Ser59
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Home > Phosphorylation Site Page: > Ser59  -  CRYAB (human)

Site Information
PsFLRAPsWFDTGLS   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448783

In vivo Characterization
Methods used to characterize site in vivo:
2D analysis ( 18 ) , [32P] bio-synthetic labeling ( 26 ) , immunoassay ( 1 ) , immunoprecipitation ( 9 ) , mass spectrometry ( 1 , 3 , 5 , 6 , 11 , 13 , 22 , 25 , 26 , 27 ) , mutation of modification site ( 2 , 4 , 8 , 9 , 19 , 20 , 21 , 23 ) , phospho-antibody ( 1 , 4 , 8 , 14 , 15 , 18 , 23 , 24 , 26 ) , western blotting ( 2 , 8 , 9 , 14 , 15 , 21 )
Disease tissue studied:
Alexander's disease ( 24 ) , brain cancer ( 4 , 23 , 26 ) , astrocytoma ( 23 , 26 ) , glioblastoma ( 4 ) , glioblastoma multiforme ( 4 ) , glioma ( 4 ) , breast cancer ( 5 ) , HER2 positive breast cancer ( 3 ) , luminal A breast cancer ( 3 ) , luminal B breast cancer ( 3 ) , breast cancer, triple negative ( 3 , 5 ) , hepatocellular carcinoma, surrounding tissue ( 13 ) , Down syndrome ( 15 )
Relevant cell line - cell type - tissue:
'brain, cerebral cortex' ( 15 ) , 'muscle, skeletal' ( 11 ) , astrocyte ( 1 ) , brain ( 1 ) , breast ( 3 , 5 ) , C2C12 (myoblast) ( 14 ) , COS7 (fibroblast) ( 2 ) , heart ( 18 ) , HeLa (cervical) ( 8 , 9 , 19 , 20 , 21 ) , hepatocyte-liver ( 13 ) , lens ( 22 , 25 , 27 ) , liver ( 6 ) , U-118MG (glial) ( 4 ) , U373 MG (glial) ( 4 , 23 , 26 )

Upstream Regulation
Putative in vivo kinases:
P38A (human) ( 1 , 14 )
Phosphatases, in vitro:
PPP1CA (human) ( 25 )
Treatments:
anisomycin ( 26 ) , arsenite ( 26 ) , cuprizone ( 1 ) , H2O2 ( 26 ) , heart failure ( 18 ) , heat_shock ( 26 ) , ischemia ( 5 ) , LPS ( 1 ) , menadione ( 8 ) , methylglyoxal ( 12 ) , mutation ( 8 ) , okadaic_acid ( 23 ) , oxidative_stress ( 1 ) , phorbol_ester ( 23 ) , SB203580 ( 1 ) , serum ( 14 )

Downstream Regulation
Effects of modification on CRYAB:
activity, induced ( 2 , 16 , 17 ) , intracellular localization ( 1 , 9 , 19 , 20 ) , molecular association, regulation ( 1 , 9 , 23 ) , protein conformation ( 8 , 16 ) , protein stabilization ( 8 )
Effects of modification on biological processes:
apoptosis, inhibited ( 12 ) , exocytosis, inhibited ( 4 )
Induce interaction with:
GEMIN3 (human) ( 9 )
Inhibit interaction with:
CRYAB (human) ( 23 )

Disease / Diagnostics Relevance
Relevant diseases:
Down syndrome ( 15 ) , multiple sclerosis ( 1 )

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

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

4

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

5

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   Curated Info

6

Bian Y, et al. (2014) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics 96, 253-62
24275569   Curated Info

7

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   Curated Info

8

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

9

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

10

Beli P, et al. (2012) Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response. Mol Cell 46, 212-25
22424773   Curated Info

11

Lundby A, et al. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun 3, 876
22673903   Curated Info

12

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

13

Han G, et al. (2010) Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis. Electrophoresis 31, 1080-9
20166139   Curated Info

14

Singh BN, Rao KS, Rao ChM (2010) Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shock protein, during muscle differentiation. Biochim Biophys Acta 1803, 288-99
20005263   Curated Info

15

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

16

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

17

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

18

Dohke T, et al. (2006) Proteomic analysis reveals significant alternations of cardiac small heat shock protein expression in congestive heart failure. J Card Fail 12, 77-84
16500585   Curated Info

19

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

20

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

21

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

22

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

23

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

24

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

25

Kamei A, et al. (2000) Post-translational modification of alphaB-crystallin of normal human lens. Biol Pharm Bull 23, 226-30
10706390   Curated Info

26

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

27

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