TRAP100

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Name
Thyroid hormone receptor-associated protein (100 kDa)
Symbol
TRAP100

Overview

TRAP100 was originally isolated as part of a biochemical screen for in vitro thyroid hormone receptor-associated proteins (TRAPs). It was subsequently identified as a nuclear receptor coregulator based on its role as a coactivator for the androgen receptor (AR).

Expression

TRAP100 is expressed at low to moderate levels in tissues in major physiological systems (central nervous system (CNS), endocrine, metabolic, gastrointestinal, immune, reproductive, structural) with particularly high levels in the testis, thymus, adrenal gland and brain.

Diseases

TRAP100 has been shown to be overexpressed in breast cancer.

Phenotypes

Targeted disruption (knockout) of the murine TRAP100 component of this complex has revealed that it is not essential for cell viability per se. However, null mutant mice die at an early developmental stage with severe malformations

View TRAP100 Diseases & Phenotypes section


 Coregulator Pages User Guide (updated Oct 2008)

At a Glance
Nomenclature
Activator-recruited cofactor complex 100 kDa component (ARC100); Negative regulator of activated transcription complex, 95 kDa component (NAT-p95); Thyroid hormone receptor-associated protein (100 kDa) (TRAP100); Vitamin D receptor-interacting protein (100kD) (DRIP100); Thyroid hormone receptor associated protein 4 (THRAP4)

Primary References
Wang Q, Sharma D, Ren Y and Fondell JD (2002) A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression. J Biol Chem 277, 42852-8. View Abstract | View PubMed
Rachez C, Suldan Z, Ward J, Chang CP, Burakov D, Erdjument-Bromage H, Tempst P and Freedman LP (1998) A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system. Genes Dev 12, 1787-800. View Abstract | View PubMed
Fondell JD, Ge H and Roeder RG (1996) Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci U S A 93, 8329-33. View Abstract | View PubMed

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