It has recently been proposed by Gavin et al. (Nature 2006, 440, 631-636) that protein complexes in the cell exist in different forms. The proteins within each complex were proposed to exist as three different classes, being core, module or attachment proteins. This study investigates whether the core-module-attachment classification of proteins within each complex is supported by other high-throughput protein data. Core proteins were found to have lower abundance, and shorter half-life as compared to attachment proteins, whilst the abundance and half-life of core and module proteins were similar. When the cell was perturbed, core proteins had smaller changes in abundance as compared to module and attachment proteins. Comparisons between six different pairwise interaction types of core, module and attachment proteins within a complex showed interaction types involving core or module proteins were more likely to be mediated by domain-domain interactions (DDIs) than interaction types involving attachment proteins. Interaction types that involve attachment proteins had a relatively higher ratio of abundance and ratio of half-life. So we conclude that, the core, module and attachment model of protein complexes is supported by data from these proteomic scale datasets, and describe a model for a typical protein complex that considers the above results.