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ProteomicsStructural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
Deregulation of the ubiquitin ligase E6AP is causally linked to the development of human disease, including cervical cancer. In complex with the E6 oncoprotein of human papillomaviruses, E6AP targets the tumor suppressor p53 for degradation, thereby contributing to carcinogenesis. Moreover, E6 acts ...
ORGANISM(S): Human papillomavirus type 16 Homo sapiens (Human) 
2018-10-23 | PXD010002 | Pride
Xl-ms E6 oncoprotein Ubiquitin E6ap/ube3a P53 Papillomavirus 
ProteomicsMembers of the RhoA subfamily of Rho GTPases interfere with HPV E6-mediated stimulation of the ubiquitin ligase E6AP
The E3 ubiquitin ligase E6AP, encoded by the UBE3A gene, plays a prominent role in cancers induced by human papillomaviruses (HPVs). In complex with the HPV E6 oncoprotein, it targets for instance the tumor suppressor p53 for degradation, thereby contributing to HPV-induced cellular transformation. ...
ORGANISM(S): Homo sapiens (Human) 
2026-09-14 | PXD069396 | Pride
E6ap Rhoa Hpv E6 Ube3a Ubiquitination Xl-ms 
ProteomicsMembers of the RhoA subfamily of Rho GTPases interfere with HPV E6-mediated stimulation of the ubiquitin ligase E6AP
The E3 ubiquitin ligase E6AP, encoded by the UBE3A gene, plays a prominent role in cancers induced by human papillomaviruses (HPVs). In complex with the HPV E6 oncoprotein, it targets for instance the tumor suppressor p53 for degradation, thereby contributing to HPV-induced cellular transformation. ...
ORGANISM(S): Homo sapiens (Human) 
2026-09-14 | PXD069463 | Pride
E6ap Rhoa Hpv E6 Ube3a Ubiquitination Mass spectrometry In-gel 
ProteomicsA ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6
The E6 protein of both mucosal high risk human papillomaviruses (HPVs) such as HPV-16, which have been causally associated with malignant tumors, and low risk HPVs such as HPV-11, which cause the development of benign tumors, interacts with the cellular E3 ubiquitin ligase E6AP. This indicates that ...
ORGANISM(S): Homo sapiens (Human) 
2020-08-31 | PXD020660 | Pride
Tumor virus Tmt E6ap/ube3a Human papillomavirus E3 ubiquitin ligase E6 oncoprotein Oncogene Protein degradation Ubiquitin 
ProteomicsMembers of the RhoA subfamily of Rho GTPases interfere with HPV E6-mediated stimulation of the ubiquitin ligase E6AP
The E3 ubiquitin ligase E6AP, encoded by the UBE3A gene, plays a prominent role in cancers induced by human papillomaviruses (HPVs). In complex with the HPV E6 oncoprotein, it targets for instance the tumor suppressor p53 for degradation, thereby contributing to HPV-induced cellular transformation. ...
ORGANISM(S): Homo sapiens (Human) 
2026-09-14 | PXD069419 | Pride
E6ap Rhoa Hpv E6 Ube3a Lip-ms Ubiquitination 
ProteomicsA dedicated ubiquitin-K48/63R variant-based affinity approach specifically identifies both high-risk and low-risk substrates of the HPV E6-E6AP ubiquitin ligase complex
To identify potential substrate proteins of both low risk and high risk E6 proteins, we established an affinity-based enrichment approach using a dedicated biotin-tagged ubiquitin variant that in the absence of the E6 proteins, cannot or only poorly be used by E6AP for ubiquitination. Enriched prote...
ORGANISM(S): Homo sapiens (Human) 
2020-08-31 | PXD017335 | Pride
E6 Ube3a E6-e6ap ubiquitin ligase Hpv-16 Human papillomavirus (hpv) Hpv-11 
UnknownMultiple regions of E6AP (UBE3A) contribute to interaction with papillomavirus E6 proteins and the activation of ubiquitin ligase activity.
Not available
S-EPMC6999913 | biostudies-literature
UnknownA ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6.
Not available
S-EPMC7606683 | biostudies-literature
UnknownRole of ubiquitin and the HPV E6 oncoprotein in E6AP-mediated ubiquitination.
Not available
S-EPMC4538620 | biostudies-literature
UnknownRegulation of O-Linked N-Acetyl Glucosamine Transferase (OGT) through E6 Stimulation of the Ubiquitin Ligase Activity of E6AP.
Not available
S-EPMC8508608 | biostudies-literature
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