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 |
| sspA | sspB | BSU29570 | BSU09750 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | 0.741 |
| sspA | sspE | BSU29570 | BSU08660 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (gamma-type SASP); SASP are proteins degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism. These proteins may be involved in dormant spore's high resistance to UV light. | 0.977 |
| sspA | sspF | BSU29570 | BSU00450 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (alpha/beta-type SASP); May play some important role in either sporulation or the dormant spore. | 0.697 |
| sspA | sspI | BSU29570 | BSU28660 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | 0.448 |
| sspA | sspN | BSU29570 | BSU18020 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspN family. | 0.545 |
| sspA | sspO | BSU29570 | BSU17990 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspO family. | 0.550 |
| sspA | yizC | BSU29570 | BSU11139 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.445 |
| sspA | yqfX | BSU29570 | BSU25080 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.583 |
| sspA | yrrD | BSU29570 | BSU27470 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.501 |
| sspA | yuzA | BSU29570 | BSU31380 | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.518 |
| sspB | sspA | BSU09750 | BSU29570 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | 0.741 |
| sspB | sspE | BSU09750 | BSU08660 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (gamma-type SASP); SASP are proteins degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism. These proteins may be involved in dormant spore's high resistance to UV light. | 0.962 |
| sspB | sspF | BSU09750 | BSU00450 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (alpha/beta-type SASP); May play some important role in either sporulation or the dormant spore. | 0.588 |
| sspB | sspH | BSU09750 | BSU08110 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process; Belongs to the SspH family. | 0.475 |
| sspB | sspI | BSU09750 | BSU28660 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | 0.470 |
| sspB | sspJ | BSU09750 | BSU33340 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. | 0.523 |
| sspB | sspN | BSU09750 | BSU18020 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspN family. | 0.535 |
| sspB | sspO | BSU09750 | BSU17990 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspO family. | 0.543 |
| sspB | sspP | BSU09750 | BSU17980 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspP family. | 0.556 |
| sspB | tlp | BSU09750 | BSU18030 | Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. | Small acid-soluble spore protein (thioredoxin-like protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the Tlp family. | 0.503 |
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