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Q9VCU9

- DCR1_DROME

UniProt

Q9VCU9 - DCR1_DROME

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
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Magnesium or manganese.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. protein binding Source: UniProtKB
    8. ribonuclease III activity Source: MGI
    9. 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

    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.

    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

    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.

    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

    MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL     50
    LQELSRRARR HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM 100
    QIPFDHCWTD YHVSILRPEG FLYLLETREL LLSSVELIVL EDCHDSAVYQ 150
    RIRPLFENHI MPAPPADRPR ILGLAGPLHS AGCELQQLSA MLATLEQSVL 200
    CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD VLNTHKSFLL 250
    DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR 300
    AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG 350
    SDSRQTIERY SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN 400
    RLSHTLESKC RMVDQMDQPP TETRALVATL EQILHTTEDR QTNRSAARVT 450
    PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR RHHRDHNDGS DTLCALIYCN 500
    QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE PKEAELEHRR 550
    QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK 600
    GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD 650
    DSAMPNSSGS DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP 700
    AAAQLDTSNS SDEAVSMSNT SPSESSTEQK SRRFQCELSS LTEPEDTSDT 750
    TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM LLSKCANTEP PEQEQSEAER 800
    FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT FTKLTALWRC 850
    TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL 900
    HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK 950
    RRQYYYKRIA SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP 1000
    PEDAQQGFGI LTTKRIPKLS AFSIFTRSGE VKVSLELAKE RVILTSEQIV 1050
    CINGFLNYTF TNVLRLQKFL MLFDPDSTEN CVFIVPTVKA PAGGKHIDWQ 1100
    FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY RNQDQPQYFY 1150
    VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR 1200
    LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS 1250
    LWRTAVCLPC ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD 1300
    FGWSLSEVLK KSRESKQKES LKDDTINGKD LADVEKKPTS EETQLDKDSK 1350
    DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT WSNDMADDIA SFNQEDDDED 1400
    DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK SSQNKQGGKG 1450
    KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI 1500
    DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI 1550
    GFNFKHEDQK EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE 1600
    AQVAKVSMME LLKQLLPYVN EDVLAKKLGD RRELLLSDLV ELNADWVARH 1650
    EQETYNVMGC GDSFDNYNDH HRLNLDEKQL KLQYERIEIE PPTSTKAITS 1700
    AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN LERLETIGDS 1750
    FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA 1800
    TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI 1850
    CEMVREKADA LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD 1900
    KSIADCVEAL IGAYLIECGP RGALLFMAWL GVRVLPITRQ LDGGNQEQRI 1950
    PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP NATEELDQLL SGFEEFEESL 2000
    GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD YLITRHLYED 2050
    PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV 2100
    RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN 2150
    MSLDVVWHVY SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA 2200
    DGRRVRVTVD VFCKGTFRGI GRNYRIAKCT AAKCALRQLK KQGLIAKKD 2249
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Miscellaneous databases

    GenomeRNAii 42693.
    NextBioi 830091.
    PROi Q9VCU9.

    Gene expression databases

    Bgeei Q9VCU9.

    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

    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: October 1, 2014
    This is version 109 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