STRINGSTRING
stc-1 stc-1 ZK688.5 ZK688.5 Y73B6BL.12 Y73B6BL.12 dnj-28 dnj-28 dnj-27 dnj-27 dnj-20 dnj-20 R151.6 R151.6 ebax-1 ebax-1 F44E5.4 F44E5.4 hsp-4 hsp-4 hsp-1 hsp-1 cup-2 cup-2 F11F1.1 F11F1.1 dnj-7 dnj-7 hsp-6 hsp-6 hsp-3 hsp-3 hsp-70 hsp-70
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
stc-1STCH (Truncated HSP) family. (450 aa)
ZK688.5Uncharacterized protein ZK688.5. (1620 aa)
Y73B6BL.12Thioredoxin; Belongs to the thioredoxin family. (136 aa)
dnj-28DNaJ domain (Prokaryotic heat shock protein). (494 aa)
dnj-27DNaJ domain (Prokaryotic heat shock protein). (788 aa)
dnj-20DnaJ homolog dnj-20. (355 aa)
R151.6Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. (237 aa)
ebax-1SWIM-type domain-containing protein. (1717 aa)
F44E5.4Uncharacterized protein; Belongs to the heat shock protein 70 family. (645 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)
hsp-1Heat shock 70 kDa protein A. (640 aa)
cup-2Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. (245 aa)
F11F1.1DUF148 domain-containing protein; Belongs to the heat shock protein 70 family. (607 aa)
dnj-7DNaJ domain (Prokaryotic heat shock protein). (491 aa)
hsp-6Heat shock 70 kDa protein F, mitochondrial; Belongs to the heat shock protein 70 family. (657 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)
hsp-70Heat Shock Protein; Belongs to the heat shock protein 70 family. (643 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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