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. Author manuscript; available in PMC: 2008 Sep 15.
Published in final edited form as: J Proteome Res. 2006 Oct;5(10):2554–2566. doi: 10.1021/pr050473a

Table 1.

Averaged human lens PTM spectral counts and PTM rates (for peptides containing detected modifications) for aged water-insoluble and water-soluble crystallins.

Average Aged Human Lens Spectral Counts (N=3)a,b 3-Day Old Spectral Countsc
Overall Water-Insoluble Water-Soluble Water-Soluble
Modification aa, ΔM Relative Rankd Modified Count Ratee
(%)
Modified Count Ratee
(%)
Modified Count Ratee
(%)
deamidation N,Q +1 93 1,739 18.52 796 8.77 176 2.30
S-methylation C -43f 28 390 28.80 374 20.30 6 0.45
acetylationg nt +42 24 300 84.89 355 83.78 420 80.15
oxidation M,W +16 11 143 2.76 169 3.57 153 4.27
carboxymethyl lysine K +58 8 99 4.19 107 3.95 0 0.00
phosphorylation S,T +80 7 80 3.83 113 5.46 20 1.12
carbamylation K +43 3 33 4.28 39 4.52 5 0.68
carboxyethyl lysine K +72 2 33 2.71 33 2.84 1 0.12
R +55 R +55 2 34 3.01 25 2.60 0 0.00
H-methylation H +14 2 33 5.01 21 3.33 0 0.00
S,H +28 S,H +28 1 14 0.69 14 0.72 14 1.00
a

Aged lenses were 70-year normal, 70-year mild cataract, and 93-year moderate cataract.

b

Overall spectral counts for the 11 major in vivo human lens crystallin modifications at 155 PTM sites.

c

Similar quantities for water-soluble protein from a 3-day old lens are shown as a control.

d

Relative to least abundant modification. Ranked by total modified spectral count.

e

Modification rate was calculated as the number of spectra assigned to a given amino acid modification divided by total number of spectra that contained those amino acids.

f

Net methylation mass shift after cysteine +57 Da carbamidomethylation.

g

Protein co-translational N-terminal acetylation.