The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors

Seema Verma1, Ayesha Ismail, Xiuhua Gao

  • 1Cancer Center, Criss III, Room 352, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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