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 |
| TK0882 | speE | TK0882 | TK0147 | Agmatinase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine and urea. It can also use agmatine to yield putrescine. | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1- aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The [...] | 0.986 |
| speE | TK0882 | TK0147 | TK0882 | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1- aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The [...] | Agmatinase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine and urea. It can also use agmatine to yield putrescine. | 0.986 |
| speE | speH | TK0147 | TK1592 | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1- aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The [...] | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.999 |
| speH | speE | TK1592 | TK0147 | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1- aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The [...] | 0.999 |