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0HSPB8_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionHeat-shock protein beta-8 (hspb8) (alpha crystallin c chain) (small stress protein-like protein hsp22) (e2-induced gene 1 protein) (protein kinase h11).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004674 protein serine/threonine kinase activity (NAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Prokaryotic and eukaryotic organisms respond to heat shock or otherenvironmental stress by inducing the synthesis of proteins collectively knownas heat-shock proteins (hsp) . Amongst them is a family of proteins with anaverage molecular weight of 20 Kd.nown as the hsp20 proteins . Theseseem to act as chaperones that can protect other proteins against heat-induceddenaturation and aggregation. Hsp20 proteins seem to form largeheterooligomeric aggregates. Structurally.his family is characterized by the presence of a conserved C-terminal domain of about 100 residues.
  IPR002068:Heat shock protein Hsp20
The crystallins are water-soluble structural proteins that occur in high concentration in the cytoplasm of eye lens fiber cells. Four major groups of crystallin have been distinguished on the basis of size.harge and immunological properties: alpha-.eta- and gamma-crystallins occur in all vertebrate classes (though gamma-crystallins are low or absent in avian lenses); and delta-crystallin is found exclusively in reptiles and birds . Alpha-crystallin occurs as large aggregates.omprising two types of related subunits (A and B) that are highly similar to the small (15-30kDa) heat shock proteins (HSPs).articularly in their C-terminal halves. The relationship between these families is one of classic gene duplication and divergence.rom the small HSP family.llowing adaptation to novel functions. Divergence probably occurred prior to evolution of the eye lens.lpha-crystallin being found in small amounts in tissues outside the lens .
  IPR001436:Alpha crystallin
Hsp20 is a mammalian small heat-shock protein family that occurs most abundantly in skeletal muscle and heart. It has a tendency to form dimers.ia a disulphide linkage formed by an N-terminal cysteine.ow heat stability and a poor chaperoning ability in comparison with other family members. Structurally.his and related proteins contain a beta-sandwich fold consisting of 8 strands in 2 beta-sheets in a greek-key topology .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008978:HSP20-like chaperone
SequencesProtein: HSPB8_HUMAN (196 aa)
mRNA: NM_014365
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 297 residues, 118100977-118101867Exon2: 23 residues, 118109212-118109276Exon3: 351 residues, 118115886-118116933Exon4: 2 residues, -Jump to HSPB8_HUMAN  
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