FB2026_01 , released March 12, 2026
FB2026_01 , released March 12, 2026
Physical Interaction report
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General Information
Interaction Type
physical association
Interacting Genes
dlg1
FlyBase ID
FBig0000099233
Interaction Network
Interactions Browser links
dlg1 network
Reported Interactions
FBrf0189924-1.coIP.WB
Reference
Siegrist and Doe, 2005
Description
physical association
Assay
Collection
Source/Stage
organism / embryonic stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg

bait

GFP tag

dlg1 

Dlg

prey
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Tagged construct was expressed in central nervous system.

(Siegrist and Doe, 2005)

dlg1 can form oligomers.

(Siegrist and Doe, 2005)

Source was embryos of transgenic fly line; bait produced from tagged transgenic construct; prey produced from endogenous gene.

(Siegrist and Doe, 2005)
FBrf0195273-4.PD.WB
Reference
Qian and Prehoda, 2006
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg

bait

GST tag

dlg1 

Dlg

prey

His tag

dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
PDZ3-SH3 domain
sufficient binding region
aa 481-691

coordinates relative to dlg1-PE

dlg1 
HOOK-GK domain
sufficient binding region
aa 764-960

coordinates relative to dlg1-PE

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 and labeled by in vitro translation.

(Qian and Prehoda, 2006)
FBrf0215144-1.Y2H
Reference
Marcette et al., 2009
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

DlgSH3

bait

fused to GAL4 DNA-binding domain

dlg1 

DlgGK

prey

fused to GAL4 activation domain

dlg1 
dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
GK domain
sufficient binding region
aa 771-975

coordinates relative to dlg1-PG

dlg1 
SH3 domain
sufficient binding region
aa 598-784

coordinates relative to dlg1-PG

dlg1 
GK domain
mutation disrupting interaction
aa 822

R822A, coordinates relative to dlg1-PG

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

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

(Marcette et al., 2009)

Two-hybrid system: yeast GAL4-BD/GAL4-AD. The GK domain of dlg1 interacts with its SH3 domain in trans.

(Marcette et al., 2009)
FBrf0215144-3.PD.WB
Reference
Marcette et al., 2009
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

DlgGK

bait

GST tag

dlg1 

DlgSH3

prey

His tag

dlg1 
dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
GK domain
sufficient binding region
aa 771-975

coordinates relative to dlg1-PG

dlg1 
GK domain
necessary binding region
aa 964-975

coordinates relative to dlg1-PG

dlg1 
SH3 domain
sufficient binding region
aa 598-784

coordinates relative to dlg1-PG

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.

(Marcette et al., 2009)
FBrf0215470-1.PD.A
Reference
Newman and Prehoda, 2009
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg

bait

GST tag

dlg1 

Dlg

prey

HIS tag

dlg1 
dlg1 
dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
SH3 domain
sufficient binding region
aa 581-681

coordinates relative to dlg1-PG

dlg1 
E-GK-F domain
sufficient binding region
aa 771-975

coordinates relative to dlg1-PG

dlg1 
F domain
necessary binding region
aa 962-975

coordinates relative to dlg1-PG

dlg1 
sw mutant
mutation disrupting interaction
aa 961

Frameshift mutation that deletes the F domain, coordinates relative to dlg1-PG

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 and labeled by in vitro translation.

(Newman and Prehoda, 2009)
FBrf0238227-1.CH.MW
Reference
Ghosh et al., 2018
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg1

neutral component
dlg1 

Dlg1

neutral component
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
L27 domain
sufficient binding region
aa 1-97
dlg1 
L27 domain residue 14
mutation increasing interaction
aa 14

L14G, peak broadens towards higher order oligomers larger than dimer.

dlg1 
L27 domain residue 18
mutation increasing interaction
aa 18

Y18G, peak broadens towards higher order oligomers larger than dimer.

dlg1 
L27 domain residue 14,15,18
mutation increasing interaction
aa 14,15,18

L14G,L15G,Y18G, completely forms higher order oligomer larger than dimer.

dlg1 
L27 domain residue 26
mutation increasing interaction
aa 26

Q26A, peak broadens towards higher order oligomers larger than dimer.

dlg1 
L27 domain residue 26,27
mutation increasing interaction
aa 26,27

Q26A,D27A peak broadens towards higher order oligomers larger than dimer.

dlg1 
L27 domain residue 39
mutation increasing interaction
aa 39

R39A, completely forms higher order oligomer larger than dimer.

dlg1 
L27 domain residue 39,42
mutation increasing interaction
aa 39,42

R39A,K42A completely forms higher order oligomer larger than dimer.

dlg1 
L27 domain residue 34,37,38
mutation decreasing interaction
aa 34,37,38

I34G,V37G,I38G, dimer is destabilized.

dlg1 
L27 domain residue 41
mutation decreasing interaction
aa 41

F41A, dimer is destabilized.

dlg1 
L27 domain residue 44
mutation increasing interaction
aa 44

R44A, peak broadens towards higher order oligomers larger than dimer.

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

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

(Ghosh et al., 2018)

The L27 domain of dlg1 exists as a dimer in solution. Oligomeric state of full-length protein not shown.

(Ghosh et al., 2018)
FBrf0238227-2.CS.MW
Reference
Ghosh et al., 2018
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg1

neutral component
dlg1 

Dlg1

neutral component
dlg1 
dlg1 
dlg1 
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
L27 domain
sufficient binding region
aa 1-97
dlg1 
L27 domain residue 14,15,18
mutation increasing interaction
aa 14,15,18

L14G,L15G,Y18G, 85% of the mutant protein sediments as an octamer.

dlg1 
L27 domain residue 34,37,38
mutation decreasing interaction
aa 34,37,38

I34G,V37G,I38G, dimer is destabilized.

dlg1 
L27 domain residue 41
mutation decreasing interaction
aa 41

F41A, dimer is destabilized.

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

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

(Ghosh et al., 2018)

The estimated molecular weight of the L27 domain of dlg1 is consistent with it being a dimer in solution. Oligomeric state of full-length protein not shown.

(Ghosh et al., 2018)
FBrf0238227-3.XC
Reference
Ghosh et al., 2018
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dlg1 

Dlg1

neutral component
dlg1 

Dlg1

neutral component
dlg1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dlg1 
L27 domain
sufficient binding region
aa 1-97
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

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

(Ghosh et al., 2018)

Crystal structure of the dlg1 L27 domain dimer.

(Ghosh et al., 2018)
External Crossreferences and Linkouts ( 0 )
References (5)