tudor domain-containing protein 3 (TDRD3)
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Function
- scaffolding protein
- specifically recognizes & binds dimethylarginine-containing proteins
- in nucleus, acts as a coactivator: recognizes & binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a & H4R3me2a) & recruits proteins at these arginine-methylated loci
- in cytoplasm, may play a role in the assembly &/or disassembly of mRNA stress granules & in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins
- component of mRNA stress granules
- interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 & DDX3X or DDX3Y & with the small nuclear ribonucleoprotein- associated proteins SNRPB & SNRPN
- interacts with Lys-48-linked tetra-ubiquitin
- does not interact with monoubiquitin or Lys-63-linked ubiquitin chains
Structure
- the Tudor domain specifically recognizes & binds asymmetric dimethylation of histone H3 Arg-17 (H3R17me2a) & histones H4 Arg-3, 2 tags for epigenetic transcriptional activation
- contains 1 Tudor domain
- contains 1 UBA domain
Compartment
- cytoplasm, nucleus
- predominantly cytoplasmic
- associated with actively translating polyribosomes & with mRNA stress granules
Alternative splicing
named isoforms=3
Expression
- detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney & pancreas