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 |
| CR201_G0008818 | SLC35A2 | ENSPPYP00000021755 | ENSPPYP00000022752 | SLC35D2 isoform 2. | Solute carrier family 35 member A2. | 0.469 |
| CR201_G0008818 | SLC35B1 | ENSPPYP00000021755 | ENSPPYP00000010013 | SLC35D2 isoform 2. | SLC35B1 isoform 2. | 0.582 |
| DERL1 | P4HB | ENSPPYP00000021151 | ENSPPYP00000009818 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.407 |
| DERL1 | SLC35B1 | ENSPPYP00000021151 | ENSPPYP00000010013 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | SLC35B1 isoform 2. | 0.405 |
| DNAJB11 | P4HB | ENSPPYP00000016085 | ENSPPYP00000009818 | DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.502 |
| DNAJB11 | SLC35B1 | ENSPPYP00000016085 | ENSPPYP00000010013 | DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. | SLC35B1 isoform 2. | 0.420 |
| GART | SLC35B1 | ENSPPYP00000012701 | ENSPPYP00000010013 | Trifunctional purine biosynthetic protein adenosine-3; In the C-terminal section; belongs to the GART family. In the central section; belongs to the AIR synthase family. | SLC35B1 isoform 2. | 0.415 |
| P4HB | DERL1 | ENSPPYP00000009818 | ENSPPYP00000021151 | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | 0.407 |
| P4HB | DNAJB11 | ENSPPYP00000009818 | ENSPPYP00000016085 | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. | 0.502 |
| P4HB | SLC35B1 | ENSPPYP00000009818 | ENSPPYP00000010013 | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | SLC35B1 isoform 2. | 0.443 |
| PCID2 | SLC35B1 | ENSPPYP00000006295 | ENSPPYP00000010013 | PCI domain containing 2. | SLC35B1 isoform 2. | 0.404 |
| SLC35A2 | CR201_G0008818 | ENSPPYP00000022752 | ENSPPYP00000021755 | Solute carrier family 35 member A2. | SLC35D2 isoform 2. | 0.469 |
| SLC35A2 | SLC35B1 | ENSPPYP00000022752 | ENSPPYP00000010013 | Solute carrier family 35 member A2. | SLC35B1 isoform 2. | 0.609 |
| SLC35A2 | SLC35D1 | ENSPPYP00000022752 | ENSPPYP00000001467 | Solute carrier family 35 member A2. | UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter; Antiporter transporting nucleotide sugars such as UDP-N- acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). May take part in heparan sulfate synthesis by supplying UDP-Glc-NAc, the donor substrate, and thus be involved in growth factor signaling (By similarity); Belongs to the TPT transporter family. SLC35D subfamily. | 0.511 |
| SLC35A2 | SLC35D3 | ENSPPYP00000022752 | ENSPPYP00000019079 | Solute carrier family 35 member A2. | Solute carrier family 35 member D3. | 0.471 |
| SLC35B1 | CR201_G0008818 | ENSPPYP00000010013 | ENSPPYP00000021755 | SLC35B1 isoform 2. | SLC35D2 isoform 2. | 0.582 |
| SLC35B1 | DERL1 | ENSPPYP00000010013 | ENSPPYP00000021151 | SLC35B1 isoform 2. | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | 0.405 |
| SLC35B1 | DNAJB11 | ENSPPYP00000010013 | ENSPPYP00000016085 | SLC35B1 isoform 2. | DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. | 0.420 |
| SLC35B1 | GART | ENSPPYP00000010013 | ENSPPYP00000012701 | SLC35B1 isoform 2. | Trifunctional purine biosynthetic protein adenosine-3; In the C-terminal section; belongs to the GART family. In the central section; belongs to the AIR synthase family. | 0.415 |
| SLC35B1 | P4HB | ENSPPYP00000010013 | ENSPPYP00000009818 | SLC35B1 isoform 2. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.443 |
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