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O97428 (O97428_DROME) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names

Ciboulot, isoform B EMBL AAF45920.1

EG:EG0007.11 protein EMBL CAA21832.1

RE50273p EMBL AAL90371.1
Gene names
Name:cib EMBL AAL90371.1 FlyBase FBgn0026084
Synonyms:EG:EG0007.11 EMBL CAA21832.1
ORF Names:CG4944 FlyBase FBgn0026084, Dmel_CG4944 EMBL AAF45919.1
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequences

Sequence LengthMass (Da)Tools
O97428 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 5D68BE289EC8CE2F

FASTA12914,410
        10         20         30         40         50         60 
MAAPAPALKD LPKVAENLKS QLEGFNQDKL KNASTQEKII LPTAEDVAAE KTQQSIFEGI 

        70         80         90        100        110        120 
TAFNQNNLKH TETNEKNPLP DKEAIEQEKE KNQFIAGIEN FDAKKLKHTE TNEKNVLPTK 


EVIEAEKQA 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing the distal X chromosome of Drosophila melanogaster."
Ferraz C., Vidal S., Brun C., Bucheton A., Demaille J.G.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]Benos P.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Berkeley EMBL AAL90371.1.
[6]"The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly."
Hertzog M., van Heijenoort C., Didry D., Gaudier M., Coutant J., Gigant B., Didelot G., Preat T., Knossow M., Guittet E., Carlier M.F.
Cell 117:611-623(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 10-34.
[7]"How a single residue in individual ?-thymosin/WH2 domains controls their functions in actin assembly."
Didry D., Cantrelle F.X., Husson C., Roblin P., Moorthy A.M., Perez J., Le Clainche C., Hertzog M., Guittet E., Carlier M.F., van Heijenoort C., Renault L.
EMBO J. 31:1000-1013(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-29.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF45919.1.
AE014298 Genomic DNA. Translation: AAF45920.1.
AY089633 mRNA. Translation: AAL90371.1.
AL033125 Genomic DNA. Translation: CAA21832.1.
RefSeqNP_001245516.1. NM_001258587.1.
NP_525065.1. NM_080326.4.
NP_726908.1. NM_167001.2.
UniGeneDm.74.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SQKX-ray2.50B10-34[»]
3SJHX-ray1.75B8-29[»]
3U8XX-ray2.00B/D8-29[»]
3U9DX-ray2.50B/D8-24[»]
3U9ZX-ray2.09C2-58[»]
SMRO97428. Positions 20-52, 56-91, 95-129.
ModBaseSearch...

Protein-protein interaction databases

IntActO97428. 1 interaction.
MINTMINT-925149.
STRING7227.FBpp0070609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070639; FBpp0070607; FBgn0026084.
FBtr0070641; FBpp0070609; FBgn0026084.
FBtr0307206; FBpp0298035; FBgn0026084.
GeneID31359.
KEGGdme:Dmel_CG4944.
UCSCCG4944-RA. d. melanogaster.

Organism-specific databases

CTD31359.
FlyBaseFBgn0026084. cib.

Phylogenomic databases

eggNOGNOG126035.
GeneTreeENSGT00530000065074.
InParanoidO97428.
OMAKHTETNE.
OrthoDBEOG4M907R.

Family and domain databases

Gene3D1.20.5.520. 3 hits.
InterProIPR001152. Thymosin_b4.
[Graphical view]
PfamPF01290. Thymosin. 3 hits.
[Graphical view]
ProDomPD005116. Thymosin_b4. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00152. THY. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABHD14B. drosophila.
EvolutionaryTraceO97428.
GenomeRNAi31359.
NextBio773235.

Entry information

Entry nameO97428_DROME
AccessionPrimary (citable) accession number: O97428
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)