Your Input: | |
| | ENSPPYP00000005659 | annotation not available (212 aa) |
| | ENSPPYP00000024459 | annotation not available (494 aa) |
| | ENSPPYP00000024257 | LOW QUALITY PROTEIN: stress-70 protein, mitochondrial-like. (403 aa) |
| | HSPE1-3 | Heat shock protein family E (Hsp10) member 1. (102 aa) |
| | CCT6A | T-complex protein 1 subunit zeta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). (531 aa) |
| | TOR1A | Torsin. (364 aa) |
| | HSPA5 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] (654 aa) |
| | ENSPPYP00000021086 | annotation not available (97 aa) |
| | ENSPPYP00000020876 | annotation not available (224 aa) |
| | FAM167A | FAM167A isoform 3. (214 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). (354 aa) |
| | CCT8L2 | CCT8L2 isoform 1. (168 aa) |
| | ERMARD | ERMARD isoform 4. (661 aa) |
| | TCP1 | TCP1 isoform 2. (556 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) |
| | BTBD9 | BTB domain containing 9. (641 aa) |
| | HSPA1A | Heat shock 70 kDa protein 1; 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 ADP [...] (641 aa) |
| | HSPA1L | Heat shock protein family A (Hsp70) member 1 like; Belongs to the heat shock protein 70 family. (641 aa) |
| | CD74 | CD74 isoform 2. (232 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. (127 aa) |
| | HSPA9 | Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. (679 aa) |
| | HSPA4 | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. (575 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). (99 aa) |
| | MARVELD2 | MARVEL domain containing 2. (559 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) |
| | CLGN | CLGN isoform 1. (542 aa) |
| | HSPA4L | HSPA4L isoform 1. (804 aa) |
| | PDCL2 | PDCL2 isoform 1. (240 aa) |
| | ENSPPYP00000016113 | annotation not available (483 aa) |
| | ZMYND10 | Zinc finger MYND domain-containing protein 10; Plays a role in axonemal structure organization and motility. Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility. May act by indirectly regulating transcription of dynein proteins. Belongs to the ZMYND10 family. (474 aa) |
| | DNAJB8 | DnaJ heat shock protein family (Hsp40) member B8. (232 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) |
| | 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) |
| | 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. (542 aa) |
| | PDCL3 | Phosducin-like protein 3; Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity); Belongs to the phosducin family. (178 aa) |
| | DNAJB7 | DnaJ heat shock protein family (Hsp40) member B7. (309 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. (542 aa) |
| | HSPA13 | Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (463 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. (293 aa) |
| | TMEM59L | Transmembrane protein 59 like. (342 aa) |
| | FKBP8 | Peptidylprolyl isomerase. (413 aa) |
| | CALR3 | Calreticulin. (319 aa) |
| | DNAJB1 | DnaJ heat shock protein family (Hsp40) member B1. (340 aa) |
| | CALR | Calreticulin. (417 aa) |
| | WDR83OS | Protein Asterix. (106 aa) |
| | HSPE1-2 | Heat shock protein family E (Hsp10) member 1. (102 aa) |
| | CCDC47 | Coiled-coil domain-containing protein 47; Involved in the regulation of calcium ion homeostasis in the endoplasmic reticulum (By similarity). Required for proper protein degradation via the ERAD pathway. Has an essential role in the maintenance of endoplasmic reticulum organization during embryogenesis (By similarity). (483 aa) |
| | CCT6B | CCT6B isoform 1. (531 aa) |
| | ENSPPYP00000008522 | 10 kDa heat shock protein, mitochondrial-like. (90 aa) |
| | CLPX | ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial; ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5- aminolevulinate (ALA) synthesis, the first step in h [...] (633 aa) |
| | HSPA2 | Heat shock protein family A (Hsp70) member 2; Belongs to the heat shock protein 70 family. (639 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. (851 aa) |
| | CCT2 | Chaperonin containing TCP1 subunit 2. (535 aa) |
| | HSPE1 | HSPE1 isoform 1; Belongs to the GroES chaperonin family. (102 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) |
| | HYOU1 | Hypoxia up-regulated 1. (999 aa) |
| | PAAF1 | Proteasomal ATPase associated factor 1. (392 aa) |
| | RIC3 | RIC3 acetylcholine receptor chaperone. (368 aa) |
| | C10H10orf71 | C10orf71 isoform 1. (392 aa) |
| | HSPA14 | Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). (509 aa) |
| | DFFA | DNA fragmentation factor subunit alpha. (331 aa) |
| | LDLRAD1 | LDLRAD1 isoform 3. (222 aa) |
| | ENSPPYP00000000835 | annotation not available (124 aa) |
| | PFDN2 | Prefoldin subunit 2. (154 aa) |
| | HSPA6 | Heat shock protein family A (Hsp70) member 6; Belongs to the heat shock protein 70 family. (643 aa) |
| | ANKRD45 | ANKRD45 isoform 1. (282 aa) |
