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Protein

Splicing factor 3B subunit 6-like protein

Gene

CG13298

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the splicing of pre-mRNA.By similarity

GO - Molecular functioni

  • mRNA binding Source: FlyBase
  • nucleotide binding Source: InterPro

GO - Biological processi

  • mitotic spindle organization Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • neurogenesis Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72165. mRNA Splicing - Minor Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3B subunit 6-like protein
Alternative name(s):
Pre-mRNA branch site p14-like protein
Gene namesi
ORF Names:CG13298
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035692. CG13298.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • precatalytic spliceosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121Splicing factor 3B subunit 6-like proteinPRO_0000081728Add
BLAST

Proteomic databases

PaxDbiQ9VRV7.
PRIDEiQ9VRV7.

Expressioni

Gene expression databases

BgeeiQ9VRV7.
GenevisibleiQ9VRV7. DM.

Interactioni

Subunit structurei

Component of splicing factor SF3B complex.1 Publication

Protein-protein interaction databases

BioGridi64173. 5 interactions.
DIPiDIP-21174N.
IntActiQ9VRV7. 1 interaction.
MINTiMINT-921416.
STRINGi7227.FBpp0076723.

Structurei

3D structure databases

ProteinModelPortaliQ9VRV7.
SMRiQ9VRV7. Positions 4-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9076RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 2514Interaction with pre-mRNA branch siteBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0114. Eukaryota.
ENOG4111IHX. LUCA.
GeneTreeiENSGT00390000005908.
InParanoidiQ9VRV7.
KOiK12833.
OMAiVVYDDVM.
OrthoDBiEOG7JT6Z3.
PhylomeDBiQ9VRV7.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VRV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKRNHIRLP PEVNRLLYVR NLPYKITSDE MYDIFGKFGA IRQIRVGNTP
60 70 80 90 100
ETRGTAFVVY EDIFDAKNAC DHLSGFNVCN RYLVVLYYQS NKAFKRVDMD
110 120
KKQEELNNIK AKYNLKTPEA P
Length:121
Mass (Da):14,194
Last modified:May 1, 2000 - v1
Checksum:i926D5B5199CF6652
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50675.1.
AY089603 mRNA. Translation: AAL90341.1.
RefSeqiNP_648037.1. NM_139780.3.
UniGeneiDm.1519.

Genome annotation databases

EnsemblMetazoaiFBtr0077015; FBpp0076723; FBgn0035692.
GeneIDi38720.
KEGGidme:Dmel_CG13298.
UCSCiCG13298-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50675.1.
AY089603 mRNA. Translation: AAL90341.1.
RefSeqiNP_648037.1. NM_139780.3.
UniGeneiDm.1519.

3D structure databases

ProteinModelPortaliQ9VRV7.
SMRiQ9VRV7. Positions 4-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64173. 5 interactions.
DIPiDIP-21174N.
IntActiQ9VRV7. 1 interaction.
MINTiMINT-921416.
STRINGi7227.FBpp0076723.

Proteomic databases

PaxDbiQ9VRV7.
PRIDEiQ9VRV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077015; FBpp0076723; FBgn0035692.
GeneIDi38720.
KEGGidme:Dmel_CG13298.
UCSCiCG13298-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0035692. CG13298.

Phylogenomic databases

eggNOGiKOG0114. Eukaryota.
ENOG4111IHX. LUCA.
GeneTreeiENSGT00390000005908.
InParanoidiQ9VRV7.
KOiK12833.
OMAiVVYDDVM.
OrthoDBiEOG7JT6Z3.
PhylomeDBiQ9VRV7.

Enzyme and pathway databases

ReactomeiR-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

GenomeRNAii38720.
NextBioi810039.
PROiQ9VRV7.

Gene expression databases

BgeeiQ9VRV7.
GenevisibleiQ9VRV7. DM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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: Berkeley1 Publication.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. "Conservation of the protein composition and electron microscopy structure of Drosophila melanogaster and human spliceosomal complexes."
    Herold N., Will C.L., Wolf E., Kastner B., Urlaub H., Luhrmann R.
    Mol. Cell. Biol. 29:281-301(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SF3B COMPLEX, ELECTRON MICROSCOPY OF THE SF3B COMPLEX.

Entry informationi

Entry nameiSF3B6_DROME
AccessioniPrimary (citable) accession number: Q9VRV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.