WL94_39670 protein (Burkholderia cepacia) - STRING interaction network

Nodes:

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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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second shell of interactors

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filled nodes:
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Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.

Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

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textmining

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Score

WL94_39670

Uncharacterized protein (271 aa)

Predicted Functional Partners:

WL94_39680

0.656

WI67_11400

0.601

WL94_39665

0.512

WL94_31650

0.403

VL15_01145

0.401

Your Current Organism:

Burkholderia cepacia

NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia, Burkholderia cepacia genomovar I, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
VL15_01145	WL94_31650	DM42_2437	DM42_3244	annotation not available	Uncharacterized protein	0.652
VL15_01145	WL94_39670	DM42_2437	DM42_2986	annotation not available	Uncharacterized protein	0.401
WI67_11400	WL94_39670	DM42_2985	DM42_2986	annotation not available	Uncharacterized protein	0.601
WI67_11400	WL94_39680	DM42_2985	DM42_2984	annotation not available	33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress	0.801
WL94_31650	VL15_01145	DM42_3244	DM42_2437	Uncharacterized protein	annotation not available	0.652
WL94_31650	WL94_39670	DM42_3244	DM42_2986	Uncharacterized protein	Uncharacterized protein	0.403
WL94_39665	WL94_39670	DM42_2987	DM42_2986	annotation not available	Uncharacterized protein	0.512
WL94_39670	VL15_01145	DM42_2986	DM42_2437	Uncharacterized protein	annotation not available	0.401
WL94_39670	WI67_11400	DM42_2986	DM42_2985	Uncharacterized protein	annotation not available	0.601
WL94_39670	WL94_31650	DM42_2986	DM42_3244	Uncharacterized protein	Uncharacterized protein	0.403
WL94_39670	WL94_39665	DM42_2986	DM42_2987	Uncharacterized protein	annotation not available	0.512
WL94_39670	WL94_39680	DM42_2986	DM42_2984	Uncharacterized protein	33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress	0.656
WL94_39680	WI67_11400	DM42_2984	DM42_2985	33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress	annotation not available	0.801
WL94_39680	WL94_39670	DM42_2984	DM42_2986	33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress	Uncharacterized protein	0.656

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