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| | CLPB | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process. (677 aa) |
| | HSPB8 | Heat shock protein beta-8; Displays temperature-dependent chaperone activity. Belongs to the small heat shock protein (HSP20) family. (196 aa) |
| | LONP1 | Lon protease homolog, mitochondrial; ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand- specific manner. May regulate mi [...] (1027 aa) |
| | SUGT1 | Protein SGT1 homolog; May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. (338 aa) |
| | DNAJC7 | DnaJ heat shock protein family (Hsp40) member C7. (494 aa) |
| | DNAJA2 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (412 aa) |
| | DNAJC2 | DnaJ homolog subfamily C member 2; Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histo [...] (621 aa) |
| | HSPH1 | Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities. (859 aa) |
| | BAG2 | BAG family molecular chaperone regulator 2; Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. (211 aa) |
| | HSP90AA1 | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] (734 aa) |
| | SAMD13-2 | Uncharacterized protein LOC780805. (195 aa) |
| | PPP5C | Serine/threonine-protein phosphatase. (499 aa) |
| | HSPA9 | Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis probably via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. (679 aa) |
| | HSPD1 | 60 kDa heat shock protein, mitochondrial; Belongs to the chaperonin (HSP60) family. (573 aa) |
| | HSPA13 | Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (471 aa) |
| | HSPA1A | Heat shock 70 kDa protein 1A; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and AD [...] (641 aa) |
| | CHORDC1 | Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity). (332 aa) |
| | BAG3 | BCL2 associated athanogene 3. (585 aa) |
| | DNAJB12 | DnaJ homolog subfamily B member 12; Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of na [...] (377 aa) |
| | HSPA12A | Heat shock protein family A (Hsp70) member 12A. (692 aa) |
| | CLPP | ATP-dependent Clp protease proteolytic subunit, mitochondrial; Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. (272 aa) |
| | DNAJC5B | DnaJ homolog subfamily C member 5B. (199 aa) |
| | HSPA4 | Heat shock protein family A (Hsp70) member 4. (840 aa) |
| | DNAJA4 | DnaJ heat shock protein family (Hsp40) member A4. (549 aa) |
| | DNAJA1 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). (397 aa) |
| | MAPT | Microtubule-associated protein. (617 aa) |
| | BAG1 | BCL2 associated athanogene 1. (237 aa) |
| | STUB1 | STIP1 homology and U-box containing protein 1. (592 aa) |
| | DNAJB4 | DnaJ homolog subfamily B member 4; Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (337 aa) |
| | AHSA1 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (Yeast). (338 aa) |
| | HSPA1L | Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] (641 aa) |
| | CDC37 | Hsp90 co-chaperone Cdc37, N-terminally processed; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. (380 aa) |
| | DNAJB1 | DnaJ homolog subfamily B member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (340 aa) |
| | PPIG | Peptidylprolyl isomerase G. (753 aa) |
| | DNAJC1 | DnaJ heat shock protein family (Hsp40) member C1. (542 aa) |
| | LOC615521 | LOC615521; Belongs to the GrpE family. (194 aa) |
| | AHSA2 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity. (260 aa) |
| | HSPA6 | Heat shock protein family A (Hsp70) member 6; Belongs to the heat shock protein 70 family. (639 aa) |
| | HSPA14 | Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). (788 aa) |
| | TMEM59 | Transmembrane protein 59; Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding. (334 aa) |
| | HSPA8 | Heat shock cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] (654 aa) |
| | ENSBTAP00000058802 | Uncharacterized protein. (461 aa) |
| | HSPD1-2 | 60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] (573 aa) |
| | STIP1-2 | Stress-induced-phosphoprotein 1; Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90. (543 aa) |
| | STIP1 | Stress-induced-phosphoprotein 1. (650 aa) |
| | ENSBTAP00000060468 | Uncharacterized protein. (305 aa) |
| | DNAJA1-2 | J domain-containing protein. (118 aa) |
| | ENSBTAP00000060867 | Uncharacterized protein. (204 aa) |
| | DNAJB6 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). (364 aa) |
| | HSPA2 | Heat shock-related 70 kDa protein 2; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis [...] (636 aa) |
| | ENSBTAP00000063738 | Uncharacterized protein. (76 aa) |
| | HSPA4L | Heat shock protein family A (Hsp70) member 4 like. (1013 aa) |
| | ENSBTAP00000064525 | Uncharacterized protein. (121 aa) |
| | ENSBTAP00000066216 | Uncharacterized protein. (307 aa) |
| | HSPE1 | 10 kDa heat shock protein, mitochondrial; Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per [...] (259 aa) |
| | DNAJA3 | Uncharacterized protein. (480 aa) |
| | ENSBTAP00000067980 | Uncharacterized protein; Belongs to the GroES chaperonin family. (101 aa) |
| | ENSBTAP00000068131 | J domain-containing protein. (397 aa) |
| | HSPBP1 | HSPA (Heat shock 70kDa) binding protein, cytoplasmic cochaperone 1. (357 aa) |
| | ENSBTAP00000069080 | J domain-containing protein. (98 aa) |
| | HSP90AB1 | Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] (724 aa) |
| | HSPA12B | Uncharacterized protein. (686 aa) |
| | TRAP1 | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. (706 aa) |
| | CLPX | Caseinolytic mitochondrial matrix peptidase chaperone subunit. (690 aa) |
| | ENSBTAP00000074523 | TPR_REGION domain-containing protein. (229 aa) |
