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 |
| Dnaja1 | Dnaja2 | ENSRNOP00000010061 | ENSRNOP00000022573 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | 0.815 |
| Dnaja1 | Dnaja3 | ENSRNOP00000010061 | ENSRNOP00000073394 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member A3. | 0.549 |
| Dnaja1 | Dnaja4 | ENSRNOP00000010061 | ENSRNOP00000017053 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member A4. | 0.639 |
| Dnaja1 | Dnajb1 | ENSRNOP00000010061 | ENSRNOP00000032313 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.868 |
| Dnaja1 | Dnajb12 | ENSRNOP00000010061 | ENSRNOP00000049600 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member B12. | 0.400 |
| Dnaja1 | Dnajb13 | ENSRNOP00000010061 | ENSRNOP00000024256 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ (Hsp40) related, subfamily B, member 13, isoform CRA_a. | 0.611 |
| Dnaja1 | Dnajb2 | ENSRNOP00000010061 | ENSRNOP00000074369 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member B2. | 0.643 |
| Dnaja1 | Dnajb4 | ENSRNOP00000010061 | ENSRNOP00000075386 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ (Hsp40) homolog, subfamily B, member 4, isoform CRA_a. | 0.700 |
| Dnaja1 | Dnajb5 | ENSRNOP00000010061 | ENSRNOP00000075003 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member B5. | 0.599 |
| Dnaja1 | Dnajb6 | ENSRNOP00000010061 | ENSRNOP00000041883 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | 0.491 |
| Dnaja1 | Dnajb8 | ENSRNOP00000010061 | ENSRNOP00000049331 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member B8. | 0.405 |
| Dnaja1 | Dnajb9 | ENSRNOP00000010061 | ENSRNOP00000005363 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily B member 9; Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (By similarity). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similar [...] | 0.606 |
| Dnaja1 | Dnajc2 | ENSRNOP00000010061 | ENSRNOP00000016909 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily C member 2; Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histo [...] | 0.422 |
| Dnaja1 | Dnajc5 | ENSRNOP00000010061 | ENSRNOP00000020581 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily C member 5; Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). | 0.437 |
| Dnaja1 | Dnajc9 | ENSRNOP00000010061 | ENSRNOP00000009009 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ (Hsp40) homolog, subfamily C, member 9 (Predicted). | 0.510 |
| Dnaja1 | Samd13 | ENSRNOP00000010061 | ENSRNOP00000021984 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | Sterile alpha motif domain-containing 13. | 0.448 |
| Dnaja2 | Dnaja1 | ENSRNOP00000022573 | ENSRNOP00000010061 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | 0.815 |
| Dnaja2 | Dnaja3 | ENSRNOP00000022573 | ENSRNOP00000073394 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | DnaJ heat shock protein family (Hsp40) member A3. | 0.571 |
| Dnaja2 | Dnaja4 | ENSRNOP00000022573 | ENSRNOP00000017053 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | DnaJ heat shock protein family (Hsp40) member A4. | 0.733 |
| Dnaja2 | Dnajb1 | ENSRNOP00000022573 | ENSRNOP00000032313 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.817 |
page 1 of 8