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 |
| Col5a2 | Fbn1 | ENSMUSP00000083620 | ENSMUSP00000099524 | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | 0.944 |
| Col5a2 | Fkbp7 | ENSMUSP00000083620 | ENSMUSP00000002809 | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | 0.465 |
| Col5a2 | Ppic | ENSMUSP00000083620 | ENSMUSP00000025419 | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. | Peptidyl-prolyl cis-trans isomerase C; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. | 0.441 |
| Erp44 | Fkbp7 | ENSMUSP00000030028 | ENSMUSP00000002809 | Endoplasmic reticulum resident protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | 0.477 |
| Erp44 | Hspa5 | ENSMUSP00000030028 | ENSMUSP00000028222 | Endoplasmic reticulum resident protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimeriz [...] | 0.789 |
| Fbn1 | Col5a2 | ENSMUSP00000099524 | ENSMUSP00000083620 | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. | 0.944 |
| Fbn1 | Fkbp7 | ENSMUSP00000099524 | ENSMUSP00000002809 | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | 0.443 |
| Fbn1 | Ppic | ENSMUSP00000099524 | ENSMUSP00000025419 | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | Peptidyl-prolyl cis-trans isomerase C; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. | 0.509 |
| Fbn1 | Rcn3 | ENSMUSP00000099524 | ENSMUSP00000019683 | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | Reticulocalbin-3; Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant- associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3. By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis. Has an anti-fibrotic activity by negatively regulating the secretion of type [...] | 0.404 |
| Fkbp6 | Fkbp7 | ENSMUSP00000043193 | ENSMUSP00000002809 | Inactive peptidyl-prolyl cis-trans isomerase FKBP6; Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be re [...] | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | 0.514 |
| Fkbp7 | Col5a2 | ENSMUSP00000002809 | ENSMUSP00000083620 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. | 0.465 |
| Fkbp7 | Erp44 | ENSMUSP00000002809 | ENSMUSP00000030028 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Endoplasmic reticulum resident protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). | 0.477 |
| Fkbp7 | Fbn1 | ENSMUSP00000002809 | ENSMUSP00000099524 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] | 0.443 |
| Fkbp7 | Fkbp6 | ENSMUSP00000002809 | ENSMUSP00000043193 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Inactive peptidyl-prolyl cis-trans isomerase FKBP6; Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be re [...] | 0.514 |
| Fkbp7 | Hspa5 | ENSMUSP00000002809 | ENSMUSP00000028222 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimeriz [...] | 0.694 |
| Fkbp7 | Plekha3 | ENSMUSP00000002809 | ENSMUSP00000107551 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Pleckstrin homology domain-containing family A member 3; Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferentially to phosphatidylinositol 4- phosphate (PtdIns4P) (By similarity). | 0.515 |
| Fkbp7 | Ppic | ENSMUSP00000002809 | ENSMUSP00000025419 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Peptidyl-prolyl cis-trans isomerase C; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. | 0.498 |
| Fkbp7 | Ppig | ENSMUSP00000002809 | ENSMUSP00000045945 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Peptidyl-prolyl cis-trans isomerase G; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. | 0.519 |
| Fkbp7 | Rcn3 | ENSMUSP00000002809 | ENSMUSP00000019683 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Reticulocalbin-3; Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant- associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3. By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis. Has an anti-fibrotic activity by negatively regulating the secretion of type [...] | 0.495 |
| Fkbp7 | Sumf2 | ENSMUSP00000002809 | ENSMUSP00000126036 | Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. | Inactive C-alpha-formylglycine-generating enzyme 2; Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1. Belongs to the sulfatase-modifying factor family. | 0.522 |
page 1 of 2