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Article

Regulation of co-repressive activity of and HDAC recruitment to RIP140 by site-specific phosphorylation.

Molecular & cellular proteomics : MCP - 1 Nov 2005

Gupta Pawan, Huq M D Mostaqul, Khan Shaukat Ali, Tsai Nien-Pei, Wei Li-Na

Abstract excerpt

Receptor interacting protein 140 (RIP140) is a versatile transcriptional co-repressor that contains several autonomous repressive domains (RDs). The N-terminal RD acts by recruiting histone deacetylases (HDACs). In a comprehensive proteomic analysis of RIP140 by MS, 11 phosphorylation sites of RIP140 are identified; among them five sites are located in the N-terminal RD including Ser104, Thr202, Thr207, Ser358,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16093479
DOI: 10.1074/mcp.M500236-MCP200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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