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Primary Information | |
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| BoMiProt ID | Bomi7289 |
| Protein Name | Myoglobin |
| Organism | Bos taurus |
| Uniprot ID | P02192 |
| Milk Fraction | Whey |
| Aminoacid Length | 154 |
| Molecular Weight | 17078 |
| FASTA Sequence | Download |
| Gene Name | MB |
| Gene ID | 280695 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Protein Function | hemoprotein mainly to the heart and oxidative myofibers in skeletal muscle. Function is short- and long-term buffering of muscle O2 concentrations during bursts of exercise or breath-hold diving and the facilitated diffusion of O2 from blood to mitochondria. |
| Biochemical Properties | Binds to oxygen |
| PTMs | Phosphorylation on Ser and Thr.Nitration. |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P02192|MYG_BOVIN Myoglobin OS=Bos taurus OX=9913 GN=MB PE=1 SV=3 MGLS*4DGEWQLVLNAWGKVEADVAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASE DLKKHGNT*68VLTALGGILKKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHAKH PSDFGADAQAAMSKALELFRNDMAAQYKVLGFHG |
| CATH | Matched CATH superfamily n/a |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | In human Mb,nitration of Tyr103, Tyr146, Trp7 and Trp14 results in altered internal cavities and forms a water channel, representing an initial stage of Mb unfolding.. electron-rich Tyr43 conjugated to the heme group, exhibited a dramatically enhanced ability to activate H2O2(enhanced peroxidase activity). Methylglyoxal (MG), a reactive α-oxoaldehyde, increases in diabetic condition and reacts with proteins to form advanced glycation end products (AGEs) following Maillard-like reaction. MG modifies several lysine and arginine residues of Mb in a time-dependent manner.MG-derived advanced glycation end products induce structural alterations of Mb which leads to amyloid-like aggregation of Mb at longer incubation time. |
| PDB ID | 1Z2H,1Z2S, |
| Bibliography | 1.Banerjee, S., Maity, S., & Chakraborti, A. S. (2016). Methylglyoxal-induced modification causes aggregation of myoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 155, 1-10. 2.Yan, D. J., Li, W., Xiang, Y., Wen, G. B., Lin, Y. W., & Tan, X. (2015). A Novel Tyrosine–Heme C O Covalent Linkage in F43Y Myoglobin: A New Post‐translational Modification of Heme Proteins. ChemBioChem, 16(1), 47-50. 3.Lin, Y. W., Shu, X. G., Du, K. J., Nie, C. M., & Wen, G. B. (2014). Computational insight into nitration of human myoglobin. Computational biology and chemistry, 52, 60-65. |