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 |
| glpK | jamm1 | HVO_1541 | HVO_2505 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | 0.936 |
| glpK | panA | HVO_1541 | HVO_0850 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | 0.939 |
| glpK | panB | HVO_1541 | HVO_1957 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase- [...] | 0.939 |
| glpK | rpl40e | HVO_1541 | HVO_0439 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | 50S ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.905 |
| jamm1 | glpK | HVO_2505 | HVO_1541 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | 0.936 |
| jamm1 | panA | HVO_2505 | HVO_0850 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | 0.922 |
| jamm1 | panB | HVO_2505 | HVO_1957 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase- [...] | 0.861 |
| jamm1 | rpl40e | HVO_2505 | HVO_0439 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | 50S ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.893 |
| jamm1 | rps19 | HVO_2505 | HVO_2560 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | 30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | 0.876 |
| jamm1 | rps3 | HVO_2505 | HVO_2558 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | 30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family. | 0.857 |
| jamm1 | samp1 | HVO_2505 | HVO_2619 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Ubiquitin-like modifier protein SAMP1; Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in molybdenum cofactor (MoCo) biosynthesis. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP1 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes. | 0.861 |
| jamm1 | samp2 | HVO_2505 | HVO_0202 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Ubiquitin-like modifier protein SAMP2; Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C- terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins. May serve as a proteolytic signal in the cell to target proteins for degradati [...] | 0.926 |
| jamm1 | tif2a | HVO_2505 | HVO_0699 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | Translation initiation factor aIF-2 alpha subunit; eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. Belongs to the eIF-2-alpha family. | 0.846 |
| jamm1 | ubaA | HVO_2505 | HVO_0558 | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | SAMP-activating enzyme E1; Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus. In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs. | 0.948 |
| panA | glpK | HVO_0850 | HVO_1541 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA. | 0.939 |
| panA | jamm1 | HVO_0850 | HVO_2505 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | Metalloprotease JAMM1, desampylating; Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. | 0.922 |
| panA | panB | HVO_0850 | HVO_1957 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase- [...] | 0.902 |
| panA | rpl40e | HVO_0850 | HVO_0439 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | 50S ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.772 |
| panA | rps3 | HVO_0850 | HVO_2558 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | 30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family. | 0.494 |
| panA | samp1 | HVO_0850 | HVO_2619 | Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPas [...] | Ubiquitin-like modifier protein SAMP1; Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in molybdenum cofactor (MoCo) biosynthesis. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP1 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes. | 0.541 |
page 1 of 4