This gene encodes a member of thesorting nexin family. Members of this family contain aphox (PX) domain, which is aphosphoinositide binding domain, and are involved in intracellular trafficking. This protein associates with formin-binding protein 17, but its function is unknown. This protein may formoligomeric complexes with family members.[6]
^Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (Nov 2003). "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance".FEBS Letters.554 (1–2):10–6.doi:10.1016/S0014-5793(03)01063-9.PMID14596906.S2CID19552309.
Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides".Gene.138 (1–2):171–4.doi:10.1016/0378-1119(94)90802-8.PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library".Gene.200 (1–2):149–56.doi:10.1016/S0378-1119(97)00411-3.PMID9373149.
Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (Nov 2003). "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance".FEBS Letters.554 (1–2):10–6.doi:10.1016/S0014-5793(03)01063-9.PMID14596906.S2CID19552309.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization".Nature Biotechnology.24 (10):1285–92.doi:10.1038/nbt1240.PMID16964243.S2CID14294292.
