DM42_2021 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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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 to each other.

Known Interactions

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experimentally determined

Predicted Interactions

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Score

DM42_2021

annotation not available (110 aa)

Predicted Functional Partners:

efeU_1

0.962

DM42_2861

0.789

efeU_2

0.763

DM42_2858

0.706

coxB

0.524

aauA

0.426

Your Current Organism:

Burkholderia cepacia

NCBI taxonomy Id: 292
Other names: ATCC 25416, B. 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
DM42_2021	DM42_2858	DM42_2021	DM42_2858	annotation not available	annotation not available	0.706
DM42_2021	DM42_2861	DM42_2021	DM42_2861	annotation not available	annotation not available	0.789
DM42_2021	aauA	DM42_2021	DM42_5689	annotation not available	Belongs to the aromatic amine dehydrogenase light chain family	0.426
DM42_2021	coxB	DM42_2021	DM42_2222	annotation not available	Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.524
DM42_2021	efeU_1	DM42_2021	DM42_2022	annotation not available	annotation not available	0.962
DM42_2021	efeU_2	DM42_2021	DM42_2860	annotation not available	annotation not available	0.763
DM42_2858	DM42_2021	DM42_2858	DM42_2021	annotation not available	annotation not available	0.706
DM42_2858	DM42_2861	DM42_2858	DM42_2861	annotation not available	annotation not available	0.945
DM42_2858	efeU_1	DM42_2858	DM42_2022	annotation not available	annotation not available	0.779
DM42_2858	efeU_2	DM42_2858	DM42_2860	annotation not available	annotation not available	0.954
DM42_2861	DM42_2021	DM42_2861	DM42_2021	annotation not available	annotation not available	0.789
DM42_2861	DM42_2858	DM42_2861	DM42_2858	annotation not available	annotation not available	0.945
DM42_2861	coxB	DM42_2861	DM42_2222	annotation not available	Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.526
DM42_2861	efeU_1	DM42_2861	DM42_2022	annotation not available	annotation not available	0.528
DM42_2861	efeU_2	DM42_2861	DM42_2860	annotation not available	annotation not available	0.968
aauA	DM42_2021	DM42_5689	DM42_2021	Belongs to the aromatic amine dehydrogenase light chain family	annotation not available	0.426
coxB	DM42_2021	DM42_2222	DM42_2021	Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	annotation not available	0.524
coxB	DM42_2861	DM42_2222	DM42_2861	Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	annotation not available	0.526
efeU_1	DM42_2021	DM42_2022	DM42_2021	annotation not available	annotation not available	0.962
efeU_1	DM42_2858	DM42_2022	DM42_2858	annotation not available	annotation not available	0.779

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