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|Title:||Cloning and characterization of AWP1, a novel protein that associates with serine/threonine kinase PRK1 in vivo|
|Authors:||Duan, W. |
|Source:||Duan, W., Sun, B., Li, T.W., Tan, B.J., Lee, M.K., Teo, T.S. (2000). Cloning and characterization of AWP1, a novel protein that associates with serine/threonine kinase PRK1 in vivo. Gene 256 (1-2) : 113-121. ScholarBank@NUS Repository. https://doi.org/10.1016/S0378-1119(00)00365-6|
|Abstract:||We describe the cloning and expression of cDNAs encoding a novel human protein of 208 amino acid residues with a predicted molecular mass of 22.6kDa and its mouse homologue. We name this protein as AWP1 (associated with PRK1). AWP1 is a ubiquitously expressed protein, and the Awp1 gene is switched on during early human and mouse development. When expressed in COS-1 cells, the Myc-tagged AWP1 has an apparent molecular mass higher than that deduced from its amino acid sequence. AWP1 possesses a conserved zf-A20 zinc finger domain at its N-terminal and a zf-AN1 zinc finger domain at its C-terminal. Co-immunoprecipitation experiments revealed that mouse AWP1 specifically interacts with a rat serine/threonine protein kinase PRK1 in vivo. Hence, AWP1 may play a regulatory role in mammalian signal transduction pathways. Copyright (C) 2000 Elsevier Science B.V.|
|Appears in Collections:||Staff Publications|
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