Curated Information
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Home > Curated Information Page > PubMed Id: 15117944
Aquilina JA, et al. (2004) Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. J Biol Chem 279, 28675-80 15117944
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S19-p - CRYAB (human)
Modsite: RPFFPFHsPsrLFDQ SwissProt Entrez-Gene
Orthologous residues
CRYAB (human): S19‑p, CRYAB (mouse): S19‑p, CRYAB (rat): S19‑p, CRYAB (rabbit): S19‑p, CRYAB (pig): S19‑p, CRYAB (cow): S19‑p
Characterization
Methods used to characterize site in vivo mass spectrometry (in vitro)
Comments:  may be associated with catracts and degenerative brain disease

S45-p - CRYAB (human)
Modsite: FPTSTsLsPFYLrPP SwissProt Entrez-Gene
Orthologous residues
CRYAB (human): S45‑p, CRYAB (mouse): S45‑p, CRYAB (rat): S45‑p, CRYAB (rabbit): S45‑p, CRYAB (pig): S45‑p, CRYAB (cow): S45‑p
Characterization
Methods used to characterize site in vivo mass spectrometry (in vitro)
Comments:  may be associated with catracts and degenerative brain disease
Downstream Regulation
Effect of modification (function):  molecular association, regulation, protein conformation
Comments:  S45 phosphorylation induces uncontrolled aggregation and affects its chaperone activity.