Q7K480 · MEPCE_DROME
- Protein7SK snRNA methylphosphate capping enzyme bin3
- Genebin3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1367 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- a 5'-end triphospho-guanosine-ribonucleotide-snRNA + S-adenosyl-L-methionine = a 5'-end methyltriphosphate-guanosine-ribonucleotide-snRNA + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 808 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 828-830 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GCN | ||||||
Binding site | 851-852 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DI | ||||||
Binding site | 988-989 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 1010 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | methyltransferase activity | |
Molecular Function | O-methyltransferase activity | |
Molecular Function | RNA methyltransferase activity | |
Molecular Function | RNA polymerase II-specific DNA-binding transcription factor binding | |
Molecular Function | snRNA binding | |
Biological Process | developmental process | |
Biological Process | methylation | |
Biological Process | negative regulation of translation | |
Biological Process | snRNA modification |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name7SK snRNA methylphosphate capping enzyme bin3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ7K480
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000289269 | 1-1367 | 7SK snRNA methylphosphate capping enzyme bin3 | |||
Sequence: MEKRLSDSPGDCRVTRSTMTPTLRLDQTSRQEPLPQQPDNGPAAAPGKSKSPTPLPGKSQAAQHHQFRAPQQQQGPKNRNKAWSKRQHKAGGKHNPSACVGASSGQAQSTGSSVIAATLLPTAASAHKADLENIQNIHNKNLTAGGGVNHHGNAGTAHHGGGGGAGAHHAAAGGHHHHHNTRLAQNAAAGGASGGGTIQMHKKMLRGHHHHVLCAGNNANHTCCLVTGCNGSSIGGVGVAGSGGATASAGGGGASCKEAQSCKDTSSLSGNSSIAGSAGAGNAVHYCCGRSKFFLPEKRLRKEVIVPPTKFLLGGNISDPLNLNSLQNENTSNASSTNNTPATTPRQSPITTPPKVEVIIPPNIHDPLHLLDPVDSMEYEKQLTSPMKRAGPGGGMLHHRQHHYRTRKNRKRRRFDSNNTSHAGDEGGVGSELTDEPPLPAATSSLAASPVAAPLNVGGSLLLSESAAPAPGETAEMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQHVAAAAEELPTPETSAAAETPAEEMLLSCSATSASLVASTLAERRASRDLRLDLSSTCYGVGGTGLSFGGSISSSVGSSFGGGGRKRKISESSTSQKSKKFHRHDAMDKIVSPVVPQPGAWKRPPRILQPSGARKPSTRRSTSVSESELLSPVEEQPPKQLPLIGVEIPRDDTPDLPDHGLGSPLSTTSGATSHTAGEQDSLAGVDISMGDTLGSGVVGKAPLTSSLMLEPAKIPPIKMLPKFRADGLKYRYGNFDRYVDFRQMNEFRDVRLQVFQRHVELFENKDILDIGCNVGHMTITVARHLAPKTIVGIDIDRELVARARRNLSIFVRIPKEEKLLEVKAEPTVDAKANIAVKDETSGAAHKKTRRGKRRRKVHQGIHHHHHHHHDLEQLQQQQKLNSLLVKPHEFFPISFPLTYGRIPRILSSSKSPNMLGNKNQFPANVFFRHTNYVLKDESLMASDTQQYDLILCLSVTKWIHLNFGDNGLKMAFKRMFNQLRPGGKLILEAQNWASYKKKKNLTPEIYNNYKQIEFFPNKFHEYLLSSEVGFSHSYTLGVPRHMNKGFCRPIQLYAKGDYTPNHVRWSDAYYPQTPYEAYRGIYATLPVHRMGGGGSSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNPLETDSYQPSYDMEYLNHMYVFASPLYQTVWSPPASLRKSSSHTPVFGSVRDAELDGDGSGGGGSGGGSYHRHVYPPNDDTCSPNANACNAFNSIRDADTDDSNQLPGGSRRHVYATNCGESSSSPQVNHHDAVGEFVDGLMDDEQKSSTGGGTGGAAYCDLSDA | ||||||
Modified residue | 688 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1116 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1123 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1242 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1251 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7K480 | bcd P09081 | 4 | EBI-180984, EBI-196628 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-107 | Disordered | ||||
Sequence: MEKRLSDSPGDCRVTRSTMTPTLRLDQTSRQEPLPQQPDNGPAAAPGKSKSPTPLPGKSQAAQHHQFRAPQQQQGPKNRNKAWSKRQHKAGGKHNPSACVGASSGQA | ||||||
Compositional bias | 11-36 | Polar residues | ||||
Sequence: DCRVTRSTMTPTLRLDQTSRQEPLPQ | ||||||
Compositional bias | 53-80 | Polar residues | ||||
Sequence: TPLPGKSQAAQHHQFRAPQQQQGPKNRN | ||||||
Region | 143-181 | Disordered | ||||
Sequence: TAGGGVNHHGNAGTAHHGGGGGAGAHHAAAGGHHHHHNT | ||||||
Compositional bias | 323-351 | Polar residues | ||||
Sequence: LNSLQNENTSNASSTNNTPATTPRQSPIT | ||||||
Region | 323-355 | Disordered | ||||
Sequence: LNSLQNENTSNASSTNNTPATTPRQSPITTPPK | ||||||
Region | 381-443 | Disordered | ||||
Sequence: KQLTSPMKRAGPGGGMLHHRQHHYRTRKNRKRRRFDSNNTSHAGDEGGVGSELTDEPPLPAAT | ||||||
Compositional bias | 395-415 | Basic residues | ||||
Sequence: GMLHHRQHHYRTRKNRKRRRF | ||||||
Region | 468-559 | Disordered | ||||
Sequence: APAPGETAEMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQHVAAAAEELPTPETSAAAETPA | ||||||
Compositional bias | 476-538 | Polar residues | ||||
Sequence: EMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQH | ||||||
Region | 608-734 | Disordered | ||||
Sequence: SISSSVGSSFGGGGRKRKISESSTSQKSKKFHRHDAMDKIVSPVVPQPGAWKRPPRILQPSGARKPSTRRSTSVSESELLSPVEEQPPKQLPLIGVEIPRDDTPDLPDHGLGSPLSTTSGATSHTAG | ||||||
Compositional bias | 627-646 | Basic and acidic residues | ||||
Sequence: SESSTSQKSKKFHRHDAMDK | ||||||
Compositional bias | 671-687 | Polar residues | ||||
Sequence: RKPSTRRSTSVSESELL | ||||||
Compositional bias | 719-734 | Polar residues | ||||
Sequence: GSPLSTTSGATSHTAG | ||||||
Domain | 806-1115 | Bin3-type SAM | ||||
Sequence: DVRLQVFQRHVELFENKDILDIGCNVGHMTITVARHLAPKTIVGIDIDRELVARARRNLSIFVRIPKEEKLLEVKAEPTVDAKANIAVKDETSGAAHKKTRRGKRRRKVHQGIHHHHHHHHDLEQLQQQQKLNSLLVKPHEFFPISFPLTYGRIPRILSSSKSPNMLGNKNQFPANVFFRHTNYVLKDESLMASDTQQYDLILCLSVTKWIHLNFGDNGLKMAFKRMFNQLRPGGKLILEAQNWASYKKKKNLTPEIYNNYKQIEFFPNKFHEYLLSSEVGFSHSYTLGVPRHMNKGFCRPIQLYAKGDY | ||||||
Region | 894-927 | Disordered | ||||
Sequence: KDETSGAAHKKTRRGKRRRKVHQGIHHHHHHHHD | ||||||
Compositional bias | 903-926 | Basic residues | ||||
Sequence: KKTRRGKRRRKVHQGIHHHHHHHH | ||||||
Region | 1150-1203 | Disordered | ||||
Sequence: GGSSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNP | ||||||
Compositional bias | 1152-1203 | Polar residues | ||||
Sequence: SSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNP | ||||||
Region | 1236-1281 | Disordered | ||||
Sequence: PASLRKSSSHTPVFGSVRDAELDGDGSGGGGSGGGSYHRHVYPPND | ||||||
Region | 1345-1367 | Disordered | ||||
Sequence: DDEQKSSTGGGTGGAAYCDLSDA |
Sequence similarities
Belongs to the methyltransferase superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,367
- Mass (Da)146,234
- Last updated2006-10-03 v1
- ChecksumFA3EDD8FDAA7A551
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E2QC61 | E2QC61_DROME | bin3 | 1367 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-36 | Polar residues | ||||
Sequence: DCRVTRSTMTPTLRLDQTSRQEPLPQ | ||||||
Compositional bias | 53-80 | Polar residues | ||||
Sequence: TPLPGKSQAAQHHQFRAPQQQQGPKNRN | ||||||
Compositional bias | 323-351 | Polar residues | ||||
Sequence: LNSLQNENTSNASSTNNTPATTPRQSPIT | ||||||
Compositional bias | 395-415 | Basic residues | ||||
Sequence: GMLHHRQHHYRTRKNRKRRRF | ||||||
Compositional bias | 476-538 | Polar residues | ||||
Sequence: EMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQH | ||||||
Sequence conflict | 573 | in Ref. 1; AAF63187 | ||||
Sequence: L → LA | ||||||
Compositional bias | 627-646 | Basic and acidic residues | ||||
Sequence: SESSTSQKSKKFHRHDAMDK | ||||||
Compositional bias | 671-687 | Polar residues | ||||
Sequence: RKPSTRRSTSVSESELL | ||||||
Compositional bias | 719-734 | Polar residues | ||||
Sequence: GSPLSTTSGATSHTAG | ||||||
Compositional bias | 903-926 | Basic residues | ||||
Sequence: KKTRRGKRRRKVHQGIHHHHHHHH | ||||||
Sequence conflict | 1152 | in Ref. 5; AAO47868 | ||||
Sequence: S → G | ||||||
Compositional bias | 1152-1203 | Polar residues | ||||
Sequence: SSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNP | ||||||
Sequence conflict | 1267 | in Ref. 5; AAO47868 | ||||
Sequence: S → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |