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 GeneticVariation group BEFREE Because Parkin/FRA6E has genomic similarities to FHIT/FRA3B and WWOX/FRA16D, two other large tumor-suppressor genes that are within CFS regions, we were interested in characterizing Parkin gene alterations and their possible association with cancer. 15101042 2004
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 Biomarker group BEFREE Recently, work on the mechanism of action of the von Hippel-Lindau tumour suppressor protein (pVHL) and studies on hypoxic gene regulation have converged, providing insights into both cellular oxygen sensing and cancer pathogenesis. pVHL is the recognition component of the E3-ubiquitin ligase complex involved in the degradation of hypoxia-inducible factor-1 (HIF) alpha-subunits, a process regulated by oxygen availability and blocked by disease causing pVHL mutations. 12507560 2003
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm
0.100 AlteredExpression group BEFREE These data suggest that the LOH observed at chromosome 6q25-q26 may contribute to the initiation andor progression of cancer by inactivating or reducing the expression of the Parkin gene. 12719539 2003