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The PX domain is a phosphoinositide-binding structural domain involved in targeting of proteins to cell membranes.
Additional recommended knowledge
This domain was first found in P40phox and p47phox domains of NADPH oxidase (phox stands for phagocytic oxidase). It was also identified in many other proteins involved in membrane trafficing, including nexins, Phospholipase D, and phosphoinositide-3-kinases.
The PX domain is structurally conserved in eukaryotes, although amino acid sequenves show little similarity. PX domains interact primarily with PtdIns(3)P lipids. However some of them bind to phosphatidic acid, (PtdIns(3,4)P2), PtdIns(3,5)P2, PtdIns(4,5)P2), and PtdIns(3,4,5)P3. The PX-domain can also interact with other domains and proteins.
Human proteins containing this domain
A-388D4.1; C20orf161; C20orf23; HS1BP3; NCF1; NCF1C; NCF4; NISCH; PIK3C2A; PIK3C2B; PIK3C2G; PLD1; PLD2; PXK; RPS6KC1; SGK3; SGKL; SH3PX3; SH3PXD2A; SLIC1; SNAG1; SNX1; SNX10; SNX11; SNX12; SNX13; SNX14; SNX15; SNX16; SNX17; SNX19; SNX2; SNX21; SNX22; SNX24; SNX25; SNX27; SNX3; SNX30; SNX4; SNX5; SNX6; SNX7; SNX8; SNX9;
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "PX_domain". A list of authors is available in Wikipedia.|