Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| C14E2.4 | dpy-18 | C14E2.4.1 | Y47D3B.10.1 | Fe2OG dioxygenase domain-containing protein. | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.419 |
| C14E2.4 | pdi-2 | C14E2.4.1 | C07A12.4a.1 | Fe2OG dioxygenase domain-containing protein. | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.818 |
| C14E2.4 | phy-2 | C14E2.4.1 | F35G2.4.1 | Fe2OG dioxygenase domain-containing protein. | Prolyl 4-hydroxylase subunit alpha-2; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.412 |
| crt-1 | enpl-1 | Y38A10A.5.2 | T05E11.3a.1 | Calreticulin; 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 [...] | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.989 |
| crt-1 | ero-1 | Y38A10A.5.2 | Y105E8B.8c.2 | Calreticulin; 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 [...] | Endoplasmic 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). | 0.568 |
| crt-1 | hsp-3 | Y38A10A.5.2 | C15H9.6a.5 | Calreticulin; 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 [...] | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.948 |
| crt-1 | pdi-2 | Y38A10A.5.2 | C07A12.4a.1 | Calreticulin; 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 [...] | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.914 |
| crt-1 | pdi-6 | Y38A10A.5.2 | B0403.4.1 | Calreticulin; 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 [...] | Protein disulfide-isomerase A6 homolog; May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors ; Belongs to the protein disulfide isomerase family. | 0.855 |
| dpy-18 | C14E2.4 | Y47D3B.10.1 | C14E2.4.1 | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | Fe2OG dioxygenase domain-containing protein. | 0.419 |
| dpy-18 | pdi-2 | Y47D3B.10.1 | C07A12.4a.1 | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.946 |
| dpy-18 | pdi-6 | Y47D3B.10.1 | B0403.4.1 | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | Protein disulfide-isomerase A6 homolog; May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors ; Belongs to the protein disulfide isomerase family. | 0.502 |
| dpy-18 | phy-2 | Y47D3B.10.1 | F35G2.4.1 | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | Prolyl 4-hydroxylase subunit alpha-2; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.978 |
| dsc-4 | pdi-2 | K02D7.4.1 | C07A12.4a.1 | Microsomal triglyceride transfer protein. | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.942 |
| enpl-1 | crt-1 | T05E11.3a.1 | Y38A10A.5.2 | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | Calreticulin; 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 [...] | 0.989 |
| enpl-1 | ero-1 | T05E11.3a.1 | Y105E8B.8c.2 | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | Endoplasmic 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). | 0.428 |
| enpl-1 | hsp-3 | T05E11.3a.1 | C15H9.6a.5 | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.981 |
| enpl-1 | pdi-2 | T05E11.3a.1 | C07A12.4a.1 | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.888 |
| enpl-1 | pdi-6 | T05E11.3a.1 | B0403.4.1 | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | Protein disulfide-isomerase A6 homolog; May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors ; Belongs to the protein disulfide isomerase family. | 0.965 |
| ero-1 | crt-1 | Y105E8B.8c.2 | Y38A10A.5.2 | Endoplasmic 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). | Calreticulin; 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 [...] | 0.568 |
| ero-1 | enpl-1 | Y105E8B.8c.2 | T05E11.3a.1 | Endoplasmic 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). | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.428 |
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