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ahsa-1 | Aha1_N domain-containing protein. (342 aa) | ||||
dnj-4 | J domain-containing protein. (274 aa) | ||||
hsp-70 | Heat Shock Protein; Belongs to the heat shock protein 70 family. (643 aa) | ||||
hsp-110 | Heat shock protein 110. (776 aa) | ||||
hsp-90 | Heat shock protein 90; 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. By stabilizing the receptor-type guanylate cyclase daf-11 or another sig [...] (702 aa) | ||||
cyn-8 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (466 aa) | ||||
D1054.3 | SGS domain-containing protein. (198 aa) | ||||
F11F1.1 | DUF148 domain-containing protein; Belongs to the heat shock protein 70 family. (607 aa) | ||||
dnj-9 | J domain-containing protein. (564 aa) | ||||
hsp-1 | Heat shock 70 kDa protein A. (640 aa) | ||||
fkb-6 | Peptidylprolyl isomerase. (431 aa) | ||||
dnj-11 | DNaJ domain (Prokaryotic heat shock protein). (589 aa) | ||||
dnj-12 | DNaJ domain (Prokaryotic heat shock protein). (402 aa) | ||||
F44E5.5 | annotation not available (645 aa) | ||||
stc-1 | STCH (Truncated HSP) family. (450 aa) | ||||
dnj-13 | J domain-containing protein. (331 aa) | ||||
bag-1 | BAG family molecular chaperone regulator 1; May inhibit the chaperone activity of HSP70/HSC70 by promoting substrate release in an ATP-dependent manner. (210 aa) | ||||
unc-23 | BAG domain-containing protein. (458 aa) | ||||
dnj-14 | J domain-containing protein. (217 aa) | ||||
K07E8.6 | CDC37_M domain-containing protein. (339 aa) | ||||
sti-1 | Stress-induced-phosphoprotein 1; Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity. (320 aa) | ||||
hsp-75 | HATPase_c domain-containing protein. (672 aa) | ||||
dnj-18 | J domain-containing protein. (249 aa) | ||||
dnj-19 | DNaJ domain (Prokaryotic heat shock protein). (439 aa) | ||||
cyn-9 | Peptidyl-prolyl cis-trans isomerase 9; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. (309 aa) | ||||
cdc-37 | Probable Hsp90 co-chaperone cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (By similarity). Inhibits daf-21/Hsp90 ATPase activity ; Belongs to the CDC37 family. (403 aa) | ||||
chp-1 | CHORD containing protein. (321 aa) | ||||
Y22D7AL.9 | TPR_REGION domain-containing protein. (836 aa) | ||||
pph-5 | Serine/threonine-protein phosphatase 5; Serine/threonine-protein phosphatase. Dephosphorylates cdc-37. Probably by dephosphorylating separase sep-1, may be involved in sep-1-mediated exocytosis of cortical granules during meiotic anaphase and mitotic cytokinesis. (496 aa) | ||||
daf-41 | Co-chaperone protein daf-41; Co-chaperone for hsp90/daf-21. Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures. Belongs to the p23/wos2 family. (175 aa) |