STRINGSTRING
hsp-70 hsp-70 cpr-5 cpr-5 W07B8.4 W07B8.4 cpr-8 cpr-8 cpr-3 cpr-3 cpl-1 cpl-1 timp-1 timp-1 F57F5.1 F57F5.1 cpr-4 cpr-4 hif-1 hif-1 cpr-2 cpr-2 F32H5.1 F32H5.1 pax-3 pax-3 cpr-1 cpr-1 hsp-90 hsp-90 cpr-6 cpr-6
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:
hsp-70Heat Shock Protein; Belongs to the heat shock protein 70 family. (643 aa)
cpr-5Cathepsin B-like cysteine proteinase 5; Belongs to the peptidase C1 family. (344 aa)
W07B8.4Pept_C1 domain-containing protein; Belongs to the peptidase C1 family. (335 aa)
cpr-8Pept_C1 domain-containing protein; Belongs to the peptidase C1 family. (335 aa)
cpr-3Cathepsin B-like cysteine proteinase 3; Belongs to the peptidase C1 family. (370 aa)
cpl-1Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] (337 aa)
timp-1NTR domain-containing protein. (154 aa)
F57F5.1Pept_C1 domain-containing protein; Belongs to the peptidase C1 family. (351 aa)
cpr-4Cathepsin B-like cysteine proteinase 4; Thiol protease which shows activity against the fluorogenic substrate z-Arg-Arg-AMC; Belongs to the peptidase C1 family. (335 aa)
hif-1Hypoxia-inducible factor 1; A transcription factor which is a key regulator in various cellular processes; including environment stress resistance (oxygen levels, hydrogen sulfide and cyanide levels and heat), negative regulation of cell apoptosis in ASJ neurons by inhibition of cep-1 via transcriptional activation of tyr-2, resistance/susceptibility to pathogenic bacteria, lifespan and brood size. Involved in mediating susceptibility to enteropathogenic E.coli. Increased levels of hif-1 activity confer resistance to P.aeruginosa-mediated death but also confer susceptibility to S.aureu [...] (721 aa)
cpr-2Pept_C1 domain-containing protein; Belongs to the peptidase C1 family. (326 aa)
F32H5.1Pept_C1 domain-containing protein; Belongs to the peptidase C1 family. (356 aa)
pax-3PAX (Paired box) transcription factor. (308 aa)
cpr-1Gut-specific cysteine proteinase; Thiol protease. Has a role as a digestive enzyme. Belongs to the peptidase C1 family. (329 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)
cpr-6Cathepsin B-like cysteine proteinase 6; Belongs to the peptidase C1 family. (379 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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