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Q3EBC8

- DCL2_ARATH

UniProt

Q3EBC8 - DCL2_ARATH

Protein

Endoribonuclease Dicer homolog 2

Gene

At3g03300

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Involved in the processing of natural small interfering RNAs (nat-siRNAs, derived from cis-natural antisense transcripts) by cleaving small dsRNAs into 24 nucleotide nat-siRNAs. Plays an essential role in transitive silencing of transgenes by processing secondary siRNAs. This pathway, which requires DCL4 and RDR6, amplifies silencing by using the target RNA as substrate to generate secondary siRNAs, providing an efficient mechanism for long-distance silencing. May participate with DCL3 in the production of 24 nucleotide repeat-associated siRNAs (ra-siRNAs) which derive from heterochromatin and DNA repeats such as transposons. Plays a role in antiviral RNA silencing. Involved in the production of viral siRNAs derived from the turnip crinkle virus (TCV) and tobacco rattle virus (TRV). Targeted by the viral silencing suppressor (VSR) protein 2b of the cucumber mosaic virus (CMV) that inactivates DCL2 function in RNA silencing. Does not seem to be involved in microRNAs (miRNAs) processing.6 Publications

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1188 – 11881Magnesium or manganeseBy similarity
    Sitei1278 – 12781Important for activityBy similarity
    Metal bindingi1282 – 12821Magnesium or manganeseBy similarity
    Metal bindingi1285 – 12851Magnesium or manganeseBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi44 – 518ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. helicase activity Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. ribonuclease III activity Source: InterPro
    6. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. defense response to virus Source: TAIR
    2. maintenance of DNA methylation Source: TAIR
    3. production of ta-siRNAs involved in RNA interference Source: TAIR

    Keywords - Molecular functioni

    Endonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    Plant defense, RNA-mediated gene silencing

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciARA:AT3G03300-MONOMER.
    ARA:GQT-1567-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoribonuclease Dicer homolog 2 (EC:3.1.26.-)
    Alternative name(s):
    Dicer-like protein 2
    Short name:
    AtDCL2
    Gene namesi
    Ordered Locus Names:At3g03300
    ORF Names:T17B22.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G03300.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13881388Endoribonuclease Dicer homolog 2PRO_0000404660Add
    BLAST

    Proteomic databases

    PaxDbiQ3EBC8.
    PRIDEiQ3EBC8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ3EBC8.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DRB1O044922EBI-2464030,EBI-632620

    Protein-protein interaction databases

    IntActiQ3EBC8. 4 interactions.
    STRINGi3702.AT3G03300.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3EBC8.
    SMRiQ3EBC8. Positions 11-510, 558-638, 1152-1385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 210180Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini380 – 544165Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini559 – 64587Dicer dsRNA-binding foldPROSITE-ProRule annotationAdd
    BLAST
    Domaini807 – 935129PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini962 – 1113152RNase III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1149 – 1296148RNase III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1315 – 138470DRBMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi152 – 1554DECH box

    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 ATP-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

    eggNOGiCOG1111.
    HOGENOMiHOG000006099.
    InParanoidiQ3EBC8.
    KOiK11592.
    OMAiHILHASH.
    PhylomeDBiQ3EBC8.

    Family and domain databases

    Gene3Di1.10.1520.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProiIPR005034. Dicer_dimerisation_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014720. dsRNA-bd_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR003100. PAZ_dom.
    IPR000999. RNase_III_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF03368. Dicer_dimer. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF02170. PAZ. 1 hit.
    PF00636. Ribonuclease_3. 2 hits.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00358. DSRM. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00949. PAZ. 1 hit.
    SM00535. RIBOc. 2 hits.
    [Graphical view]
    SUPFAMiSSF101690. SSF101690. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF69065. SSF69065. 4 hits.
    PROSITEiPS51327. DICER_DSRBF. 1 hit.
    PS50137. DS_RBD. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3EBC8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTMDADAMET ETTDQVSASP LHFARSYQVE ALEKAIKQNT IVFLETGSGK     50
    TLIAIMLLRS YAYLFRKPSP CFCVFLVPQV VLVTQQAEAL KMHTDLKVGM 100
    YWGDMGVDFW DSSTWKQEVD KYEVLVMTPA ILLDALRHSF LSLSMIKVLI 150
    VDECHHAGGK HPYACIMREF YHKELNSGTS NVPRIFGMTA SLVKTKGENL 200
    DSYWKKIHEL ETLMNSKVYT CENESVLAGF VPFSTPSFKY YQHIKIPSPK 250
    RASLVEKLER LTIKHRLSLG TLDLNSSTVD SVEKRLLRIS STLTYCLDDL 300
    GILLAQKAAQ SLSASQNDSF LWGELNMFSV ALVKKFCSDA SQEFLAEIPQ 350
    GLNWSVANIN GNAEAGLLTL KTVCLIETLL GYSSLENIRC IIFVDRVITA 400
    IVLESLLAEI LPNCNNWKTK YVAGNNSGLQ NQTRKKQNEI VEDFRRGLVN 450
    IIVATSILEE GLDVQSCNLV IRFDPASNIC SFIQSRGRAR MQNSDYLMMV 500
    ESGDLLTQSR LMKYLSGGKR MREESLDHSL VPCPPLPDDS DEPLFRVEST 550
    GATVTLSSSV SLIYHYCSRL PSDEYFKPAP RFDVNKDQGS CTLYLPKSCP 600
    VKEVKAEANN KVLKQAVCLK ACIQLHKVGA LSDHLVPDMV VAETVSQKLE 650
    KIQYNTEQPC YFPPELVSQF SAQPETTYHF YLIRMKPNSP RNFHLNDVLL 700
    GTRVVLEDDI GNTSFRLEDH RGTIAVTLSY VGAFHLTQEE VLFCRRFQIT 750
    LFRVLLDHSV ENLMEALNGL HLRDGVALDY LLVPSTHSHE TSLIDWEVIR 800
    SVNLTSHEVL EKHENCSTNG ASRILHTKDG LFCTCVVQNA LVYTPHNGYV 850
    YCTKGVLNNL NGNSLLTKRN SGDQTYIEYY EERHGIQLNF VDEPLLNGRH 900
    IFTLHSYLHM AKKKKEKEHD REFVELPPEL CHVILSPISV DMIYSYTFIP 950
    SVMQRIESLL IAYNLKKSIP KVNIPTIKVL EAITTKKCED QFHLESLETL 1000
    GDSFLKYAVC QQLFQHCHTH HEGLLSTKKD GMISNVMLCQ FGCQQKLQGF 1050
    IRDECFEPKG WMVPGQSSAA YSLVNDTLPE SRNIYVASRR NLKRKSVADV 1100
    VESLIGAYLS EGGELAALMF MNWVGIKVDF TTTKIQRDSP IQAEKLVNVG 1150
    YMESLLNYSF EDKSLLVEAL THGSYMMPEI PRCYQRLEFL GDSVLDYLIT 1200
    KHLYDKYPCL SPGLLTDMRS ASVNNECYAL VAVKANLHKH ILYASHHLHK 1250
    HISRTVSEFE QSSLQSTFGW ESDISFPKVL GDVIESLAGA IFVDSGYNKE 1300
    VVFASIKPLL GCMITPETVK LHPVRELTEL CQKWQFELSK AKDFDSFTVE 1350
    VKAKEMSFAH TAKASDKKMA KKLAYKEVLN LLKNSLDY 1388
    Length:1,388
    Mass (Da):156,865
    Last modified:January 15, 2008 - v2
    Checksum:i385D5A28E048B10D
    GO
    Isoform 2 (identifier: Q3EBC8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-83: MTMDADAMET...VFLVPQVVLV → MLLCLLGSSS...IISAFFLVCF

    Note: No experimental confirmation available.

    Show »
    Length:1,374
    Mass (Da):155,286
    Checksum:i8A374D2F3B727D53
    GO

    Sequence cautioni

    The sequence ABF19797.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF26098.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At3g03300 has been split into 2 genes: At3g03300 and At3g03305.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti511 – 5111L → S in ABF19797. (PubMed:16638569)Curated
    Sequence conflicti511 – 5111L → S in ABF19798. (PubMed:16638569)Curated
    Sequence conflicti693 – 6931F → L in ABF19797. (PubMed:16638569)Curated
    Sequence conflicti693 – 6931F → L in ABF19798. (PubMed:16638569)Curated
    Sequence conflicti738 – 7381Q → R in ABF19797. (PubMed:16638569)Curated
    Sequence conflicti738 – 7381Q → R in ABF19798. (PubMed:16638569)Curated
    Sequence conflicti1130 – 11301F → L in ABF19797. (PubMed:16638569)Curated
    Sequence conflicti1130 – 11301F → L in ABF19798. (PubMed:16638569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8383MTMDA…QVVLV → MLLCLLGSSSGSCHSGIGVR IGVVDKGIHQYTDLSFVLQF LHYYTCSFSKFRNFSVTFSI ISAFFLVCF in isoform 2. 1 PublicationVSP_040615Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ479970 mRNA. Translation: ABF19797.1. Different initiation.
    DQ479971 mRNA. Translation: ABF19798.1.
    AC012328 Genomic DNA. Translation: AAF26098.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE73924.1.
    CP002686 Genomic DNA. Translation: AEE73925.1.
    CP002686 Genomic DNA. Translation: AEE73926.1.
    RefSeqiNP_001078101.1. NM_001084632.1. [Q3EBC8-2]
    NP_001189798.1. NM_001202869.1. [Q3EBC8-1]
    NP_566199.4. NM_111200.5. [Q3EBC8-1]
    UniGeneiAt.43488.

    Genome annotation databases

    EnsemblPlantsiAT3G03300.1; AT3G03300.1; AT3G03300. [Q3EBC8-1]
    AT3G03300.3; AT3G03300.3; AT3G03300. [Q3EBC8-1]
    GeneIDi821300.
    KEGGiath:AT3G03300.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ479970 mRNA. Translation: ABF19797.1 . Different initiation.
    DQ479971 mRNA. Translation: ABF19798.1 .
    AC012328 Genomic DNA. Translation: AAF26098.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE73924.1 .
    CP002686 Genomic DNA. Translation: AEE73925.1 .
    CP002686 Genomic DNA. Translation: AEE73926.1 .
    RefSeqi NP_001078101.1. NM_001084632.1. [Q3EBC8-2 ]
    NP_001189798.1. NM_001202869.1. [Q3EBC8-1 ]
    NP_566199.4. NM_111200.5. [Q3EBC8-1 ]
    UniGenei At.43488.

    3D structure databases

    ProteinModelPortali Q3EBC8.
    SMRi Q3EBC8. Positions 11-510, 558-638, 1152-1385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3EBC8. 4 interactions.
    STRINGi 3702.AT3G03300.1-P.

    Proteomic databases

    PaxDbi Q3EBC8.
    PRIDEi Q3EBC8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G03300.1 ; AT3G03300.1 ; AT3G03300 . [Q3EBC8-1 ]
    AT3G03300.3 ; AT3G03300.3 ; AT3G03300 . [Q3EBC8-1 ]
    GeneIDi 821300.
    KEGGi ath:AT3G03300.

    Organism-specific databases

    TAIRi AT3G03300.

    Phylogenomic databases

    eggNOGi COG1111.
    HOGENOMi HOG000006099.
    InParanoidi Q3EBC8.
    KOi K11592.
    OMAi HILHASH.
    PhylomeDBi Q3EBC8.

    Enzyme and pathway databases

    BioCyci ARA:AT3G03300-MONOMER.
    ARA:GQT-1567-MONOMER.

    Gene expression databases

    Genevestigatori Q3EBC8.

    Family and domain databases

    Gene3Di 1.10.1520.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR005034. Dicer_dimerisation_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014720. dsRNA-bd_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR003100. PAZ_dom.
    IPR000999. RNase_III_dom.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF03368. Dicer_dimer. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF02170. PAZ. 1 hit.
    PF00636. Ribonuclease_3. 2 hits.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00358. DSRM. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00949. PAZ. 1 hit.
    SM00535. RIBOc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF101690. SSF101690. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF69065. SSF69065. 4 hits.
    PROSITEi PS51327. DICER_DSRBF. 1 hit.
    PS50137. DS_RBD. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. Cited for: SUBCELLULAR LOCATION.
    5. "Partially redundant functions of Arabidopsis DICER-like enzymes and a role for DCL4 in producing trans-acting siRNAs."
      Gasciolli V., Mallory A.C., Bartel D.P., Vaucheret H.
      Curr. Biol. 15:1494-1500(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "An antagonistic function for Arabidopsis DCL2 in development and a new function for DCL4 in generating viral siRNAs."
      Bouche N., Lauressergues D., Gasciolli V., Vaucheret H.
      EMBO J. 25:3347-3356(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Suppression of antiviral silencing by cucumber mosaic virus 2b protein in Arabidopsis is associated with drastically reduced accumulation of three classes of viral small interfering RNAs."
      Diaz-Pendon J.A., Li F., Li W.X., Ding S.W.
      Plant Cell 19:2053-2063(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Transitivity in Arabidopsis can be primed, requires the redundant action of the antiviral Dicer-like 4 and Dicer-like 2, and is compromised by viral-encoded suppressor proteins."
      Moissiard G., Parizotto E.A., Himber C., Voinnet O.
      RNA 13:1268-1278(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Structural and genetic requirements for the biogenesis of tobacco rattle virus-derived small interfering RNAs."
      Donaire L., Barajas D., Martinez-Garcia B., Martinez-Priego L., Pagan I., Llave C.
      J. Virol. 82:5167-5177(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "DICER-LIKE2 plays a primary role in transitive silencing of transgenes in Arabidopsis."
      Mlotshwa S., Pruss G.J., Peragine A., Endres M.W., Li J., Chen X., Poethig R.S., Bowman L.H., Vance V.
      PLoS ONE 3:E1755-E1755(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiDCL2_ARATH
    AccessioniPrimary (citable) accession number: Q3EBC8
    Secondary accession number(s): Q1KL57, Q1KL58, Q9M9P8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3