| Tbio | YTH domain-containing family protein 2 |
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (PubMed:24284625, PubMed:26046440, PubMed:26318451). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:22575960, PubMed:24284625, PubMed:25412658, PubMed:25412661). Acts as a regulator of mRNA stability: binding to m6A-containing mRNAs results in the localization to mRNA decay sites, such as processing bodies (P-bodies), leading to mRNA degradation (PubMed:24284625, PubMed:26046440). Also acts as a promoter of cap-independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation (PubMed:26458103).
This gene encodes a member of the YTH (YT521-B homology) superfamily containing YTH domain. The YTH domain is typical for the eukaryotes and is particularly abundant in plants. The YTH domain is usually located in the middle of the protein sequence and may function in binding to RNA. In addition to a YTH domain, this protein has a proline rich region which may be involved in signal transduction. An Alu-rich domain has been identified in one of the introns of this gene, which is thought to be associated with human longevity. In addition, reciprocal translocations between this gene and the Runx1 (AML1) gene on chromosome 21 has been observed in patients with acute myeloid leukemia. This gene was initially mapped to chromosome 14, which was later turned out to be a pseudogene. Alternatively spliced transcript variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Oct 2012]
This gene encodes a member of the YTH (YT521-B homology) superfamily containing YTH domain. The YTH domain is typical for the eukaryotes and is particularly abundant in plants. The YTH domain is usually located in the middle of the protein sequence and may function in binding to RNA. In addition to a YTH domain, this protein has a proline rich region which may be involved in signal transduction. An Alu-rich domain has been identified in one of the introns of this gene, which is thought to be associated with human longevity. In addition, reciprocal translocations between this gene and the Runx1 (AML1) gene on chromosome 21 has been observed in patients with acute myeloid leukemia. This gene was initially mapped to chromosome 14, which was later turned out to be a pseudogene. Alternatively spliced transcript variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Oct 2012]
Comments
| Species | Source |
|---|---|
| Chimp | OMA EggNOG |
| Macaque | OMA EggNOG Inparanoid |
| Mouse | OMA EggNOG Inparanoid |
| Rat | OMA Inparanoid |
| Dog | OMA EggNOG Inparanoid |
| Cow | OMA EggNOG Inparanoid |
| Opossum | OMA EggNOG Inparanoid |
| Platypus | OMA EggNOG |
| Anole lizard | OMA EggNOG Inparanoid |
| PMID | Text |
|---|---|
| 26318451 | binding affinities of the YTH domains of three human proteins and yeast YTH domain protein Pho92 |
| 25412661 | The basic residues K416 and R527 on the surface of the YTH domain of YTHDF2 are involved in binding to the RNA backbone, and residues W432 and W486 within the hydrophobic pocket contribute to the specific recognition of N6-methyladenosine. |
| 25412658 | The study presents the structure of YTH-YTHDF2 in complex with an N6-methyladenosine mononucleotide. |
| 24284625 | m(6)A is selectively recognized by the human YTH domain family 2 (YTHDF2) 'reader' protein to regulate mRNA degradation |
| 16799135 | Observational study of gene-disease association. (HuGE Navigator) |
| 16799135 | YTHDF2 messenger RNA resulted to be mainly expressed in testis and placenta. The data suggest a possible role of this locus in human longevity. |
| 10508479 | PMID:10508479 reported that AF155095 (clone REN-2) may be involved in signal transduction and the gene is on chromosome 14. It turns out that it is the pseudogene, not the real gene, is located on chromosome 14. |
MSASSLLEQRPKGQGNKVQNGSVHQKDGLNDDDFEPYLSPQARPNNAYTAMSDSYLPSYYSPSIGFSYSL 1 - 70 GEAAWSTGGDTAMPYLTSYGQLSNGEPHFLPDAMFGQPGALGSTPFLGQHGFNFFPSGIDFSAWGNNSSQ 71 - 140 GQSTQSSGYSSNYAYAPSSLGGAMIDGQSAFANETLNKAPGMNTIDQGMAALKLGSTEVASNVPKVVGSA 141 - 210 VGSGSITSNIVASNSLPPATIAPPKPASWADIASKPAKQQPKLKTKNGIAGSSLPPPPIKHNMDIGTWDN 211 - 280 KGPVAKAPSQALVQNIGQPTQGSPQPVGQQANNSPPVAQASVGQQTQPLPPPPPQPAQLSVQQQAAQPTR 281 - 350 WVAPRNRGSGFGHNGVDGNGVGQSQAGSGSTPSEPHPVLEKLRSINNYNPKDFDWNLKHGRVFIIKSYSE 351 - 420 DDIHRSIKYNIWCSTEHGNKRLDAAYRSMNGKGPVYLLFSVNGSGHFCGVAEMKSAVDYNTCAGVWSQDK 421 - 490 WKGRFDVRWIFVKDVPNSQLRHIRLENNENKPVTNSRDTQEVPLEKAKQVLKIIASYKHTTSIFDDFSHY 491 - 560 EKRQEEEESVKKERQGRGK 561 - 579 //
| PMID | Year | Title |
|---|---|---|
| 26458103 | 2015 | Dynamic m(6)A mRNA methylation directs translational control of heat shock response. |
| 26318451 | 2015 | Structural Basis for the Discriminative Recognition of N6-Methyladenosine RNA by the Human YT521-B Homology Domain Family of Proteins. |
| 26046440 | 2015 | N(6)-methyladenosine Modulates Messenger RNA Translation Efficiency. |
| 25412661 | 2014 | Crystal structure of the YTH domain of YTHDF2 reveals mechanism for recognition of N6-methyladenosine. |
| 25412658 | 2014 | Structure of the YTH domain of human YTHDF2 in complex with an m(6)A mononucleotide reveals an aromatic cage for m(6)A recognition. |
| 24965446 | 2014 | Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex. |
| 24284625 | 2014 | N6-methyladenosine-dependent regulation of messenger RNA stability. |
| 24206186 | 2014 | A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. |
| 23186163 | 2013 | Toward a comprehensive characterization of a human cancer cell phosphoproteome. |
| 22814378 | 2012 | N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. |
| More... |
