(17 nodes) Stress response, and DnaJ domain network (Agrobacterium vitis)

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Your Input:
	hslU	Heat shock chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (435 aa)
	hslV	Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (186 aa)
	dnaK	DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
	dnaJ	Molecular chaperone DnaJ family; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwee [...] (380 aa)
	hrcA	Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (360 aa)
	grpE	GRPE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] (204 aa)
	dnaJ-2	Molecular chaperone DnaJ family. (429 aa)
	Avi_1385	Molecular chaperone Hsp70 family. (430 aa)
	lon	ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. (867 aa)
	dnaJ-3	Molecular chaperone DnaJ family. (203 aa)
	Avi_3078	Possible heat shock protein. (838 aa)
	ibpA	Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (155 aa)
	dnaJ-4	Molecular chaperone DnaJ family. (223 aa)
	trx	Thioredoxin. (334 aa)
	htpG	Chaperonine hsp90 protein; Molecular chaperone. Has ATPase activity. (643 aa)
	groES	10 KD chaperonin (protein CPN10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)
	groEL	Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (547 aa)

Your Current Organism:

Agrobacterium vitis

NCBI taxonomy Id: 311402
Other names: A. vitis S4, Agrobacterium vitis S4, Agrobacterium vitis str. S4, Agrobacterium vitis strain S4

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Avi_1385	dnaJ	Avi_1385	Avi_0308	Molecular chaperone Hsp70 family.	Molecular chaperone DnaJ family; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwee [...]	0.785
Avi_1385	dnaJ-2	Avi_1385	Avi_1023	Molecular chaperone Hsp70 family.	Molecular chaperone DnaJ family.	0.819
Avi_1385	dnaJ-3	Avi_1385	Avi_1945	Molecular chaperone Hsp70 family.	Molecular chaperone DnaJ family.	0.764
Avi_1385	dnaJ-4	Avi_1385	Avi_4048	Molecular chaperone Hsp70 family.	Molecular chaperone DnaJ family.	0.781
Avi_1385	groEL	Avi_1385	Avi_5830	Molecular chaperone Hsp70 family.	Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.835
Avi_1385	groES	Avi_1385	Avi_5829	Molecular chaperone Hsp70 family.	10 KD chaperonin (protein CPN10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.802
Avi_1385	grpE	Avi_1385	Avi_0399	Molecular chaperone Hsp70 family.	GRPE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]	0.908
Avi_1385	hrcA	Avi_1385	Avi_0398	Molecular chaperone Hsp70 family.	Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.787
Avi_1385	hslU	Avi_1385	Avi_0031	Molecular chaperone Hsp70 family.	Heat shock chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	0.549
Avi_1385	hslV	Avi_1385	Avi_0032	Molecular chaperone Hsp70 family.	Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.415
Avi_1385	htpG	Avi_1385	Avi_4272	Molecular chaperone Hsp70 family.	Chaperonine hsp90 protein; Molecular chaperone. Has ATPase activity.	0.938
Avi_1385	ibpA	Avi_1385	Avi_3739	Molecular chaperone Hsp70 family.	Small heat shock protein; Belongs to the small heat shock protein (HSP20) family.	0.440
Avi_1385	lon	Avi_1385	Avi_1700	Molecular chaperone Hsp70 family.	ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.	0.577
Avi_3078	dnaJ	Avi_3078	Avi_0308	Possible heat shock protein.	Molecular chaperone DnaJ family; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwee [...]	0.960
Avi_3078	dnaJ-2	Avi_3078	Avi_1023	Possible heat shock protein.	Molecular chaperone DnaJ family.	0.911
Avi_3078	dnaJ-3	Avi_3078	Avi_1945	Possible heat shock protein.	Molecular chaperone DnaJ family.	0.844
Avi_3078	dnaJ-4	Avi_3078	Avi_4048	Possible heat shock protein.	Molecular chaperone DnaJ family.	0.758
Avi_3078	dnaK	Avi_3078	Avi_0306	Possible heat shock protein.	DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.928
Avi_3078	groEL	Avi_3078	Avi_5830	Possible heat shock protein.	Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.852
Avi_3078	groES	Avi_3078	Avi_5829	Possible heat shock protein.	10 KD chaperonin (protein CPN10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.792