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Q9UPY3

- DICER_HUMAN

UniProt

Q9UPY3 - DICER_HUMAN

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Protein
Endoribonuclease Dicer
Gene
DICER1, DICER, HERNA, KIAA0928
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Inferred.1 Publication

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.1 Publication
DICER1 mutations have been found in uterine cervix embryonal rhabdomyosarcoma, primitive neuroectodermal tumor, Wilms tumor, pulmonary sequestration and juvenile intestinal polyp (1 Publication). 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 (1 Publication).

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 Dicer
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ9UPY3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 227177Helicase ATP-binding
Add
BLAST
Domaini433 – 602170Helicase C-terminal
Add
BLAST
Domaini630 – 72293Dicer dsRNA-binding fold
Add
BLAST
Domaini891 – 1042152PAZ
Add
BLAST
Domaini1276 – 1403128RNase III 1
Add
BLAST
Domaini1666 – 1824159RNase III 2
Add
BLAST
Domaini1849 – 191466DRBM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 595340Required for interaction with PRKRA and TARBP2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi175 – 1784DECH box

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 2 RNase III domains.

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.

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.
VSP_055341Add
BLAST
Alternative sequencei14 – 11151102Missing in isoform 3.
VSP_055342Add
BLAST
Alternative sequencei1789 – 1922134LRRSE…QVPNS → KSFLQMYPVPLCENCLKWNQ KLPNLARLRELTTGRSESLW K in isoform 2.
VSP_042832Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 9016VLLTK…RGDFS → STTLLKSCLYLDLGETSA in BAA78691. 1 Publication
Add
BLAST
Sequence conflicti189 – 1891I → F in BAA78691. 1 Publication
Sequence conflicti195 – 1951N → I in BAA78691. 1 Publication
Sequence conflicti214 – 2141C → W in BAA78691. 1 Publication
Sequence conflicti218 – 2181E → D in BAA78691. 1 Publication
Sequence conflicti223 – 2231I → F in BAA78691. 1 Publication
Sequence conflicti393 – 3942QQ → HS in BAA78691. 1 Publication
Sequence conflicti492 – 4932KQ → NT in BAA78691. 1 Publication
Sequence conflicti609 – 6091D → H in BAA78691. 1 Publication

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.
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 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 138 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

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