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| 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) | |||
| MKKS | McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex 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; Belongs to the TCP-1 chaperonin family (570 aa) | |||
| CCT7 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity); Chaperonins (543 aa) | |||
| WSB1 | WD repeat and SOCS box-containing protein 1; Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes type II iodothyronine deiodinase/DIO2. Confers constitutive instability to HIPK2 through proteasomal degradation; WD repeat domain containing (421 aa) | |||
| CCT5 | T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (541 aa) | |||
| CCT8 | T-complex protein 1 subunit theta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family (548 aa) | |||
| WDR90 | WD repeat-containing protein 90; WD repeat domain containing (1748 aa) | |||
| CCT3 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (545 aa) | |||
| CCT2 | T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (535 aa) | |||
| MAT2A | S-adenosylmethionine synthase isoform type-2; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme- formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate; Belongs to the AdoMet synthase family (395 aa) | |||
| WDR49 | WD repeat-containing protein 49; WD repeat domain containing (697 aa) | |||
| PAAF1 | Proteasomal ATPase-associated factor 1; Inhibits proteasome 26S assembly and proteolytic activity by impairing the association of the 19S regulatory complex with the 20S core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 promoter, where it promotes the recruitment of 19S regulatory complex through dissociation of the proteasome 26S. This presumably promotes provirus transcription efficiency. Protects SUPT6H from proteasomal degradation; WD repeat domain containing (392 aa) | |||
| TCP1 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family (556 aa) | |||
| WDR5B | WD repeat-containing protein 5B; May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex; WD repeat domain containing (330 aa) | |||
| WDR16 | Cilia- and flagella-associated protein 52; May play a role in cell growth and/or survival (620 aa) | |||
| WDR88 | WD repeat-containing protein 88; WD repeat domain containing (472 aa) | |||
| WDR5 | WD repeat-containing protein 5; Contributes to histone modification. May position the N- terminus of histone H3 for efficient trimethylation at ’Lys-4’. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at ’Lys-4’ of histone H3. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation; Belongs to the WD repeat WDR5/wds family (334 aa) | |||
| CCT8L2 | T-complex protein 1 subunit theta-like 2; Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis; Belongs to the TCP-1 chaperonin family (557 aa) | |||
| AHI1 | Jouberin; Involved in vesicle trafficking and required for ciliogenesis, formation of primary non-motile cilium, and recruitment of RAB8A to the basal body of primary cilium. Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in neuronal differentiation; WD repeat domain containing (1196 aa) | |||
| MAT1A | S-adenosylmethionine synthase isoform type-1; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme- formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate (395 aa) | |||
| PCYT1B | Choline-phosphate cytidylyltransferase B; Controls phosphatidylcholine synthesis (369 aa) | |||
| BBS10 | Bardet-Biedl syndrome 10 protein; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation; Belongs to the TCP-1 chaperonin family (723 aa) | |||
| CCT4 | T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (539 aa) | |||
| VKORC1L1 | Vitamin K epoxide reductase complex subunit 1 like 1 (177 aa) | |||
| CKAP5 | Cytoskeleton-associated protein 5; Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stab [...] (2032 aa) | |||
| HSPE1-MOB4 | HSPE1-MOB4 readthrough; Belongs to the GroES chaperonin family (261 aa) | |||
