A bioinformatics-based approach for the prediction and identification of novel proteins potentially involved in phosphorylation signalling pathways.
Together with the explosion in the availability of genome data of a number of organisms including human and mouse, various methods and programs for computational prediction of protein-coding genes and annotation of functional proteins have dramatically increased. For the last decade there has been intense interest in the role of protein phosphorylation which is involved in post-translation modification mechanisms critically regulating inter/intracellular communication, patho/physiological responses and homeostasis during many biological processes. In the present study a total of 202 functionally uncharacterized human full-coding cDNA sequences were investigated using a bioinformatics-based approach. Ten novel potential substrates for protein kinases have been identified which may play multiple roles in regulating intracellular phosphorylation signalling pathways. In addition, 5 of those may be involved in the human-only post-translation mechanism regulated by specific protein kinases. The data presented here therefore would greatly contribute toward the understanding of human molecular basis and cellular signalling networks.
Ahn
Sung K
SK
Laboratory of Cell Biology, Korea Cancer Center Hospital, Nowon-gu, Seoul 139-240, Korea. genomicslab@hanmail.net
D020816:Amino Acid Motifs; D000818:Animals; D019295:Computational Biology; D006801:Humans; D051379:Mice; D008967:Molecular Biology; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D017346:Protein Serine-Threonine Kinases; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D051057:Proto-Oncogene Proteins c-akt; D015398:Signal Transduction / Q000502:physiology*
D011518:Proto-Oncogene Proteins; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt