The protein encoded by this gene is an integral peroxisomal membrane protein. An inactivating nonsense mutation localized to this gene was observed in a patient with Zellweger syndrome of the complementation group CGD/CG9. Expression of this gene product morphologically and biochemically restores the formation of new peroxisomes, suggesting a role in peroxisome organization and biogenesis. Alternative splicing has been observed for this gene and two variants have been described.
PEX16 involved in several pathways and played different roles in them. We selected most pathways PEX16 participated on our site, such as Peroxisome, which may be useful for your reference. Also, other proteins which involved in the same pathway with PEX16 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
PEX16 has several biochemical functions, for example, protein C-terminus binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by PEX16 itself. We selected most functions PEX16 had, and list some proteins which have the same functions with PEX16. You can find most of the proteins on our site.
Function protein C-terminus binding
Related Protein HIC2; ERCC1; PQBP1; ECM1; CEP135; PIAS3; TRP53; ATP1B1; DYNLL1; PEX16
Function protein binding
Related Protein CAPRIN2; KLHL35; CEP55; TMIGD2; HSP90AA1.1; CD19; EIF3I; ACTN4; STOX1; BRAP
PEX16 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PEX16 here. Most of them are supplied by our site. Hope this information will be useful for your research of PEX16.
PEX19; PEX3; PEX14
PEX16 Related Articles
Liu, JB; Yu, B; et al. Effects of intrauterine growth retardation and maternal folic acid supplementation on hepatic mitochondrial function and gene expression in piglets. ARCHIVES OF ANIMAL NUTRITION 66:357-371(2012).
Nedeau, AE; Gallagher, KA; et al. Elevation of hemopexin-like fragment of matrix metalloproteinase-2 tissue levels inhibits ischemic wound healing and angiogenesis. JOURNAL OF VASCULAR SURGERY 54:1430-1438(2011).