Q7K480 · MEPCE_DROME

Function

function

S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it (By similarity).
Required for dorso-ventral patterning in oogenesis and for anterior-posterior pattern formation during embryogenesis, possibly by binding and stabilizing 7SK RNA, thereby promoting formation of a repressive RNA-protein complex (PubMed:21262214).

Catalytic activity

Features

Showing features for binding site.

113671002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Binding site808S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site828-830S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site851-852S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site988-989S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1010S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionmethyltransferase activity
Molecular FunctionO-methyltransferase activity
Molecular FunctionRNA methyltransferase activity
Molecular FunctionRNA polymerase II-specific DNA-binding transcription factor binding
Molecular FunctionsnRNA binding
Biological Processdevelopmental process
Biological Processmethylation
Biological Processnegative regulation of translation
Biological ProcesssnRNA modification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    7SK snRNA methylphosphate capping enzyme bin3
  • EC number
  • Alternative names
    • Bicoid-interacting protein 3

Gene names

    • Name
      bin3
    • ORF names
      CG8276

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q7K480
  • Secondary accessions
    • Q86LF5
    • Q9NJV6

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Severe defect in oogenesis: females lay eggs, however, up to 50% do not initiate development and many show a dorsalized phenotype. Among the eggs that do initiate development, up to 20% fail to complete embryogenesis and of these, nearly all display severe head defects and die as unhatched larvae or die soon after hatching. Mutants show anterior pattern defects and fail to repress the translation of caudal mRNA and exhibit head involution defects. Mutants also display a severe reduction in the level of 7SK RNA and reduced binding of bicoid/bcd to the caudal 3' UTR.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002892691-13677SK snRNA methylphosphate capping enzyme bin3
Modified residue688Phosphoserine
Modified residue1116Phosphothreonine
Modified residue1123Phosphoserine
Modified residue1242Phosphoserine
Modified residue1251Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Distributed throughout the early embryo.

Developmental stage

Detectable in early embryos. Present coincident with bicoid/bcd expression, with peak levels detected in 0-2 hours embryos. Expression is lower during cellularization stages (2-4 hours) and drops dramatically during late embryonic development (4-24 hours). Very little, if any expression is detected in unfertilized eggs.

Gene expression databases

Interaction

Subunit

Interacts with bicoid/bcd.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q7K480bcd P090814EBI-180984, EBI-196628
View interactors in UniProtKB
View CPX-2830 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-107Disordered
Compositional bias11-36Polar residues
Compositional bias53-80Polar residues
Region143-181Disordered
Compositional bias323-351Polar residues
Region323-355Disordered
Region381-443Disordered
Compositional bias395-415Basic residues
Region468-559Disordered
Compositional bias476-538Polar residues
Region608-734Disordered
Compositional bias627-646Basic and acidic residues
Compositional bias671-687Polar residues
Compositional bias719-734Polar residues
Domain806-1115Bin3-type SAM
Region894-927Disordered
Compositional bias903-926Basic residues
Region1150-1203Disordered
Compositional bias1152-1203Polar residues
Region1236-1281Disordered
Region1345-1367Disordered

Sequence similarities

Belongs to the methyltransferase superfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,367
  • Mass (Da)
    146,234
  • Last updated
    2006-10-03 v1
  • Checksum
    FA3EDD8FDAA7A551
MEKRLSDSPGDCRVTRSTMTPTLRLDQTSRQEPLPQQPDNGPAAAPGKSKSPTPLPGKSQAAQHHQFRAPQQQQGPKNRNKAWSKRQHKAGGKHNPSACVGASSGQAQSTGSSVIAATLLPTAASAHKADLENIQNIHNKNLTAGGGVNHHGNAGTAHHGGGGGAGAHHAAAGGHHHHHNTRLAQNAAAGGASGGGTIQMHKKMLRGHHHHVLCAGNNANHTCCLVTGCNGSSIGGVGVAGSGGATASAGGGGASCKEAQSCKDTSSLSGNSSIAGSAGAGNAVHYCCGRSKFFLPEKRLRKEVIVPPTKFLLGGNISDPLNLNSLQNENTSNASSTNNTPATTPRQSPITTPPKVEVIIPPNIHDPLHLLDPVDSMEYEKQLTSPMKRAGPGGGMLHHRQHHYRTRKNRKRRRFDSNNTSHAGDEGGVGSELTDEPPLPAATSSLAASPVAAPLNVGGSLLLSESAAPAPGETAEMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQHVAAAAEELPTPETSAAAETPAEEMLLSCSATSASLVASTLAERRASRDLRLDLSSTCYGVGGTGLSFGGSISSSVGSSFGGGGRKRKISESSTSQKSKKFHRHDAMDKIVSPVVPQPGAWKRPPRILQPSGARKPSTRRSTSVSESELLSPVEEQPPKQLPLIGVEIPRDDTPDLPDHGLGSPLSTTSGATSHTAGEQDSLAGVDISMGDTLGSGVVGKAPLTSSLMLEPAKIPPIKMLPKFRADGLKYRYGNFDRYVDFRQMNEFRDVRLQVFQRHVELFENKDILDIGCNVGHMTITVARHLAPKTIVGIDIDRELVARARRNLSIFVRIPKEEKLLEVKAEPTVDAKANIAVKDETSGAAHKKTRRGKRRRKVHQGIHHHHHHHHDLEQLQQQQKLNSLLVKPHEFFPISFPLTYGRIPRILSSSKSPNMLGNKNQFPANVFFRHTNYVLKDESLMASDTQQYDLILCLSVTKWIHLNFGDNGLKMAFKRMFNQLRPGGKLILEAQNWASYKKKKNLTPEIYNNYKQIEFFPNKFHEYLLSSEVGFSHSYTLGVPRHMNKGFCRPIQLYAKGDYTPNHVRWSDAYYPQTPYEAYRGIYATLPVHRMGGGGSSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNPLETDSYQPSYDMEYLNHMYVFASPLYQTVWSPPASLRKSSSHTPVFGSVRDAELDGDGSGGGGSGGGSYHRHVYPPNDDTCSPNANACNAFNSIRDADTDDSNQLPGGSRRHVYATNCGESSSSPQVNHHDAVGEFVDGLMDDEQKSSTGGGTGGAAYCDLSDA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E2QC61E2QC61_DROMEbin31367

Sequence caution

The sequence AAO47868.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias11-36Polar residues
Compositional bias53-80Polar residues
Compositional bias323-351Polar residues
Compositional bias395-415Basic residues
Compositional bias476-538Polar residues
Sequence conflict573in Ref. 1; AAF63187
Compositional bias627-646Basic and acidic residues
Compositional bias671-687Polar residues
Compositional bias719-734Polar residues
Compositional bias903-926Basic residues
Sequence conflict1152in Ref. 5; AAO47868
Compositional bias1152-1203Polar residues
Sequence conflict1267in Ref. 5; AAO47868

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF097636
EMBL· GenBank· DDBJ
AAF63187.1
EMBL· GenBank· DDBJ
mRNA
AE013599
EMBL· GenBank· DDBJ
AAF57267.2
EMBL· GenBank· DDBJ
Genomic DNA
AY052142
EMBL· GenBank· DDBJ
AAK93566.1
EMBL· GenBank· DDBJ
mRNA
BT004890
EMBL· GenBank· DDBJ
AAO47868.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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