InterPro domain: IPR007275

The YTH (YT521-B homology) domain has been suggested to be an evolutionarily conserved m6A-dependent RNA binding domain [ 1 ]. Proteins containing this domain includes mammalian YTHD and YTDC proteins, Arabidopsis CPSF30 (At1g30460), budding yeast Pho92 and fission yeast Mmi1.

In Saccharomyces cerevisiae, Pho92 is a posttranscriptional regulator that regulates Pho4 mRNA stability by binding to the 3'-UTR in a phosphate-dependent manner. Its YTH domain exhibits RNA-binding activity [ 2 ]. In Schizosaccharomyces pombe, Mmi1 has been identified as eliminating meiosis-specific mRNAs [ 3 ].

Rat YTHDC1 (also known as YT521-B) is an alternative splicing regulator that recognizes and binds N6-methyladenosine (m6A)-containing RNAs. The YTH domain of YT521-B is a RNA-binding domain with a very degenerate sequence-specificity [ 4 ].

1. Structural Basis for the Discriminative Recognition of N6-Methyladenosine RNA by the Human YT521-B Homology Domain Family of Proteins. J. Biol. Chem. 290, 24902-13
2. A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. Biochem. J. 457, 391-400
3. Selective elimination of messenger RNA prevents an incidence of untimely meiosis. Nature 442, 45-50
4. Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA. Nucleic Acids Res. 42, 13911-9