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 |
| CLPP | DEF | WS2210 | WS2212 | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.909 |
| CLPP | RPLD | WS2210 | WS1715 | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 50S RIBOSOMAL PROTEIN L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. | 0.411 |
| CLPP | TIG | WS2210 | WS2209 | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | PUTATIVE TRIGGER FACTOR PROTEIN; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.939 |
| CLPP | WS2213 | WS2210 | WS2213 | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | SIGMA-54 INTERACTING PROTEIN. | 0.760 |
| CLPP | rplT | WS2210 | WS0823 | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | RIBOSOMAL PROTEIN L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.579 |
| DEF | CLPP | WS2212 | WS2210 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.909 |
| DEF | FMT | WS2212 | WS0507 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | METHIONYL-TRNA FORMYLTRANSFERASE; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.983 |
| DEF | RPLD | WS2212 | WS1715 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 50S RIBOSOMAL PROTEIN L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. | 0.881 |
| DEF | RPLR | WS2212 | WS1701 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 50S RIBOSOMAL PROTEIN L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.863 |
| DEF | TIG | WS2212 | WS2209 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | PUTATIVE TRIGGER FACTOR PROTEIN; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.962 |
| DEF | WS2213 | WS2212 | WS2213 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | SIGMA-54 INTERACTING PROTEIN. | 0.942 |
| DEF | rplT | WS2212 | WS0823 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | RIBOSOMAL PROTEIN L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.867 |
| DEF | rplU | WS2212 | WS0503 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | RIBOSOMAL PROTEIN L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.871 |
| DEF | rpsP | WS2212 | WS0548 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 30S ribosomal protein S16, WSU0548; Belongs to the bacterial ribosomal protein bS16 family. | 0.862 |
| DEF | rpsT | WS2212 | WS0817 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 30S RIBOSOMAL PROTEIN S20; Binds directly to 16S ribosomal RNA. | 0.888 |
| FMT | DEF | WS0507 | WS2212 | METHIONYL-TRNA FORMYLTRANSFERASE; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.983 |
| FMT | rplU | WS0507 | WS0503 | METHIONYL-TRNA FORMYLTRANSFERASE; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | RIBOSOMAL PROTEIN L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.653 |
| RPLD | CLPP | WS1715 | WS2210 | 50S RIBOSOMAL PROTEIN L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. | ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.411 |
| RPLD | DEF | WS1715 | WS2212 | 50S RIBOSOMAL PROTEIN L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.881 |
| RPLD | RPLR | WS1715 | WS1701 | 50S RIBOSOMAL PROTEIN L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. | 50S RIBOSOMAL PROTEIN L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.995 |
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