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Reviewed, UniProtKB/Swiss-Prot Q9V535 (RBM8A_DROME)

Last modified November 25, 2008. Version 59. 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

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Names and origin

Protein namesRecommended name:
    RNA-binding protein 8A
Alternative name(s):
    Protein tsunagi
Gene names
Name: tsu
Synonyms: Y14
ORF Names: CG8781
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.

Subunit structure

Heterodimer; interacts with mago. Part of the exon junction complex (EJC), an essential splicing-dependent multiprotein complex.

Subcellular location

Nucleus. Cytoplasm. Note= Part of the EJC assembled on mRNAs in the nucleus and remains part of the complex when mRNA moves into the cytoplasm.

Developmental stage

Expressed throughout development.

Domain

The RNA-binding (RRM) is involved in the interaction with mago. The RNA-binding activity of such domain is therefore unsure.

Miscellaneous

'Tsunagi' means 'connection' or 'link' in Japanese.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

magoP490285EBI-172458,EBI-159609

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165RNA-binding protein 8A
PRO_0000081765

Regions

Domain73 – 15179RRM

Experimental info

Sequence conflict861E → G in AAL29185. Ref.1
Sequence conflict1011N → S in AAL48627. Ref.4
Sequence conflict1351N → R in AAL29185. Ref.1
Sequence conflict1591K → R in AAL48627. Ref.4
Sequence conflict1621K → M in AAL29185. Ref.1

Secondary structure

1 ..................... 165
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9V535-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A47BE9ED37CCA045

FASTA16519,010
        10         20         30         40         50         60 
MADVLDIDNA EEFEVDEDGD QGIVRLKEKA KHRKGRGFGS DSNTREAIHS YERVRNEDDD 

        70         80         90        100        110        120 
ELEPGPQRSV EGWILFVTSI HEEAQEDEIQ EKFCDYGEIK NIHLNLDRRT GFSKGYALVE 

       130        140        150        160 
YETHKQALAA KEALNGAEIM GQTIQVDWCF VKGPKRVKKS EKRRR

« Hide

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References

« Hide 'large scale' references
[1]"The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis."
Mohr S.E., Dillon S.T., Boswell R.E.
Genes Dev. 15:2886-2899(2001) [PubMed: 11691839] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAGO, DEVELOPMENTAL STAGE.
[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.
[5]"A novel mode of RBD-protein recognition in the Y14-Mago complex."
Fribourg S., Gatfield D., Izaurralde E., Conti E.
Nat. Struct. Biol. 10:433-439(2003) [PubMed: 12730685] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGO, FUNCTION, SUBCELLULAR LOCATION.
[6]"Crystal structure of the Drosophila Mago nashi-Y14 complex."
Shi H., Xu R.-M.
Genes Dev. 17:971-976(2003) [PubMed: 12704080] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 47-156 IN COMPLEX WITH MAGO.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF173550 mRNA. Translation: AAL29185.1.
AE013599 Genomic DNA. Translation: AAF58987.1.
AY071005 mRNA. Translation: AAL48627.1.
RefSeqNP_610454.2.
UniGeneDm.19884

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HL6X-ray2.50A/C1-165[»]
1OO0X-ray1.85B47-156[»]
1RK8X-ray1.90A1-165[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9V535.

Genome annotation databases

EnsemblCG8781. Drosophila melanogaster. [Contig view]
GeneID35924.
KEGGdme:Dmel_CG8781.
NMPDRfig|7227.3.peg.4004.

Organism-specific databases

FlyBaseFBgn0033378. tsu.

Phylogenomic databases

HOGENOMQ9V535.

Gene expression databases

ArrayExpressQ9V535.
GermOnlineCG8781. Drosophila melanogaster.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR008111. RNA_bd_8.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSPR01738. RNABINDINGM8.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio795852.

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Entry information

Entry nameRBM8A_DROME
AccessionPrimary (citable) accession number: Q9V535
Secondary accession number(s): Q8SZA6, Q95X08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: May 1, 2000
Last modified: November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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