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 |
| B0432.14 | cpi-2 | B0432.14a.1 | R01B10.1a.1 | Uncharacterized protein. | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | 0.853 |
| T28H10.3 | cpi-2 | T28H10.3.1 | R01B10.1a.1 | Uncharacterized protein. | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | 0.788 |
| T28H10.3 | cpl-1 | T28H10.3.1 | T03E6.7a.1 | Uncharacterized protein. | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | 0.858 |
| T28H10.3 | cpz-1 | T28H10.3.1 | F32B5.8a.1 | Uncharacterized protein. | Cathepsin Z-1; Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Probably, required for the degradation of the old cuticle. Belongs to the peptidase C1 family. | 0.737 |
| W01A8.8 | cpi-2 | W01A8.8a.1 | R01B10.1a.1 | Uncharacterized protein. | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | 0.516 |
| W01A8.8 | famk-1 | W01A8.8a.1 | H03A11.1.1 | Uncharacterized protein. | Extracellular serine/threonine protein kinase CeFam20; Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Belongs to the FAM20 family. | 0.499 |
| cpi-2 | B0432.14 | R01B10.1a.1 | B0432.14a.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Uncharacterized protein. | 0.853 |
| cpi-2 | T28H10.3 | R01B10.1a.1 | T28H10.3.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Uncharacterized protein. | 0.788 |
| cpi-2 | W01A8.8 | R01B10.1a.1 | W01A8.8a.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Uncharacterized protein. | 0.516 |
| cpi-2 | cpl-1 | R01B10.1a.1 | T03E6.7a.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | 0.670 |
| cpi-2 | cpz-1 | R01B10.1a.1 | F32B5.8a.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Cathepsin Z-1; Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Probably, required for the degradation of the old cuticle. Belongs to the peptidase C1 family. | 0.705 |
| cpi-2 | famk-1 | R01B10.1a.1 | H03A11.1.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Extracellular serine/threonine protein kinase CeFam20; Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Belongs to the FAM20 family. | 0.499 |
| cpi-2 | mif-4 | R01B10.1a.1 | Y73B6BL.13.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | MIF (Macrophage migration Inhibitory Factor) related. | 0.815 |
| cpi-2 | scl-3 | R01B10.1a.1 | F49E11.11.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | SCP domain-containing protein; Belongs to the CRISP family. | 0.763 |
| cpi-2 | spi-1 | R01B10.1a.1 | R10H1.4.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Serine protease inhibitor 1 protein. | 0.698 |
| cpi-2 | vap-2 | R01B10.1a.1 | T05A10.5b.1 | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | Venom-Allergen-like Protein; Belongs to the CRISP family. | 0.485 |
| cpl-1 | T28H10.3 | T03E6.7a.1 | T28H10.3.1 | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | Uncharacterized protein. | 0.858 |
| cpl-1 | cpi-2 | T03E6.7a.1 | R01B10.1a.1 | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | Cystatin cpi-2; Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation. Belongs to the cystatin family. | 0.670 |
| cpl-1 | cpz-1 | T03E6.7a.1 | F32B5.8a.1 | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | Cathepsin Z-1; Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Probably, required for the degradation of the old cuticle. Belongs to the peptidase C1 family. | 0.638 |
| cpl-1 | vap-2 | T03E6.7a.1 | T05A10.5b.1 | Cathepsin L-like; Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome- like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval de [...] | Venom-Allergen-like Protein; Belongs to the CRISP family. | 0.436 |
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