FB2026_03 , released September 17, 2026
Physical Interaction report
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General Information
Interaction Type
physical association
Interacting Genes
Rbp, Aplip1
FlyBase ID
FBig0000105379
Interaction Network
Interactions Browser links
Rbp network
Aplip1 network
Reported Interactions
FBrf0229297-3.Y2H
Reference
Siebert et al., 2015
Description
physical association
Assay
Collection
Source/Stage
adult head / adult stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
Rbp 

RBP

bait

fused to LexA DNA-binding domain

Rbp 
Rbp 
Rbp 
Rbp 
Aplip1 

Aplip1

prey

fused to GAL4 activation domain

Aplip1 
Aplip1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Rbp 
SH3-II domain
sufficient binding region
aa 1301-1383

coordinates relative to Rbp-PF

Rbp 
SH3-III domain
sufficient binding region
aa 1442-1510

coordinates relative to Rbp-PF

Rbp 
SH3-II domain residue P1374
mutation disrupting interaction
aa 1374

P1374L, coordinates relative to Rbp-PF

Rbp 
SH3-III domain residue P1501
mutation disrupting interaction
aa 1501

P1501L, coordinates relative to Rbp-PF

Aplip1 
N-terminal region
sufficient binding region
aa 77-215

contains only the first PxxP motif, coordinates relative to Aplip1-PB

Aplip1 
PxxP motif 1
necessary binding region
aa 156-159

PEIP to AEIA, coordinates relative to Aplip1-PB

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

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

(Siebert et al., 2015)

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey from adult head cDNA expression library).

(Siebert et al., 2015)

14 independent Aplip1 clones were recovered in the screen. Binding is mediated by the first, but not the second Aplip1 PxxP motif and either Rbp SH3 domain.

(Siebert et al., 2015)
FBrf0229297-4.ITC
Reference
Siebert et al., 2015
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
Rbp 

RBP

bait
Rbp 
Rbp 
Aplip1 

Aplip1

prey
Aplip1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Rbp 
SH3-II domain
sufficient binding region
aa 1301-1383

Kd = 4.1 uM, coordinates relative to Rbp-PF

Rbp 
SH3-III domain
sufficient binding region
aa 1442-1510

Kd = 1.4 uM, coordinates relative to Rbp-PF

Aplip1 
PxxP motif 1
sufficient binding region
TRRRRKLPEIPKNKK
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 synthesized in vitro.

(Siebert et al., 2015)

Together, both SH3 domains of Rbp bind more strongly to Aplip1 (Kd = 0.54 uM) than either SH3 domain alone. The Rbp-Aplip1 interaction is about ten-fold stronger than Rbp-cac and Rbp-Rim interactions.

(Siebert et al., 2015)
FBrf0229297-7a.XC
Reference
Siebert et al., 2015
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
Rbp 

RBP

neutral component
Rbp 

RBP

neutral component
Rbp 
Rbp 

RBP

neutral component
Rbp 
Aplip1 

Aplip1

neutral component
Aplip1 
Aplip1 

Aplip1

neutral component
Aplip1 

Aplip1

neutral component
Aplip1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Rbp 
SH3-II domain
sufficient binding region
aa 1301-1383

coordinates relative to Rbp-PF

Aplip1 
PxxP motif 1
sufficient binding region
TRRRRKLPEIPKNKK
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; peptide synthesized in vitro..

(Siebert et al., 2015)
FBrf0245633-10.Y2H
Reference
Petzoldt et al., 2020
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
Aplip1 

Aplip1

bait

fused to lexA DNA-binding domain

Aplip1 
Rbp 

RIM-BP

prey

fused to GAL4 activation domain

Rbp 
Rbp 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Rbp 
SH3-II domain
sufficient binding region
aa 1040-1382

coordinates relative to Rbp-PF

Rbp 
SH3-III domain
sufficient binding region
aa 1441-1507

coordinates relative to Rbp-PF

Aplip1 
PxxP domain
sufficient binding region
aa 1-250
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Two-hybrid system: yeast lexA-BD/GAL4-AD. Positive control.

(Petzoldt et al., 2020)

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

(Petzoldt et al., 2020)
FBrf0245633-9.Y2H
Reference
Petzoldt et al., 2020
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
Rbp 

RIM-BP

bait

fused to lexA DNA-binding domain

Rbp 
Rbp 
Aplip1 

Aplip1

prey

fused to GAL4 activation domain

Aplip1 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
Rbp 
SH3-II domain
sufficient binding region
aa 1040-1382

coordinates relative to Rbp-PF

Rbp 
SH3-III domain
sufficient binding region
aa 1441-1507

coordinates relative to Rbp-PF

Aplip1 
PxxP domain
sufficient binding region
aa 1-250
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).

(Petzoldt et al., 2020)

Two-hybrid system: yeast lexA-BD/GAL4-AD. Positive control.

(Petzoldt et al., 2020)
External Crossreferences and Linkouts ( 1 )
Linkouts
MIST - An integrated Molecular Interaction Database
References (2)