FB2025_01 , released February 20, 2025
Physical Interaction report
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General Information
Interaction Type
Interacting Genes
FlyBase ID
FBig0000098999
Interaction Network
Interactions Browser links
Sfmbt network
His3 network
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Protein
RNA
Selected Interactor(s)
Common Interactor(s)
Reported Interactions
FBrf0190547-18.FPS
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

dSfMBT

bait
His3 

H3

prey

fluorescein label

His3 
His3 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
His3 
histone tail
sufficient binding region
aa 1-15aa 19-35
His3 
methylation site
sufficient binding region
aa 9

H3K9me1 or H3K9me2

MBT repeats
sufficient binding region
aa 531-980
Isoform-specific participants
Corresponds to
Description
Role
Note
Comments concerning this interaction

Interaction in vitro; bait peptide synthesized in vitro; prey derived from wild-type embryonic extract.

Sfmbt binds to His3 histone tail that is monomethylated at Lys 9 (Kd = 7 uM) or dimethylated at Lys 9 (Kd = 9 uM). His3 peptides that are unmodified or trimethylated at Lys 9 bind with over ten-fold reduced affinity. No binding was observed for His3 peptides methylated at residues Lys 4 or Lys 27.

FBrf0208372-3.ITC
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

Sfmbt

bait
His3 

H3

prey
His3 
His3 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
His3 
histone tail
sufficient binding region
aa 1-15aa 19-35aa 28-43

ARTKQTARKSTGGKA

QLATKAARKSAPATGGV

SAPATGGVKKPHRYRPG

His3 
methylation site
necessary binding region
aa 4aa 9aa 27aa 36

H3K4me1 or H3K4me2

H3K9me1 or H3K9me2

H3K27me1 or H3K27me2

H3K36me1 or H3K36me2

4MBT domain
sufficient binding region
aa 532-980
methyl-lysine contact
mutation disrupting interaction
aa 917

D917A

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 peptide synthesized in vitro.

Sfmbt binds to various mono- and dimethylated lysines in His3 and His4 with very low micromolar affinity, but not to unmethylated or trimethylated peptides.

The lack of Sfmbt specificity for different His3 and His4 mono- or dimethylated lysine residues observed in this study contrasts with work in Klymenko et al., 2006 (FBrf0190547) and may reflect technical differences.

FBrf0208372-5.FPS
Description
physical association
Collection
Source/Stage
Cell line used
Participants
Corresponds to
Reported as
Role
Note

dSfMBT

bait
His3 

H3

prey

fluorescein label

His3 
His3 
Experimental entities
Corresponds to
Identifier
Reported
Role
Note
Subregions with role in interaction
Corresponds to
Description
Role
Coordinates
Note
His3 
histone tail
sufficient binding region
aa 1-15aa 19-35aa 28-43

ARTKQTARKSTGGKA

QLATKAARKSAPATGGV

SAPATGGVKKPHRYRPG

His3 
methylation site
necessary binding region
aa 4aa 9aa 27aa 36

H3K4me1 or H3K4me2

H3K9me1 or H3K9me2

H3K27me1 or H3K27me2

H3K36me1 or H3K36me2

4MBT domain
sufficient binding region
aa 532-980
methyl-lysine contact
mutation disrupting interaction
aa 917

D917A

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

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

Sfmbt binds to various mono- and dimethylated lysines in His3 and His4 with very low micromolar affinity, but not to unmethylated or trimethylated peptides.

The lack of Sfmbt specificity for different His3 and His4 mono- or dimethylated lysine residues observed in this study contrasts with work in Klymenko et al., 2006 (FBrf0190547) and may reflect technical differences.

External Crossreferences and Linkouts ( 0 )
References (2)