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Protein

Endoribonuclease Dicer

Gene

DICER1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium or manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1316Magnesium or manganese 1By similarity1
Metal bindingi1395Magnesium or manganese 1By similarity1
Metal bindingi1398Magnesium or manganese 1By similarity1
Metal bindingi1705Magnesium or manganese 21
Sitei1806Important for activityBy similarity1
Metal bindingi1810Magnesium or manganese 21
Metal bindingi1813Magnesium or manganese 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi64 – 71ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • deoxyribonuclease I activity Source: GO_Central
  • double-stranded RNA binding Source: UniProtKB
  • endoribonuclease activity Source: BHF-UCL
  • helicase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • pre-miRNA binding Source: BHF-UCL
  • protein domain specific binding Source: BHF-UCL
  • ribonuclease III activity Source: UniProtKB
  • siRNA binding Source: BHF-UCL

GO - Biological processi

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

BioCyciZFISH:ENSG00000100697-MONOMER.
BRENDAi3.1.26.3. 2681.
ReactomeiR-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-426486. Small interfering RNA (siRNA) biogenesis.
SIGNORiQ9UPY3.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:17098. DICER1.

Subcellular locationi

GO - Cellular componenti

  • ARC complex Source: BHF-UCL
  • axon Source: Ensembl
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • dendrite Source: Ensembl
  • endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  • growth cone Source: Ensembl
  • nucleus Source: GO_Central
  • RISC-loading complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Pleuropulmonary blastoma (PPB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:601200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0631501583L → R in PPB. 1 PublicationCorresponds to variant rs137852976dbSNPEnsembl.1
Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA common disorder characterized by nodular overgrowth of the thyroid gland. Some individuals may also develop Sertoli-Leydig cell tumors, usually of the ovary.
See also OMIM:138800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065301839S → F in MNG1. 1 PublicationCorresponds to variant rs387906934dbSNPEnsembl.1
Rhabdomyosarcoma, embryonal, 2 (RMSE2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:180295

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).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi960F → A: 2-fold decrease in activity. 1
Mutagenesisi971Y → A: 10-fold decrease in activity; when associated with Y-972. 1
Mutagenesisi972Y → A: 10-fold decrease in activity; when associated with Y-971. 1
Mutagenesisi1036E → A: 5-fold decrease in activity. 1
Mutagenesisi1313E → A: No effect on activity. 1 Publication1
Mutagenesisi1320D → A: Decreased activity. Loss of activity; when associated with D-1709. 1 Publication1
Mutagenesisi1340E → A: No effect on activity. 1 Publication1
Mutagenesisi1444E → A: Decreased activity. Loss of activity; when associated with E-1813. 1 Publication1
Mutagenesisi1702Q → A: No effect on activity. 1 Publication1
Mutagenesisi1709D → A: Decreased activity. Loss of activity; when associated with D-1320. 1 Publication1
Mutagenesisi1729P → E: No effect on activity. 1 Publication1
Mutagenesisi1813E → A: Decreased activity. Loss of activity; when associated with E-1444. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23405.
MalaCardsiDICER1.
MIMi138800. phenotype.
180295. phenotype.
601200. phenotype.
OpenTargetsiENSG00000100697.
Orphaneti276399. Familial multinodular goiter.
404476. Global developmental delay-lung cysts-overgrowth-Wilms tumor syndrome.
99914. Gynandroblastoma.
99915. Maligant granulosa cell tumor of ovary.
99916. Malignant Sertoli-Leydig cell tumor of ovary.
284343. Pleuropulmonary blastoma family tumor susceptibility syndrome.
PharmGKBiPA38437.

Chemistry databases

ChEMBLiCHEMBL2311232.

Polymorphism and mutation databases

BioMutaiDICER1.
DMDMi257051056.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001804701 – 1922Endoribonuclease DicerAdd BLAST1922

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei413PhosphoserineCombined sources1
Modified residuei415PhosphoserineCombined sources1
Modified residuei1016PhosphoserineCombined sources1
Modified residuei1160PhosphoserineCombined sources1
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1468PhosphoserineBy similarity1
Modified residuei1470PhosphoserineCombined sources1
Modified residuei1868PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UPY3.
PaxDbiQ9UPY3.
PeptideAtlasiQ9UPY3.
PRIDEiQ9UPY3.

PTM databases

iPTMnetiQ9UPY3.
PhosphoSitePlusiQ9UPY3.

Expressioni

Gene expression databases

BgeeiENSG00000100697.
CleanExiHS_DICER1.
ExpressionAtlasiQ9UPY3. baseline and differential.
GenevisibleiQ9UPY3. HS.

Organism-specific databases

HPAiCAB068185.
HPA000694.

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. Interacts with AGO2, TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC) (PubMed:17507929).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
AGO2Q9UKV819EBI-395506,EBI-528269
Ago2Q8CJG02EBI-395506,EBI-528299From a different organism.
DHX58Q96C102EBI-395506,EBI-744193
EIF2AK2P195252EBI-395506,EBI-640775
PIWIL1Q96J942EBI-395506,EBI-527417
PRKRAO755697EBI-395506,EBI-713955
TARBP2Q1563321EBI-395506,EBI-978581

GO - Molecular functioni

  • protein domain specific binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116978. 73 interactors.
DIPiDIP-29664N.
IntActiQ9UPY3. 34 interactors.
MINTiMINT-1957525.
STRINGi9606.ENSP00000343745.

Structurei

Secondary structure

11922
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi268 – 282Combined sources15
Helixi297 – 313Combined sources17
Helixi315 – 335Combined sources21
Helixi339 – 361Combined sources23
Beta strandi363 – 367Combined sources5
Helixi375 – 385Combined sources11
Beta strandi768 – 780Combined sources13
Helixi783 – 785Combined sources3
Helixi795 – 797Combined sources3
Beta strandi801 – 808Combined sources8
Beta strandi816 – 820Combined sources5
Beta strandi823 – 836Combined sources14
Helixi840 – 855Combined sources16
Beta strandi877 – 883Combined sources7
Beta strandi890 – 892Combined sources3
Helixi894 – 902Combined sources9
Beta strandi906 – 908Combined sources3
Beta strandi916 – 918Combined sources3
Helixi924 – 927Combined sources4
Beta strandi931 – 937Combined sources7
Beta strandi939 – 941Combined sources3
Beta strandi945 – 951Combined sources7
Helixi968 – 976Combined sources9
Beta strandi987 – 992Combined sources6
Helixi1016 – 1030Combined sources15
Helixi1035 – 1037Combined sources3
Beta strandi1038 – 1040Combined sources3
Helixi1045 – 1051Combined sources7
Helixi1054 – 1061Combined sources8
Turni1662 – 1665Combined sources4
Helixi1666 – 1673Combined sources8
Helixi1680 – 1687Combined sources8
Helixi1702 – 1722Combined sources21
Helixi1729 – 1739Combined sources11
Helixi1742 – 1751Combined sources10
Helixi1754 – 1756Combined sources3
Helixi1763 – 1778Combined sources16
Helixi1806 – 1822Combined sources17
Helixi1827 – 1847Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WYQX-ray3.20A/D267-389[»]
ProteinModelPortaliQ9UPY3.
SMRiQ9UPY3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UPY3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 227Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST177
Domaini433 – 602Helicase C-terminalPROSITE-ProRule annotationAdd BLAST170
Domaini630 – 722Dicer dsRNA-binding foldPROSITE-ProRule annotationAdd BLAST93
Domaini891 – 1042PAZPROSITE-ProRule annotationAdd BLAST152
Domaini1276 – 1403RNase III 1PROSITE-ProRule annotationAdd BLAST128
Domaini1666 – 1824RNase III 2PROSITE-ProRule annotationAdd BLAST159
Domaini1849 – 1914DRBMPROSITE-ProRule annotationAdd BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni256 – 595Required for interaction with PRKRA and TARBP2Add BLAST340

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi175 – 178DECH box4

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

eggNOGiKOG0701. Eukaryota.
COG0571. LUCA.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000001567.
HOVERGENiHBG107811.
InParanoidiQ9UPY3.
KOiK11592.
OMAiRQYQQTK.
OrthoDBiEOG091G00M8.
PhylomeDBiQ9UPY3.
TreeFamiTF330258.

Family and domain databases

CDDicd00593. RIBOc. 2 hits.
Gene3Di1.10.1520.10. 4 hits.
3.30.160.20. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR005034. Dicer_dimerisation_dom.
IPR014720. dsRBD_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. AlignAdd to basket

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

        10         20         30         40         50
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE
60 70 80 90 100
LLEAALDHNT IVCLNTGSGK TFIAVLLTKE LSYQIRGDFS RNGKRTVFLV
110 120 130 140 150
NSANQVAQQV SAVRTHSDLK VGEYSNLEVN ASWTKERWNQ EFTKHQVLIM
160 170 180 190 200
TCYVALNVLK NGYLSLSDIN LLVFDECHLA ILDHPYREIM KLCENCPSCP
210 220 230 240 250
RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL VVLDRYTSQP
260 270 280 290 300
CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK
310 320 330 340 350
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT
360 370 380 390 400
FLRKIHALCE EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW
410 420 430 440 450
YNNRNQDNYV SWSDSEDDDE DEEIEEKEKP ETNFPSPFTN ILCGIIFVER
460 470 480 490 500
RYTAVVLNRL IKEAGKQDPE LAYISSNFIT GHGIGKNQPR NKQMEAEFRK
510 520 530 540 550
QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP TEYRSYVQSK
560 570 580 590 600
GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGETD
610 620 630 640 650
IDPVMDDDDV FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA
660 670 680 690 700
PKCRTRELPD GTFYSTLYLP INSPLRASIV GPPMSCVRLA ERVVALICCE
710 720 730 740 750
KLHKIGELDD HLMPVGKETV KYEEELDLHD EEETSVPGRP GSTKRRQCYP
760 770 780 790 800
KAIPECLRDS YPRPDQPCYL YVIGMVLTTP LPDELNFRRR KLYPPEDTTR
810 820 830 840 850
CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFMLSL QMLELITRLH
860 870 880 890 900
QYIFSHILRL EKPALEFKPT DADSAYCVLP LNVVNDSSTL DIDFKFMEDI
910 920 930 940 950
EKSEARIGIP STKYTKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV
960 970 980 990 1000
YTDLTPLSKF PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL
1010 1020 1030 1040 1050
TPRHLNQKGK ALPLSSAEKR KAKWESLQNK QILVPELCAI HPIPASLWRK
1060 1070 1080 1090 1100
AVCLPSILYR LHCLLTAEEL RAQTASDAGV GVRSLPADFR YPNLDFGWKK
1110 1120 1130 1140 1150
SIDSKSFISI SNSSSAENDN YCKHSTIVPE NAAHQGANRT SSLENHDQMS
1160 1170 1180 1190 1200
VNCRTLLSES PGKLHVEVSA DLTAINGLSY NQNLANGSYD LANRDFCQGN
1210 1220 1230 1240 1250
QLNYYKQEIP VQPTTSYSIQ NLYSYENQPQ PSDECTLLSN KYLDGNANKS
1260 1270 1280 1290 1300
TSDGSPVMAV MPGTTDTIQV LKGRMDSEQS PSIGYSSRTL GPNPGLILQA
1310 1320 1330 1340 1350
LTLSNASDGF NLERLEMLGD SFLKHAITTY LFCTYPDAHE GRLSYMRSKK
1360 1370 1380 1390 1400
VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW LPPGYVVNQD KSNTDKWEKD
1410 1420 1430 1440 1450
EMTKDCMLAN GKLDEDYEEE DEEEESLMWR APKEEADYED DFLEYDQEHI
1460 1470 1480 1490 1500
RFIDNMLMGS GAFVKKISLS PFSTTDSAYE WKMPKKSSLG SMPFSSDFED
1510 1520 1530 1540 1550
FDYSSWDAMC YLDPSKAVEE DDFVVGFWNP SEENCGVDTG KQSISYDLHT
1560 1570 1580 1590 1600
EQCIADKSIA DCVEALLGCY LTSCGERAAQ LFLCSLGLKV LPVIKRTDRE
1610 1620 1630 1640 1650
KALCPTRENF NSQQKNLSVS CAAASVASSR SSVLKDSEYG CLKIPPRCMF
1660 1670 1680 1690 1700
DHPDADKTLN HLISGFENFE KKINYRFKNK AYLLQAFTHA SYHYNTITDC
1710 1720 1730 1740 1750
YQRLEFLGDA ILDYLITKHL YEDPRQHSPG VLTDLRSALV NNTIFASLAV
1760 1770 1780 1790 1800
KYDYHKYFKA VSPELFHVID DFVQFQLEKN EMQGMDSELR RSEEDEEKEE
1810 1820 1830 1840 1850
DIEVPKAMGD IFESLAGAIY MDSGMSLETV WQVYYPMMRP LIEKFSANVP
1860 1870 1880 1890 1900
RSPVRELLEM EPETAKFSPA ERTYDGKVRV TVEVVGKGKF KGVGRSYRIA
1910 1920
KSAAARRALR SLKANQPQVP NS
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75 – 90VLLTK…RGDFS → STTLLKSCLYLDLGETSA in BAA78691 (PubMed:10786632).CuratedAdd BLAST16
Sequence conflicti189I → F in BAA78691 (PubMed:10786632).Curated1
Sequence conflicti195N → I in BAA78691 (PubMed:10786632).Curated1
Sequence conflicti214C → W in BAA78691 (PubMed:10786632).Curated1
Sequence conflicti218E → D in BAA78691 (PubMed:10786632).Curated1
Sequence conflicti223I → F in BAA78691 (PubMed:10786632).Curated1
Sequence conflicti393 – 394QQ → HS in BAA78691 (PubMed:10786632).Curated2
Sequence conflicti492 – 493KQ → NT in BAA78691 (PubMed:10786632).Curated2
Sequence conflicti609D → H in BAA78691 (PubMed:10786632).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065301839S → F in MNG1. 1 PublicationCorresponds to variant rs387906934dbSNPEnsembl.1
Natural variantiVAR_0631501583L → R in PPB. 1 PublicationCorresponds to variant rs137852976dbSNPEnsembl.1
Natural variantiVAR_0670911705E → K in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication1
Natural variantiVAR_0670921709D → E in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication1
Natural variantiVAR_0670931709D → G in non-epithelial ovarian tumor; somatic mutation. 1 Publication1
Natural variantiVAR_0670941709D → N in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity. 1 Publication1
Natural variantiVAR_0670951810D → H in non-epithelial ovarian tumor; somatic mutation. 1 Publication1
Natural variantiVAR_0670961810D → N in non-epithelial ovarian tumor; somatic mutation. 1 PublicationCorresponds to variant rs775912475dbSNPEnsembl.1
Natural variantiVAR_0670971810D → Y in non-epithelial ovarian tumor; somatic mutation. 1 Publication1
Natural variantiVAR_0670981813E → G in non-epithelial ovarian tumor; somatic mutation. 1 Publication1
Natural variantiVAR_0670991813E → K in non-epithelial ovarian tumor; somatic mutation. 1 Publication1
Natural variantiVAR_0671001813E → Q in non-epithelial ovarian tumor; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0553411 – 13MKSPA…LSMAG → MLAWESDHFLRIL in isoform 3. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_05534214 – 1115Missing in isoform 3. 1 PublicationAdd BLAST1102
Alternative sequenceiVSP_0428321789 – 1922LRRSE…QVPNS → KSFLQMYPVPLCENCLKWNQ KLPNLARLRELTTGRSESLW K in isoform 2. 1 PublicationAdd BLAST134

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011534901.1. XM_011536599.1. [Q9UPY3-1]
XP_011534902.1. XM_011536600.2. [Q9UPY3-1]
XP_011534903.1. XM_011536601.2. [Q9UPY3-1]
XP_011534904.1. XM_011536602.2. [Q9UPY3-1]
XP_016876609.1. XM_017021120.1. [Q9UPY3-1]
XP_016876610.1. XM_017021121.1. [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.4. human. [Q9UPY3-1]

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:
EMBLi
GenBanki
DDBJi
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]
XP_011534901.1. XM_011536599.1. [Q9UPY3-1]
XP_011534902.1. XM_011536600.2. [Q9UPY3-1]
XP_011534903.1. XM_011536601.2. [Q9UPY3-1]
XP_011534904.1. XM_011536602.2. [Q9UPY3-1]
XP_016876609.1. XM_017021120.1. [Q9UPY3-1]
XP_016876610.1. XM_017021121.1. [Q9UPY3-1]
UniGeneiHs.738957.
Hs.87889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WYQX-ray3.20A/D267-389[»]
ProteinModelPortaliQ9UPY3.
SMRiQ9UPY3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116978. 73 interactors.
DIPiDIP-29664N.
IntActiQ9UPY3. 34 interactors.
MINTiMINT-1957525.
STRINGi9606.ENSP00000343745.

Chemistry databases

ChEMBLiCHEMBL2311232.

PTM databases

iPTMnetiQ9UPY3.
PhosphoSitePlusiQ9UPY3.

Polymorphism and mutation databases

BioMutaiDICER1.
DMDMi257051056.

Proteomic databases

EPDiQ9UPY3.
PaxDbiQ9UPY3.
PeptideAtlasiQ9UPY3.
PRIDEiQ9UPY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [Q9UPY3-1]

Organism-specific databases

CTDi23405.
DisGeNETi23405.
GeneCardsiDICER1.
HGNCiHGNC:17098. DICER1.
HPAiCAB068185.
HPA000694.
MalaCardsiDICER1.
MIMi138800. phenotype.
180295. phenotype.
601200. phenotype.
606241. gene.
neXtProtiNX_Q9UPY3.
OpenTargetsiENSG00000100697.
Orphaneti276399. Familial multinodular goiter.
404476. Global developmental delay-lung cysts-overgrowth-Wilms tumor syndrome.
99914. Gynandroblastoma.
99915. Maligant granulosa cell tumor of ovary.
99916. Malignant Sertoli-Leydig cell tumor of ovary.
284343. Pleuropulmonary blastoma family tumor susceptibility syndrome.
PharmGKBiPA38437.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0701. Eukaryota.
COG0571. LUCA.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000001567.
HOVERGENiHBG107811.
InParanoidiQ9UPY3.
KOiK11592.
OMAiRQYQQTK.
OrthoDBiEOG091G00M8.
PhylomeDBiQ9UPY3.
TreeFamiTF330258.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100697-MONOMER.
BRENDAi3.1.26.3. 2681.
ReactomeiR-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-426486. Small interfering RNA (siRNA) biogenesis.
SIGNORiQ9UPY3.

Miscellaneous databases

ChiTaRSiDICER1. human.
EvolutionaryTraceiQ9UPY3.
GeneWikiiDICER1.
GenomeRNAii23405.
PROiQ9UPY3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100697.
CleanExiHS_DICER1.
ExpressionAtlasiQ9UPY3. baseline and differential.
GenevisibleiQ9UPY3. HS.

Family and domain databases

CDDicd00593. RIBOc. 2 hits.
Gene3Di1.10.1520.10. 4 hits.
3.30.160.20. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR005034. Dicer_dimerisation_dom.
IPR014720. dsRBD_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]
ProtoNetiSearch...

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: November 30, 2016
This is version 163 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

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.