alpha-crystallin A chain isoform 1 [Homo sapiens]
Hsp20/alpha crystallin family protein; p23/wos2 family protein( domain architecture ID 10455210)
Hsp20/alpha crystallin family protein is a small, stress-induced protein, between 12-43 kDa, which functions as an ATP-independent chaperone that prevents aggregation and protects against cell stress, induced by heat, osmotic, or acid shock| p23/wos2 family protein similar to Arabidopsis thaliana co-chaperone protein p23, Saccharomyces cerevisiae Sba1 and Schizosaccharomyces pombe protein wos2
List of domain hits
Name | Accession | Description | Interval | E-value | |||
ACD_alphaA-crystallin_HspB4 | cd06497 | Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, ... |
60-145 | 1.13e-58 | |||
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract. : Pssm-ID: 107245 Cd Length: 86 Bit Score: 177.88 E-value: 1.13e-58
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Crystallin | pfam00525 | Alpha crystallin A chain, N terminal; |
1-54 | 1.19e-25 | |||
Alpha crystallin A chain, N terminal; : Pssm-ID: 425732 Cd Length: 56 Bit Score: 92.86 E-value: 1.19e-25
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Name | Accession | Description | Interval | E-value | |||
ACD_alphaA-crystallin_HspB4 | cd06497 | Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, ... |
60-145 | 1.13e-58 | |||
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract. Pssm-ID: 107245 Cd Length: 86 Bit Score: 177.88 E-value: 1.13e-58
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Crystallin | pfam00525 | Alpha crystallin A chain, N terminal; |
1-54 | 1.19e-25 | |||
Alpha crystallin A chain, N terminal; Pssm-ID: 425732 Cd Length: 56 Bit Score: 92.86 E-value: 1.19e-25
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HSP20 | pfam00011 | Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ... |
63-162 | 1.32e-24 | |||
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts. Pssm-ID: 459629 Cd Length: 100 Bit Score: 91.52 E-value: 1.32e-24
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IbpA | COG0071 | Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ... |
69-140 | 3.17e-10 | |||
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 439841 Cd Length: 105 Bit Score: 54.39 E-value: 3.17e-10
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Name | Accession | Description | Interval | E-value | |||
ACD_alphaA-crystallin_HspB4 | cd06497 | Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, ... |
60-145 | 1.13e-58 | |||
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract. Pssm-ID: 107245 Cd Length: 86 Bit Score: 177.88 E-value: 1.13e-58
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ACD_HspB4-5-6 | cd06478 | Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the ... |
63-145 | 5.91e-52 | |||
Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the small heat shock protein (sHsp) HspB6, also known as Hsp20. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 on the other hand is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. HspB5's functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy. Mutations in HspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). HspB6 (Hsp20) is ubiquitous and is involved in diverse functions including regulation of glucose transport and contraction of smooth muscle, in platelet aggregation, in cardioprotection, and in the prevention of apoptosis. It interacts with the universal scaffolding and adaptor protein 14-3-3, and also with the proapoptotic protein Bax. Pssm-ID: 107233 Cd Length: 83 Bit Score: 160.69 E-value: 5.91e-52
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metazoan_ACD | cd06526 | Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ... |
63-145 | 4.70e-41 | |||
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. Pssm-ID: 107247 Cd Length: 83 Bit Score: 133.03 E-value: 4.70e-41
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ACD_alphaB-crystallin_HspB5 | cd06498 | Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, ... |
63-145 | 1.81e-39 | |||
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. HspB4 does not belong to this group. HspB5 shows increased synthesis in response to stress. HspB5 is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. Its functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy. Pssm-ID: 107246 [Multi-domain] Cd Length: 84 Bit Score: 128.98 E-value: 1.81e-39
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ACD_HspB1_like | cd06475 | Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also ... |
60-144 | 2.48e-36 | |||
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. Pssm-ID: 107230 Cd Length: 86 Bit Score: 121.11 E-value: 2.48e-36
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Crystallin | pfam00525 | Alpha crystallin A chain, N terminal; |
1-54 | 1.19e-25 | |||
Alpha crystallin A chain, N terminal; Pssm-ID: 425732 Cd Length: 56 Bit Score: 92.86 E-value: 1.19e-25
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HSP20 | pfam00011 | Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ... |
63-162 | 1.32e-24 | |||
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts. Pssm-ID: 459629 Cd Length: 100 Bit Score: 91.52 E-value: 1.32e-24
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ACD_sHsps-like | cd06464 | Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ... |
63-145 | 1.73e-22 | |||
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. Pssm-ID: 107221 Cd Length: 88 Bit Score: 85.68 E-value: 1.73e-22
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ACD_HspB2_like | cd06476 | Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB2/heat ... |
64-145 | 2.32e-22 | |||
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB2/heat shock 27kDa protein 2 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. HspB2 is preferentially and constitutively expressed in skeletal muscle and heart. HspB2 shows homooligomeric activity and forms aggregates in muscle cytosol. Although its expression is not induced by heat shock, it redistributes to the insoluble fraction in response to heat shock. In the mouse heart, HspB2 plays a role in maintaining energetic balance, by protecting cardiac energetics during ischemia/reperfusion, and allowing for increased work during acute inotropic challenge. hHspB2 [previously also known as myotonic dystrophy protein kinase (DMPK) binding protein (MKBP)] is selectively up-regulated in skeletal muscles from myotonic dystrophy patients. The ACD of hHspB2 binds the DMPK kinase domain. In vitro, hHspB2 enhances the kinase activity of DMPK and confers thermoresistance. The hHspB2 gene lies less than 1kb from the 5 prime end of the related alphaB (HspB4)-crystallin gene, with the opposite transcription direction. These two genes may share regulatory elements for their expression. Pssm-ID: 107231 Cd Length: 83 Bit Score: 85.36 E-value: 2.32e-22
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ACD_sHsps_p23-like | cd00298 | This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ... |
67-145 | 9.44e-19 | |||
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Pssm-ID: 107219 Cd Length: 80 Bit Score: 76.09 E-value: 9.44e-19
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ACD_HspB9_like | cd06481 | Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 and ... |
69-144 | 7.19e-17 | |||
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 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. Human (h) HspB9 is expressed exclusively in the normal testis and in various tumor samples and is a cancer/testis antigen. hHspB9 interacts with TCTEL1 (T-complex testis expressed protein -1), a subunit of dynein. hHspB9 and TCTEL1 are co-expressed in similar cells within the testis and in tumor cells. Included in this group is Xenopus Hsp30, a developmentally-regulated heat-inducible molecular chaperone. Pssm-ID: 107236 Cd Length: 87 Bit Score: 71.28 E-value: 7.19e-17
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ACD_HspB3_Like | cd06477 | Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein ... |
65-139 | 6.61e-16 | |||
Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein 27-like protein (HSPL27, 17-kDa) 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. HspB3 is expressed in adult skeletal muscle, smooth muscle, and heart, and in several other fetal tissues. In muscle cells HspB3 forms an oligomeric 150 kDa complex with myotonic dystrophy protein kinase-binding protein (MKBP/ HspB2), this complex may comprise one of two independent muscle-cell specific chaperone systems. The expression of HspB3 is induced during muscle differentiation controlled by the myogenic factor MyoD. HspB3 may also interact with Hsp22 (HspB8). Pssm-ID: 107232 Cd Length: 83 Bit Score: 68.68 E-value: 6.61e-16
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ACD_HspB8_like | cd06480 | Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) ... |
75-145 | 1.31e-15 | |||
Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) HspB8, also denoted as Hsp22 in humans, 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. A chaperone complex formed of HspB8 and Bag3 stimulates degradation of protein complexes by macroautophagy. HspB8 also forms complexes with Hsp27 (HspB1), MKBP (HspB2), HspB3, alphaB-crystallin (HspB5), Hsp20 (HspB6), and cvHsp (HspB7). These latter interactions may depend on phosphorylation of the respective partner sHsp. HspB8 may participate in the regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis. Point mutations in HspB8 have been correlated with the development of several congenital neurological diseases, including Charcot Marie tooth disease and distal motor neuropathy type II. Pssm-ID: 107235 Cd Length: 91 Bit Score: 68.05 E-value: 1.31e-15
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IbpA | COG0071 | Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ... |
69-140 | 3.17e-10 | |||
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 439841 Cd Length: 105 Bit Score: 54.39 E-value: 3.17e-10
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ACD_HspB7_like | cd06479 | Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also ... |
64-140 | 5.57e-09 | |||
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), 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. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies. Pssm-ID: 107234 Cd Length: 81 Bit Score: 50.69 E-value: 5.57e-09
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ACD_IbpA-B_like | cd06470 | Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ... |
64-124 | 3.50e-05 | |||
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers. Pssm-ID: 107227 Cd Length: 90 Bit Score: 40.59 E-value: 3.50e-05
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ACD_ScHsp26_like | cd06472 | Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ... |
69-145 | 5.37e-04 | |||
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 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. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers. Pssm-ID: 107229 Cd Length: 92 Bit Score: 37.28 E-value: 5.37e-04
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ACD_HspB10 | cd06482 | Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB10, also ... |
67-136 | 1.25e-03 | |||
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB10, also known as sperm outer dense fiber protein (ODFP), 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. Human (h) HspB10 occurs exclusively in the axoneme of sperm cells and may have a cytoskeletal role. Pssm-ID: 107237 Cd Length: 87 Bit Score: 36.40 E-value: 1.25e-03
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Blast search parameters | ||||
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