Thymopoietin

LAP2alpha ( lamina -associated polypeptide 2alpha ) is a protein of the cell nucleus, which could only be detected in mammalian cells.

LAP2alpha is one of six splice variants of the gene LAP2, four of which ( LAP2beta, LAP2gamma, LAP2delta and LAP2epsilon ) transmembrane proteins. In amphibians and fish could be a more developmentally expressed variant, LAP2omega be detected, which is also membrane bound. LAP2alpha structurally and functionally differs significantly from the other LAP2 proteins and shares with them only the N-terminus (the first three exons).

LAP2alpha is localized in the interphase in the interior of the nucleus and is a binding partner of A- type lamins. During mitosis LAP2alpha is specifically phosphorylated and loses its binding to the chromosomes. Very early at the end of mitosis, in early telophase, LAP2alpha is localized in the core regions back to the chromosomes. A domain characteristic of all proteins is the LAP2 LEM domain which mediates the binding to the DNA binding protein BAF (barrier to drive integration factor).

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