Search by BoMiProt ID - Bomi7

Primary Information

BoMiProt ID Bomi7
Protein Name Keratin, type I cytoskeletal 10
Organism Bos taurus
Uniprot IdP06394
Milk FractionWhey
Ref Sequence Id NP_776802.1
Amino Acid Lenth 526
Molecular Weight 54848
Fasta Sequence
Gene Name KRT10
Gene Id 281888
Protein Existence Status Reviewed: Protein inferred from homology

Secondry Information

Presence in other biological fluids/tissue/cells expressed in epithelial cells
Protein Function Keratins—types I and II—are the intermediate-filament (IF)-forming proteins; one of the primary roles of keratin filaments is to provide structural support; resist chemical stresses and assist the cell in maintaining a polarized cytoarchitecture; contribute to the mechanical resilience;
Biochemical Properties pI range is 4.5 to 9.5; type I keratin proteins tend to be smaller (40–56.5 kDa) and acidic in overall charge (pI 4.5–6.0), whereas type II keratins are larger (50–70 kDa) and basic-neutral in charge (pI 6.5–8.5); Types I and II keratins are strictly interdependent for assembly into 10-nm filaments, initially forming coiled-coil heterodimers at the very first stage of the process; Keratin dimers and even tetramers can form under very harsh denaturing conditions,signifying unusual strength of the interactions between type I and type II keratins; Keratin monomers appear very unstable in most biological settings, whereas keratin assemblies are more stable but can undergo rapid turnover and/or be remodeled depending on the circumstances of the cell such as mitosis;
Significance in milk Keratin from teat canal lining represent the homogeneous populations of luminal epithelial cells from milk
PTMs undergo several posttranslational modifications (PTMs), including phosphorylation, O-linked glycosylation, ubiquitination, acetylation, SUMOylation, and transamidation; known keratin phosphorylation sites are serine/threonine residues that are located in the head and tail domains of the keratins; glycosylation of keratins also occurs on serine residues
Significance of PTMs function of keratin phosphorylation is to enhance keratin solubility, which in turn triggers reorganization of the keratin filament network; keratin phosphorylation provides cytoprotection by iserving as a phosphate sponge which shunt undesirable phosphorylation of proapoptotic proteins; Keratin glycosylation appears to modulate the K8–K18 signaling scaffold; Keratin SUMOylation is barely detectable under basal conditions but is markedly enhanced during apoptosis, exposure to oxidative stress, phosphatase inhibition; ubiquitination is crucial for the turnover of keratins by the proteasome, which occurs during proteotoxic stress;
Linking IDs Bomi3207 Bomi2881 Bomi2362 Bomi3258 Bomi3259 Bomi3268 Bomi3356 Bomi3291 Bomi3267 Bomi3270 Bomi2926 Bomi2887 Bomi3253 Bomi3269
Bibliography 1. Ku, N.-O., Michie, S., Resurreccion, E. Z., Broome, R. L., & Omary, M. B. (2002). Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression. Proceedings of the National Academy of Sciences of the United States of America, 99(7), 4373–4378.
2. Smolenski, G. A., Cursons, R. T., Hine, B. C., & Wheeler, T. T. (2015). Keratin and S100 calcium-binding proteins are major constituents of the bovine teat canal lining. Veterinary Research, 46(1).
3. Taylor-Papadimitriou, J., Stampfer, M., Bartek, J., Lewis, A., Boshell, M., Lane, E. B., & Leigh, I. M. (1989). Keratin expression in human mammary epithelial cells cultured from normal and malignant tissue: relation to in vivo phenotypes and influence of medium. Journal of Cell Science, 94 ( Pt 3), 403–413. Retrieved from
4. Snider, N. T., & Omary, M. B. (2014, March). Post-translational modifications of intermediate filament proteins: Mechanisms and functions. Nature Reviews Molecular Cell Biology, Vol. 15, pp. 163–177.
5. Kim, S., & Coulombe, P. A. (2007). Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes & Development, 21(13), 1581–1597.
6. Moll, R., Franke, W. W., Schiller, D. L., Geiger, B., & Krepler, R. (1982). The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells. Cell, Vol. 31, pp. 11–24.