Vasopressin controls osmotic water transport in the renal collecting duct through regulation of aquaporin-2. We carried out bioinformatic analysis of quantitative proteomic data from the accompanying paper to investigate mechanisms involved. The experiments used SILAC (Stable Isotope Labeling by Amino acids in Cell culture) in cultured mpkCCD cells to quantify each protein species in each of 5 differential-centrifugation (DC) fractions with or without the vasopressin analog (dDAVP). The mass spectrometry data and parallel western blotting experiments confirmed that dDAVP addition is associated with an increase of aquaporin-2 abundance in the 17,000 Xg pellet and a corresponding decrease in the 200,000 Xg pellet. Remarkably, all subunits of the cytoplasmic ribosome also increased in the 17,000 Xg pellet in response to dDAVP (P<10^-34) with a concomitant decrease in the 200,000 Xg pellet. Eukaryotic translation initiation complex 3 (eIF-3) subunits underwent parallel changes (P<10^-6). These findings are consistent with translocation of assembled ribosomes and eIF-3 complexes into the rough endoplasmic reticulum in response to dDAVP. Conversely, there was a systematic decrease in small GTPase abundances in the 17,000 Xg fraction. In contrast, most proteins showed no systematic redistribution among DC fractions including protein kinases. 246 of the 521 protein kinases coded by the mouse genome were identified, but many fewer were found to colocalize with aquaporin-2 among DC fractions. Bayes' Rule was used to integrate the new colocalization data with prior data in order to identify protein kinases most likely to phosphorylate aquaporin-2 at Ser256 (Camk2b>Camk2d>Prkaca) and Ser261 (Mapk1=Mapk3>Mapk14).