STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
AARI_25410RHBT family amino acid transporter; Resistance to homoserine/threonine (RhtB) family protein (TC 2.A.76.y.z). The family includes homoserine, threonine and leucine efflux proteins. The transport reaction presumably catalyzed by members of the RhtB family is: amino acid (in) + nH+ (out) <--> amino acid (out) + nH+ (in). (207 aa)    
Predicted Functional Partners:
Putative MarR-family transcriptional regulator; Identified by match to protein family PF01047. Regulators with the marR-type HTH domain are present in bacteria and archaea and control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents and regulation of the virulence factor synthesis in pathogens of humans and plants. Many of the marR-like regulators respond to aromatic compounds.
Aminodeoxychorismate synthase catalyzes the biosynthesis of 4-amino-4-deoxychorismate from chorismate and glutamine. It is involved in folate biosynthesis.
Low molecular weight protein-tyrosine-phosphatase; Identified by match to protein family PF01451. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC: catalyse the removal of a phosphate group attached to a tyrosine residue, [...]
Putative drug exporter of the RND superfamily; Resistance-Nodulation-Cell Division (RND) superfamily (TC 2.A.6.y.z).
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
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