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 |
| F47B7.2 | dpy-18 | F47B7.2b.1 | Y47D3B.10.1 | Sulfhydryl oxidase. | 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. | 0.564 |
| F47B7.2 | pdi-3 | F47B7.2b.1 | H06O01.1.3 | Sulfhydryl oxidase. | Protein disulfide-isomerase. | 0.730 |
| F47B7.2 | pdi-6 | F47B7.2b.1 | B0403.4.1 | Sulfhydryl oxidase. | 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. | 0.463 |
| F47B7.2 | phy-2 | F47B7.2b.1 | F35G2.4.1 | Sulfhydryl oxidase. | 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. | 0.418 |
| cnx-1 | crt-1 | ZK632.6a.1 | Y38A10A.5.2 | Calnexin; 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. | 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 [...] | 0.956 |
| cnx-1 | hsp-3 | ZK632.6a.1 | C15H9.6a.5 | Calnexin; 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. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.929 |
| cnx-1 | hsp-4 | ZK632.6a.1 | F43E2.8a.2 | Calnexin; 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. | 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. | 0.924 |
| cnx-1 | pdi-3 | ZK632.6a.1 | H06O01.1.3 | Calnexin; 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. | Protein disulfide-isomerase. | 0.888 |
| cnx-1 | pdi-6 | ZK632.6a.1 | B0403.4.1 | Calnexin; 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. | 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. | 0.471 |
| cnx-1 | trx-4 | ZK632.6a.1 | Y44E3A.3.1 | Calnexin; 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. | Thioredoxin; Belongs to the thioredoxin family. | 0.430 |
| crt-1 | cnx-1 | Y38A10A.5.2 | ZK632.6a.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 [...] | Calnexin; 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. | 0.956 |
| 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-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 | 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 |
| crt-1 | trx-4 | Y38A10A.5.2 | Y44E3A.3.1 | 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 [...] | Thioredoxin; Belongs to the thioredoxin family. | 0.549 |
| dpy-18 | F47B7.2 | Y47D3B.10.1 | F47B7.2b.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. | Sulfhydryl oxidase. | 0.564 |
| dpy-18 | pdi-3 | Y47D3B.10.1 | H06O01.1.3 | 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. | 0.764 |
| 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 |
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