TRIM37 (Tripartite motif containing 37) restricts centriole reduplication during centriole biogenesis. It participates in epigenetic transcriptional repression by facilitating monoubiquitination of ′Lys-119′ of histone H2A (H2AK119Ub). TRIM37 also possesses anti-HIV activity. Mutation in TRIM37 causes an autosomal recessive prenatal-onset growth disorder, mulibrey nanism with dysmorphic features, cardiomyopathy, and hepatomegaly.
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The Journal of general virology, 95(Pt 4), 960-967 (2013-12-10)
Trim 5α was the first member of the tripartite motif (TRIM) family of proteins that was identified to potently restrict human immunodeficiency virus type 1 (HIV-1) replication. The breadth of antiretroviral activity of TRIM family members is an active area
Centrioles are essential for forming cilia, flagella, and centrosomes and are thus critical for a range of fundamental cellular processes. Despite their importance, the mechanisms governing centriole biogenesis remain incompletely understood. We performed a high-content genome-wide small-interfering-RNA-based screen to identify
The TRIM37 (also known as MUL) gene is located in the 17q23 chromosomal region, which is amplified in up to ∼ 40% of breast cancers. TRIM37 contains a RING finger domain, a hallmark of E3 ubiquitin ligases, but its protein
Mulibrey nanism is an autosomal recessive prenatal-onset growth disorder characterized by dysmorphic features, cardiomyopathy, and hepatomegaly. Mutations in TRIM37 encoding a tripartite motif (TRIM, RING-B-box-coiled-coil)-family protein underlie mulibrey nanism. We investigated the ubiquitin ligase activity predicted for the RING domain
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