Sureni V Mullegama, Kaitlyn A Kiernan, Erin Torti, Ethan Pavlovsky, Nicholas Tilton, Austin Sekula, Hua Gao, Joseph T Alaimo, Kendra Engleman, Eric T Rush, Karli Blocker, Katrina M Dipple, Veronica M Fettig, Heather Hare, Ian Glass, Dorothy K Grange, Michael Griffin, Chanika Phornphutkul, Lauren Massingham, Lakshmi Mehta, Danny E Miller, Jenny Thies, J Lawrence Merritt, Eric Muller, Matthew Osmond, Sarah L Sawyer, Rachel Slaugh, Rachel E Hickey, Barry Wolf, Sanjeev Choudhary, Miljan Simonović, Yueqing Zhang, Timothy Blake Palculict, Aida Telegrafi, Deanna Alexis Carere, Ingrid M Wentzensen, Michelle M Morrow, Kristin G Monaghan, Jun Yang, Jane Juusola
Selenophosphate synthetase (SEPHS) plays an essential role in selenium metabolism. Two mammalian SEPHS paralogues, SEPHS1 and SEPHS2, share high sequence identity and structural homology with SEPHS. Here, we report nine individuals from eight families with developmental delay, growth and feeding problems, hypotonia, and dysmorphic features, all with heterozygous missense variants in SEPHS1. Eight of these individuals had a recurrent variant at amino acid position 371 of SEPHS1 (p.Arg371Trp, p.Arg371Gln, and p...
March 21, 2024: American Journal of Human Genetics