Primary Information |
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| BoMiProt ID | Bomi294 |
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| Protein Name | Integrin-linked protein kinase |
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| Organism | Bos taurus |
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| Uniprot ID | Q3SWY2 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001029865.1 |
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| Aminoacid Length | 452 |
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| Molecular Weight | 51447 |
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| FASTA Sequence |
Download |
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| Gene Name | ILK |
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| Gene ID | 540207 |
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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 | involved in diverse cell
adhesion-dependent physiological and pathological responses; binding partner of integrin cytoplasmic tails and was found to critically
regulate fatty acids; can act as a scaffold protein to function
through cellematrix interactions, cell signaling, and cytoskeletal organization; mediates many important cellular processes, including survival, proliferation, differentiation,
adhesion, migration, contractility; plays some role in the activation of endothelial progenitor
cells and neovascularization, and may also enhance vascular endothelial growth factor expression.
Increased ILK activity may promote epithelial-to-mesenchymal transition and induce a
transformed, tumorigenic phenotype |
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| Biochemical Properties | ILK has kinase activity and a preference for manganese
when phosphorylating GSK-3; ILK was
capable of directly phosphorylating diverse substrates including
a generic substrate myelin basic protein and physiological
targets including integrin ß 1 cytoplasmic tails, myosin light chain kinase
LC20, cell survival kinase AKT/PKB,
and glycogen synthase kinase-3 (GSK-3 ); localizes to focal adhesions, and interacts with the cytoplasmic tail of b
subunits of integrins and couples them to the actin cytoskeleton |
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| Significance in milk | Forced expression of a dominant negative, kinase-dead
form of ILK subtly altered mouse mammary epithelial cell
morphogenesis but it did not prevent differentiative milk
protein expression |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Fukuda, K. et al. (2011) ‘Biochemical, Proteomic, Structural, and Thermodynamic Characterizations of Integrin-linked Kinase (ILK)’, Journal of Biological Chemistry, 286(24), pp. 21886–21895. doi: 10.1074/jbc.M111.240093.
2. Somasiri, A. et al. (2001) ‘Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells.’, Journal of cell science, 114(Pt 6), pp. 1125–36. Available at: http://www.ncbi.nlm.nih.gov/pubmed/11228156 (Accessed: 4 October 2019). |
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