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Q9UPY3

- DICER_HUMAN

UniProt

Q9UPY3 - DICER_HUMAN

Protein

Endoribonuclease Dicer

Gene

DICER1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes.10 Publications

    Catalytic activityi

    Endonucleolytic cleavage to 5'-phosphomonoester.2 Publications

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1316 – 13161Magnesium or manganese 1By similarity
    Metal bindingi1395 – 13951Magnesium or manganese 1By similarity
    Metal bindingi1398 – 13981Magnesium or manganese 1By similarity
    Metal bindingi1705 – 17051Magnesium or manganese 2
    Sitei1806 – 18061Important for activityBy similarity
    Metal bindingi1810 – 18101Magnesium or manganese 2
    Metal bindingi1813 – 18131Magnesium or manganese 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi64 – 718ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. double-stranded RNA binding Source: UniProtKB
    3. helicase activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. miRNA binding Source: Ensembl
    6. protein binding Source: UniProtKB
    7. ribonuclease III activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. branching morphogenesis of an epithelial tube Source: Ensembl
    3. cardiac muscle cell development Source: Ensembl
    4. cerebral cortex development Source: Ensembl
    5. defense response to virus Source: Ensembl
    6. embryonic hindlimb morphogenesis Source: Ensembl
    7. gene expression Source: Reactome
    8. hair follicle cell proliferation Source: Ensembl
    9. hair follicle morphogenesis Source: Ensembl
    10. inner ear receptor cell development Source: Ensembl
    11. intestinal epithelial cell development Source: Ensembl
    12. lung development Source: Ensembl
    13. multicellular organism growth Source: Ensembl
    14. negative regulation of Schwann cell proliferation Source: BHF-UCL
    15. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    16. nerve development Source: BHF-UCL
    17. neuron projection morphogenesis Source: BHF-UCL
    18. olfactory bulb interneuron differentiation Source: Ensembl
    19. peripheral nervous system myelin formation Source: BHF-UCL
    20. positive regulation of miRNA metabolic process Source: Ensembl
    21. positive regulation of myelination Source: BHF-UCL
    22. positive regulation of Schwann cell differentiation Source: BHF-UCL
    23. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    24. post-embryonic development Source: Ensembl
    25. pre-miRNA processing Source: UniProtKB
    26. production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
    27. production of siRNA involved in RNA interference Source: UniProtKB
    28. regulation of cell cycle Source: Ensembl
    29. regulation of enamel mineralization Source: Ensembl
    30. regulation of neuron differentiation Source: Ensembl
    31. regulation of oligodendrocyte differentiation Source: Ensembl
    32. regulation of viral genome replication Source: Ensembl
    33. RNA phosphodiester bond hydrolysis Source: GOC
    34. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    35. spinal cord motor neuron differentiation Source: Ensembl
    36. spindle assembly Source: Ensembl
    37. spleen development Source: Ensembl
    38. stem cell maintenance Source: Ensembl
    39. targeting of mRNA for destruction involved in RNA interference Source: UniProtKB
    40. zygote asymmetric cell division Source: Ensembl

    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

    BRENDAi3.1.26.3. 2681.
    ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoribonuclease Dicer (EC:3.1.26.3)
    Alternative name(s):
    Helicase with RNase motif
    Short name:
    Helicase MOI
    Gene namesi
    Name:DICER1
    Synonyms:DICER, HERNA, KIAA0928
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:17098. DICER1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytosol Source: Reactome
    3. dendrite Source: Ensembl
    4. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    5. growth cone Source: Ensembl
    6. RISC complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Pleuropulmonary blastoma (PPB) [MIM:601200]: A rare pediatric intrathoracic neoplasm. The tumor arises from the lung, pleura, or both, and appears to be purely mesenchymal in phenotype. It lacks malignant epithelial elements, a feature that distinguishes it from the classic adult-type pulmonary blastoma. It arises during fetal lung development and is often part of an inherited cancer syndrome. The tumor contain both epithelial and mesenchymal cells. Early in tumorigenesis, cysts form in lung airspaces, and these cysts are lined with benign-appearing epithelium. Mesenchymal cells susceptible to malignant transformation reside within the cyst walls and form a dense layer beneath the epithelial lining. In a subset of patients, overgrowth of the mesenchymal cells produces a sarcoma, a transition that is associated with a poorer prognosis. Some patients have multilocular cystic nephroma, a benign kidney tumor.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1583 – 15831L → R in PPB. 1 Publication
    VAR_063150
    Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1) [MIM:138800]: A common disorder characterized by nodular overgrowth of the thyroid gland. Some individuals may also develop Sertoli-Leydig cell tumors, usually of the ovary.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti839 – 8391S → F in MNG1. 1 Publication
    VAR_065301
    Rhabdomyosarcoma, embryonal, 2 (RMSE2) [MIM:180295]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    DICER1 mutations have been found in uterine cervix embryonal rhabdomyosarcoma, primitive neuroectodermal tumor, Wilms tumor, pulmonary sequestration and juvenile intestinal polyp (PubMed:21882293). Somatic missense mutations affecting the RNase IIIb domain of DICER1 are common in non-epithelial ovarian tumors. These mutations do not abolish DICER1 function but alter it in specific cell types, a novel mechanism through which perturbation of microRNA processing may be oncogenic (PubMed:22187960).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi960 – 9601F → A: 2-fold decrease in activity.
    Mutagenesisi971 – 9711Y → A: 10-fold decrease in activity; when associated with Y-972.
    Mutagenesisi972 – 9721Y → A: 10-fold decrease in activity; when associated with Y-971.
    Mutagenesisi1036 – 10361E → A: 5-fold decrease in activity.
    Mutagenesisi1313 – 13131E → A: No effect on activity. 1 Publication
    Mutagenesisi1320 – 13201D → A: Decreased activity. Loss of activity; when associated with D-1709. 1 Publication
    Mutagenesisi1340 – 13401E → A: No effect on activity. 1 Publication
    Mutagenesisi1444 – 14441E → A: Decreased activity. Loss of activity; when associated with E-1813. 1 Publication
    Mutagenesisi1702 – 17021Q → A: No effect on activity. 1 Publication
    Mutagenesisi1709 – 17091D → A: Decreased activity. Loss of activity; when associated with D-1320. 1 Publication
    Mutagenesisi1729 – 17291P → E: No effect on activity. 1 Publication
    Mutagenesisi1813 – 18131E → A: Decreased activity. Loss of activity; when associated with E-1444. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi138800. phenotype.
    180295. phenotype.
    601200. phenotype.
    Orphaneti276399. Familial multinodular goiter.
    99916. Ovarian malignant Sertoli-Leydig cell tumor.
    284343. Pleuropulmonary blastoma family tumor susceptibility syndrome.
    PharmGKBiPA38437.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19221922Endoribonuclease DicerPRO_0000180470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei415 – 4151Phosphoserine1 Publication
    Modified residuei1016 – 10161Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UPY3.
    PaxDbiQ9UPY3.
    PRIDEiQ9UPY3.

    PTM databases

    PhosphoSiteiQ9UPY3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UPY3.
    BgeeiQ9UPY3.
    CleanExiHS_DICER1.
    GenevestigatoriQ9UPY3.

    Organism-specific databases

    HPAiHPA000694.

    Interactioni

    Subunit structurei

    Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Associates with the 60S ribosome. Interacts with BCDIN3D.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P0C2057EBI-395506,EBI-8332963From a different organism.
    ADARP55265-14EBI-395506,EBI-6913056
    ADARP55265-58EBI-395506,EBI-6913210
    AGO1Q9UL185EBI-395506,EBI-527363
    AGO2Q9UKV813EBI-395506,EBI-528269
    Ago2Q8CJG02EBI-395506,EBI-528299From a different organism.
    DHX58Q96C102EBI-395506,EBI-744193
    EIF2AK2P195252EBI-395506,EBI-640775
    PIWIL1Q96J942EBI-395506,EBI-527417
    PRKRAO755692EBI-395506,EBI-713955
    TARBP2Q1563315EBI-395506,EBI-978581

    Protein-protein interaction databases

    BioGridi116978. 42 interactions.
    DIPiDIP-29664N.
    IntActiQ9UPY3. 21 interactions.
    MINTiMINT-1957525.
    STRINGi9606.ENSP00000343745.

    Structurei

    Secondary structure

    1
    1922
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi768 – 78013
    Helixi783 – 7853
    Helixi795 – 7973
    Beta strandi801 – 8088
    Beta strandi816 – 8205
    Beta strandi823 – 83614
    Helixi840 – 85516
    Beta strandi877 – 8837
    Beta strandi890 – 8923
    Helixi894 – 9029
    Beta strandi906 – 9083
    Beta strandi916 – 9183
    Helixi924 – 9274
    Beta strandi931 – 9377
    Beta strandi939 – 9413
    Beta strandi945 – 9517
    Helixi968 – 9769
    Beta strandi987 – 9926
    Helixi1016 – 103015
    Helixi1035 – 10373
    Beta strandi1038 – 10403
    Helixi1045 – 10517
    Helixi1054 – 10618
    Turni1662 – 16654
    Helixi1666 – 16738
    Helixi1680 – 16878
    Helixi1702 – 172221
    Helixi1729 – 173911
    Helixi1742 – 175110
    Helixi1754 – 17563
    Helixi1763 – 177816
    Helixi1806 – 182217
    Helixi1827 – 184721

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EB1X-ray2.00A/B/C1660-1852[»]
    4NGBX-ray2.25A765-1065[»]
    4NGCX-ray2.10A765-1065[»]
    4NGDX-ray1.96A765-1065[»]
    4NGFX-ray3.10A/B/C/D765-1065[»]
    4NGGX-ray2.60A765-1065[»]
    4NH3X-ray2.62A765-1065[»]
    4NH5X-ray2.55A765-1065[»]
    4NH6X-ray2.55A765-1065[»]
    4NHAX-ray3.40A765-1065[»]
    ProteinModelPortaliQ9UPY3.
    SMRiQ9UPY3. Positions 45-208, 444-582, 766-1063, 1654-1916.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UPY3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini51 – 227177Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 602170Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini630 – 72293Dicer dsRNA-binding foldPROSITE-ProRule annotationAdd
    BLAST
    Domaini891 – 1042152PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini1276 – 1403128RNase III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1666 – 1824159RNase III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1849 – 191466DRBMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni256 – 595340Required for interaction with PRKRA and TARBP2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi175 – 1784DECH 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.
    HOGENOMiHOG000001567.
    HOVERGENiHBG107811.
    InParanoidiQ9UPY3.
    KOiK11592.
    OMAiMKLCENC.
    OrthoDBiEOG78PV82.
    PhylomeDBiQ9UPY3.
    TreeFamiTF330258.

    Family and domain databases

    Gene3Di1.10.1520.10. 4 hits.
    3.30.160.20. 1 hit.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UPY3-1) [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

    MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE     50
    LLEAALDHNT IVCLNTGSGK TFIAVLLTKE LSYQIRGDFS RNGKRTVFLV 100
    NSANQVAQQV SAVRTHSDLK VGEYSNLEVN ASWTKERWNQ EFTKHQVLIM 150
    TCYVALNVLK NGYLSLSDIN LLVFDECHLA ILDHPYREIM KLCENCPSCP 200
    RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL VVLDRYTSQP 250
    CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK 300
    QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT 350
    FLRKIHALCE EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW 400
    YNNRNQDNYV SWSDSEDDDE DEEIEEKEKP ETNFPSPFTN ILCGIIFVER 450
    RYTAVVLNRL IKEAGKQDPE LAYISSNFIT GHGIGKNQPR NKQMEAEFRK 500
    QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP TEYRSYVQSK 550
    GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGETD 600
    IDPVMDDDDV FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA 650
    PKCRTRELPD GTFYSTLYLP INSPLRASIV GPPMSCVRLA ERVVALICCE 700
    KLHKIGELDD HLMPVGKETV KYEEELDLHD EEETSVPGRP GSTKRRQCYP 750
    KAIPECLRDS YPRPDQPCYL YVIGMVLTTP LPDELNFRRR KLYPPEDTTR 800
    CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFMLSL QMLELITRLH 850
    QYIFSHILRL EKPALEFKPT DADSAYCVLP LNVVNDSSTL DIDFKFMEDI 900
    EKSEARIGIP STKYTKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV 950
    YTDLTPLSKF PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL 1000
    TPRHLNQKGK ALPLSSAEKR KAKWESLQNK QILVPELCAI HPIPASLWRK 1050
    AVCLPSILYR LHCLLTAEEL RAQTASDAGV GVRSLPADFR YPNLDFGWKK 1100
    SIDSKSFISI SNSSSAENDN YCKHSTIVPE NAAHQGANRT SSLENHDQMS 1150
    VNCRTLLSES PGKLHVEVSA DLTAINGLSY NQNLANGSYD LANRDFCQGN 1200
    QLNYYKQEIP VQPTTSYSIQ NLYSYENQPQ PSDECTLLSN KYLDGNANKS 1250
    TSDGSPVMAV MPGTTDTIQV LKGRMDSEQS PSIGYSSRTL GPNPGLILQA 1300
    LTLSNASDGF NLERLEMLGD SFLKHAITTY LFCTYPDAHE GRLSYMRSKK 1350
    VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW LPPGYVVNQD KSNTDKWEKD 1400
    EMTKDCMLAN GKLDEDYEEE DEEEESLMWR APKEEADYED DFLEYDQEHI 1450
    RFIDNMLMGS GAFVKKISLS PFSTTDSAYE WKMPKKSSLG SMPFSSDFED 1500
    FDYSSWDAMC YLDPSKAVEE DDFVVGFWNP SEENCGVDTG KQSISYDLHT 1550
    EQCIADKSIA DCVEALLGCY LTSCGERAAQ LFLCSLGLKV LPVIKRTDRE 1600
    KALCPTRENF NSQQKNLSVS CAAASVASSR SSVLKDSEYG CLKIPPRCMF 1650
    DHPDADKTLN HLISGFENFE KKINYRFKNK AYLLQAFTHA SYHYNTITDC 1700
    YQRLEFLGDA ILDYLITKHL YEDPRQHSPG VLTDLRSALV NNTIFASLAV 1750
    KYDYHKYFKA VSPELFHVID DFVQFQLEKN EMQGMDSELR RSEEDEEKEE 1800
    DIEVPKAMGD IFESLAGAIY MDSGMSLETV WQVYYPMMRP LIEKFSANVP 1850
    RSPVRELLEM EPETAKFSPA ERTYDGKVRV TVEVVGKGKF KGVGRSYRIA 1900
    KSAAARRALR SLKANQPQVP NS 1922
    Length:1,922
    Mass (Da):218,682
    Last modified:September 1, 2009 - v3
    Checksum:i9452B96A601D4551
    GO
    Isoform 2 (identifier: Q9UPY3-2) [UniParc]FASTAAdd to Basket

    Also known as: t-Dicer

    The sequence of this isoform differs from the canonical sequence as follows:
         1789-1922: LRRSEEDEEK...KANQPQVPNS → KSFLQMYPVP...TTGRSESLWK

    Show »
    Length:1,829
    Mass (Da):208,448
    Checksum:i8F52FAB99C876358
    GO
    Isoform 3 (identifier: Q9UPY3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MKSPALQPLSMAG → MLAWESDHFLRIL
         14-1115: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:820
    Mass (Da):92,726
    Checksum:i006901B4B9E96382
    GO

    Sequence cautioni

    The sequence CAB38857.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 9016VLLTK…RGDFS → STTLLKSCLYLDLGETSA in BAA78691. (PubMed:10786632)CuratedAdd
    BLAST
    Sequence conflicti189 – 1891I → F in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti195 – 1951N → I in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti214 – 2141C → W in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti218 – 2181E → D in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti223 – 2231I → F in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti393 – 3942QQ → HS in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti492 – 4932KQ → NT in BAA78691. (PubMed:10786632)Curated
    Sequence conflicti609 – 6091D → H in BAA78691. (PubMed:10786632)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti839 – 8391S → F in MNG1. 1 Publication
    VAR_065301
    Natural varianti1583 – 15831L → R in PPB. 1 Publication
    VAR_063150
    Natural varianti1705 – 17051E → K in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication
    VAR_067091
    Natural varianti1709 – 17091D → E in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication
    VAR_067092
    Natural varianti1709 – 17091D → G in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067093
    Natural varianti1709 – 17091D → N in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication
    VAR_067094
    Natural varianti1810 – 18101D → H in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067095
    Natural varianti1810 – 18101D → N in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067096
    Natural varianti1810 – 18101D → Y in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067097
    Natural varianti1813 – 18131E → G in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067098
    Natural varianti1813 – 18131E → K in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067099
    Natural varianti1813 – 18131E → Q in non-epithelial ovarian tumor; somatic mutation. 1 Publication
    VAR_067100

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MKSPA…LSMAG → MLAWESDHFLRIL in isoform 3. 1 PublicationVSP_055341Add
    BLAST
    Alternative sequencei14 – 11151102Missing in isoform 3. 1 PublicationVSP_055342Add
    BLAST
    Alternative sequencei1789 – 1922134LRRSE…QVPNS → KSFLQMYPVPLCENCLKWNQ KLPNLARLRELTTGRSESLW K in isoform 2. 1 PublicationVSP_042832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028449 mRNA. Translation: BAA78691.1.
    HM595745 mRNA. Translation: ADK25182.1.
    AJ132261 mRNA. Translation: CAB38857.2. Different initiation.
    AB023145 mRNA. Translation: BAA76772.2.
    AK091513 mRNA. Translation: BAG52376.1.
    AL356017 Genomic DNA. No translation available.
    AL390254 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81596.1.
    BC150287 mRNA. Translation: AAI50288.1.
    CCDSiCCDS55941.1. [Q9UPY3-2]
    CCDS9931.1. [Q9UPY3-1]
    RefSeqiNP_001182502.1. NM_001195573.1. [Q9UPY3-2]
    NP_001258211.1. NM_001271282.2. [Q9UPY3-1]
    NP_001278557.1. NM_001291628.1. [Q9UPY3-1]
    NP_085124.2. NM_030621.4. [Q9UPY3-1]
    NP_803187.1. NM_177438.2. [Q9UPY3-1]
    UniGeneiHs.738957.
    Hs.87889.

    Genome annotation databases

    EnsembliENST00000343455; ENSP00000343745; ENSG00000100697. [Q9UPY3-1]
    ENST00000393063; ENSP00000376783; ENSG00000100697. [Q9UPY3-1]
    ENST00000526495; ENSP00000437256; ENSG00000100697. [Q9UPY3-1]
    ENST00000527414; ENSP00000435681; ENSG00000100697. [Q9UPY3-1]
    ENST00000541352; ENSP00000444719; ENSG00000100697. [Q9UPY3-2]
    ENST00000556045; ENSP00000451041; ENSG00000100697. [Q9UPY3-3]
    GeneIDi23405.
    KEGGihsa:23405.
    UCSCiuc001ydv.3. human. [Q9UPY3-1]
    uc021sbc.1. human. [Q9UPY3-2]

    Polymorphism databases

    DMDMi257051056.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The dark side of RNA - Issue 87 of October 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028449 mRNA. Translation: BAA78691.1 .
    HM595745 mRNA. Translation: ADK25182.1 .
    AJ132261 mRNA. Translation: CAB38857.2 . Different initiation.
    AB023145 mRNA. Translation: BAA76772.2 .
    AK091513 mRNA. Translation: BAG52376.1 .
    AL356017 Genomic DNA. No translation available.
    AL390254 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81596.1 .
    BC150287 mRNA. Translation: AAI50288.1 .
    CCDSi CCDS55941.1. [Q9UPY3-2 ]
    CCDS9931.1. [Q9UPY3-1 ]
    RefSeqi NP_001182502.1. NM_001195573.1. [Q9UPY3-2 ]
    NP_001258211.1. NM_001271282.2. [Q9UPY3-1 ]
    NP_001278557.1. NM_001291628.1. [Q9UPY3-1 ]
    NP_085124.2. NM_030621.4. [Q9UPY3-1 ]
    NP_803187.1. NM_177438.2. [Q9UPY3-1 ]
    UniGenei Hs.738957.
    Hs.87889.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EB1 X-ray 2.00 A/B/C 1660-1852 [» ]
    4NGB X-ray 2.25 A 765-1065 [» ]
    4NGC X-ray 2.10 A 765-1065 [» ]
    4NGD X-ray 1.96 A 765-1065 [» ]
    4NGF X-ray 3.10 A/B/C/D 765-1065 [» ]
    4NGG X-ray 2.60 A 765-1065 [» ]
    4NH3 X-ray 2.62 A 765-1065 [» ]
    4NH5 X-ray 2.55 A 765-1065 [» ]
    4NH6 X-ray 2.55 A 765-1065 [» ]
    4NHA X-ray 3.40 A 765-1065 [» ]
    ProteinModelPortali Q9UPY3.
    SMRi Q9UPY3. Positions 45-208, 444-582, 766-1063, 1654-1916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116978. 42 interactions.
    DIPi DIP-29664N.
    IntActi Q9UPY3. 21 interactions.
    MINTi MINT-1957525.
    STRINGi 9606.ENSP00000343745.

    Chemistry

    ChEMBLi CHEMBL2311232.

    PTM databases

    PhosphoSitei Q9UPY3.

    Polymorphism databases

    DMDMi 257051056.

    Proteomic databases

    MaxQBi Q9UPY3.
    PaxDbi Q9UPY3.
    PRIDEi Q9UPY3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343455 ; ENSP00000343745 ; ENSG00000100697 . [Q9UPY3-1 ]
    ENST00000393063 ; ENSP00000376783 ; ENSG00000100697 . [Q9UPY3-1 ]
    ENST00000526495 ; ENSP00000437256 ; ENSG00000100697 . [Q9UPY3-1 ]
    ENST00000527414 ; ENSP00000435681 ; ENSG00000100697 . [Q9UPY3-1 ]
    ENST00000541352 ; ENSP00000444719 ; ENSG00000100697 . [Q9UPY3-2 ]
    ENST00000556045 ; ENSP00000451041 ; ENSG00000100697 . [Q9UPY3-3 ]
    GeneIDi 23405.
    KEGGi hsa:23405.
    UCSCi uc001ydv.3. human. [Q9UPY3-1 ]
    uc021sbc.1. human. [Q9UPY3-2 ]

    Organism-specific databases

    CTDi 23405.
    GeneCardsi GC14M095552.
    HGNCi HGNC:17098. DICER1.
    HPAi HPA000694.
    MIMi 138800. phenotype.
    180295. phenotype.
    601200. phenotype.
    606241. gene.
    neXtProti NX_Q9UPY3.
    Orphaneti 276399. Familial multinodular goiter.
    99916. Ovarian malignant Sertoli-Leydig cell tumor.
    284343. Pleuropulmonary blastoma family tumor susceptibility syndrome.
    PharmGKBi PA38437.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1111.
    HOGENOMi HOG000001567.
    HOVERGENi HBG107811.
    InParanoidi Q9UPY3.
    KOi K11592.
    OMAi MKLCENC.
    OrthoDBi EOG78PV82.
    PhylomeDBi Q9UPY3.
    TreeFami TF330258.

    Enzyme and pathway databases

    BRENDAi 3.1.26.3. 2681.
    Reactomei REACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    ChiTaRSi DICER1. human.
    EvolutionaryTracei Q9UPY3.
    GeneWikii DICER1.
    GenomeRNAii 23405.
    NextBioi 35469529.
    PROi Q9UPY3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UPY3.
    Bgeei Q9UPY3.
    CleanExi HS_DICER1.
    Genevestigatori Q9UPY3.

    Family and domain databases

    Gene3Di 1.10.1520.10. 4 hits.
    3.30.160.20. 1 hit.
    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. "Molecular cloning and characterization of a novel human gene (HERNA) which encodes a putative RNA-helicase."
      Matsuda S., Ichigotani Y., Okuda T., Irimura T., Nakatsugawa S., Hamaguchi M.
      Biochim. Biophys. Acta 1490:163-169(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel splice variant of the human dicer gene is expressed in neuroblastoma cells."
      Potenza N., Papa U., Scaruffi P., Mosca N., Tonini G.P., Russo A.
      FEBS Lett. 584:3452-3457(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
      Tissue: Neuroblastoma.
    3. "RNA binding and processing by recombinant human Dicer."
      Provost P., Dishart D., Doucet D., Hermansson A., Frendewey D., Samuelsson B., Radmark O.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    4. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    7. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1248-1922 (ISOFORM 1).
      Tissue: Lung.
    11. "Single processing center models for human Dicer and bacterial RNase III."
      Zhang H., Kolb F.A., Jaskiewicz L., Westhof E., Filipowicz W.
      Cell 118:57-68(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-1313; ASP-1320; GLU-1340; GLU-1444; GLN-1702; ASP-1709; PRO-1729 AND GLU-1813.
    12. "Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer."
      Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W., Hobman T.C.
      EMBO Rep. 5:189-194(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIWIL1.
    13. "Human RISC couples microRNA biogenesis and posttranscriptional gene silencing."
      Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.
      Cell 123:631-640(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AGO2 AND TARBP2.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO1 AND AGO2.
    15. "TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing."
      Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A., Filipowicz W.
      EMBO Rep. 6:961-967(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TARBP2.
    16. "A human, ATP-independent, RISC assembly machine fueled by pre-miRNA."
      Maniataki E., Mourelatos Z.
      Genes Dev. 19:2979-2990(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AGO2.
    17. "TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing."
      Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N., Nishikura K., Shiekhattar R.
      Nature 436:740-744(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO2 AND TARBP2.
    18. "The role of PACT in the RNA silencing pathway."
      Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.
      EMBO J. 25:522-532(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKRA AND TARBP2, SUBCELLULAR LOCATION.
    19. "Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA."
      Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.
      J. Biol. Chem. 282:17649-17657(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKRA AND TARBP2.
    20. "RNA helicase A interacts with RISC in human cells and functions in RISC loading."
      Robb G.B., Rana T.M.
      Mol. Cell 26:523-537(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DHX9.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AGO2; EIF6; MOV10 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AGO2.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO2 AND TARBP2.
    25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: FUNCTION.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: INVOLVEMET IN RMSE2.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Human RNA methyltransferase BCDIN3D regulates microRNA processing."
      Xhemalce B., Robson S.C., Kouzarides T.
      Cell 151:278-288(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCDIN3D.
    31. Cited for: INVOLVEMENT IN NON-EPITHELIAL OVARIAN TUMORS, VARIANTS LYS-1705; ASN-1709; GLU-1709; GLY-1709; HIS-1810; TYR-1810; ASN-1810; GLN-1813; GLY-1813 AND LYS-1813, CHARACTERIZATION OF VARIANTS LYS-1705; ASN-1709 AND GLU-1709.
    32. "Homodimeric structure and double-stranded RNA cleavage activity of the C-terminal RNase III domain of human dicer."
      Takeshita D., Zenno S., Lee W.C., Nagata K., Saigo K., Tanokura M.
      J. Mol. Biol. 374:106-120(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1660-1852, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
    33. Cited for: VARIANT PPB ARG-1583.
    34. Cited for: VARIANT MNG1 PHE-839.

    Entry informationi

    Entry nameiDICER_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPY3
    Secondary accession number(s): A7E2D3
    , B3KRG4, E0AD28, O95943, Q9UQ02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2002
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3