A homology model of human claudin-1 utilizing automated protein modeling option was retrieved through I-TASSER server. Through this option five models were received from the server utilizing five different templates namely: model 1-5. Among the five, one that covered all amino acids with alpha helix structure and beta pleated sheet, and high C-value was selected. This model showed that predicted Yin Yang sites have high surface accessibility for the phosphorylation and O-glycosylation interplay. The Ser and Thr residues are denoted by red and green colors.