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| | Scg5 | Neuroendocrine protein 7B2; Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro; Belongs to the 7B2 family. (210 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. (539 aa) |
| | Hspb2 | Heat shock protein beta-2; May regulate the kinase DMPK. (182 aa) |
| | Cct5 | T-complex protein 1 subunit epsilon; 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. (541 aa) |
| | Cdc37l1 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90. (335 aa) |
| | Dnaja4 | DnaJ heat shock protein family (Hsp40) member A4. (555 aa) |
| | Ccdc115 | Similar to 2310061I09Rik protein (Predicted). (180 aa) |
| | Pfdn5 | Prefoldin 5 (Predicted), isoform CRA_a. (154 aa) |
| | Erlec1 | Endoplasmic reticulum lectin 1. (482 aa) |
| | Hspa8 | Heat shock cognate 71 kDa protein; Belongs to the heat shock protein 70 family. (645 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). (357 aa) |
| | Canx | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at t [...] (591 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. (804 aa) |
| | Hspb1 | Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. (206 aa) |
| | Dnajb1 | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. (371 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) |
| | Syvn1 | Synovial apoptosis inhibitor 1, synoviolin, isoform CRA_b. (612 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. (162 aa) |
| | Tomm20 | Mitochondrial import receptor subunit TOM20 homolog; Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases. Belongs to the Tom20 family. (145 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) |
| | 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 via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. (679 aa) |
| | St13 | Hsc70-interacting protein; One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. Belongs to the FAM10 family. (368 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) |
| | Tapbp | Tap-binding protein (Tapasin). (464 aa) |
| | Dnajb8 | DnaJ heat shock protein family (Hsp40) member B8. (235 aa) |
| | Clpx | ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial; ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5- aminolevulinate (ALA) synthesis, the first step in h [...] (633 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. (378 aa) |
| | Shq1 | SHQ1, H/ACA ribonucleoprotein assembly factor. (603 aa) |
| | Cryab | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions; Belongs to the small heat shock protein (HSP20) family. (175 aa) |
| | LOC680121 | 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 [...] (646 aa) |
| | Dnajb7 | DnaJ heat shock protein family (Hsp40) member B7. (303 aa) |
| | Calr4 | Calreticulin. (439 aa) |
| | Tor1a | Torsin-1A; Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular traffickin [...] (333 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) |
| | 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; Belongs to the prefoldin subunit beta family. (139 aa) |
| | Cryaa | Alpha-crystallin A(1-151); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. (196 aa) |
| | Naca | Nascent polypeptide-associated complex subunit alpha. (2163 aa) |
| | LOC102553845 | Chaperonin-containing TCP1, subunit 8 (theta)-like 1. (561 aa) |
| | Cct8l1 | Chaperonin containing TCP1, subunit 8 (theta)-like 1. (561 aa) |
| | M0RCB1_RAT | Uncharacterized protein; Belongs to the heat shock protein 70 family. (641 aa) |
| | Pet100 | PET100 cytochrome c oxidase chaperone. (76 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) |
| | 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 [...] (89 aa) |
| | A0A0G2JVI0_RAT | Uncharacterized protein; Belongs to the GroES chaperonin family. (102 aa) |
| | Nudcd2 | NudC domain-containing protein 2; May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. (157 aa) |
| | Calr | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. (416 aa) |
| | Ptges3 | Prostaglandin E synthase 3; Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (By similarity). (160 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) |
| | Cct8 | Chaperonin subunit 8 (Theta) (Predicted), isoform CRA_a. (548 aa) |
| | Cct6a | Chaperonin containing Tcp1, subunit 6A (Zeta 1). (531 aa) |
| | Aip | AH receptor-interacting protein; May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting. (330 aa) |
| | Calr3 | Calreticulin. (379 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) |
| | Uggt1 | UDP-glucose:glycoprotein glucosyltransferase 1; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Belongs to the glycosyltransferase 8 family. (1551 aa) |
| | Heatr3 | HEAT repeat-containing 3. (682 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). (509 aa) |
| | Cct7 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (544 aa) |
| | Tmem67 | Meckelin; Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (sftpc) (By similarity). (997 aa) |
| | Samd13 | Sterile alpha motif domain-containing 13. (223 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) |
| | Serpinh1 | Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. (417 aa) |
| | Dnajb13 | DnaJ (Hsp40) related, subfamily B, member 13, isoform CRA_a. (316 aa) |
| | Dnajb3 | DnaJ heat shock protein family (Hsp40) member B3. (241 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 [...] (654 aa) |
| | Pfdn1 | Prefoldin 1 (Predicted). (122 aa) |
| | Ern2 | Endoplasmic reticulum (ER) to nucleus signalling 2 (Predicted). (927 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 [...] (633 aa) |
| | Ssuh2 | Ssu-2 homolog. (319 aa) |
| | Ndufaf1 | NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, assembly factor 1 (Predicted), isoform CRA_a. (328 aa) |
| | Npm1 | Nucleophosmin; Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. M [...] (292 aa) |
| | Mkks | McKusick-Kaufman syndrome protein, isoform CRA_b. (570 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) |
| | Pfdn6 | MHC class II region expressed gene KE2, isoform CRA_a. (127 aa) |
| | Hsp90aa1 | Heat shock protein 90 alpha family class A member 1. (733 aa) |
| | Hspa1b | Heat shock protein family A (Hsp70) member 1B. (641 aa) |
| | Dnajb4 | DnaJ (Hsp40) homolog, subfamily B, member 4, isoform CRA_a. (337 aa) |
| | Dnajb5 | DnaJ heat shock protein family (Hsp40) member B5. (420 aa) |
| | Dnajb2 | DnaJ heat shock protein family (Hsp40) member B2. (277 aa) |
| | Nacad | NAC alpha domain-containing. (1416 aa) |
| | Nudc | Nuclear migration protein nudC; Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity); Belongs to the nudC family. (332 aa) |
| | Dnaja3 | DnaJ heat shock protein family (Hsp40) member A3. (480 aa) |
| | Ern1 | Similar to protein kinase/endoribonuclease(IRE1) alpha (Predicted), isoform CRA_a. (977 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) |
| | Clu | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysos [...] (447 aa) |
| | Nudcd3 | NudC domain-containing 3. (183 aa) |
| | LOC100911422 | Nuclear migration protein nudC-like. (279 aa) |
| | Grpel1 | GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins; Belongs to the GrpE family. (230 aa) |
| | Hspa13 | Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (471 aa) |
| | LOC103692716 | 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 [...] (733 aa) |
| | Cct6b | Chaperonin containing Tcp1, subunit 6B (Zeta 2). (531 aa) |
| | Clgn | Calmegin. (611 aa) |
| | Dnaja1 | DnaJ homolog subfamily A member 1; 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. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. (397 aa) |
