Primary Information |
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BoMiProt ID | Bomi315 |
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Protein Name | Serine/threonine-protein kinase N1 |
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Organism | Bos taurus |
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Uniprot ID | A1A4I4 |
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Milk Fraction | Exosome |
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Ref Sequence ID | NP_001073715.1 |
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Aminoacid Length | 944 |
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Molecular Weight | 104133 |
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FASTA Sequence |
Download |
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Gene Name | PKN1 |
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Gene ID | 509080 |
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Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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Protein Function | Interact with
diverse substrates ranging from enzymes, including other
kinases, to transcription factors, receptors, and other regulatory proteins |
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Significance in milk | Increase in protein supports milk protein synthesis during the periparturient period |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | 528-547, 557-607, 764-794, 898-909 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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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. Manning, G. et al. (2002) ‘The Protein Kinase Complement of the Human Genome’, Science, 298(5600), pp. 1912–1934. doi: 10.1126/science.1075762. |