FB2026_03 , released September 17, 2026
Physical Interaction report
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General Information
Interaction Type
Interacting Genes
FlyBase ID
FBig0000097403
Interaction Network
Interactions Browser links
Nrx-1 network
RhoGAP100F network
Reported Interactions
FBrf0219330-1.coIP.WB
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

Nrx-1

bait

Syd-1

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

Immunoprecipitation of Nrx-1 from membrane fractions enriched for presynaptic active zone vesicles.

Source was adult heads of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.

FBrf0219330-2.Y2H
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

Nrx-1

bait

fused to GAL4 DNA binding domain

Syd-1

prey

fused to GAL4 activation domain

Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
C-terminal region
sufficient binding region
PDZ domain
mutation decreasing interaction
aa 165-170

R165A, L170A

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

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

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

FBrf0229911-3.Y2H
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

Nrx-1

bait

fused to LexA DNA-binding domain

Syd-1

prey

fused to GAL4 activation domain

Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
C-terminal region
sufficient binding region
NGDRGYKTESEKAAAYGSHNPNAALLGNTSTNGSYHQQRQHHMHGGGGGGGAGQQQHHAQQQMHNGHNGNGNGGGGGGGGMMSSGSGSLGYGSDGRPQMAGLVQPKAKKRDSKDVKEWYV
PDZ binding motif
necessary binding region
KEWYV

"C-term*" construct

N-terminal region
sufficient binding region
ENGRSVPDVTASPGRAPPGPLPANQMPAMGNQQHHGNQQHHGNQQQHHGNQHSNHRGQSGSLSNAAGVKDPVMLQGDFRKVSGISSEIFRQIEAVENDHDPNTAAALEAVERRGEMIVRVLEPRCMGSKQAVDAAHKLMNKADARHTVQLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIALESAVYNSGCLRVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVLAIRQRRGNRGTGSPGPPTLSRPEQKPPPVVVIKRDLRDEDLDETDRMPRPRSSRDRRTGDGREMTESRSRLGLGLNNYSPQSEQLDMYYNTRGGGGGAMGEPPNWGYKPPPPPSSVITEQPTKAHAFAPSHAYYQNAGTLESLAEKVHAFYPGQPGGPPVGPSRRMSTGT
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

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

Positive control.

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

FBrf0229911-5.ITC
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

Nrx-1

bait

Syd-1

prey

MBP tag

Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
PDZ domain
sufficient binding region
AVDAAHKLMNKADARHTVQLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIALESAVYNSGCLRVGDEILAVNLVDVTHMSLDDVVI
PDZ binding motif
sufficient binding region
DSKDVKEWYV
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

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

The RhoGAP100F PDZ domain binds the Nrx-1 PDZ binding motif peptide with Kd = 5uM (ten-fold greater affinity than interaction of the Spn PDZ domain with the Nrx-1 peptide).

Positive control.

External Crossreferences and Linkouts ( 1 )
Linkouts
MIST - An integrated Molecular Interaction Database
References (2)