STRINGSTRING
hsp-16.1 hsp-16.1 dnj-24 dnj-24 catp-6 catp-6 cdc-37 cdc-37 ero-1 ero-1 cyn-13 cyn-13 Y17G9B.4 Y17G9B.4 fkb-2 fkb-2 fkb-8 fkb-8 Y22D7AL.10 Y22D7AL.10 hsp-60 hsp-60 Y22D7AL.9 Y22D7AL.9 tor-1 tor-1 tor-2 tor-2 crt-1 crt-1 dnj-26 dnj-26 tbca-1 tbca-1 hsp-16.41 hsp-16.41 hsp-16.2 hsp-16.2 dnj-27 dnj-27 cyn-1 cyn-1 dnj-28 dnj-28 cct-8 cct-8 Y55F3BR.6 Y55F3BR.6 tbcc-1 tbcc-1 cyn-7 cyn-7 cyn-3 cyn-3 ZC250.5 ZC250.5 daf-41 daf-41 fkb-4 fkb-4 ZK1128.7 ZK1128.7 cyn-2 cyn-2 ZK616.2 ZK616.2 ZK616.3 ZK616.3 cnx-1 cnx-1 pfd-4 pfd-4 B0281.5 B0281.5 ahsa-1 ahsa-1 fkb-3 fkb-3 txdc-9 txdc-9 erp-44.2 erp-44.2 pdi-2 pdi-2 cct-5 cct-5 pfd-1 pfd-1 hsp-25 hsp-25 hsp-70 hsp-70 pdi-1 pdi-1 unc-45 unc-45 pfd-6 pfd-6 evl-20 evl-20 dnj-10 dnj-10 hsp-1 hsp-1 fkb-6 fkb-6 cyn-5 cyn-5 hsp-12.6 hsp-12.6 hsp-12.3 hsp-12.3 dnj-11 dnj-11 fkb-1 fkb-1 hsp-12.2 hsp-12.2 C14B9.2 C14B9.2 hsp-43 hsp-43 hsp-3 hsp-3 ttc-4 ttc-4 ooc-5 ooc-5 hsp-110 hsp-110 erp-44.1 erp-44.1 C34C12.8 C34C12.8 C47A4.1 C47A4.1 hsp-90 hsp-90 fkb-5 fkb-5 coel-1 coel-1 cyn-8 cyn-8 cct-6 cct-6 F08H9.3 F08H9.3 F08H9.4 F08H9.4 bmy-1 bmy-1 pfd-5 pfd-5 hsp-75 hsp-75 sti-1 sti-1 ddx-52 ddx-52 M04D5.1 M04D5.1 poml-1 poml-1 K10B2.4 K10B2.4 tbce-1 tbce-1 K07E8.6 K07E8.6 cct-4 cct-4 F11C1.1 F11C1.1 F11F1.1 F11F1.1 tbcd-1 tbcd-1 hsp-6 hsp-6 erp-44.3 erp-44.3 dnj-12 dnj-12 F35H10.6 F35H10.6 pfd-2 pfd-2 pdi-3 pdi-3 cyn-11 cyn-11 cct-1 cct-1 dnj-19 dnj-19 enpl-1 enpl-1 pfd-3 pfd-3 cyn-6 cyn-6 F42H10.2 F42H10.2 sip-1 sip-1 hsp-4 hsp-4 idha-1 idha-1 F44E5.4 F44E5.4 F47B7.2 F47B7.2 hsp-17 hsp-17 nud-1 nud-1 F53A3.7 F53A3.7 cct-3 cct-3 stc-1 stc-1 dnj-13 dnj-13 let-607 let-607 bag-1 bag-1 cct-7 cct-7 T10H10.2 T10H10.2 hip-1 hip-1 dnj-20 dnj-20 cct-2 cct-2 hsp-12.1 hsp-12.1 ogdh-1 ogdh-1 T22F3.12 T22F3.12 ucr-2.3 ucr-2.3 cyn-9 cyn-9 hsp-16.48 hsp-16.48 dnj-2 dnj-2 dnj-1 dnj-1 F35G2.1 F35G2.1 snpc-4 snpc-4
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
hsp-16.1Heat shock protein Hsp-16.1/Hsp-16.11. (145 aa)
dnj-24J domain-containing protein. (249 aa)
catp-6Probable cation-transporting ATPase W08D2.5; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily. (1256 aa)
cdc-37Probable 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)
ero-1Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). (513 aa)
cyn-13Peptidyl-prolyl cis-trans isomerase E; Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. (331 aa)
Y17G9B.4Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (262 aa)
fkb-2Peptidylprolyl isomerase. (108 aa)
fkb-8Peptidylprolyl isomerase. (290 aa)
Y22D7AL.10Uncharacterized protein; Belongs to the GroES chaperonin family. (108 aa)
hsp-60Chaperonin homolog Hsp-60, mitochondrial; Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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 (By similarity). (568 aa)
Y22D7AL.9TPR_REGION domain-containing protein. (836 aa)
tor-1Torsin. (310 aa)
tor-2Torsin. (310 aa)
crt-1Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] (395 aa)
dnj-26J domain-containing protein. (365 aa)
tbca-1Tubulin-specific chaperone A; Belongs to the TBCA family. (111 aa)
hsp-16.41Heat shock protein Hsp-16.41; Belongs to the small heat shock protein (HSP20) family. (143 aa)
hsp-16.2Heat shock protein Hsp-16.2; Belongs to the small heat shock protein (HSP20) family. (145 aa)
dnj-27DNaJ domain (Prokaryotic heat shock protein). (788 aa)
cyn-1Peptidyl-prolyl cis-trans isomerase 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (192 aa)
dnj-28DNaJ domain (Prokaryotic heat shock protein). (494 aa)
cct-8T-complex protein 1 subunit theta; 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). Required for correct subcellular localization of pgl-1; Belongs to the TCP-1 chaperonin family. (548 aa)
Y55F3BR.6SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (253 aa)
tbcc-1C-CAP/cofactor C-like domain-containing protein. (303 aa)
cyn-7Peptidyl-prolyl cis-trans isomerase 7; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (171 aa)
cyn-3Peptidyl-prolyl cis-trans isomerase 3; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (173 aa)
ZC250.5PPIase cyclophilin-type domain-containing protein. (204 aa)
daf-41Co-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)
fkb-4Peptidylprolyl isomerase. (259 aa)
ZK1128.7SHSP domain-containing protein. (205 aa)
cyn-2Peptidyl-prolyl cis-trans isomerase 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (172 aa)
ZK616.2Uncharacterized protein. (97 aa)
ZK616.3CHCH domain-containing protein. (134 aa)
cnx-1Calnexin; 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 (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. (619 aa)
pfd-4Probable 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 (By similarity); Belongs to the prefoldin subunit beta family. (126 aa)
B0281.5BTB domain-containing protein. (207 aa)
ahsa-1Aha1_N domain-containing protein. (342 aa)
fkb-3Peptidylprolyl isomerase. (261 aa)
txdc-9Thioredoxin domain-containing protein 9; Required for normal microtubule organization and function. Regulates tubulin acetylation in ALM and PLM neurons. (208 aa)
erp-44.2Endoplasmic reticulum resident protein 44.2. (413 aa)
pdi-2Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. (493 aa)
cct-5T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (542 aa)
pfd-1Probable 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). Has a role in gonadogenesis; Belongs to the prefoldin subunit beta family. (117 aa)
hsp-25SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (219 aa)
hsp-70Heat Shock Protein; Belongs to the heat shock protein 70 family. (643 aa)
pdi-1Protein disulfide-isomerase 1; Belongs to the protein disulfide isomerase family. (485 aa)
unc-45TPR_REGION domain-containing protein. (961 aa)
pfd-6Probable 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). Required for positioning of the mitotic spindle. (126 aa)
evl-20ADP-ribosylation factor-like protein 2; GTP-binding protein that functions in embryogenesis, cytokinesis, germline development and microtubulule cytoskeleton dynamics. (184 aa)
dnj-10DnaJ homolog dnj-10. (456 aa)
hsp-1Heat shock 70 kDa protein A. (640 aa)
fkb-6Peptidylprolyl isomerase. (431 aa)
cyn-5Peptidyl-prolyl cis-trans isomerase 5; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (204 aa)
hsp-12.6SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (110 aa)
hsp-12.3SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (109 aa)
dnj-11DNaJ domain (Prokaryotic heat shock protein). (589 aa)
fkb-1Peptidylprolyl isomerase. (139 aa)
hsp-12.2Heat shock protein Hsp-12.2; Belongs to the small heat shock protein (HSP20) family. (110 aa)
C14B9.2Probable protein disulfide-isomerase A4; Belongs to the protein disulfide isomerase family. (618 aa)
hsp-43SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (393 aa)
hsp-3Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. (661 aa)
ttc-4TeTratriCopeptide repeat domain protein related. (419 aa)
ooc-5Torsin-like protein; May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins; Belongs to the ClpA/ClpB family. Torsin subfamily. (356 aa)
hsp-110Heat shock protein 110. (776 aa)
erp-44.1Thioredoxin domain-containing protein. (411 aa)
C34C12.8GrpE protein homolog, 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). (237 aa)
C47A4.1Uncharacterized protein. (157 aa)
hsp-90Heat 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)
fkb-5Peptidylprolyl isomerase. (300 aa)
coel-1Tubulin folding COfactor E-Like protein. (432 aa)
cyn-8Peptidyl-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)
cct-6T-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). (539 aa)
F08H9.3SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (147 aa)
F08H9.4SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (147 aa)
bmy-1Boca/MESD chaperone for YWTD beta-propeller-EGF. (186 aa)
pfd-5Probable 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 (By similarity); Belongs to the prefoldin subunit alpha family. (152 aa)
hsp-75HATPase_c domain-containing protein. (672 aa)
sti-1Stress-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)
ddx-52DEAD boX helicase homolog. (581 aa)
M04D5.1Uncharacterized protein. (332 aa)
poml-1PON (Paraoxonase) and MEC-6 Like. (349 aa)
K10B2.4Protein Asterix. (113 aa)
tbce-1CAP-Gly domain-containing protein. (493 aa)
K07E8.6CDC37_M domain-containing protein. (339 aa)
cct-4T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (540 aa)
F11C1.1CHCH domain-containing protein. (126 aa)
F11F1.1DUF148 domain-containing protein; Belongs to the heat shock protein 70 family. (607 aa)
tbcd-1Tubulin-specific chaperone D; Tubulin-folding protein; involved in the first step of the tubulin folding pathway (By similarity). Plays a role in microtubule polymerization ; Belongs to the TBCD family. (1232 aa)
hsp-6Heat shock 70 kDa protein F, mitochondrial; Belongs to the heat shock protein 70 family. (657 aa)
erp-44.3Thioredoxin domain-containing protein. (434 aa)
dnj-12DNaJ domain (Prokaryotic heat shock protein). (402 aa)
F35H10.6Uncharacterized protein. (158 aa)
pfd-2Prefoldin 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 (By similarity); Belongs to the prefoldin subunit beta family. (141 aa)
pdi-3Protein disulfide-isomerase. (488 aa)
cyn-11Peptidyl-prolyl cis-trans isomerase 11; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase H subfamily. (183 aa)
cct-1T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (549 aa)
dnj-19DNaJ domain (Prokaryotic heat shock protein). (439 aa)
enpl-1Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. (760 aa)
pfd-3Probable 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); Belongs to the prefoldin subunit alpha family. (185 aa)
cyn-6Peptidyl-prolyl cis-trans isomerase 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (201 aa)
F42H10.2Uncharacterized protein F42H10.2. (115 aa)
sip-1Stress-induced protein 1; Belongs to the small heat shock protein (HSP20) family. (159 aa)
hsp-4Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. (657 aa)
idha-1Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (358 aa)
F44E5.4Uncharacterized protein; Belongs to the heat shock protein 70 family. (645 aa)
F47B7.2Sulfhydryl oxidase. (678 aa)
hsp-17SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (149 aa)
nud-1CS domain-containing protein. (320 aa)
F53A3.7DNL-type domain-containing protein. (119 aa)
cct-3T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization. (543 aa)
stc-1STCH (Truncated HSP) family. (450 aa)
dnj-13J domain-containing protein. (331 aa)
let-607BZIP domain-containing protein. (690 aa)
bag-1BAG family molecular chaperone regulator 1; May inhibit the chaperone activity of HSP70/HSC70 by promoting substrate release in an ATP-dependent manner. (210 aa)
cct-7T-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. (535 aa)
T10H10.2Sulfhydryl oxidase. (574 aa)
hip-1TPR_REGION domain-containing protein. (422 aa)
dnj-20DnaJ homolog dnj-20. (355 aa)
cct-2T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family. (529 aa)
hsp-12.1SHSP domain-containing protein; Belongs to the small heat shock protein (HSP20) family. (112 aa)
ogdh-12-oxoglutarate dehydrogenase, mitochondrial; The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). (1029 aa)
T22F3.12Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (174 aa)
ucr-2.3Peptidase_M16 domain-containing protein. (427 aa)
cyn-9Peptidyl-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)
hsp-16.48Heat shock protein Hsp-16.48/Hsp-16.49; Belongs to the small heat shock protein (HSP20) family. (143 aa)
dnj-2DnaJ homolog dnj-2. (337 aa)
dnj-1DnaJ homolog subfamily B member 1; Acts as a co-chaperone with Hsp70 required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). Acts by determining Hsp70's ATPase and polypeptide-binding activities (By similarity). Can also act as a chaperone that promotes maturation of potassium channel unc-103 by stabilizing nascent channel subunits and assembling them into tetramers ; Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily. (401 aa)
F35G2.1Sulfhydryl oxidase. (601 aa)
snpc-4snRNA-activating protein complex subunit 4 homolog; Binds to the promoter regions of RNA polymerase II and III small-nuclear RNA genes, type 3 RNA polymerase III non-coding RNA genes, small nucleolar RNAs and transfer RNA genes. Required for expression of mature 21U-RNAs. (944 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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