Type I collagen is a member of group I collagen (fibrillar forming collagen). Trimers of one alpha 2(I) and two alpha 1(I) chains. Expressed in bones. Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. These protein fragments were extracted from an ancient humerus epiphysis bone collected in Haiti. Belongs to the fibrillar collagen family.