RNF4-knockdown and RNF4-TULIP identified proteins
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Permanent Cell Line Cell
SUBMITTER: 
Román González-Prieto
LAB HEAD: Alfred CO Vertegaal
PROVIDER: PXD005425 | Pride | 2017-11-23
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Samplenumbering.xlsx | Xlsx | |||
| peptides.txt | Txt | |||
| proteinGroups.txt | Txt | |||
| q100532b.raw | Raw | |||
| q100532c.raw | Raw |
Items per page: 5 1 - 5 of 75 |
Publications
The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery.
Kumar Ramesh R González-Prieto Román R Xiao Zhenyu Z Verlaan-de Vries Matty M Vertegaal Alfred C O ACO
Nature communications 20171127 1
SUMO-targeted ubiquitin ligases (STUbLs) mediate the ubiquitylation of SUMOylated proteins to modulate their functions. In search of direct targets for the STUbL RNF4, we have developed TULIP (targets for ubiquitin ligases identified by proteomics) to covalently trap targets for ubiquitin E3 ligases. TULIP methodology could be widely employed to delineate E3 substrate wiring. Here we report that the single SUMO E2 Ubc9 and the SUMO E3 ligases PIAS1, PIAS2, PIAS3, ZNF451, and NSMCE2 are direct RN ...[more]
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