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HSPB11 is a component of IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20. HSPB11 is detected in the placenta.

HSPA13 belongs to the heat shock protein 70 family and is related to microsomes. Members of this protein family take part in the processing of cytosolic and secretory proteins, in addition to the exclusion of denatured or incorrectly-folded proteins. HSPA13 is known to cooperate with PLIC-1 and PLIC-2, proteins which have a role in the signaling connection between the membrane receptors for thrombospondin and the cytoskeleton.

The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization.
HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer.
Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts.
HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 having an anti-oxidative role.
NF-kappaB and HSF1 are systemically activated in human acute pancreatitis.
HSF1 activation protects against severity of pancreatitis.
HSF is a vital transcription factor which plays a role in up-regulation of VDUP1 expression through stresses such as elevated density and serum deprivation cultures.

HSP27 (also known as the Estrogen-Regulated 24K protein, and hsp 28) is a member of the mammalian small heat shock protein family. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants. Also, Hsp27 is phosphorylated in vivo on three phosphorylation sites (Ser15, Ser78 and Ser82) by protein kinases including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38).

HSP27 (also known as the Estrogen-Regulated 24K protein, and hsp 28) is a member of the mammalian small heat shock protein family. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants. Also, Hsp27 is phosphorylated in vivo on three phosphorylation sites (Ser15, Ser78 and Ser82) by protein kinases including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38).

HSF2BP, also known as HSF2 binding protein links with HSF2. This interaction takes place between the trimerization domain of HSF2 and the amino terminal hydrophilic region of HSF2BP which contains two leucine zipper motifs. Therefore, HSF2BP is involved in modulating HSF2 activation.

HSPH1 analysis is used as an indicator and as a diagnostic aid in problematic lesions.
HSPH1 chaperones the responses to endoplasmic reticulum (ER) stress during its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process.
HSPH1 is highly expressed in a variety of human tumors.
HSPH1 is a mammalian member of the HSP105/110 family, a diverged subgroup of the HSP70 family. HSP105 has 2 isoforms, alpha and beta. Hsp105a associates with Hsp70/Hsc70 as complexes in vivo and regulates the chaperone activity of Hsp70/Hsc70 negatively in vitro and in vivo.

Heat shock protein beta-2 (HSPB2) is a member of the small heat shock protein (HSP20) family. HSPB2 is a regulator of DMPK kinase.

The HSP70 family is found in many intracellular compartments such as chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variation of biological stresses, including heat stress, in every organism. HSP70 has a range of functions. For example: HSP70 acts as molecular chaperones facilitating the assembly of multi-protein complexes, HSP70 take part in the translocation of polypeptides across cell membranes and to the nucleus, and HSP70 assists in the proper folding of nascent polypeptide chains.
HSP70 is a mitochondrial import equipment and has a crucial part in the cytosolic endoplasmic reticulum. Lately, extracellular localized HSP was discovered to take an important part in the induction of a cellular immune response.

HSPB8 is part of the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. HSPB8 is induced by estrogen in estrogen receptor-positive breast cancer cells. HSPB8 protein functions as a chaperone in association with BAG3, a stimulator of macroautophagy. HSPB8 participates in the regulation of cell proliferation, apoptosis, and carcinogenesis. Mutations in HSPB8 gene have been related with different neuromuscular diseases, including Charcot-Marie-Tooth disease.

Heat Shock Protein B9 (HSPB9) is a member of the small heat shock protein (HSP20) family. HSPB9 is found in the cytoplasm as well as in the nucleus. HSPB9 is expressed specifically in the testis.

Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.

HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.

HSP90 has been identified in the cytosol, nucleus and endoplasmic reticulum, and is reported to exist in many tissue types. In several tissues, including smooth muscle, HSP90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer, assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration.

AHA1 is a cochaperone that stimulates hsp90 ATPase activity. AHSA1 binds the middle domain of Hsp90 (amino acid 272-627) and functions as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding.
AHA1 affects a step in the endoplasmic reticulum to golgi trafficking.

Hsp70-binding protein 1 (HSPBP1) is a member of a family of eukaryotic proteins identified as nucleotide exchange factors for HSP 70 that exhibit varying degrees of compartment and species specificity. HSPBP1 is localized mainly in cytoplasm and nucleus but is also found extracellularly. HSPBP1 is mostly expressed in heart and skeletal muscle .HSPBP1 binds to HSP 70, inhibits its activity and promotes dissociation of nucleotides from the HSP 70 ATPase domain. In addition, HSPBP1 inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and obstructing the ATP binding. HSPBP1 may also have a role in tumor (dys)regulation of chaperone proteins. Furthermore, HSPBP1 hinders ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.

DnaJB2 is a member of the DnaJ family. The DnaJ family is one of the largest of all the chaperone families which has evolved with diverse cellular localization and functions. DnaJB2 are important mediators of proteolysis which are involved in the regulation of protein degradation, exocytosis and endocytosis. The DnaJ proteins play a significant role in the HSP70 chaperone machine by interacting with HSP70 to stimulate ATP hydrolysis. DnaJB2 is expressed almost solely in the brain, with the highest levels in the frontal cortex and hippocampus.

Human HSP40 (heat shock protein with molecular size of 40kDa) is one of the mammalian homologues of bacterial DnaJ heat shock protein and regulates cellular processes by aiding in the folding, transport and assembly. HSP40 protein contains the J-domain which controls interaction with the ATPase domain of DnaK.

Heat Shock Factor Binding Protein 1-Like 1 (HSBP1L1) is a part of a family of eukaryotic proteins known as nucleotide exchange factors for HSP 70. HSBP1L1 is a protein coding gene whose expression is regulated mainly at the transcription level.

Heat shock prtein beta-6, also known as HSPB6 is a member of the small heat shock protein (HSP20) family. This locus encodes a heat shock protein. HSPB6 plays a role in smooth muscle relaxation. Among the diseases which are associated with HSPB6: Cerebral hemorrhage and Cerebral amyloid angiopathy.

Heat Shock Transcription Factor, Y-Linked 1 (HSFY1) is a member of the heat shock factor (HSF) family of transcriptional activators for heat shock proteins. HSFY1 is localizes to an area of chromosome Y which is from time to time deleted in infertile males and therefore is considered a gene for azoospermia. The genome has 2 identical duplicates of HSFY1 within a palindromic area.

HSP70 is a human heat shock protein. HSP-70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the HSP70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc...).

HSPA8 is part of the heat shock protein 70 family which includes both heat-inducible and constitutively expressed proteins (heat-shock cognate proteins). HSPA8 is a heat-shock cognate protein that binds to nascent polypeptides to facilitate correct folding. HSPA8 plays a role as an ATPase in the disassembly of clathrin-coated vesicles through transport of membrane components through the cell. HSPA8 is expressed in colon cancer cells, HSPA8 takes part in reovirus outer capsid disassembly, through membrane penetration, to plan the entering particle for gene expression and replication. serum HSPA8 concentrations are reduced in normal human pregnancy. HSPA8 plays a role in androgen action on dermal papilla cells. HSPA8 is directly linked with Influenza virus matrix protein 1 and thus required for viral production.

HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein.
GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.