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| | Rbbp7 | Histone-binding protein RBBP7; Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and [...] (425 aa) |
| | Psmd10 | 26S proteasome non-ATPase regulatory subunit 10; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. (231 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) |
| | Cotl1 | Coactosin-like protein; Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). (142 aa) |
| | Ccs | Copper chaperone for superoxide dismutase; Delivers copper to copper zinc superoxide dismutase (SOD1). (274 aa) |
| | Pdia2 | Protein disulfide-isomerase A2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity). (527 aa) |
| | Nploc4 | Nuclear protein localization protein 4 homolog; The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and UFD1, which binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination [...] (608 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) |
| | Hspb8 | Heat shock protein beta-8; Displays temperature-dependent chaperone activity; Belongs to the small heat shock protein (HSP20) family. (196 aa) |
| | Rsad1 | Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl- L-methionine (By similarity). (442 aa) |
| | Ankrd13c | Ankyrin repeat domain-containing protein 13C; Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER. (541 aa) |
| | Tbca | Tubulin-specific chaperone A; Tubulin-folding protein; involved in the early step of the tubulin folding pathway; Belongs to the TBCA family. (108 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) |
| | Cybc1 | Cytochrome b-245 chaperone 1; Necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 heterodimer. Controls the phagocyte respiratory burst and is essential for innate immunity. Belongs to the CYBC1 family. (187 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. (210 aa) |
| | Dnajc17 | DnaJ homolog subfamily C member 17; May negatively affect PAX8-induced thyroglobulin/TG transcription. (303 aa) |
| | Sgtb | Small glutamine-rich tetratricopeptide repeat-containing protein beta; Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity; Belongs to the SGT family. (304 aa) |
| | Dnajc12 | DnaJ homolog subfamily C member 12. (198 aa) |
| | Sdhaf3 | Succinate dehydrogenase assembly factor 3, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1. (125 aa) |
| | Timm8b | Mitochondrial import inner membrane translocase subunit Tim8 B; Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity); Belongs to the small Tim family. (83 aa) |
| | Atpaf2 | ATP synthase mitochondrial F1 complex assembly factor 2; May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase). (298 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. (532 aa) |
| | Hspe1-rs1 | Heat shock protein 1 (chaperonin 10),-related sequence 1; Belongs to the GroES chaperonin family. (102 aa) |
| | Sco2 | Protein SCO2 homolog, mitochondrial; Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2. Belongs to the SCO1/2 family. (255 aa) |
| | Dnajc15 | DnaJ homolog subfamily C member 15; Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9 (By similarity). Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP. (149 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) |
| | 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. (175 aa) |
| | Dnajb13 | DnaJ homolog subfamily B member 13; Plays a role in the formation of the central complex of ciliary and flagellar axonemes. (316 aa) |
| | Nap1l4 | Nucleosome assembly protein 1-like 4; Acts as histone chaperone in nucleosome assembly. In condensing spermatids, mediates the loading of the heterodimer composed of histones H2AB1 and H2BC1/TH2B onto the nucleosomes, thereby promoting the replacement of histones to protamine in male germ cells. (386 aa) |
| | Hspa4l | Heat shock 70 kDa protein 4L; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. (838 aa) |
| | Dnajb2 | DnaJ homolog subfamily B member 2; Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family. In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins. Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes. Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER- associated protein de [...] (324 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) |
| | Mdn1 | Midasin; Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits; Belongs to the midasin family. (5582 aa) |
| | Dnajc4 | DnaJ homolog subfamily C member 4. (244 aa) |
| | Hspa1b | Heat shock 70 kDa protein 1B; 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 [...] (642 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) |
| | Dnajc28 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone. (409 aa) |
| | Ndufaf2 | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2; Acts as a molecular chaperone for mitochondrial complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. (168 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 (By similarity). (371 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. 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). 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. (397 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) |
| | Daxx | Death domain-associated protein 6; Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 throu [...] (740 aa) |
| | Anp32e | Acidic leucine-rich nuclear phosphoprotein 32 family member E; Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state. Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar [...] (260 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) |
| | Serpinh1 | Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. (417 aa) |
| | Dnajc1 | DnaJ homolog subfamily C member 1; May modulate protein synthesis. (552 aa) |
| | Timm9 | Mitochondrial import inner membrane translocase subunit Tim9; Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity); Belongs to the small Tim family. (89 aa) |
| | Hyou1 | Hypoxia up-regulated protein 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (By similarity). (999 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 [...] (376 aa) |
| | Lyrm7 | Complex III assembly factor LYRM7; Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane (By similarity). (104 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. (154 aa) |
| | Dnajc21 | DnaJ homolog subfamily C member 21; May act as a co-chaperone for HSP70. May play a role in ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S subunit. Binds the precursor 45S rRNA. (531 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) |
| | Psmg4 | Proteasome assembly chaperone 4; Chaperone protein which promotes assembly of the 20S proteasome; Belongs to the PSMG4 family. (123 aa) |
| | Uxt | Protein UXT; Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription. Together with URI1, associates with chromatin to the NKX3-1 promoter region. Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm. May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity. Potential component of mitochondrial-associated LRPPRC, a multidomain orga [...] (157 aa) |
| | Dnajc5b | DnaJ homolog subfamily C member 5B. (199 aa) |
| | Dnajb3 | DnaJ homolog subfamily B member 3; May operate as a co-chaperone of the male germ cell- and haploid stage-specific Hsp70 proteins. (242 aa) |
| | Gm21987 | Cytochrome c oxidase copper chaperone; Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2). (63 aa) |
| | Lmf1 | Lipase maturation factor 1; Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL. (574 aa) |
| | Fkbp5 | Peptidyl-prolyl cis-trans isomerase FKBP5; Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. (456 aa) |
| | Tsc1 | Hamartin; In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity). Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1. Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity. Competes with the activating co-chaperone AH [...] (1161 aa) |
| | Pdcl | Phosducin-like protein; Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers. Acts also as a positive regulator of hedgehog signaling and regulates ciliary function ; Belongs to the phosducin family. (301 aa) |
| | Mkks | McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin; Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis (By similarity). Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (By similarity). (570 aa) |
| | Atox1 | Copper transport protein ATOX1; Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense (By similarity); Belongs to the ATX1 family. (68 aa) |
| | Spata5 | ATPase family protein 2 homolog; ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (By similarity). May be involved in morphological and functional mitochondrial transformations during spermatogenesis. (893 aa) |
| | Tsacc | TSSK6-activating co-chaperone protein; Co-chaperone that facilitates HSP-mediated activation of TSSK6. (124 aa) |
| | Dnajc6 | Putative tyrosine-protein phosphatase auxilin; Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin- mediated endocytosis in neurons. (968 aa) |
| | Ppih | Peptidyl-prolyl cis-trans isomerase H; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. Belongs to the cyclophilin-type PPIase family. PPIase H subfamily. (188 aa) |
| | Park7 | Protein/nucleic acid deglycase DJ-1; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminoca [...] (189 aa) |
| | Dnajb7 | DnaJ homolog subfamily B member 7; Probably acts as a co-chaperone. (312 aa) |
| | Anp32b | Acidic leucine-rich nuclear phosphoprotein 32 family member B; Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome (By similarity); Belongs to the ANP32 family. (272 aa) |
| | Set | Protein SET; Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF- mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysi [...] (289 aa) |
| | Hspb7 | Heat shock protein beta-7. (169 aa) |
| | Tbcd | Tubulin-specific chaperone D; Tubulin-folding protein implicated in the first step of the tubulin folding pathway and required for tubulin complex assembly. Involved in the regulation of microtubule polymerization or depolymerization, it modulates microtubule dynamics by capturing GTP- bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Acts as a GTPase-activating protein (GAP) for ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes ep [...] (1196 aa) |
| | Psmd9 | 26S proteasome non-ATPase regulatory subunit 9; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process (By similarity); Belongs to the proteasome subunit p27 family. (222 aa) |
| | Sdhaf1 | Succinate dehydrogenase assembly factor 1, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDH [...] (118 aa) |
| | Cd74 | H-2 class II histocompatibility antigen gamma chain; Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Enhance also the stimulation of T-cell responses through interaction with CD44. (279 aa) |
| | Dnajc30 | DnaJ homolog subfamily C member 30, mitochondrial; Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration. Associates with the ATP synthase complex and facilitates ATP synthesis. (219 aa) |
| | Dnajc25 | DnaJ homolog subfamily C member 25; Belongs to the DNAJC25 family. (357 aa) |
| | Dnajc8 | DnaJ homolog subfamily C member 8; Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells. (253 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 [...] (733 aa) |
| | Mesd | LRP chaperone MESD; Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell- surface expression of LRP4. May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells. Belongs to the MESD family. (224 aa) |
| | Sco1 | Protein SCO1 homolog, mitochondrial; Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT- CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (By similarity). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 ; Belongs to the SCO1/2 family. (284 aa) |
| | Dnajb14 | DnaJ homolog subfamily B member 14; 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 DNAJB12, 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 [...] (379 aa) |
| | Sacs | Sacsin; Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. (768 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) |
| | Dnajb5 | DnaJ homolog subfamily B member 5. (348 aa) |
| | Alyref2 | Aly/REF export factor 2; Export adapter involved in spliced and unspliced mRNA nuclear export. Binds mRNA which is transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway); enhances NXF1-NXT1 RNA-binding activity. (218 aa) |
| | Abce1 | ATP-binding cassette sub-family E member 1; Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'- linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway (By similarity); Belongs to the ABC transporter superfamily. ABCE family. (599 aa) |
| | Mrpl18 | 39S ribosomal protein L18, mitochondrial; Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA (By similarity). (180 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) |
| | 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 [...] (102 aa) |
| | Dnajc5 | DnaJ homolog subfamily C member 5; Acts as a co-chaperone for the SNARE protein SNAP-25. Involved in the calcium-mediated control of a late stage of exocytosis. Acts as a general chaperone in regulated exocytosis (By similarity). May have an important role in presynaptic function (By similarity). May be involved in calcium- dependent neurotransmitter release at nerve endings (By similarity). (198 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. (134 aa) |
| | Dnaja4 | DnaJ homolog subfamily A member 4. (397 aa) |
| | Npm3 | Nucleoplasmin-3; Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning. Modulates the histone chaperone function and the RNA- binding activity of nucleolar phosphoprotein B23/NPM. Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM. (175 aa) |
| | Hscb | Iron-sulfur cluster co-chaperone protein HscB, mitochondrial; Acts as a co-chaperone in iron-sulfur cluster assembly in both mitochondria and the cytoplasm. Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain. Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20. Also mediates complex formation between components o [...] (234 aa) |
| | Cdc37l1 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90; Belongs to the CDC37 family. (335 aa) |
| | C1galt1c1 | C1GALT1-specific chaperone 1; Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3- galactosyltransferase (C1GALT1) (By similarity). (316 aa) |
| | Npm2 | Nucleoplasmin-2; Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. (207 aa) |
| | Dnajb8 | DnaJ homolog subfamily B member 8; Efficient suppressor of aggregation and toxicity of disease- associated polyglutamine proteins. (227 aa) |
| | Dnajc22 | DnaJ homolog subfamily C member 22; May function as a co-chaperone. (339 aa) |
| | Hjurp | Holliday junction recognition protein; Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions. (667 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) |
| | Dnaja3 | DnaJ homolog subfamily A member 3, mitochondrial; Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity (By similarity). Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway. (480 aa) |
| | Grpel2 | GrpE protein homolog 2, 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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70; Belongs to the GrpE family. (224 aa) |
| | Pdia6 | Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (By similarity). May also regulate the UPR via the EIF2AK3 UPR sensor (By similarity). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). Belongs to the protein disulfide isomerase family. (445 aa) |
| | Dnajc11 | DnaJ homolog subfamily C member 11; Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex. Belongs to the DNAJC11 family. (559 aa) |
| | Bag5 | BAG family molecular chaperone regulator 5; May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity). (447 aa) |
| | Cnpy3 | Protein canopy homolog 3; Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses. (276 aa) |
| | Timm8a1 | Mitochondrial import inner membrane translocase subunit Tim8 A; Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8- TIMM13 complex mediates the import of proteins [...] (97 aa) |
| | Bbs10 | Bardet-Biedl syndrome 10 protein homolog; Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. (713 aa) |
| | Mmaa | Methylmalonic aciduria type A homolog, mitochondrial; GTPase, binds and hydrolyzes GTP. Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis. Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT) and reactivation of the enzyme during catalysis. Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB subfamily. (415 aa) |
| | Tbcc | Tubulin-specific chaperone C; Tubulin-folding protein; involved in the final step of the tubulin folding pathway. (341 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) |
| | 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). (331 aa) |
| | Supt6 | Transcription elongation factor SPT6; Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C- terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex [...] (1726 aa) |
| | Clgn | Calmegin; Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions. Belongs to the calreticulin family. (611 aa) |
| | Chaf1a | Chromatin assembly factor 1 subunit A; Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly [...] (911 aa) |
| | Timmdc1 | Complex I assembly factor TIMMDC1, mitochondrial; Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity). (285 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 (By similarity); Belongs to the calreticulin family. (416 aa) |
| | Sgta | Small glutamine-rich tetratricopeptide repeat-containing protein alpha; Co-chaperone that binds misfolded and hydrophobic patches- containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in [...] (315 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 (By similarity). (209 aa) |
| | Asf1b | Histone chaperone ASF1B; Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. (202 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) |
| | 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) |
| | Tbcb | Tubulin-folding cofactor B; Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer (By similarity). Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth ; Belongs to the TBCB family. (244 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). (365 aa) |
| | Dnajc19 | Mitochondrial import inner membrane translocase subunit TIM14; Probable 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. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity); Belongs to the TIM14 family. (157 aa) |
| | Dnajc7 | DnaJ homolog subfamily C member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes (By similarity). Recruits NR1I3 to the cytoplasm. (494 aa) |
| | Dnajb9 | DnaJ homolog subfamily B member 9; Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also invol [...] (222 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 [...] (634 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 [...] (646 aa) |
| | Tomm34 | Mitochondrial import receptor subunit TOM34; Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state (By similarity). (309 aa) |
| | Unc45b | Protein unc-45 homolog B; Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development. Is necessary for normal early lens development (By similarity). (929 aa) |
| | Cryaa | Alpha-crystallin A chain; 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). (196 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 (By similarity); Belongs to the CDC37 family. (379 aa) |
| | Rcn3 | Reticulocalbin-3; Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant- associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3. By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis. Has an anti-fibrotic activity by negatively regulating the secretion of type [...] (328 aa) |
| | Calr3 | Calreticulin-3; CALR3 capacity for calcium-binding may be absent or much lower than that of CALR (By similarity). During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility. (380 aa) |
| | Sec63 | Translocation protein SEC63 homolog; Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER). Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen (By similarity). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane [...] (760 aa) |
| | Asf1a | Histone chaperone ASF1A; Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. Belongs to the ASF1 family. (204 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) (By similarity). Has ATPase activity ; Belongs to the heat shock protein 90 family. (802 aa) |
| | Timm13 | Mitochondrial import inner membrane translocase subunit Tim13; Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8- TIMM13 complex mediates the import of proteins [...] (95 aa) |
| | Ahsa2 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity. Belongs to the AHA1 family. (331 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; Belongs to the TCP-1 chaperonin family. (531 aa) |
| | Ahsa1 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co- chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. (338 aa) |
| | Btf3 | Transcription factor BTF3; When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription (By similarity); Belongs to the NAC-beta family. (204 aa) |
| | Dnajc9 | DnaJ homolog subfamily C member 9; May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8. (259 aa) |
| | Clu | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins (By similarity). 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 [...] (448 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) |
| | 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) |
| | Psmg1 | Proteasome assembly chaperone 1; Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). (289 aa) |
| | 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. (212 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) |
| | 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). (127 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) |
| | Dnajc18 | DnaJ homolog subfamily C member 18. (357 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 (By similarity). Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. Belongs to the heat shock protein 70 family. (679 aa) |
| | Bag6 | Large proline-rich protein BAG6; ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endo [...] (1154 aa) |
| | Psmg2 | Proteasome assembly chaperone 2; Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). (264 aa) |
| | Sdhaf2 | Succinate dehydrogenase assembly factor 2, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer; Belongs to the SDHAF2 family. (164 aa) |
| | P4hb | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] (509 aa) |
| | Alyref | THO complex subunit 4; Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription- independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a regio [...] (255 aa) |
| | Dnajc14 | DnaJ homolog subfamily C member 14; Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. (703 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) |
| | Hspd1 | 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) |
| | 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. 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) |
| | Sdhaf4 | Succinate dehydrogenase assembly factor 4, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit Sdha in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron [...] (104 aa) |
| | Bcs1l | Mitochondrial chaperone BCS1; Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity). (418 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). Belongs to the heat shock protein 70 family. (509 aa) |
| | Tor1b | Torsin-1B; May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non- neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. (336 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) |
| | Hspa5 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. 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. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimeriz [...] (655 aa) |
| | Psmd5 | 26S proteasome non-ATPase regulatory subunit 5; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5 (By similarity). (504 aa) |
| | Dnlz | DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. (177 aa) |
| | Timm10 | Mitochondrial import inner membrane translocase subunit Tim10; Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity); Belongs to the small Tim family. (90 aa) |
| | Ndufaf1 | Complex I intermediate-associated protein 30, mitochondrial; Chaperone protein involved in early stages of the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). (330 aa) |
| | Pdrg1 | P53 and DNA damage-regulated protein 1; May play a role in chaperone-mediated protein folding. Belongs to the prefoldin subunit beta family. (133 aa) |
| | Ppid | Peptidyl-prolyl cis-trans isomerase D; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor co [...] (370 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). (406 aa) |
| | Bag1 | BAG family molecular chaperone regulator 1; 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. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate- binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death [...] (355 aa) |
| | Calr4 | Calreticulin. (420 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) |
| | 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 (By similarity). (217 aa) |
| | Psmg3 | Proteasome assembly chaperone 3; Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes; Belongs to the PSMG3 family. (122 aa) |
| | Pomp | Proteasome maturation protein; Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation (By similarity). Mediates the association of 20S preproteasome with the endoplasmic reticulum (By similarity). (141 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. (544 aa) |
| | Fkbp4 | Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May [...] (458 aa) |
| | Unc45a | Protein unc-45 homolog A; May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen. (944 aa) |
| | Tmem126b | Complex I assembly factor TMEM126B, mitochondrial; Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity). (230 aa) |
| | Bag3 | BAG family molecular chaperone regulator 3; 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. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport. (577 aa) |
| | Tbce | Tubulin-specific chaperone E; Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network (By similarity). Belongs to the TBCE family. (524 aa) |
| | Wrap53 | Telomerase Cajal body protein 1; RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies. Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes (By similarity). In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex. Acts b [...] (532 aa) |
| | Timm8a2 | Putative mitochondrial import inner membrane translocase subunit Tim8 A-B; Putative mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity); Belongs to the small [...] (97 aa) |
| | Cct8l1 | Chaperonin-containing TCP1, subunit 8 (theta)-like 1. (562 aa) |
| | Bag4 | BAG family molecular chaperone regulator 4; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Prevents constitutive TNFRSF1A signaling (By similarity). Negative regulator of PRKN translocation to damaged mitochondria (By similarity). (457 aa) |
| | Pdilt | Protein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis. (588 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). (196 aa) |
| | Igbp1 | Immunoglobulin-binding protein 1; Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits; Belongs to the IGBP1/TAP42 family. (340 aa) |
