Conserved Protein Domain Family
ACD_HspB1_like

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cd06475: ACD_HspB1_like 
Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also denoted HspB1 in human) and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Hsp27 shows enhanced synthesis in response to stress. It is a molecular chaperone which interacts with a large number of different proteins. It is found in many types of human cells including breast, uterus, cervix, platelets and cancer cells. Hsp27 has diverse cellular functions including, chaperoning, regulation of actin polymerization, keratinocyte differentiation, regulation of inflammatory pathways in keratinocytes, and protection from oxidative stress through modulating glutathione levels. It is also a subunit of AUF1-containing protein complexes. It has been linked to several transduction pathways regulating cellular functions including differentiation, cell growth, development, and apoptosis. Its activity can be regulated by phosphorylation. Its unphosphorylated state is a high molecular weight aggregated form (100-800kDa) composed of up to 24 subunits, which forms as a result of multiple interactions within the ACD, and is required for chaperone function and resistance to oxidative stress. Upon phosphorylation these large aggregates rapidly disassociate to smaller oligomers and chaperone activity is modified. High constitutive levels of Hsp27 have been detected in various cancer cells, in particular those of carcinoma origin. Over-expression of Hsp27 has a protective effect against various diseases-processes, including Huntington's disease. Mutations in Hsp27 have been associated with a form of distal hereditary motor neuropathy type II and Charcot-Marie-Tooth disease type 2.
Statistics
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PSSM-Id: 107230
View PSSM: cd06475
Aligned: 5 rows
Threshold Bit Score: 160.784
Threshold Setting Gi: 74096257
Created: 25-Mar-2008
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
putative dimer
Feature 1:putative dimer interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #####         # # ##                                    #                    ## 
P04792        84 GVSEIRHTadRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDeHGYISRCFTRKYTLPPGVDPtqVSSSLSPEGTL 163 Homo sapiens
O13224        91 GMSEIKQTqdNWKISLDVPHFSPEELVVKTKDGVLEISGKHEERKDeHGFVSRSFTRKYTLPPTANIekVTSSLSPEGVL 170 Poeciliopsis lu...
NP_001087283  91 GISEIRQTsdRWKISLDVNHFAPEELVVKTKDGIVEITGKHEEKQDeHGFVSRCFTRKYTLPPGVDInaVASSLSPDGIL 170 African clawed ...
232277        82 GISEIRQSadSWKVTLDVNHFAPEELVVKTKDNIVEITGKHEEKQDeHGFISRCFTRKYTLPPGVEAtaVRSSLSPDGML 161 chicken
NP_001027772  85 GMSQVTTDenKFKVTLDVKHFTPEEITVKTVDGAIEVHGKHHEKEDdHGVVSRDFTRKYTIPPNVDPltVTSSLSPDGIL 164 Ciona intestinalis
Feature 1              
P04792       164 TVEAPM 169 Homo sapiens
O13224       171 TVEAPI 176 Poeciliopsis lucida
NP_001087283 171 TVEAPL 176 African clawed frog
232277       162 TVEAPL 167 chicken
NP_001027772 165 TVEAPI 170 Ciona intestinalis

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