Reviewed, UniProtKB/Swiss-Prot Q9UPY3 (DICER_HUMAN)

Names and origin

Protein names

Recommended name:
    Endoribonuclease Dicer
    EC=3.1.26.-
Alternative name(s):
    Helicase with RNase motif
      Short name=Helicase MOI

Gene names

Name:	DICER1
Synonyms:	DICER, HERNA, KIAA0928

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1922 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, EIF2C2/AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto EIF2C2/AGO2. EIF2C2/AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Also cleaves double-stranded RNA to produce short interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.22 Ref.24
Cofactor	Binds 2 magnesium or manganese ions per subunit Probable.
Subunit structure	Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, EIF2C2/AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, EIF2C1, PIWIL1 and PRKRA. Associates with the 60S ribosome. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.22 Ref.10 Ref.19 Ref.20 Ref.21 Ref.26
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the helicase family. Dicer subfamily. Contains 1 Dicer dsRNA-binding fold domain. Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 PAZ domain. Contains 2 RNase III domains.
Caution	It is uncertain whether Met-1 or Met-11 is the initiator.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Endonuclease Helicase Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	pre-microRNA processing Ref.15 Inferred from direct assay. Source: UniProtKB production of siRNA involved in RNA interference Ref.15 Ref.18 Inferred from direct assay. Source: UniProtKB targeting of mRNA for destruction involved in RNA interference Ref.15 Ref.18 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	RNA-induced silencing complex Ref.15 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro double-stranded RNA binding Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.10 Ref.13 Ref.15 Ref.18 Inferred from physical interaction. Source: UniProtKB ribonuclease III activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2C1	Q9UL18	2	EBI-395506,EBI-527363
EIF2C2	Q9UKV8	1	EBI-395506,EBI-528269
Eif2c2	Q8CJG0	2	EBI-395506,EBI-528299	From a different organism.
PIWIL1	Q96J94	1	EBI-395506,EBI-527417
TARBP2	Q15633	4	EBI-395506,EBI-978581

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1922

1922

Endoribonuclease Dicer

PRO_0000180470

Regions

Domain

51 – 227

177

Helicase ATP-binding

Domain

433 – 602

170

Helicase C-terminal

Domain

630 – 722

93

Dicer dsRNA-binding fold

Domain

891 – 1042

152

PAZ

Domain

1276 – 1403

128

RNase III 1

Domain

1666 – 1824

159

RNase III 2

Domain

1849 – 1914

66

DRBM

Nucleotide binding

64 – 71

8

ATP By similarity

Region

256 – 595

340

Required for interaction with PRKRA and TARBP2

Motif

175 – 178

4

DECH box

Sites

Metal binding

1316

1

Magnesium or manganese 1 By similarity

Metal binding

1395

1

Magnesium or manganese 1 By similarity

Metal binding

1398

1

Magnesium or manganese 1 By similarity

Metal binding

1705

1

Magnesium or manganese 2

Metal binding

1810

1

Magnesium or manganese 2

Metal binding

1813

1

Magnesium or manganese 2

Site

1806

1

Important for activity By similarity

Amino acid modifications

Modified residue

664

1

Phosphotyrosine Ref.16

Modified residue

1016

1

Phosphoserine Ref.23

Experimental info

Mutagenesis

960

1

F → A: 2-fold decrease in activity.

Mutagenesis

971

1

Y → A: 10-fold decrease in activity; when associtated with Y-972.

Mutagenesis

972

1

Y → A: 10-fold decrease in activity; when associtated with Y-971.

Mutagenesis

1036

1

E → A: 5-fold decrease in activity.

Mutagenesis

1313

1

E → A: No effect on activity. Ref.9

Mutagenesis

1320

1

D → A: Decreased activity. Loss of activity; when associated with D-1709. Ref.9

Mutagenesis

1340

1

E → A: No effect on activity. Ref.9

Mutagenesis

1444

1

E → A: Decreased activity. Loss of activity; when associated with E-1813. Ref.9

Mutagenesis

1702

1

Q → A: No effect on activity. Ref.9

Mutagenesis

1709

1

D → A: Decreased activity. Loss of activity; when associated with D-1320. Ref.9

Mutagenesis

1729

1

P → E: No effect on activity. Ref.9

Mutagenesis

1813

1

E → A: Decreased activity. Loss of activity; when associated with E-1444. Ref.9

Sequence conflict

75 – 90

16

VLLTK…RGDFS → STTLLKSCLYLDLGETSA in BAA78691. Ref.1

Sequence conflict

189

1

I → F in BAA78691. Ref.1

Sequence conflict

195

1

N → I in BAA78691. Ref.1

Sequence conflict

214

1

C → W in BAA78691. Ref.1

Sequence conflict

218

1

E → D in BAA78691. Ref.1

Sequence conflict

223

1

I → F in BAA78691. Ref.1

Sequence conflict

393 – 394

2

QQ → HS in BAA78691. Ref.1

Sequence conflict

492 – 493

2

KQ → NT in BAA78691. Ref.1

Sequence conflict

609

1

D → H in BAA78691. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1922

Helix Strand Turn

Details...

Turn

1662 – 1665

4

Helix

1666 – 1673

8

Helix

1680 – 1687

8

Helix

1702 – 1722

21

Helix

1729 – 1739

11

Helix

1742 – 1751

10

Helix

1754 – 1756

3

Helix

1763 – 1778

16

Helix

1806 – 1822

17

Helix

1827 – 1847

21

Sequences

	Sequence		Length	Mass (Da)
	Q9UPY3-1 [UniParc]. Last modified September 1, 2009. Version 3. Checksum: 9452B96A601D4551	FASTA	1,922	218,682
	10 20 30 40 50 60 MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT 70 80 90 100 110 120 IVCLNTGSGK TFIAVLLTKE LSYQIRGDFS RNGKRTVFLV NSANQVAQQV SAVRTHSDLK 130 140 150 160 170 180 VGEYSNLEVN ASWTKERWNQ EFTKHQVLIM TCYVALNVLK NGYLSLSDIN LLVFDECHLA 190 200 210 220 230 240 ILDHPYREIM KLCENCPSCP RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL 250 260 270 280 290 300 VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK 310 320 330 340 350 360 QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT FLRKIHALCE 370 380 390 400 410 420 EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDE 430 440 450 460 470 480 DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT 490 500 510 520 530 540 GHGIGKNQPR NKQMEAEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP 550 560 570 580 590 600 TEYRSYVQSK GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGETD 610 620 630 640 650 660 IDPVMDDDDV FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA PKCRTRELPD 670 680 690 700 710 720 GTFYSTLYLP INSPLRASIV GPPMSCVRLA ERVVALICCE KLHKIGELDD HLMPVGKETV 730 740 750 760 770 780 KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRDS YPRPDQPCYL YVIGMVLTTP 790 800 810 820 830 840 LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFMLSL 850 860 870 880 890 900 QMLELITRLH QYIFSHILRL EKPALEFKPT DADSAYCVLP LNVVNDSSTL DIDFKFMEDI 910 920 930 940 950 960 EKSEARIGIP STKYTKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF 970 980 990 1000 1010 1020 PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR 1030 1040 1050 1060 1070 1080 KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTASDAGV 1090 1100 1110 1120 1130 1140 GVRSLPADFR YPNLDFGWKK SIDSKSFISI SNSSSAENDN YCKHSTIVPE NAAHQGANRT 1150 1160 1170 1180 1190 1200 SSLENHDQMS VNCRTLLSES PGKLHVEVSA DLTAINGLSY NQNLANGSYD LANRDFCQGN 1210 1220 1230 1240 1250 1260 QLNYYKQEIP VQPTTSYSIQ NLYSYENQPQ PSDECTLLSN KYLDGNANKS TSDGSPVMAV 1270 1280 1290 1300 1310 1320 MPGTTDTIQV LKGRMDSEQS PSIGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD 1330 1340 1350 1360 1370 1380 SFLKHAITTY LFCTYPDAHE GRLSYMRSKK VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW 1390 1400 1410 1420 1430 1440 LPPGYVVNQD KSNTDKWEKD EMTKDCMLAN GKLDEDYEEE DEEEESLMWR APKEEADYED 1450 1460 1470 1480 1490 1500 DFLEYDQEHI RFIDNMLMGS GAFVKKISLS PFSTTDSAYE WKMPKKSSLG SMPFSSDFED 1510 1520 1530 1540 1550 1560 FDYSSWDAMC YLDPSKAVEE DDFVVGFWNP SEENCGVDTG KQSISYDLHT EQCIADKSIA 1570 1580 1590 1600 1610 1620 DCVEALLGCY LTSCGERAAQ LFLCSLGLKV LPVIKRTDRE KALCPTRENF NSQQKNLSVS 1630 1640 1650 1660 1670 1680 CAAASVASSR SSVLKDSEYG CLKIPPRCMF DHPDADKTLN HLISGFENFE KKINYRFKNK 1690 1700 1710 1720 1730 1740 AYLLQAFTHA SYHYNTITDC YQRLEFLGDA ILDYLITKHL YEDPRQHSPG VLTDLRSALV 1750 1760 1770 1780 1790 1800 NNTIFASLAV KYDYHKYFKA VSPELFHVID DFVQFQLEKN EMQGMDSELR RSEEDEEKEE 1810 1820 1830 1840 1850 1860 DIEVPKAMGD IFESLAGAIY MDSGMSLETV WQVYYPMMRP LIEKFSANVP RSPVRELLEM 1870 1880 1890 1900 1910 1920 EPETAKFSPA ERTYDGKVRV TVEVVGKGKF KGVGRSYRIA KSAAARRALR SLKANQPQVP NS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10786632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Lung.
[3]	"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: 10231032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"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: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"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: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Interaction of 5-lipoxygenase with cellular proteins." Provost P., Samuelsson B., Radmark O. Proc. Natl. Acad. Sci. U.S.A. 96:1881-1885(1999) [PubMed: 10051563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1248-1922. Tissue: Lung.
[9]	"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: 15242644] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-1313; ASP-1320; GLU-1340; GLU-1444; GLN-1702; ASP-1709; PRO-1729 AND GLU-1813.
[10]	"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: 14749716] [Abstract] Cited for: INTERACTION WITH PIWIL1.
[11]	"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: 16271387] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF2C2 AND TARBP2.
[12]	"Identification of novel argonaute-associated proteins." Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R., Tuschl T. Curr. Biol. 15:2149-2155(2005) [PubMed: 16289642] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH EIF2C1 AND EIF2C2.
[13]	"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: 16142218] [Abstract] Cited for: FUNCTION, INTERACTION WITH TARBP2.
[14]	"A human, ATP-independent, RISC assembly machine fueled by pre-miRNA." Maniataki E., Mourelatos Z. Genes Dev. 19:2979-2990(2005) [PubMed: 16357216] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF2C2.
[15]	"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: 15973356] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH EIF2C2 AND TARBP2.
[16]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-664, MASS SPECTROMETRY.
[17]	"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: 16424907] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKRA AND TARBP2, SUBCELLULAR LOCATION.
[18]	"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: 17452327] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKRA AND TARBP2.
[19]	"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: 17531811] [Abstract] Cited for: INTERACTION WITH DHX9.
[20]	"MicroRNA silencing through RISC recruitment of eIF6." Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I., Liebhaber S.A., Pasquinelli A.E., Shiekhattar R. Nature 447:823-828(2007) [PubMed: 17507929] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2C2; EIF6; MOV10 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
[21]	"Prolyl 4-hydroxylation regulates Argonaute 2 stability." Qi H.H., Ongusaha P.P., Myllyharju J., Cheng D., Pakkanen O., Shi Y., Lee S.W., Peng J., Shi Y. Nature 455:421-424(2008) [PubMed: 18690212] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2C2.
[22]	"In vitro reconstitution of the human RISC-loading complex." MacRae I.J., Ma E., Zhou M., Robinson C.V., Doudna J.A. Proc. Natl. Acad. Sci. U.S.A. 105:512-517(2008) [PubMed: 18178619] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH EIF2C2 AND TARBP2.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, MASS SPECTROMETRY.
[24]	"A TARBP2 mutation in human cancer impairs microRNA processing and DICER1 function." Melo S.A., Ropero S., Moutinho C., Aaltonen L.A., Yamamoto H., Calin G.A., Rossi S., Fernandez A.F., Carneiro F., Oliveira C., Ferreira B., Liu C.-G., Villanueva A., Capella G., Schwartz S. Jr., Shiekhattar R., Esteller M. Nat. Genet. 41:365-370(2009) [PubMed: 19219043] [Abstract] Cited for: FUNCTION.
[25]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	"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: 17920623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1660-1852, COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The dark side of RNA - Issue 87 of October 2007

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB028449 mRNA. Translation: BAA78691.1.
AJ132261 mRNA. Translation: CAB38857.2. Different initiation.
AB023145 mRNA. Translation: BAA76772.2.
AL356017 Genomic DNA. No translation available.
AL390254 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81596.1.
BC150287 mRNA. Translation: AAI50288.1.

IPI

IPI00219036.

RefSeq

NP_085124.2.
NP_803187.1.

UniGene

Hs.87889

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EB1	X-ray	2.00	A/B/C	1660-1852	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UPY3. 10 interactions.

STRING

Q9UPY3.

PTM databases

PhosphoSite

Q9UPY3.

Proteomic databases

PRIDE

Q9UPY3.

Genome annotation databases

Ensembl

ENST00000343455; ENSP00000343745; ENSG00000100697; Homo sapiens. [Genome view]
ENST00000393063; ENSP00000376783; ENSG00000100697; Homo sapiens. [Genome view]

GeneID

23405.

KEGG

hsa:23405.

UCSC

uc001ydv.2. human.

Organism-specific databases

CTD

23405.

GeneCards

GC14M094622.

H-InvDB

HIX0011933.

HGNC

HGNC:17098. DICER1.

HPA

HPA000694.

MIM

606241. gene.

Orphanet

64742. Pleuro-pulmonary blastoma.

PharmGKB

PA38437.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UPY3.

HOVERGEN

Q9UPY3.

OMA

QPQVPNS

Enzyme and pathway databases

Reactome

REACT_12472. Regulatory RNA pathways.

Gene expression databases

ArrayExpress

Q9UPY3.

Bgee

Q9UPY3.

CleanEx

HS_DICER1.

Genevestigator

Q9UPY3.

GermOnline

ENSG00000100697. Homo sapiens.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR005034. Dicer_dsRNA_binding_fold.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR001159. Ds-RNA_bd.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR003100. PAZ.
IPR000999. RNase_III.
[Graphical view]

Gene3D

G3DSA:1.10.1520.10. RNase_III. 2 hits.

Pfam

PF00270. DEAD. 1 hit.
PF00035. dsrm. 1 hit.
PF03368. dsRNA_bind. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]

PROSITE

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]

ProtoNet

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Other Resources

NextBio

45577.

SOURCE

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Entry information

Entry name

DICER_HUMAN

Accession

Primary (citable) accession number: Q9UPY3
Secondary accession number(s): A7E2D3, O95943, Q9UQ02

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	September 1, 2009
Last modified:	November 24, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.