Colorectal cancer is a leading cause of cancer-related death. It develops from normal enterocytes, through a benign adenoma stage, into the cancer and finally into the metastatic form. We previously compared the proteomes of normal colorectal enterocytes (N), cancer (C) and nodal metastasis (M) to a depth of 8,100 proteins and found extensive quantitative remodeling between normal and cancer but not cancer and metastasis (Wi?niewski et al. PMID 22968445). Here we utilize advances in the proteomic workflow to perform an in depth analysis of the normal tissue (N), the adenoma (A) and the cancer (C). Absolute proteomics of 10,000 proteins per patient from microdissected formalin fixed and paraffin embedded clinical material established a quantitative protein repository of the disease. Between N and A 23% of all proteins changed significantly, 17.8% from A to C and 21.6% from N to C. Together with principal component analysis of the patient groups, this suggests that N, A and C are equidistant rather than on one developmental line. Our proteomics approach allowed us to assess changes in varied cell size, the composition of different subcellular components, and alterations in basic biological processes including the energy metabolism, plasma membrane transport, DNA replication and transcription. This revealed several-fold higher concentrations of enzymes in fatty acid metabolism in C compared to N, and unexpectedly, the same held true of plasma membrane transporters.