Kontopodis, E.; Pierros, V.; Vorgias, C.; Papassideri, I.; Stravopodis, D. J.; Tsangaris, G. T.

Cellular and molecular uniqueness has recently gained eminent importance, due to the large amount of data produced by -omics technologies. Herein, we have constructed and decoded the \'Uniquome\' by introduction of the new peptide entities: (a) \'Core Unique Peptide\' (CrUP), defined as the peptide whose sequence is accommodated, specifically and exclusively, only in one protein in a given proteome, and also bears the minimum length of amino acid sequence; (b) \'Composite Unique Peptide\' (CmUP), defined as the peptide composed by the linear unification of CrUPs, when two or more successive in order CrUPs overlap one another; (c) \'Family Unique Peptide\' (FUP), defined as the CrUPs that are common between all members of a given family, but unique only for the protein members of the particular family, and (d) \'Universal Unique Peptides\' (UUPs), which are the common CrUPs in a given protein across organisms, carrying the important ability to securely identify a protein independently of an organism. By these entities as a tool-box, we have analyzed the human and model organisms, respective, proteomes. We demonstrate that these novel peptide entities play a crucial role for protein identification, protein-function prediction, cell physiology, tissue pathology, therapeutic oncology and translational medicine. Finally, we suggest that across species the conserved sequences are not DNA nucleotides but CrUPs entities.