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Q9VCU9

- DCR1_DROME

UniProt

Q9VCU9 - DCR1_DROME

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Protein

Endoribonuclease Dcr-1

Gene

Dcr-1

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

Functioni

Essential for RNA interference (RNAi); double-stranded RNA (dsRNA) induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger. May carry out the initiation step of RNAi by cleaving dsRNA to produce 22 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs. During embryogenesis, involved in germline fate determination.3 Publications

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2032 – 20321Magnesium or manganeseBy similarity
Sitei2132 – 21321Important for activityBy similarity
Metal bindingi2136 – 21361Magnesium or manganeseBy similarity
Metal bindingi2139 – 21391Magnesium or manganeseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 448ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. bidentate ribonuclease III activity Source: FlyBase
  3. double-stranded RNA binding Source: FlyBase
  4. helicase activity Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. pre-miRNA binding Source: FlyBase
  7. ribonuclease III activity Source: MGI
  8. single-stranded RNA binding Source: FlyBase

GO - Biological processi

  1. dendrite morphogenesis Source: FlyBase
  2. dsRNA transport Source: FlyBase
  3. germarium-derived female germ-line cyst formation Source: FlyBase
  4. germarium-derived oocyte fate determination Source: FlyBase
  5. germ-line stem cell division Source: FlyBase
  6. mitotic cell cycle, embryonic Source: FlyBase
  7. pole cell formation Source: FlyBase
  8. pre-miRNA processing Source: FlyBase
  9. production of miRNAs involved in gene silencing by miRNA Source: FlyBase
  10. production of siRNA involved in RNA interference Source: UniProtKB
  11. RNA interference Source: FlyBase
  12. RNA phosphodiester bond hydrolysis Source: GOC
  13. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  14. segment polarity determination Source: FlyBase
  15. siRNA loading onto RISC involved in RNA interference Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_181252. Small interfering RNA (siRNA) biogenesis.
REACT_262818. MicroRNA (miRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease Dcr-1 (EC:3.1.26.-)
Short name:
Protein dicer-1
Gene namesi
Name:Dcr-1Imported
ORF Names:CG4792
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039016. Dcr-1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. RISC complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22492249Endoribonuclease Dcr-1PRO_0000180474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1423 – 14231Phosphoserine1 Publication
Modified residuei1877 – 18771Phosphoserine1 Publication
Modified residuei1880 – 18801Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VCU9.
PRIDEiQ9VCU9.

Expressioni

Gene expression databases

BgeeiQ9VCU9.
ExpressionAtlasiQ9VCU9. differential.

Interactioni

Subunit structurei

Interacts with AGO2 to form components of the RISC. Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, AGO2 and Rm62. Interacts with piwi and vas; these interactions occur in the polar granules.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
loqsQ9VJY93EBI-112170,EBI-638074

Protein-protein interaction databases

BioGridi67642. 5 interactions.
DIPiDIP-23028N.
IntActiQ9VCU9. 4 interactions.
MINTiMINT-923321.

Structurei

3D structure databases

ProteinModelPortaliQ9VCU9.
SMRiQ9VCU9. Positions 549-615, 973-1266, 1981-2240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini485 – 648164Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini825 – 92096Dicer dsRNA-binding foldPROSITE-ProRule annotationAdd
BLAST
Domaini1099 – 1246148PAZPROSITE-ProRule annotationAdd
BLAST
Domaini1698 – 1919222RNase III 1PROSITE-ProRule annotationAdd
BLAST
Domaini1993 – 2150158RNase III 2PROSITE-ProRule annotationAdd
BLAST
Domaini2175 – 224167DRBMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the helicase family. Dicer subfamily.PROSITE-ProRule annotation
Contains 1 Dicer dsRNA-binding fold domain.PROSITE-ProRule annotation
Contains 1 DRBM (double-stranded RNA-binding) domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 PAZ domain.PROSITE-ProRule annotation
Contains 2 RNase III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0571.
GeneTreeiENSGT00510000046789.
InParanoidiQ9VCU9.
KOiK11592.
OMAiKYAITTY.
OrthoDBiEOG78PV82.
PhylomeDBiQ9VCU9.

Family and domain databases

Gene3Di1.10.1520.10. 4 hits.
3.40.50.300. 1 hit.
InterProiIPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEiPS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VCU9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL
60 70 80 90 100
LQELSRRARR HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM
110 120 130 140 150
QIPFDHCWTD YHVSILRPEG FLYLLETREL LLSSVELIVL EDCHDSAVYQ
160 170 180 190 200
RIRPLFENHI MPAPPADRPR ILGLAGPLHS AGCELQQLSA MLATLEQSVL
210 220 230 240 250
CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD VLNTHKSFLL
260 270 280 290 300
DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR
310 320 330 340 350
AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG
360 370 380 390 400
SDSRQTIERY SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN
410 420 430 440 450
RLSHTLESKC RMVDQMDQPP TETRALVATL EQILHTTEDR QTNRSAARVT
460 470 480 490 500
PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR RHHRDHNDGS DTLCALIYCN
510 520 530 540 550
QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE PKEAELEHRR
560 570 580 590 600
QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK
610 620 630 640 650
GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD
660 670 680 690 700
DSAMPNSSGS DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP
710 720 730 740 750
AAAQLDTSNS SDEAVSMSNT SPSESSTEQK SRRFQCELSS LTEPEDTSDT
760 770 780 790 800
TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM LLSKCANTEP PEQEQSEAER
810 820 830 840 850
FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT FTKLTALWRC
860 870 880 890 900
TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL
910 920 930 940 950
HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK
960 970 980 990 1000
RRQYYYKRIA SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP
1010 1020 1030 1040 1050
PEDAQQGFGI LTTKRIPKLS AFSIFTRSGE VKVSLELAKE RVILTSEQIV
1060 1070 1080 1090 1100
CINGFLNYTF TNVLRLQKFL MLFDPDSTEN CVFIVPTVKA PAGGKHIDWQ
1110 1120 1130 1140 1150
FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY RNQDQPQYFY
1160 1170 1180 1190 1200
VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR
1210 1220 1230 1240 1250
LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS
1260 1270 1280 1290 1300
LWRTAVCLPC ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD
1310 1320 1330 1340 1350
FGWSLSEVLK KSRESKQKES LKDDTINGKD LADVEKKPTS EETQLDKDSK
1360 1370 1380 1390 1400
DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT WSNDMADDIA SFNQEDDDED
1410 1420 1430 1440 1450
DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK SSQNKQGGKG
1460 1470 1480 1490 1500
KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI
1510 1520 1530 1540 1550
DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI
1560 1570 1580 1590 1600
GFNFKHEDQK EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE
1610 1620 1630 1640 1650
AQVAKVSMME LLKQLLPYVN EDVLAKKLGD RRELLLSDLV ELNADWVARH
1660 1670 1680 1690 1700
EQETYNVMGC GDSFDNYNDH HRLNLDEKQL KLQYERIEIE PPTSTKAITS
1710 1720 1730 1740 1750
AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN LERLETIGDS
1760 1770 1780 1790 1800
FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA
1810 1820 1830 1840 1850
TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI
1860 1870 1880 1890 1900
CEMVREKADA LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD
1910 1920 1930 1940 1950
KSIADCVEAL IGAYLIECGP RGALLFMAWL GVRVLPITRQ LDGGNQEQRI
1960 1970 1980 1990 2000
PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP NATEELDQLL SGFEEFEESL
2010 2020 2030 2040 2050
GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD YLITRHLYED
2060 2070 2080 2090 2100
PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV
2110 2120 2130 2140 2150
RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN
2160 2170 2180 2190 2200
MSLDVVWHVY SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA
2210 2220 2230 2240
DGRRVRVTVD VFCKGTFRGI GRNYRIAKCT AAKCALRQLK KQGLIAKKD
Length:2,249
Mass (Da):255,330
Last modified:May 1, 2000 - v1
Checksum:iD693F0432AC8033D
GO

Sequence cautioni

The sequence AAK84929.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1338 – 13392PT → AI(PubMed:12537569)Curated
Sequence conflicti1345 – 13451L → I(PubMed:12537569)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56056.1.
AY050230 mRNA. Translation: AAK84929.1. Different initiation.
RefSeqiNP_524453.1. NM_079729.3.
UniGeneiDm.1283.

Genome annotation databases

EnsemblMetazoaiFBtr0084324; FBpp0083717; FBgn0039016.
GeneIDi42693.
KEGGidme:Dmel_CG4792.
UCSCiCG4792-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56056.1 .
AY050230 mRNA. Translation: AAK84929.1 . Different initiation.
RefSeqi NP_524453.1. NM_079729.3.
UniGenei Dm.1283.

3D structure databases

ProteinModelPortali Q9VCU9.
SMRi Q9VCU9. Positions 549-615, 973-1266, 1981-2240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67642. 5 interactions.
DIPi DIP-23028N.
IntActi Q9VCU9. 4 interactions.
MINTi MINT-923321.

Proteomic databases

PaxDbi Q9VCU9.
PRIDEi Q9VCU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0084324 ; FBpp0083717 ; FBgn0039016 .
GeneIDi 42693.
KEGGi dme:Dmel_CG4792.
UCSCi CG4792-RA. d. melanogaster.

Organism-specific databases

CTDi 42693.
FlyBasei FBgn0039016. Dcr-1.

Phylogenomic databases

eggNOGi COG0571.
GeneTreei ENSGT00510000046789.
InParanoidi Q9VCU9.
KOi K11592.
OMAi KYAITTY.
OrthoDBi EOG78PV82.
PhylomeDBi Q9VCU9.

Enzyme and pathway databases

Reactomei REACT_181252. Small interfering RNA (siRNA) biogenesis.
REACT_262818. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

GenomeRNAii 42693.
NextBioi 830091.
PROi Q9VCU9.

Gene expression databases

Bgeei Q9VCU9.
ExpressionAtlasi Q9VCU9. differential.

Family and domain databases

Gene3Di 1.10.1520.10. 4 hits.
3.40.50.300. 1 hit.
InterProi IPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR000999. RNase_III_dom.
[Graphical view ]
Pfami PF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view ]
SMARTi SM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view ]
SUPFAMi SSF101690. SSF101690. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEi PS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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] OF 1338-2249.
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. "Role for a bidentate ribonuclease in the initiation step of RNA interference."
    Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J.
    Nature 409:363-366(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Argonaute2, a link between genetic and biochemical analyses of RNAi."
    Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.
    Science 293:1146-1150(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO2.
  6. "A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins."
    Ishizuka A., Siomi M.C., Siomi H.
    Genes Dev. 16:2497-2508(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FMR1.
  7. "The role of PIWI and the miRNA machinery in Drosophila germline determination."
    Megosh H.B., Cox D.N., Campbell C., Lin H.
    Curr. Biol. 16:1884-1894(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIWI AND VAS.
  8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423; SER-1877 AND SER-1880, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDCR1_DROME
AccessioniPrimary (citable) accession number: Q9VCU9
Secondary accession number(s): Q961S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 111 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

External Data

Dasty 3