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Protein Page:
HSPB8 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
HSPB8 Displays temperature-dependent chaperone activity. Monomer. Interacts with HSPB1. Interacts with DNAJB6. By 17-beta-estradiol. Predominantly expressed in skeletal muscle and heart. Belongs to the small heat shock protein (HSP20) family. Note: This description may include information from UniProtKB.
Protein type: Heat shock protein
Cellular Component: cytoplasm; intracellular; nucleus
Molecular Function: identical protein binding; protein binding; protein kinase activity
Biological Process: cell death; response to stress
Reference #:  Q9UJY1 (UniProtKB)
Alt. Names/Synonyms: Alpha-crystallin C chain; CMT2L; CRYAC; DHMN2; E2-induced gene 1 protein; E2IG1; H11; heat shock 22kDa protein 8; heat shock 27kDa protein 8; Heat shock protein beta-8; HMN2; HMN2A; HSP22; HSPB8; Protein kinase H11; Small stress protein-like protein HSP22
Gene Symbols: HSPB8
Molecular weight: 21,604 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HSPB8

Protein Structure Not Found.


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Sites Implicated In
protein conformation: S24‑p, S27‑p, S57‑p, T87‑p
protein degradation: S57‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S14-p PFSCHYPsRLRRDPF
2 6 S24-p RRDPFRDsPLsSRLL
2 0 S27-p PFRDsPLsSRLLDDG
1 1 S57-p DWALPRLsSAWPGtL
1 0 T63-p LsSAWPGtLRSGMVP
0 1 R65 SAWPGtLRSGMVPrG
0 2 R71-m1 LRSGMVPrGPTATAr
0 1 R71 LRSGMVPRGPTATAr
0 2 R78-m1 rGPTATArFGVPAEG
0 1 R78-m2 rGPTATArFGVPAEG
2 9 T87-p GVPAEGRtPPPFPGE
0 2 Y118-p MVKTKDGyVEVSGKH
  mouse

 
S14 PFPCSYPSRLRRDPF
S24-p RRDPFRDsPLSSRLL
S27 PFRDsPLSSRLLDDG
S57-p EWALPRLsSAWPGTL
T63 LsSAWPGTLrSGMVP
R65-m1 SAWPGTLrSGMVPrG
R71-m1 LrSGMVPrGPPATAr
R71-m2 LrSGMVPrGPPATAr
R78-m1 rGPPATArFGVPAEG
R78-m2 rGPPATArFGVPAEG
S87-p GVPAEGRsPPPFPGE
Y118 MVKTKDGYVEVSGKH
  rat

 
S14 PFPCSYPSRLRRDPF
S24 RRDPFRDSPLSSRLL
S27 PFRDSPLSSRLLDDG
S57 EWALPRLSSAWPGTL
T63 LSSAWPGTLRSGMVP
R65 SAWPGTLRSGMVPrG
R71-m1 LRSGMVPrGPTATAr
R71 LRSGMVPRGPTATAr
R78-m1 rGPTATArFGVPAEG
R78 rGPTATARFGVPAEG
N87 GVPAEGRNPPPFPGE
Y118 MVKTKDGYVEVSGKH
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