|Protein Name||Serine/threonine-protein kinase 25|
|Ref Sequence Id||NP_899666.1|
|Amino Acid Lenth||426|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||As found in rats, expression was highest in the small and large intestine and the brain, compared with heart, skeletal muscle, spleen, liver, lung, kidney and adipose tissues;|
|Protein Function||Might be involved in the regulation of a novel intracellular signalling pathway; regulation of cell migration and modulation of cell death; pays a role in determining the proper localisation and morphology of the Golgi complex: STK25 inhibition perturbs perinuclear Golgi organisation, cell migration and invasion into type I collagen|
|Biochemical Properties||STK25 has been shown to be slightly activated by reactive oxygen intermediates but unaffected by growth factors, heat shock or osmolar stress; interact with diverse substrates ranging from enzymes to transcription factors, receptors, and other regulatory proteins; associate with the Golgi matrix proteins- Golgi matrix (GM)130 and binding to GM130 was shown to activate the kinase by promoting autophosphorylation of STK25|
|Significance in milk||increase in protein supports milk protein synthesis during the periparturient period|
|Bibliography||1. Ma, Y. F. et al. (2019) ‘Phosphorylation of AKT serine/threonine kinase and abundance of milk protein synthesis gene networks in mammary tissue in response to supply of methionine in periparturient Holstein cows’, Journal of Dairy Science, 102(5), pp. 4264–4274. doi: 10.3168/jds.2018-15451. |
2. Nerstedt, A. et al. (2012) ‘Serine/threonine protein kinase 25 (STK25): a novel negative regulator of lipid and glucose metabolism in rodent and human skeletal muscle’, Diabetologia, 55(6), pp. 1797–1807. doi: 10.1007/s00125-012-2511-7.
3. Kostich, M. et al. (2002) ‘Human members of the eukaryotic protein kinase family.’, Genome Biology, 3(9), p. research0043.1. doi: 10.1186/gb-2002-3-9-research0043.