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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cltca | cltcb | ENSDARP00000063848 | ENSDARP00000119038 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.922 |
| cltca | cltcl1 | ENSDARP00000063848 | ENSDARP00000109883 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.900 |
| cltcb | cltca | ENSDARP00000119038 | ENSDARP00000063848 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.922 |
| cltcb | cltcl1 | ENSDARP00000119038 | ENSDARP00000109883 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.900 |
| cltcl1 | cltca | ENSDARP00000109883 | ENSDARP00000063848 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.900 |
| cltcl1 | cltcb | ENSDARP00000109883 | ENSDARP00000119038 | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. | 0.900 |
| fkbp16 | hsp90aa1.1 | ENSDARP00000009132 | ENSDARP00000022302 | Peptidylprolyl isomerase. | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | 0.433 |
| fkbp16 | hsp90aa1.2 | ENSDARP00000009132 | ENSDARP00000026065 | Peptidylprolyl isomerase. | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | 0.433 |
| fkbp16 | hsp90ab1 | ENSDARP00000009132 | ENSDARP00000014978 | Peptidylprolyl isomerase. | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.433 |
| fkbp8 | hsp90aa1.1 | ENSDARP00000000956 | ENSDARP00000022302 | Peptidylprolyl isomerase. | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | 0.727 |
| fkbp8 | hsp90aa1.2 | ENSDARP00000000956 | ENSDARP00000026065 | Peptidylprolyl isomerase. | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | 0.440 |
| fkbp8 | hsp90ab1 | ENSDARP00000000956 | ENSDARP00000014978 | Peptidylprolyl isomerase. | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.433 |
| hsp90aa1.1 | fkbp16 | ENSDARP00000022302 | ENSDARP00000009132 | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | Peptidylprolyl isomerase. | 0.433 |
| hsp90aa1.1 | fkbp8 | ENSDARP00000022302 | ENSDARP00000000956 | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | Peptidylprolyl isomerase. | 0.727 |
| hsp90aa1.1 | hsp90aa1.2 | ENSDARP00000022302 | ENSDARP00000026065 | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | 0.905 |
| hsp90aa1.1 | hsp90ab1 | ENSDARP00000022302 | ENSDARP00000014978 | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.902 |
| hsp90aa1.2 | fkbp16 | ENSDARP00000026065 | ENSDARP00000009132 | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | Peptidylprolyl isomerase. | 0.433 |
| hsp90aa1.2 | fkbp8 | ENSDARP00000026065 | ENSDARP00000000956 | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | Peptidylprolyl isomerase. | 0.440 |
| hsp90aa1.2 | hsp90aa1.1 | ENSDARP00000026065 | ENSDARP00000022302 | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | Heat shock protein HSP 90-alpha 1; 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 which is essential for its chaperone 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. Engages with a [...] | 0.905 |
| hsp90aa1.2 | hsp90ab1 | ENSDARP00000026065 | ENSDARP00000014978 | Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.902 |
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