FB2024_03 , released June 25, 2024
Physical Interaction report
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General Information
Interaction Type
physical association
Interacting Genes
dx, N
FlyBase ID
FBig0000098473
Interaction Network
Interactions Browser links
dx network
N network
esyN Network Diagram
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Protein
RNA
Selected Interactor(s)
Common Interactor(s)
Reported Interactions
FBrf0076125-1.Y2H
Reference
Diederich et al., 1994
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
N 

Notch

bait

fused to LexA DNA-binding domain

N 
dx 

deltex

prey

fused to B42 activation domain

Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
intracellular domain
sufficient binding region
aa 1827-2258
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Two-hybrid system: yeast LexA-BD/B42-AD

(Diederich et al., 1994)

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

(Diederich et al., 1994)
FBrf0083287-1.Y2H
Reference
Matsuno et al., 1995
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dx 

Dx

bait

fused to LexA DNA-binding domain

N 

N

prey

fused to B42 activation domain

N 
N 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
ankyrin repeats 1-5
sufficient binding region
aa 1889-2076
N 
intracellular domain
necessary binding region
aa 1885-2110

deletion of ankryin repeats from aa 1885-2110

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

Two-hybrid system: yeast LexA-BD/B42-AD

(Matsuno et al., 1995)

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

(Matsuno et al., 1995)

No interaction detected between N and Mam, E(spl), or cact.

(Matsuno et al., 1995)
FBrf0083287-2a.Y2H
Reference
Matsuno et al., 1995
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
N 

N

bait

fused to LexA DNA-binding domain

dx 

Dx

prey

fused to B42 activation domain

dx 
dx 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
dx 
domain I
sufficient binding region
aa 1-204aa 46-303

does not contain opa repeat

contains opa repeat

dx 
domain I
necessary binding region
aa 1-305

construct dxII-III

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).

(Matsuno et al., 1995)

Two-hybrid system: yeast LexA-BD/B42-AD

(Matsuno et al., 1995)
FBrf0216353-2.Y2H
Reference
Muñoz-Descalzo et al., 2010
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
dx 

Dx

bait

fused to GAL4 DNA-binding domain

dx 
N 

N

prey

fused to GAL4 activation domain

N 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
Ank domain
sufficient binding region
aa 1894-2157
dx 
N-terminal domain
sufficient binding region
aa 1-394
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).

(Muñoz-Descalzo et al., 2010)

Two-hybrid system: yeast GAL4-BD/GAL4-AD

(Muñoz-Descalzo et al., 2010)
FBrf0225088-1.coIP.WB
Reference
Shimizu et al., 2014
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2-DGRC
Participants
Corresponds to
Reported as
Role
Note
dx 

Dx

bait

GFP tag

N 

N

prey
N 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
intracellular domain
mutation disrupting interaction
aa 2027

R2027A

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.

(Shimizu et al., 2014)

The N R2027A mutation, but not the D505A mutation of the N ligand binding domain, disrupts the N-dx interaction.

(Shimizu et al., 2014)
FBrf0256440-1.NMR
Reference
Carter et al., 2023
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
N 

Notch

neutral component
N 

Notch

neutral component
N 
N 

Notch

neutral component
N 
dx 

Dx

neutral component
dx 
dx 

Dx

neutral component
dx 

Dx

neutral component
dx 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
Ankyrin domain residue 2027
mutation disrupting interaction
aa 2027

R2027A, coordinates relative to N-PA; within the context of aa 1901-2048.

dx 
WWE2 domain
sufficient binding region
aa 26-261

coordinates relative to dx-PA

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.

(Carter et al., 2023)
FBrf0256440-2.CS
Reference
Carter et al., 2023
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
N 

dGB1

neutral component
N 
N 

dGB1

neutral component
N 
N 

dGB1

neutral component
dx 
dx 

dGB2

neutral component
dx 

dGB2

neutral component
dx 
dx 

dGB2

neutral component
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
Ankyrin domain
sufficient binding region
aa 1901-2048

coordinates relative to N-PA

dx 
WWE2 domain residues 74 and 91
mutation disrupting interaction
aa 74 and 91

K74A, Y91A, coordinates relative to dx-PA; within the context of aa 26-261.

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.

(Carter et al., 2023)
FBrf0256440-3.coIP.WB
Reference
Carter et al., 2023
Description
physical association
Assay
Collection
Source/Stage
Cell line used
S2R+
Participants
Corresponds to
Reported as
Role
Note
N 

AA

bait

FLAG tag

N 
dx 

BB

prey

V5 tag

dx 
dx 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
N 
intracellular domain residue 2027
sufficient binding region
aa 2027

R2027A; coordinates relative to N-PA; within the context of aa 1767-2703

dx 
WWE2 domain residue 74
mutation disrupting interaction
aa 74

K74A, coordinates relative to dx-PA

dx 
WWE2 domain residue 91
mutation disrupting interaction
aa 91

Y91A, coordinates relative to dx-PA

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.

(Carter et al., 2023)

dx K74A mutation disrupts interaction with N. N R2027A mutation only disrupts interaction with dx K74A or Y91A mutants. Note: complete deletion of dx WWE2 domain does not disrupt interaction with N.

(Carter et al., 2023)
External Crossreferences and Linkouts ( 1 )
Linkouts
MIST - An integrated Molecular Interaction Database
References (5)