Even after a nascent protein emerges from the ribosome, its fate is still c
ontrolled by its own amino acid sequence information. Namely, it may be co-
/posttranslationally modified (e.g., phosphorylated, N-/O-glycosylated, and
lipidated); it may be inserted into the membrane, translocated to an organ
elle, or secreted to the outside milieu; it may be processed for maturation
or selective degradation; finally, its fragment may be presented on the ce
ll surface as an antigen. Here, prediction methods of such protein fates fr
om their amino acid sequences are reviewed. In many cases, artificial neura
l network techniques have been effectively used. The prediction of in vivo
fates of proteins will be useful for characterizing newly identified candid
ate genes in a genome or for interpreting multiple spots in proteome analys
es. (C) 2001 Academic Press.