Table 2

Protein modifications of crystallins from a 4-year congenital cataract

Protein/accession no.%*PhosphorylationOxidationAcetylationMethylation
Crystallin, α A chain gi|1706112|sp|P02489|90.2T13, S45, S122, T140Y18, Y34, M138K70, K78, K88, K145R21, K88
Crystallin, α B chain gi|117385|sp|P02511|94.9S19, S21, S43§, S45, S53, S59, S76Y48, W60, M68K92§R22, R50
Crystallin, β A1 gi|4885155|ref|NP_005199.1|65.6T127, S160M126§K122, K125, K131R137
Crystallin, β A4 gi|4503059|ref|NP_001877.1|78.1S35, T43W149
Crystallin, β B1 gi|4503061|ref|NP_001878.1|88.9S10, T12W216, M226K6, K160R230, R231, K235
Crystallin, β B2 gi|1169091|spl|P43320|85.4T118W59, M122, W151K76, K121K42, K68, K121
Crystallin, β B3 gi|4758074|ref|NP_004067.1|54.0Y29M129K128K128
Crystallin, γ B gi|4885157|ref|NP_005201.1|60.6Y63, Y66W69, M70
Crystallin, γ C gi|10518338|ref|NP_066269.1|61.5Y63, Y66Y56, W69, M70, W131
Crystallin, γ D gi|2506321|sp|P07320|58.0Y46
Crystallin, γ S gi|1362852|pir∥S5526380.6M41, M101, M106K6
  • Database (human, Homosapiens) was downloaded from on 11/29/00 and has 57,847 entries. 

  • * Percentage of amino acid sequence coverage obtained for proteins using the DTASelect filter cutoff values chosen for this study. 

  • Acetylation [M+42]+ was indistinguishable from carbamylation [M+43]+ in this study. 

  • Modification sites reported in literature (33, 35, 42, 44, 45, and 58). 

  • § Modification site identified by a single peptide only.