FB2026_03 , released September 17, 2026
Physical Interaction report
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General Information
Interaction Type
physical association
Interacting Genes
egr, grnd
FlyBase ID
FBig0000103740
Interaction Network
Interactions Browser links
egr network
grnd network
Reported Interactions
FBrf0228803-2.coIP.WB
Reference
Andersen et al., 2015
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2R+
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

bait

HA tag

egr 
grnd 

Grnd

prey

FLAG tag

grnd 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
TNF domain
necessary binding region

"ΔTNF" construct

grnd 
extracellular domain
sufficient binding region
aa 1-122

"extra" construct

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Source was cell extract of S2R+ cell line; bait produced from transfected construct; prey produced from transfected construct.

(Andersen et al., 2015)

The egr-grnd interaction is not affected by the E202A mutation to the grnd Traf6-binding motif.

(Andersen et al., 2015)
FBrf0228803-4.coIP.WB
Reference
Andersen et al., 2015
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2R+
Participants
Corresponds to
Reported as
Role
Note
grnd 

Grnd

bait

FLAG tag

grnd 
egr 

Egr

prey

HA tag

egr 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
TNF domain
necessary binding region

"ΔTNF" construct

grnd 
extracellular domain
sufficient binding region
aa 1-122

"extra" construct

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Source was cell extract of S2R+ cell line; bait produced from transfected construct; prey produced from transfected construct.

(Andersen et al., 2015)
FBrf0248618-1.CH.MW
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

neutral component
egr 
egr 

Egr

neutral component
egr 
egr 

Egr

neutral component
grnd 
grnd 

Grnd

neutral component
grnd 

Grnd

neutral component
grnd 
grnd 

Grnd

neutral component
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
extracellular domain
sufficient binding region
aa 146-409
grnd 
extracellular domain
sufficient binding region
aa 30-97
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

(Palmerini et al., 2021)
FBrf0248618-10.coIP.WB
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2-unspecified
Participants
Corresponds to
Reported as
Role
Note
egr 

Eiger

bait

HA tag

grnd 

Grnd

prey

FLAG tag

grnd 
grnd 
grnd 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
grnd 
interaction domain residue 46
mutation disrupting interaction
aa 46

F46A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66,67
mutation disrupting interaction
aa 66,67

H66A,N67A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66
mutation decreasing interaction
aa 66

H66A, coordinates relative to grnd-PB

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

(Palmerini et al., 2021)
FBrf0248618-11.coIP.WB
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2-unspecified
Participants
Corresponds to
Reported as
Role
Note
grnd 

Grnd

bait

FLAG tag

grnd 
grnd 
egr 

Eiger

prey

HA tag

Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
grnd 
interaction domain residue 46
mutation disrupting interaction
aa 46

F46A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66,67
mutation disrupting interaction
aa 66,67

H66A,N67A, coordinates relative to grnd-PB

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

(Palmerini et al., 2021)
FBrf0248618-4.SLS
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

neutral component
egr 
egr 

Egr

neutral component
egr 
egr 

Egr

neutral component
grnd 
grnd 

Grnd

neutral component
grnd 

Grnd

neutral component
grnd 
grnd 

Grnd

neutral component
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
extracellular domain
sufficient binding region
aa 146-409
grnd 
extracellular domain
sufficient binding region
aa 30-97
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

(Palmerini et al., 2021)

The grnd extracellular domain bound to the egr extracellular domain is a hetero-hexamer in solution.

(Palmerini et al., 2021)
FBrf0248618-6.ITC
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

bait
egr 
grnd 

Grnd

prey
grnd 
grnd 
grnd 
grnd 
grnd 
grnd 
grnd 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
extracellular domain
sufficient binding region
aa 146-409
grnd 
extracellular domain
sufficient binding region
aa 30-97
grnd 
interaction domain residue 51
mutation disrupting interaction
aa 51

T51A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66,67
mutation disrupting interaction
aa 66,67

H66A,N67A, coordinates relative to grnd-PB

grnd 
interaction domain residue 52
mutation decreasing interaction
aa 52

E52A, coordinates relative to grnd-PB, Kd = 1.3uM

grnd 
interaction domain residue 66
mutation decreasing interaction
aa 66

H66A, coordinates relative to grnd-PB, Kd = 4.8uM

grnd 
interaction domain residue 67
mutation decreasing interaction
aa 67

N67A, coordinates relative to grnd-PB, Kd = 4.5uM

grnd 
interaction domain residue 46
mutation disrupting interaction
aa 46

F46A, coordinates relative to grnd-PB

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Kd = 30.8nM

(Palmerini et al., 2021)

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

(Palmerini et al., 2021)
FBrf0248618-8.XC
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

neutral component
egr 

Egr

neutral component
egr 
egr 

Egr

neutral component
egr 
grnd 

Grnd

neutral component
grnd 
grnd 

Grnd

neutral component
grnd 

Grnd

neutral component
grnd 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
extracellular domain
sufficient binding region
aa 269-409
grnd 
extracellular domain
sufficient binding region
aa 30-81
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

The grnd extracellular domain bound to the egr extracellular domain is a hetero-hexamer in crystallo with 3:3 stoichiometry.

(Palmerini et al., 2021)

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

(Palmerini et al., 2021)
FBrf0248618-9.PD.MW
Reference
Palmerini et al., 2021
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
egr 

Egr

bait

Strep tag

egr 
egr 
egr 
egr 
grnd 

Grnd

prey
grnd 
grnd 
grnd 
grnd 
grnd 
grnd 
grnd 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
egr 
extracellular domain
sufficient binding region
aa 146-409
grnd 
extracellular domain
sufficient binding region
aa 30-97
egr 
interaction domain residue 337
mutation disrupting interaction
aa 337

D337A, coordinates relative to egr-PB

egr 
interaction domain residues 388,391
mutation disrupting interaction
aa 388,391

H388A,R391A, coordinates relative to egr-PB

egr 
interaction domain residues 396,401
mutation disrupting interaction
aa 396,401

R396A,R401A, coordinates relative to egr-PB

grnd 
interaction domain residue 51
mutation disrupting interaction
aa 51

T51A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66,67
mutation disrupting interaction
aa 66,67

H66A,N67A, coordinates relative to grnd-PB

grnd 
interaction domain residue 52
mutation decreasing interaction
aa 52

E52A, coordinates relative to grnd-PB

grnd 
interaction domain residue 66
mutation decreasing interaction
aa 66

H66A, coordinates relative to grnd-PB

grnd 
interaction domain residue 67
mutation decreasing interaction
aa 67

N67A, coordinates relative to grnd-PB

grnd 
interaction domain residue 46
mutation disrupting interaction
aa 46

F46A, coordinates relative to grnd-PB

Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

(Palmerini et al., 2021)
External Crossreferences and Linkouts ( 1 )
Linkouts
MIST - An integrated Molecular Interaction Database
References (2)