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 |
| atf-6 | crt-1 | F45E6.2.1 | Y38A10A.5.2 | BZIP domain-containing protein. | 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 [...] | 0.871 |
| atf-6 | hsp-3 | F45E6.2.1 | C15H9.6a.5 | BZIP domain-containing protein. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.755 |
| atf-6 | hsp-4 | F45E6.2.1 | F43E2.8a.2 | BZIP domain-containing protein. | Endoplasmic 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. | 0.837 |
| atf-6 | pek-1 | F45E6.2.1 | F46C3.1.1 | BZIP domain-containing protein. | Eukaryotic translation initiation factor 2-alpha kinase pek-1; Phosphorylates the alpha subunit of eukaryotic translation- initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. May phosphorylate eIF2alpha during hypoxia. Proposed to have a role in alleviating endoplasmic reticulum stress ; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. | 0.978 |
| atf-6 | xbp-1 | F45E6.2.1 | R74.3a.1 | BZIP domain-containing protein. | BZIP domain-containing protein. | 0.995 |
| crt-1 | atf-6 | Y38A10A.5.2 | F45E6.2.1 | 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 [...] | BZIP domain-containing protein. | 0.871 |
| 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 | hsp-4 | Y38A10A.5.2 | F43E2.8a.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 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. | 0.881 |
| 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-3 | Y38A10A.5.2 | H06O01.1.3 | 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. | 0.965 |
| crt-1 | pek-1 | Y38A10A.5.2 | F46C3.1.1 | 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 [...] | Eukaryotic translation initiation factor 2-alpha kinase pek-1; Phosphorylates the alpha subunit of eukaryotic translation- initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. May phosphorylate eIF2alpha during hypoxia. Proposed to have a role in alleviating endoplasmic reticulum stress ; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. | 0.470 |
| crt-1 | xbp-1 | Y38A10A.5.2 | R74.3a.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 [...] | BZIP domain-containing protein. | 0.913 |
| hsp-3 | atf-6 | C15H9.6a.5 | F45E6.2.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | BZIP domain-containing protein. | 0.755 |
| hsp-3 | crt-1 | C15H9.6a.5 | Y38A10A.5.2 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 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 [...] | 0.948 |
| hsp-3 | hsp-4 | C15H9.6a.5 | F43E2.8a.2 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Endoplasmic 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. | 0.913 |
| hsp-3 | pdi-2 | C15H9.6a.5 | C07A12.4a.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Protein disulfide-isomerase 2; Involved in cuticle formation. May play a role in the unfolded protein response. Belongs to the protein disulfide isomerase family. | 0.929 |
| hsp-3 | pdi-3 | C15H9.6a.5 | H06O01.1.3 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Protein disulfide-isomerase. | 0.840 |
| hsp-3 | pek-1 | C15H9.6a.5 | F46C3.1.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Eukaryotic translation initiation factor 2-alpha kinase pek-1; Phosphorylates the alpha subunit of eukaryotic translation- initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. May phosphorylate eIF2alpha during hypoxia. Proposed to have a role in alleviating endoplasmic reticulum stress ; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. | 0.860 |
| hsp-3 | xbp-1 | C15H9.6a.5 | R74.3a.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | BZIP domain-containing protein. | 0.853 |
| hsp-4 | atf-6 | F43E2.8a.2 | F45E6.2.1 | Endoplasmic 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. | BZIP domain-containing protein. | 0.837 |
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