FB2026_03 , released September 17, 2026
Physical Interaction report
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General Information
Interaction Type
Interacting Genes
FlyBase ID
FBig0000095314
Interaction Network
Interactions Browser links
ph-p network
Reported Interactions
FBrf0102354-12.Y2H
Description
physical association
Assay
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
ph-p 

ph

bait

fused to LexA DNA-binding domain

ph-p 

ph

prey

fused to B42 activation domain

ph-p 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
ph-p 
N-terminal region
sufficient binding region
aa 1-522

numbering corresponds to ph-p-PA

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

ph-p protein interacts with itself.

Two-hybrid system: yeast LexA/B42.

FBrf0217832-1.CS.MW
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
ph-p 

ph-p

self
ph-p 

ph-p

self
ph-p 
ph-p 
ph-p 
ph-p 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
ph-p 
interaction domain
sufficient binding region
aa 1291-1577

coordinates relative to ph-p-PA

ph-p 
interaction domain
mutation increasing interaction
aa 1291-1501

coordinates relative to ph-p-PA, further truncation of ph-p to SAM domain only (aa. 1502-1577) leads to an increase in polymerization

ph-p 
SAM domain residue 1547
mutation decreasing interaction
aa 1547

L1547R, coordinates relative to ph-p-PA

ph-p 
SAM domain residue 1565
mutation decreasing interaction
aa 1565

L1565R, coordinates relative to ph-p-PA

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.

FBrf0217832-2.AFM
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
ph-p 

ph-p

self
ph-p 

ph-p

self
ph-p 
ph-p 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
ph-p 
linker and SAM domain
sufficient binding region
aa 1397-1577

coordinates relative to ph-p-PA

ph-p 
linker domain
mutation increasing interaction
aa 1397-1501

coordinates relative to ph-p-PA, further truncation of ph-p leads to an increase in polymerization

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.

FBrf0217832-3.NMR
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note
ph-p 

ph-p

self
ph-p 

ph-p

self
ph-p 
ph-p 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
ph-p 
linker domain
sufficient binding region
aa 1397-1507

coordinates relative to ph-p-PA

ph-p 
SAM domain
sufficient binding region
aa 1502-1577

coordinates relative to ph-p-PA

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.

NMR data suggests that linker domain and SAM domain can interact in trans.

External Crossreferences and Linkouts ( 0 )
References (2)