Ser45
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Home > Phosphorylation Site Page: > Ser45  -  CRYAB (human)

Site Information
FPTSTsLsPFYLrPP   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448748

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 18 ) , immunoassay ( 1 ) , immunoprecipitation ( 5 ) , mass spectrometry ( 14 , 18 , 19 ) , mass spectrometry (in vitro) ( 12 ) , mutation of modification site ( 2 , 3 , 4 , 5 , 10 , 11 , 13 , 15 ) , phospho-antibody ( 1 , 3 , 4 , 7 , 11 , 15 , 16 , 18 ) , western blotting ( 2 , 4 , 5 , 7 , 11 , 13 )
Disease tissue studied:
Alexander's disease ( 16 ) , brain cancer ( 3 , 15 , 18 ) , astrocytoma ( 15 , 18 ) , glioblastoma ( 3 ) , glioblastoma multiforme ( 3 ) , glioma ( 3 ) , Down syndrome ( 7 )
Relevant cell line - cell type - tissue:
'brain, cerebral cortex' ( 7 ) , astrocyte ( 1 ) , COS7 (fibroblast) ( 2 ) , HeLa (cervical) ( 4 , 5 , 10 , 11 , 13 ) , lens ( 14 , 19 ) , U-118MG (glial) ( 3 ) , U373 MG (glial) ( 3 , 15 , 18 )

Upstream Regulation
Putative in vivo kinases:
ERK1 (human) ( 1 )
Treatments:
anisomycin ( 18 ) , arsenite ( 18 ) , H2O2 ( 18 ) , heat_shock ( 18 ) , LPS ( 1 ) , menadione ( 4 ) , methylglyoxal ( 6 ) , mutation ( 4 ) , nocodazole ( 17 ) , okadaic_acid ( 15 ) , oxidative_stress ( 1 ) , PD98059 ( 1 , 17 ) , phorbol_ester ( 15 , 17 , 18 )

Downstream Regulation
Effects of modification on CRYAB:
activity, induced ( 8 , 9 ) , activity, inhibited ( 2 ) , intracellular localization ( 1 , 5 , 10 , 11 ) , molecular association, regulation ( 1 , 5 , 11 , 12 , 13 , 15 ) , protein conformation ( 4 , 8 , 12 ) , protein degradation ( 13 ) , protein stabilization ( 4 )
Effects of modification on biological processes:
apoptosis, inhibited ( 6 ) , exocytosis, inhibited ( 3 )
Induce interaction with:
FBXO4 (human) ( 11 , 13 ) , GEMIN3 (human) ( 5 )
Inhibit interaction with:
CRYAB (human) ( 15 )

Disease / Diagnostics Relevance
Relevant diseases:
Down syndrome ( 7 )

References 

1

Kuipers HF, et al. (2017) Phosphorylation of αB-crystallin supports reactive astrogliosis in demyelination. Proc Natl Acad Sci U S A 114, E1745-E1754
28196893   Curated Info

2

Ciano M, et al. (2016) Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins. Biochem Biophys Res Commun 479, 325-330
27641668   Curated Info

3

Kore RA, Abraham EC (2016) Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells. Biochim Biophys Acta 1863, 368-77
26620801   Curated Info

4

Simon S, et al. (2013) Analysis of the Dominant Effects Mediated by Wild Type or R120G Mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1). PLoS One 8, e70545
23950959   Curated Info

5

den Engelsman J, et al. (2013) Pseudophosphorylated αB-Crystallin Is a Nuclear Chaperone Imported into the Nucleus with Help of the SMN Complex. PLoS One 8, e73489
24023879   Curated Info

6

Jeong WJ, et al. (2012) Cytoplasmic and Nuclear Anti-Apoptotic Roles of αB-Crystallin in Retinal Pigment Epithelial Cells. PLoS One 7, e45754
23049853   Curated Info

7

Palminiello S, et al. (2009) Upregulation of phosphorylated alphaB-crystallin in the brain of children and young adults with Down syndrome. Brain Res 1268, 162-73
19272359   Curated Info

8

Ahmad MF, Raman B, Ramakrishna T, Rao ChM (2008) Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant. J Mol Biol 375, 1040-51
18061612   Curated Info

9

Ecroyd H, et al. (2007) Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity. Biochem J 401, 129-41
16928191   Curated Info

10

den Engelsman J, et al. (2005) Nuclear import of {alpha}B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G. J Biol Chem 280, 37139-48
16129694   Curated Info

11

den Engelsman J, et al. (2004) Mimicking phosphorylation of the small heat-shock protein alphaB-crystallin recruits the F-box protein FBX4 to nuclear SC35 speckles. Eur J Biochem 271, 4195-203
15511225   Curated Info

12

Aquilina JA, et al. (2004) Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. J Biol Chem 279, 28675-80
15117944   Curated Info

13

den Engelsman J, Keijsers V, de Jong WW, Boelens WC (2003) The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination. J Biol Chem 278, 4699-704
12468532   Curated Info

14

MacCoss MJ, et al. (2002) Shotgun identification of protein modifications from protein complexes and lens tissue. Proc Natl Acad Sci U S A 99, 7900-5
12060738   Curated Info

15

Ito H, et al. (2001) Phosphorylation-induced change of the oligomerization state of alpha B-crystallin. J Biol Chem 276, 5346-52
11096101   Curated Info

16

Kato K, et al. (2001) Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease. J Neurochem 76, 730-6
11158243   Curated Info

17

Kato K, et al. (1998) Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem 273, 28346-54
9774459   Curated Info

18

Ito H, et al. (1997) Phosphorylation of alphaB-crystallin in response to various types of stress. J Biol Chem 272, 29934-41
9368070   Curated Info

19

Miesbauer LR, et al. (1994) Post-translational modifications of water-soluble human lens crystallins from young adults. J Biol Chem 269, 12494-502
8175657   Curated Info