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Q9VSH4 (CPSF6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cleavage and polyadenylation specificity factor subunit CG7185
Gene names
ORF Names:CG7185
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in pre-mRNA 3' processing By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the RRM CPSF6/7 family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of alternative nuclear mRNA splicing, via spliceosome

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentnucleus

Inferred by curator. Source: FlyBase

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Cleavage and polyadenylation specificity factor subunit CG7185
PRO_0000372849

Regions

Domain93 – 17381RRM
Compositional bias26 – 7651Gly-rich
Compositional bias195 – 392198Gly-rich
Compositional bias521 – 651131Arg-rich

Amino acid modifications

Modified residue5961Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9VSH4 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 96B7410A48AD3F6C

FASTA65271,094
        10         20         30         40         50         60 
MADVVLDLYA EDLDKDFAGQ AQDEFGGDGV DLYDDIGGPT ESAASGGGGG GTPSADGAAG 

        70         80         90        100        110        120 
PGSGEPGERN SGGPNGVYHQ SSGSLTPTMN RRYQLYVGNL TWWTTDQDIA NSLRDIGVSD 

       130        140        150        160        170        180 
LQEVKFFENR ANGQSKGFSV ISLGSESSLR AVLDQLPKKE MHGQAPVVTY PSKQALTQFE 

       190        200        210        220        230        240 
SLQKTRPVPP PQQNGPPRGP APPSMGGGPM PTGHPGGPQG GGPPGHPPRG MNSIMQPGQY 

       250        260        270        280        290        300 
RPQHMSQVPQ VGGPNSGPPR MQPPMHPQGG LMGNQQPPPR YPSAQGQWPG QRPGGPRPGP 

       310        320        330        340        350        360 
PNGPPQRPMF QGGPMGMPVR GPAGPDWRRP PMHGGFPPQG PPRGLPPAPG PGGPHGAPAP 

       370        380        390        400        410        420 
HVNPAFFNQP GGPAQHPGMG GPPHGAPGPQ PGMNMPPQQG MNMTPQHGPP PQFAQHGPRG 

       430        440        450        460        470        480 
PWPPPQGKPP GPFPDPQQMG PQLTEVEFEE VMSRNRTVSS SAIARAVSDA AAGEYSSAIE 

       490        500        510        520        530        540 
TLVTAISLIK QSKVAHDERC KILISSLQDT LHGIEAKSYN RRERSRSRER SHRSRQRRER 

       550        560        570        580        590        600 
STSRYRERSR ERERDRDRER ERDGGSYRER SRSRERERQA PDHYRDDSRS VRPRKSPEPV 

       610        620        630        640        650 
VAEAAEAPSS KRYYEDRERY RSSDRERRDR DRDRDRERER DRDRREEHRS RH 

« Hide

References

« Hide 'large scale' references
[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. 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.
[2]"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.
Strain: Berkeley.
[3]"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.
[4]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAF50445.2.
AY058563 mRNA. Translation: AAL13792.1.
RefSeqNP_648206.1. NM_139949.2.
UniGeneDm.887.

3D structure databases

ProteinModelPortalQ9VSH4.
SMRQ9VSH4. Positions 95-172.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VSH4. 4 interactions.
MINTMINT-1562127.
STRINGQ9VSH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076710; FBpp0076433; FBgn0035872.
GeneID38937.
KEGGdme:Dmel_CG7185.
NMPDRfig|7227.3.peg.8836.
UCSCCG7185-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0035872. CG7185.

Phylogenomic databases

eggNOGinNOG10520.
GeneTreeEMGT00050000000041.
InParanoidQ9VSH4.
OMAPAFFNQP.
OrthoDBEOG4S1RQ4.
PhylomeDBQ9VSH4.

Gene expression databases

ArrayExpressQ9VSH4.
BgeeQ9VSH4.

Family and domain databases

InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
KOK14398.
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio811101.

Entry information

Entry nameCPSF6_DROME
AccessionPrimary (citable) accession number: Q9VSH4
Secondary accession number(s): Q95TS9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families