Table 2.
Potential Phosphorylation Sites of Human Grx Enzymes
Grx isoform | Residue (FASTA) | Kinase | Probability score | aLocation (relative to active site) |
---|---|---|---|---|
Human Grx1 | S34 | DNAPK | 0.6 | Opposite end of α-helix 2 |
S88 | PKC | 0.66 | Neighboring α-helix 4 | |
Human Grx2 | S16 | General | 0.73 | b |
S20 | General, PKA | 0.91, 0.68 | b | |
S39 | General | 0.69 | b | |
S48 | General | 0.99 | b | |
S73 | PKC | 0.61 | Facing active site (β-sheet 1) | |
T81 | PKC | 0.8 | Immediately after active site (α-helix 2) | |
Y113 | General | 0.73 | Opposite side of protein(α-helix 3) | |
T137 | General, PKC | 0.9, 0.84 | Neighboring α-helix(α-helix 4) | |
S158 | General, PKC | 0.9, 0.84 | b | |
Human Grx5 | S41 | General | 0.69 | c |
S156 | General | 0.87 | c |
FASTA sequences of human Grx1, Grx2, and Grx5 were entered into NetPhos 2.0 (12) and NetPhosK 1.0 (13) search engines to identify potential phosphorylation sites. Sites with probability scores ≥0.6 are included.
DNAPK, DNA-dependent protein kinase; PKC, protein kinase C; PKG, cyclic GMP–dependent protein kinase.
The hydroxyl groups of all of the indicated residues are solvent exposed and outward facing, with the exception of Grx2 T137, which faces the protein interior.
Not included in published x-ray structure.
No structural information available.