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| | EIF2AK3 | Eukaryotic translation initiation factor 2 alpha kinase 3. (1115 aa) |
| | ERO1B | Endoplasmic reticulum oxidoreductase 1 beta. (484 aa) |
| | ERMARD | ER membrane associated RNA degradation. (678 aa) |
| | FKBP7 | Peptidylprolyl isomerase. (218 aa) |
| | CLPB | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process. (677 aa) |
| | HSPB8 | Heat shock protein beta-8; Displays temperature-dependent chaperone activity. Belongs to the small heat shock protein (HSP20) family. (196 aa) |
| | LONP1 | Lon protease homolog, mitochondrial; ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand- specific manner. May regulate mi [...] (1027 aa) |
| | PDIA6 | Protein disulfide isomerase family A member 6; Belongs to the protein disulfide isomerase family. (440 aa) |
| | SUGT1 | Protein SGT1 homolog; May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. (338 aa) |
| | DNAJC7 | DnaJ heat shock protein family (Hsp40) member C7. (494 aa) |
| | TCP1 | T-complex protein 1 subunit alpha; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (556 aa) |
| | DNAJB11 | DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. (358 aa) |
| | HSP90B1 | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family. (804 aa) |
| | DNAJA2 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (412 aa) |
| | DNAJC2 | DnaJ homolog subfamily C member 2; Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histo [...] (621 aa) |
| | UGGT2 | UDP-glucose glycoprotein glucosyltransferase 2. (1450 aa) |
| | HSPH1 | Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities. (859 aa) |
| | BAG2 | BAG family molecular chaperone regulator 2; Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. (211 aa) |
| | CEBPE | CCAAT/enhancer-binding protein. (281 aa) |
| | XBP1 | X-box-binding protein 1, cytoplasmic form; Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland. Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins. Modulates the cellular response to ER stress in a PIK3R-dependent manner. Binds to the cis-acting X box present in the promoter regions of major hist [...] (376 aa) |
| | PRDX4 | Peroxiredoxin-4; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (274 aa) |
| | DNAJB7 | J domain-containing protein. (304 aa) |
| | HSP90AA1 | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] (734 aa) |
| | CCT3 | T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (545 aa) |
| | ERP29 | Endoplasmic reticulum resident protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the ER (By similarity). (258 aa) |
| | TXNDC9 | Thioredoxin domain-containing protein 9; Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. (226 aa) |
| | SAMD13-2 | Uncharacterized protein LOC780805. (195 aa) |
| | PPP5C | Serine/threonine-protein phosphatase. (499 aa) |
| | DNAJC10 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. (793 aa) |
| | PDCL3 | Phosducin-like protein 3; Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity); Belongs to the phosducin family. (240 aa) |
| | HSPA9 | Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis probably via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. (679 aa) |
| | DNAJC3 | DnaJ homolog subfamily C member 3; Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF- 2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activi [...] (504 aa) |
| | HSPD1 | 60 kDa heat shock protein, mitochondrial; Belongs to the chaperonin (HSP60) family. (573 aa) |
| | CCT7 | T-complex protein 1 subunit eta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family. (543 aa) |
| | HSPA13 | Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (471 aa) |
| | HSPA1A | Heat shock 70 kDa protein 1A; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and AD [...] (641 aa) |
| | CHORDC1 | Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity). (332 aa) |
| | BAG3 | BCL2 associated athanogene 3. (585 aa) |
| | DNAJB12 | DnaJ homolog subfamily B member 12; Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of na [...] (377 aa) |
| | HSPA12A | Heat shock protein family A (Hsp70) member 12A. (692 aa) |
| | CCT8 | T-complex protein 1 subunit theta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (548 aa) |
| | CLPP | ATP-dependent Clp protease proteolytic subunit, mitochondrial; Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. (272 aa) |
| | DNAJC5B | DnaJ homolog subfamily C member 5B. (199 aa) |
| | HSPA4 | Heat shock protein family A (Hsp70) member 4. (840 aa) |
| | DNAJA4 | DnaJ heat shock protein family (Hsp40) member A4. (549 aa) |
| | DNAJA1 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). (397 aa) |
| | E1BMD9_BOVIN | Prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit beta family. (133 aa) |
| | ERN1 | Endoplasmic reticulum to nucleus signaling 1. (975 aa) |
| | PFDN6 | Prefoldin subunit 6; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family. (129 aa) |
| | TRIB3 | Tribbles homolog 3; Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr- 308' phosphorylation site in AKT1. Binds to ATF4 and inhibits its transcriptional activation activity. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Does not display kinase activi [...] (357 aa) |
| | PDIA4 | Protein disulfide-isomerase A4. (643 aa) |
| | VBP1 | Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). (197 aa) |
| | ATF4 | Cyclic AMP-dependent transcription factor ATF-4; Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to endoplasmic reticulum (ER) stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis [...] (348 aa) |
| | MAPT | Microtubule-associated protein. (617 aa) |
| | BAG1 | BCL2 associated athanogene 1. (237 aa) |
| | CCT5 | Chaperonin containing TCP1 subunit 5; Belongs to the TCP-1 chaperonin family. (541 aa) |
| | HSPB6 | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. (198 aa) |
| | PDIA5 | Protein disulfide-isomerase A5; Belongs to the protein disulfide isomerase family. (521 aa) |
| | STUB1 | STIP1 homology and U-box containing protein 1. (592 aa) |
| | CCT2 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (535 aa) |
| | PFDN2 | Prefoldin subunit 2; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). (154 aa) |
| | CCT6B | T-complex protein 1 subunit zeta-2; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. (531 aa) |
| | DNAJB4 | DnaJ homolog subfamily B member 4; Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (337 aa) |
| | AHSA1 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (Yeast). (338 aa) |
| | HSPA1L | Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] (641 aa) |
| | CDC37 | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. (380 aa) |
| | DNAJB1 | DnaJ homolog subfamily B member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (340 aa) |
| | PPIG | Peptidylprolyl isomerase G. (753 aa) |
| | DDIT3 | DNA damage-inducible transcript 3 protein; Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer- binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression [...] (196 aa) |
| | CCT4 | T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (542 aa) |
| | MANF | Mesencephalic astrocyte-derived neurotrophic factor; Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted b [...] (179 aa) |
| | ATF6B | Activating transcription factor 6 beta. (707 aa) |
| | DNAJC1 | DnaJ heat shock protein family (Hsp40) member C1. (542 aa) |
| | PDIA2 | Rho GDP-dissociation inhibitor 3. (736 aa) |
| | MKKS | Uncharacterized protein. (570 aa) |
| | LOC615521 | LOC615521; Belongs to the GrpE family. (194 aa) |
| | CCT8L2 | Chaperonin containing TCP1 subunit 8 like 2. (534 aa) |
| | G3X861_BOVIN | Uncharacterized protein. (545 aa) |
| | AHSA2 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity. (260 aa) |
| | HSPA6 | Heat shock protein family A (Hsp70) member 6; Belongs to the heat shock protein 70 family. (639 aa) |
| | HSPA5 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] (655 aa) |
| | ATF6 | Activating transcription factor 6. (657 aa) |
| | HSPA14 | Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). (788 aa) |
| | CRELD2 | Protein disulfide isomerase CRELD2; Protein disulfide isomerase (By similarity). Might play a role in the unfolded protein response (By similarity). May regulate transport of alpha4-beta2 neuronal acetylcholine receptor (By similarity); Belongs to the CRELD family. (351 aa) |
| | TMEM59 | Transmembrane protein 59; Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding. (334 aa) |
| | PFDN4 | Prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). (170 aa) |
| | HSPA8 | Heat shock cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] (654 aa) |
| | ENSBTAP00000058621 | Reverse transcriptase domain-containing protein. (571 aa) |
| | ENSBTAP00000058802 | Uncharacterized protein. (461 aa) |
| | HSPD1-2 | 60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] (573 aa) |
| | STIP1-2 | Stress-induced-phosphoprotein 1; Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90. (543 aa) |
| | STIP1 | Stress-induced-phosphoprotein 1. (650 aa) |
| | HSBP1 | Heat shock factor-binding protein 1; Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process (By similarity). (76 aa) |
| | LOC787679 | Uncharacterized protein. (352 aa) |
| | ENSBTAP00000060468 | Uncharacterized protein. (305 aa) |
| | ATF5 | Activating transcription factor 5. (281 aa) |
| | DNAJA1-2 | J domain-containing protein. (118 aa) |
| | ENSBTAP00000060867 | Uncharacterized protein. (204 aa) |
| | DNAJB6 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). (364 aa) |
| | EIF2A | Eukaryotic translation initiation factor 2A; Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl- tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. (596 aa) |
| | HERPUD1 | Homocysteine inducible ER protein with ubiquitin like domain 1. (389 aa) |
| | PFDN5 | Prefoldin subunit 5; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC (By similarity). (154 aa) |
| | HSPA2 | Heat shock-related 70 kDa protein 2; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis [...] (636 aa) |
| | HSF1 | Heat shock factor protein 1; Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non- DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcriptio [...] (553 aa) |
| | ENSBTAP00000063686 | Uncharacterized protein. (247 aa) |
| | ENSBTAP00000063738 | Uncharacterized protein. (76 aa) |
| | TXNDC5 | Uncharacterized protein. (437 aa) |
| | HSPA4L | Heat shock protein family A (Hsp70) member 4 like. (1013 aa) |
| | ENSBTAP00000064525 | Uncharacterized protein. (121 aa) |
| | PFDN1 | Prefoldin subunit 1; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family. (122 aa) |
| | LOC618367 | LRAT domain-containing protein. (188 aa) |
| | SDF2L1 | Stromal cell-derived factor 2-like protein 1. (337 aa) |
| | ENSBTAP00000065570 | Reverse transcriptase domain-containing protein. (568 aa) |
| | ERP44 | Endoplasmic reticulum resident protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). (419 aa) |
| | ENSBTAP00000065941 | Reverse transcriptase domain-containing protein. (544 aa) |
| | ENSBTAP00000066216 | Uncharacterized protein. (307 aa) |
| | ENSBTAP00000066311 | Uncharacterized protein. (98 aa) |
| | WFS1 | Wolframin ER transmembrane glycoprotein. (888 aa) |
| | HSPE1 | 10 kDa heat shock protein, mitochondrial; Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per [...] (259 aa) |
| | DNAJA3 | Uncharacterized protein. (480 aa) |
| | ENSBTAP00000067980 | Uncharacterized protein; Belongs to the GroES chaperonin family. (101 aa) |
| | ENSBTAP00000068131 | J domain-containing protein. (397 aa) |
| | ENSBTAP00000068449 | Reverse transcriptase domain-containing protein. (424 aa) |
| | HSPBP1 | HSPA (Heat shock 70kDa) binding protein, cytoplasmic cochaperone 1. (357 aa) |
| | ENSBTAP00000068590 | Uncharacterized protein. (85 aa) |
| | ENSBTAP00000069080 | J domain-containing protein. (98 aa) |
| | CCT6A | T-complex protein 1 subunit zeta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. (531 aa) |
| | ENSBTAP00000069485 | Reverse transcriptase domain-containing protein. (512 aa) |
| | ENSBTAP00000069551 | Uncharacterized protein; Belongs to the TCP-1 chaperonin family. (128 aa) |
| | ENSBTAP00000070818 | Reverse transcriptase domain-containing protein. (563 aa) |
| | ANKRD45 | Ankyrin repeat domain 45. (261 aa) |
| | HSP90AB1 | Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] (724 aa) |
| | HSPA12B | Uncharacterized protein. (686 aa) |
| | TRAP1 | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. (706 aa) |
| | ERO1A | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate recep [...] (469 aa) |
| | CLPX | Caseinolytic mitochondrial matrix peptidase chaperone subunit. (690 aa) |
| | ENSBTAP00000074241 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. (793 aa) |
| | ENSBTAP00000074307 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. (440 aa) |
| | ENSBTAP00000074523 | TPR_REGION domain-containing protein. (229 aa) |
| | HYOU1 | Hypoxia up-regulated 1. (1021 aa) |
