Search by BoMiProt ID - Bomi294


Primary Information

BoMiProt ID Bomi294
Protein Name Integrin-linked protein kinase
Organism Bos taurus
Uniprot IdQ3SWY2
Milk FractionExosome
Ref Sequence Id NP_001029865.1
Aminoacid Length 452
Molecular Weight 51447
Fasta Sequence https://www.uniprot.org/uniprot/Q3SWY2.fasta
Gene Name ILK
Gene Id 540207
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

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
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
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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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).