FAM98A

2594072722ENSG00000119812ENSMUSG00000002017Q8NCA5Q3TJZ6NM_015475NM_001304538NM_133747NM_001357860NP_001291467NP_056290NP_001291467.1NP_056290.3NP_598508NP_001344789Family with sequence similarity 98, member A, or FAM98A, is a gene that in the human genome encodes the FAM98A protein. FAM98A has two paralogs in humans, FAM98B and FAM98C. All three are characterized by DUF2465, a conserved domain shown to bind to RNA. FAM98A is also characterized by a glycine-rich C-terminal domain. FAM98A also has homologs in vertebrates and invertebrates and has distant homologs in choanoflagellates and green algae.Number(from Time Tree)(from NCBI)Length (AA)NM_015475.3NP_598508.2XP_006192455.1XP_005963883.1XP_006882420.1XP_005416400.1XP_005526966.1XP_006273242.1XP_006131385.1XP_005296336.1XP_002934502.2BT082651.1AHH38396.1EFN74857.1XM_001846602.1JAC03102.1BT078155.1EKC33026.1GAA34581.2CDJ19758.1 Family with sequence similarity 98, member A, or FAM98A, is a gene that in the human genome encodes the FAM98A protein. FAM98A has two paralogs in humans, FAM98B and FAM98C. All three are characterized by DUF2465, a conserved domain shown to bind to RNA. FAM98A is also characterized by a glycine-rich C-terminal domain. FAM98A also has homologs in vertebrates and invertebrates and has distant homologs in choanoflagellates and green algae. The FAM98A gene is located on 2p22.3 in humans on the '-' (minus) strand. Including the 5' and 3' UTR, the gene spans 15,634 bases and contains 8 exons. The mRNA is 2745bp, comprising the 8 exons. The coding sequence starts at base 75 and continues until base 1631. The polyA tail signal sequence is a six-nucleotide sequence 20 bases from the 3' end of the transcript at base 2725-2730, and the polyA site is at base 2745. FAM98A is 518 amino acids in length with a molecular weight of 55.3 kDa, without modifications. Residues 10-329 comprise the DUF2465, and the remainder of the protein is a diglycine-rich C terminus. Glycine makes up approximately 20% of the protein, with the majority of these in the last 200 residues. FAM98A has six strongly predicted phosphorylation sites in DUF2465. These sites are predicted to phosphorylate S169, T178, S236, T243, S276, and S285 by protein kinase C. GPS also predicts phosphorylation by protein kinase C at S285 and T178.FAM98A is likely sumoylated at K183 and K195. Sumoylation may allow the cell to re-localize FAM98A between the nucleus and the cytoplasm. The glycine-rich C terminus has repeat GRG sequences, which has been shown to be susceptible to methylation of the arginine, either symmetrically or asymmetrically. Another paper explains the effects of arginine methylation on biochemical functions such as transcription activation and repression, mRNA splicing, nuclear-cytosolic shuttling, and DNA repair. The N terminus is predicted to have multiple alpha helices, though the C terminus likely is only coiled. The alpha helices do not form any channel, and FAM98A is not a transmembrane protein. The structure of FAM98A was predicted with the program Phyre2. The N-terminal region contains several alpha helices, and a C-terminal coiled region corresponding to the glycine-rich C terminus. These two regions of the protein are connected by an alpha helix approximately 50 residues long from the residues 200-256. Phyre2 found the most similar protein to be the human protein NDC80 kinetochore complex component, a nuclear protein that binds to microtubules. FAM98A has a domain of unknown function 2465 (DUF2465) from the amino acids 10-329. Within the DUF2465, there is a heptide (VPDRGGR) near the C-terminal end that is conserved in all species tested. The C-terminal end is a glycine-rich domain (glycine makes up about 40% of the C terminus) with GGRGGR repeats. At residues 149-155, there is a predicted nuclear export signal, with the sequence ICIALGM (generally -X--X--X-). Residues 173-176 are predicted to be a nuclear localization signal KKLK (K--X-). FAM98A has two paralogs: FAM98B and FAM98C. FAM98A is longest of the three paralogous protein products with 518 amino acids. It is more similar to FAM98B, whose glycine-rich C terminus is much shorter than FAM98A. FAM98C less similar than FAM98B to FAM98A, all but lacking in a C terminus after DUF2465, as well as containing more differences in the amino acid sequence within the DUF2465. All three protein products have been shown experimentally to associate non-specifically with RNA: FAM98A binds to mRNA and FAM98B is incorporated into a tRNA-splicing complex.