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Reviewed, UniProtKB/Swiss-Prot Q24562 (U2AF2_DROME)

Last modified November 4, 2008. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Splicing factor U2AF 50 kDa subunit
Alternative name(s):
    U2 auxiliary factor 50 kDa subunit
    U2 snRNP auxiliary factor large subunit
Gene names
Name: U2af50
ORF Names: CG9998
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Necessary for the splicing of pre-mRNA. Binds to the polypyrimidine tract of introns early during spliceosome assembly By similarity.

Subunit structure

Forms a heterodimer with the U2AF small subunit.

Subcellular location

Nucleus.

Developmental stage

Present throughout development.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords

   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   DomainRepeat
   LigandRNA-binding
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processmitotic spindle organization

Inferred from mutant phenotype. Source: FlyBase

nuclear export

Inferred from mutant phenotype. Source: FlyBase

regulation of alternative nuclear mRNA splicing, via spliceosome

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentsnRNP U2

Traceable author statement. Source: FlyBase

   Molecular functionpoly-pyrimidine tract binding

Inferred from direct assay. Source: FlyBase

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Splicing factor U2AF 50 kDa subunit
PRO_0000081992

Regions

Domain93 – 17583RRM 1
Domain207 – 28579RRM 2
Domain318 – 40891RRM 3
Compositional bias6 – 4136Arg/Ser-rich (RS domain)

Sequences

Sequence LengthMass (Da)Tools
Q24562-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 541F1544E276DFFE

FASTA41646,655
        10         20         30         40         50         60 
MGYDDRERDR ERRRHRSRSR DRHRERSRDR RHHRNSRRKP SLYWDVPPPG FEHITPMQYK 

        70         80         90        100        110        120 
AMQASGQIPA SVVPDTPQTA VPVVGSTITR QARRLYVGNI PFGVTEEEMM EFFNQQMHLV 

       130        140        150        160        170        180 
GLAQAAGSPV LACQINLDKN FAFLEFRSID ETTQAMAFDG INLKGQSLKI RRPHDYQPMP 

       190        200        210        220        230        240 
GITDTPAIKP AVVSSGVIST VVPDSPHKIF IGGLPNYLND DQVKELLLSF GKLRAFNLVK 

       250        260        270        280        290        300 
DAATGLSKGY AFCEYVDLSI TDQSIAGLNG MQLGDKKLIV QRASVGAKNA QNAANTTQSV 

       310        320        330        340        350        360 
MLQVPGLSNV VTSGPPTEVL CLLNMVTPDE LRDEEEYEDI LEDIKEECTK YGVVRSVEIP 

       370        380        390        400        410 
RPIEGVEVPG CGKVFVEFNS VLDCQKAQQA LTGRKFSDRV VVTSYFDPDK YHRREF 

« Hide

References

« Hide 'large scale' references
[1]"The conserved pre-mRNA splicing factor U2AF from Drosophila: requirement for viability."
Kanaar R., Roche S.E., Beall E.L., Green M.R., Rio D.C.
Science 262:569-573(1993) [PubMed: 7692602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SB2040.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

L23404 mRNA. Translation: AAA03548.1.
AE014298 Genomic DNA. Translation: AAF48596.1.
AY069320 mRNA. Translation: AAL39465.1.
PIRA48249.
RefSeqNP_476891.1.
UniGeneDm.5430

3D structure databases

HSSPHSSP built from PDB template 1JMT based on UniProtKB P26368.
SMRQ24562. Positions 314-416.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:23323N.
IntActQ24562.

Genome annotation databases

EnsemblCG9998. Drosophila melanogaster. [Contig view]
GeneID32602.
KEGGdme:Dmel_CG9998.
NMPDRfig|7227.3.peg.18159.

Organism-specific databases

FlyBaseFBgn0005411. U2af50.

Phylogenomic databases

HOGENOMQ24562.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-002154-MON.

Gene expression databases

ArrayExpressQ24562.
GermOnlineCG9998. Drosophila melanogaster.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
IPR006529. U2AF_lg.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
TIGRFAMsTIGR01642. U2AF_lg. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio779380.

Entry information

Entry nameU2AF2_DROME
AccessionPrimary (citable) accession number: Q24562
Secondary accession number(s): Q9VXH2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 4, 2008
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents