Table 2.
No | Protein Name | Swiss-prot No | Score | MW | pI | Seq Cov | GRAVY | Function* |
---|---|---|---|---|---|---|---|---|
Up-regulated proteins | ||||||||
1 | Calrecticulin | P27797 | 175 | 46890 | 4.3 | 18% | -1.104 | Molecular calcium-binding chaperone |
2 | 80 k protein H precursor | P14314 | 134 | 60245 | 4.34 | 17% | -0.910 | Protein kinase C binding |
3 | Tropomyosin alpha-3 chain | P06753 | 55 | 32857 | 4.68 | 4% | -1.051 | Regulates muscle contraction, stabilizes cytoskeleton actin filaments |
4 | Tropomyosin isoform | P09493 | 104 | 28519 | 4.89 | 14% | -1.044 | Regulates muscle contraction, stabilizes cytoskeleton actin filaments |
5 | Protein disulfide isomerase (PDI) | P07237 | 45 | 57487 | 4.76 | 19% | -0.431 | Catalyzes the formation, breakage and rearrangement of disulfide bonds |
6 | Heat shock protein 90 (HSP 90) | Q4R250 | 48 | 92572 | 4.77 | 10% | -0.719 | Molecular chaperone that functions in the processing and transport of secreted proteins |
7 | Tubulin, beta polypeptide | Q91575 | 161 | 48142 | 4.7 | 15% | -0.355 | Major constituent of microtubules |
8 | 78 kDa glucose-regulated protein | P11021 | 505 | 72404 | 5.07 | 37% | -0.487 | Anti-apoptosis, cellular response to glucose starvation |
9 | Heat shock protein 60 (HSP 60) | P10809 | 50 | 61348 | 5.7 | 17% | -0.076 | Implicated in mitochondrial protein import and macromolecular assembly |
10 | Heat shock 70 kDa protein 8 isoform 1 (HSP 70) | P11142 | 220 | 71087 | 5.28 | 17% | -0.456 | Molecular chaperone |
11 | Heat shock 70 kDa protein 1 | Q5R7D3 | 257 | 69982 | 5.48 | 14% | -0.383 | Stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol and within organelles |
12 | Protein disulfide isomerase A3 (PDI A3) | P30101 | 581 | 57167 | 5.98 | 21% | -0.506 | Catalyzes the rearrangement of disulfide bonds in proteins |
Down-regulated protein |
||||||||
13 | Tubulin alpha-1 chain | Q6P9V9 | 235 | 50816 | 4.94 | 28% | -0.23 | Major constituent of microtubules |
*Functions were obtained from www.uniprot.org.