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Protein argonaute-2 (Argonaute2) (hAgo2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (PAZ Piwi domain protein) (PPD) (Protein slicer)

 AGO2_HUMAN              Reviewed;         859 AA.
Q9UKV8; Q8TCZ5; Q8WV58; Q96ID1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
25-OCT-2017, entry version 166.
RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=hAgo2;
EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=Argonaute RISC catalytic component 2;
AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=PAZ Piwi domain protein;
Short=PPD;
AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031};
Name=AGO2; Synonyms=EIF2C2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 239-859 (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 47-859 (ISOFORM 1).
PubMed=11914277; DOI=10.1101/gad.974702;
Mourelatos Z., Dostie J., Paushkin S., Sharma A., Charroux B.,
Abel L., Rappsilber J., Mann M., Dreyfuss G.;
"miRNPs: a novel class of ribonucleoproteins containing numerous
microRNAs.";
Genes Dev. 16:720-728(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-859 (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 483-859 (ISOFORM 1).
PubMed=10534406; DOI=10.1006/geno.1999.5951;
Koesters R., Adams V., Betts D., Moos R., Schmid M., Siermann A.,
Hassam S., Weitz S., Lichter P., Heitz P.U., von Knebel Doeberitz M.,
Briner J.;
"Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence,
genomic organization, localization to chromosomal bands 1p34-p35, and
expression.";
Genomics 61:210-218(1999).
[6]
INTERACTION WITH DICER1.
PubMed=14749716; DOI=10.1038/sj.embor.7400070;
Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W.,
Hobman T.C.;
"Characterization of the interactions between mammalian PAZ PIWI
domain proteins and Dicer.";
EMBO Rep. 5:189-194(2004).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15105377; DOI=10.1101/gad.1187904;
Martinez J., Tuschl T.;
"RISC is a 5' phosphomonoester-producing RNA endonuclease.";
Genes Dev. 18:975-980(2004).
[8]
FUNCTION.
PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G.,
Tuschl T.;
"Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
siRNAs.";
Mol. Cell 15:185-197(2004).
[9]
INTERACTION WITH FMR1.
PubMed=14703574; DOI=10.1038/nn1174;
Jin P., Zarnescu D.C., Ceman S., Nakamoto M., Mowrey J., Jongens T.A.,
Nelson D.L., Moses K., Warren S.T.;
"Biochemical and genetic interaction between the fragile X mental
retardation protein and the microRNA pathway.";
Nat. Neurosci. 7:113-117(2004).
[10]
FUNCTION, AND INTERACTION WITH GEMIN4.
PubMed=15337849; DOI=10.1261/rna.7131604;
Pillai R.S., Artus C.G., Filipowicz W.;
"Tethering of human Ago proteins to mRNA mimics the miRNA-mediated
repression of protein synthesis.";
RNA 10:1518-1525(2004).
[11]
FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LEU-140; ASP-597; GLN-633;
HIS-634; ASP-669; HIS-682; PHE-704 AND THR-744, AND COFACTOR.
PubMed=15284456; DOI=10.1126/science.1102513;
Liu J., Carmell M.A., Rivas F.V., Marsden C.G., Thomson J.M.,
Song J.-J., Hammond S.M., Joshua-Tor L., Hannon G.J.;
"Argonaute2 is the catalytic engine of mammalian RNAi.";
Science 305:1437-1441(2004).
[12]
INTERACTION WITH ZFP36.
PubMed=15766526; DOI=10.1016/j.cell.2004.12.038;
Jing Q., Huang S., Guth S., Zarubin T., Motoyama A., Chen J.,
Di Padova F., Lin S.C., Gram H., Han J.;
"Involvement of microRNA in AU-rich element-mediated mRNA
instability.";
Cell 120:623-634(2005).
[13]
FUNCTION, AND INTERACTION WITH DICER1 AND TARBP2.
PubMed=16271387; DOI=10.1016/j.cell.2005.10.022;
Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.;
"Human RISC couples microRNA biogenesis and posttranscriptional gene
silencing.";
Cell 123:631-640(2005).
[14]
FUNCTION, INTERACTION WITH DDX20; DICER1; GEMIN4; MOV10; PRMT5 AND
TNRC6B, AND SUBCELLULAR LOCATION.
PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H.,
Luehrmann R., Tuschl T.;
"Identification of novel argonaute-associated proteins.";
Curr. Biol. 15:2149-2155(2005).
[15]
FUNCTION.
PubMed=16142218; DOI=10.1038/sj.embor.7400509;
Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
Filipowicz W.;
"TRBP, a regulator of cellular PKR and HIV-1 virus expression,
interacts with Dicer and functions in RNA silencing.";
EMBO Rep. 6:961-967(2005).
[16]
FUNCTION, INTERACTION WITH DICER1 AND TARBP2, AND MUTAGENESIS OF
ASP-669.
PubMed=16357216; DOI=10.1101/gad.1384005;
Maniataki E., Mourelatos Z.;
"A human, ATP-independent, RISC assembly machine fueled by pre-
miRNA.";
Genes Dev. 19:2979-2990(2005).
[17]
MUTAGENESIS OF LYS-533; GLN-545 AND LYS-570.
PubMed=15800629; DOI=10.1038/nature03514;
Ma J.-B., Yuan Y.-R., Meister G., Pei Y., Tuschl T., Patel D.J.;
"Structural basis for 5'-end-specific recognition of guide RNA by the
A. fulgidus Piwi protein.";
Nature 434:666-670(2005).
[18]
INTERACTION WITH DICER1 AND TARBP2.
PubMed=15973356; DOI=10.1038/nature03868;
Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N.,
Nishikura K., Shiekhattar R.;
"TRBP recruits the Dicer complex to Ago2 for microRNA processing and
gene silencing.";
Nature 436:740-744(2005).
[19]
SUBCELLULAR LOCATION.
PubMed=15908945; DOI=10.1038/ncb1265;
Sen G.L., Blau H.M.;
"Argonaute 2/RISC resides in sites of mammalian mRNA decay known as
cytoplasmic bodies.";
Nat. Cell Biol. 7:633-636(2005).
[20]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-597;
ASP-669; GLU-673; GLU-683 AND HIS-807.
PubMed=15800637; DOI=10.1038/nsmb918;
Rivas F.V., Tolia N.H., Song J.-J., Aragon J.P., Liu J., Hannon G.J.,
Joshua-Tor L.;
"Purified Argonaute2 and an siRNA form recombinant human RISC.";
Nat. Struct. Mol. Biol. 12:340-349(2005).
[21]
FUNCTION, INTERACTION WITH DCP1A AND XRN1, AND SUBCELLULAR LOCATION.
PubMed=16081698; DOI=10.1126/science.1115079;
Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
Basyuk E., Bertrand E., Filipowicz W.;
"Inhibition of translational initiation by Let-7 MicroRNA in human
cells.";
Science 309:1573-1576(2005).
[22]
FUNCTION.
PubMed=16936728; DOI=10.1038/nsmb1140;
Janowski B.A., Huffman K.E., Schwartz J.C., Ram R., Nordsell R.,
Shames D.S., Minna J.D., Corey D.R.;
"Involvement of AGO1 and AGO2 in mammalian transcriptional
silencing.";
Nat. Struct. Mol. Biol. 13:787-792(2006).
[23]
FUNCTION, INTERACTION WITH DDX6 AND AGO1, AND SUBCELLULAR LOCATION.
PubMed=16756390; DOI=10.1371/journal.pbio.0040210;
Chu C.-Y., Rana T.M.;
"Translation repression in human cells by microRNA-induced gene
silencing requires RCK/p54.";
PLoS Biol. 4:E210-E210(2006).
[24]
INTERACTION WITH APOBEC3G.
PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
Wichroski M.J., Robb G.B., Rana T.M.;
"Human retroviral host restriction factors APOBEC3G and APOBEC3F
localize to mRNA processing bodies.";
PLoS Pathog. 2:E41-E41(2006).
[25]
FUNCTION, INTERACTION WITH FXR1, AND SUBCELLULAR LOCATION.
PubMed=17382880; DOI=10.1016/j.cell.2007.01.038;
Vasudevan S., Steitz J.A.;
"AU-rich-element-mediated upregulation of translation by FXR1 and
Argonaute 2.";
Cell 128:1105-1118(2007).
[26]
FUNCTION, AND MUTAGENESIS OF PHE-470 AND PHE-505.
PubMed=17524464; DOI=10.1016/j.cell.2007.05.016;
Kiriakidou M., Tan G.S., Lamprinaki S., De Planell-Saguer M.,
Nelson P.T., Mourelatos Z.;
"An mRNA m7G cap binding-like motif within human Ago2 represses
translation.";
Cell 129:1141-1151(2007).
[27]
FUNCTION, ASSOCIATION WITH POLYSOMES AND MNRP, AND INTERACTION WITH
DDB1; DDX5; DHX30; DHX36; DDX47; ELAVL1; HNRNPF; IGF2BP1; ILF3; MATR3;
PABPC1; RBM4; SART3; UPF1 AND YBX1.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[28]
FUNCTION, AND INTERACTION WITH DHX9.
PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016;
Robb G.B., Rana T.M.;
"RNA helicase A interacts with RISC in human cells and functions in
RISC loading.";
Mol. Cell 26:523-537(2007).
[29]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH
DICER1; EIF6; MOV10; RPL7A AND TARBP2, AND ASSOCIATION WITH THE 60S
RIBOSOME.
PubMed=17507929; DOI=10.1038/nature05841;
Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
"MicroRNA silencing through RISC recruitment of eIF6.";
Nature 447:823-828(2007).
[30]
FUNCTION.
PubMed=18048652; DOI=10.1126/science.1149460;
Vasudevan S., Tong Y., Steitz J.A.;
"Switching from repression to activation: microRNAs can up-regulate
translation.";
Science 318:1931-1934(2007).
[31]
FUNCTION, AND MUTAGENESIS OF ASP-597.
PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
Wu L., Fan J., Belasco J.G.;
"Importance of translation and nonnucleolytic ago proteins for on-
target RNA interference.";
Curr. Biol. 18:1327-1332(2008).
[32]
FUNCTION, INTERACTION WITH DICER1; P4HA1; P4HB; TNRC6A AND TNRC6B,
SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-700, AND MUTAGENESIS OF
PRO-700.
PubMed=18690212; DOI=10.1038/nature07186;
Qi H.H., Ongusaha P.P., Myllyharju J., Cheng D., Pakkanen O., Shi Y.,
Lee S.W., Peng J., Shi Y.;
"Prolyl 4-hydroxylation regulates Argonaute 2 stability.";
Nature 455:421-424(2008).
[33]
FUNCTION, AND INTERACTION WITH DICER1 AND TARBP2.
PubMed=18178619; DOI=10.1073/pnas.0710869105;
MacRae I.J., Ma E., Zhou M., Robinson C.V., Doudna J.A.;
"In vitro reconstitution of the human RISC-loading complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:512-517(2008).
[34]
FUNCTION, INTERACTION WITH IMP8, AND SUBCELLULAR LOCATION.
PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
Kremmer E., Benes V., Urlaub H., Meister G.;
"Importin 8 is a gene silencing factor that targets argonaute proteins
to distinct mRNAs.";
Cell 136:496-507(2009).
[35]
INTERACTION WITH RBM4.
PubMed=19801630; DOI=10.1074/jbc.M109.032946;
Lin J.C., Tarn W.Y.;
"RNA-binding motif protein 4 translocates to cytoplasmic granules and
suppresses translation via argonaute2 during muscle cell
differentiation.";
J. Biol. Chem. 284:34658-34665(2009).
[36]
SUBCELLULAR LOCATION, AND INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=20616046; DOI=10.1073/pnas.0914987107;
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
Longmore G.D., Bushell M., Sharp T.V.;
"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for
microRNA-mediated gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
INTERACTION WITH TNRC6C, AND MUTAGENESIS OF PHE-470 AND PHE-505.
PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
"GW182 proteins directly recruit cytoplasmic deadenylase complexes to
miRNA targets.";
Mol. Cell 44:120-133(2011).
[39]
INTERACTION WITH MOV10.
PubMed=22791714; DOI=10.1074/jbc.M112.354001;
Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P.,
Zhang H.;
"APOBEC3G inhibits microRNA-mediated repression of translation by
interfering with the interaction between Argonaute-2 and MOV10.";
J. Biol. Chem. 287:29373-29383(2012).
[40]
SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3A; APOBEC3C;
APOBEC3F; APOBEC3G AND APOBEC3H.
PubMed=22915799; DOI=10.1128/JVI.00595-12;
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
"HIV-1 replication and APOBEC3 antiviral activity are not regulated by
P bodies.";
J. Virol. 86:11712-11724(2012).
[41]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-673; PHE-676 AND
HIS-807.
PubMed=23746446; DOI=10.1016/j.celrep.2013.05.033;
Faehnle C.R., Elkayam E., Haase A.D., Hannon G.J., Joshua-Tor L.;
"The making of a slicer: activation of human Argonaute-1.";
Cell Rep. 3:1901-1909(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-828, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
SUBCELLULAR LOCATION, AND INTERACTION WITH TRIM71.
PubMed=23125361; DOI=10.1093/nar/gks1032;
Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
"The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
function.";
Nucleic Acids Res. 41:518-532(2013).
[44]
X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 439-575 IN COMPLEX WITH AMP;
CMP; GMP AND PHOSPHATE.
PubMed=20505670; DOI=10.1038/nature09039;
Frank F., Sonenberg N., Nagar B.;
"Structural basis for 5'-nucleotide base-specific recognition of guide
RNA by human AGO2.";
Nature 465:818-822(2010).
[45]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 439-575 IN COMPLEX WITH
7-MGTPG AND ATP.
PubMed=21475248; DOI=10.1038/embor.2011.48;
Frank F., Fabian M.R., Stepinski J., Jemielity J., Darzynkiewicz E.,
Sonenberg N., Nagar B.;
"Structural analysis of 5'-mRNA-cap interactions with the human AGO2
MID domain.";
EMBO Rep. 12:415-420(2011).
[46]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH MIRNA-20A, AND
GUIDE RNA-BINDING.
PubMed=22682761; DOI=10.1016/j.cell.2012.05.017;
Elkayam E., Kuhn C.D., Tocilj A., Haase A.D., Greene E.M.,
Hannon G.J., Joshua-Tor L.;
"The structure of human argonaute-2 in complex with miR-20a.";
Cell 150:100-110(2012).
[47]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RNA AND
L-TRYPTOPHAN, AND GUIDE RNA-BINDING.
PubMed=22539551; DOI=10.1126/science.1221551;
Schirle N.T., MacRae I.J.;
"The crystal structure of human Argonaute2.";
Science 336:1037-1040(2012).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the
RNA-induced silencing complex (RISC). The 'minimal RISC' appears
to include AGO2 bound to a short guide RNA such as a microRNA
(miRNA) or short interfering RNA (siRNA). These guide RNAs direct
RISC to complementary mRNAs that are targets for RISC-mediated
gene silencing. The precise mechanism of gene silencing depends on
the degree of complementarity between the miRNA or siRNA and its
target. Binding of RISC to a perfectly complementary mRNA
generally results in silencing due to endonucleolytic cleavage of
the mRNA specifically by AGO2. Binding of RISC to a partially
complementary mRNA results in silencing through inhibition of
translation, and this is independent of endonuclease activity. May
inhibit translation initiation by binding to the 7-methylguanosine
cap, thereby preventing the recruitment of the translation
initiation factor eIF4-E. May also inhibit translation initiation
via interaction with EIF6, which itself binds to the 60S ribosomal
subunit and prevents its association with the 40S ribosomal
subunit. The inhibition of translational initiation leads to the
accumulation of the affected mRNA in cytoplasmic processing bodies
(P-bodies), where mRNA degradation may subsequently occur. In some
cases RISC-mediated translational repression is also observed for
miRNAs that perfectly match the 3' untranslated region (3'-UTR).
Can also up-regulate the translation of specific mRNAs under
certain growth conditions. Binds to the AU element of the 3'-UTR
of the TNF (TNF-alpha) mRNA and up-regulates translation under
conditions of serum starvation. Also required for transcriptional
gene silencing (TGS), in which short RNAs known as antigene RNAs
or agRNAs direct the transcriptional repression of complementary
promoter regions. {ECO:0000255|HAMAP-Rule:MF_03031,
ECO:0000269|PubMed:15105377, ECO:0000269|PubMed:15260970,
ECO:0000269|PubMed:15284456, ECO:0000269|PubMed:15337849,
ECO:0000269|PubMed:15800637, ECO:0000269|PubMed:16081698,
ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216,
ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:16936728,
ECO:0000269|PubMed:17382880, ECO:0000269|PubMed:17507929,
ECO:0000269|PubMed:17524464, ECO:0000269|PubMed:17531811,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18048652,
ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:18690212,
ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:19167051,
ECO:0000269|PubMed:23746446}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_03031,
ECO:0000269|PubMed:15105377, ECO:0000269|PubMed:23746446}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15284456};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15284456};
-!- ENZYME REGULATION: Inhibited by EDTA.
{ECO:0000269|PubMed:15284456}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 nM for a synthetic 21-nucleotide single-stranded RNA
{ECO:0000269|PubMed:15105377, ECO:0000269|PubMed:15800637};
-!- SUBUNIT: Interacts with DICER1 through its Piwi domain and with
TARBP2 during assembly of the RNA-induced silencing complex
(RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric
RISC loading complex (RLC), or micro-RNA (miRNA) loading complex
(miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to
process precursor miRNAs (pre-miRNAs) to mature miRNAs and then
load them onto AGO2. AGO2 bound to the mature miRNA constitutes
the minimal RISC and may subsequently dissociate from DICER1 and
TARBP2. Note however that the term RISC has also been used to
describe the trimeric RLC/miRLC. The formation of RISC complexes
containing siRNAs rather than miRNAs appears to occur
independently of DICER1. Interacts with AGO1. Also interacts with
DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, ELAVL, FXR1,
GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5, P4HA1,
P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with
the P-body components DCP1A and XRN1. Associates with polysomes
and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the
interaction is modulated under stress-induced conditions, occurs
under both cell proliferation and differentiation conditions and
in an RNA- and phosphorylation-independent manner. Interacts with
LIMD1, WTIP and AJUBA. Interacts with TRIM71; the interaction
increases in presence of RNA (PubMed:23125361). Interacts with
APOBEC3G in an RNA-dependent manner. Interacts with APOBEC3A,
APOBEC3C, APOBEC3F and APOBEC3H. Interacts with DICER1, TARBP2,
EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large
RNA-induced silencing complex (RISC) (PubMed:17507929). Interacts
with FMR1 (PubMed:14703574). Interacts with ZFP36
(PubMed:15766526). {ECO:0000255|HAMAP-Rule:MF_03031,
ECO:0000269|PubMed:14703574, ECO:0000269|PubMed:14749716,
ECO:0000269|PubMed:15337849, ECO:0000269|PubMed:15766526,
ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16081698,
ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642,
ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16699599,
ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:17382880,
ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:17531811,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18178619,
ECO:0000269|PubMed:18690212, ECO:0000269|PubMed:19167051,
ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:20505670,
ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21475248,
ECO:0000269|PubMed:21981923, ECO:0000269|PubMed:22539551,
ECO:0000269|PubMed:22682761, ECO:0000269|PubMed:22791714,
ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23125361}.
-!- INTERACTION:
Q9UL18:AGO1; NbExp=3; IntAct=EBI-528269, EBI-527363;
Q9UIV1:CNOT7; NbExp=2; IntAct=EBI-528269, EBI-2105113;
P26196:DDX6; NbExp=4; IntAct=EBI-528269, EBI-351257;
Q96C10:DHX58; NbExp=2; IntAct=EBI-528269, EBI-744193;
Q9UPY3:DICER1; NbExp=19; IntAct=EBI-528269, EBI-395506;
Q9UPY3-1:DICER1; NbExp=14; IntAct=EBI-528269, EBI-15569571;
P00533:EGFR; NbExp=11; IntAct=EBI-528269, EBI-297353;
Q13541:EIF4EBP1; NbExp=2; IntAct=EBI-528269, EBI-74090;
Q02790:FKBP4; NbExp=2; IntAct=EBI-528269, EBI-1047444;
Q9BVP2:GNL3; NbExp=3; IntAct=EBI-528269, EBI-641642;
O15397:IPO8; NbExp=4; IntAct=EBI-528269, EBI-358808;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-528269, EBI-5323863;
Q86UE4:MTDH; NbExp=3; IntAct=EBI-528269, EBI-1046588;
Q6IQ23:PLEKHA7; NbExp=7; IntAct=EBI-528269, EBI-2125301;
O75569:PRKRA; NbExp=5; IntAct=EBI-528269, EBI-713955;
P04156:PRNP; NbExp=4; IntAct=EBI-528269, EBI-977302;
Q15185:PTGES3; NbExp=3; IntAct=EBI-528269, EBI-1049387;
P63244:RACK1; NbExp=2; IntAct=EBI-528269, EBI-296739;
P06400:RB1; NbExp=3; IntAct=EBI-528269, EBI-491274;
Q15633:TARBP2; NbExp=12; IntAct=EBI-528269, EBI-978581;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-528269, EBI-356402;
A7MCY6:TBKBP1; NbExp=2; IntAct=EBI-528269, EBI-359969;
Q8NDV7:TNRC6A; NbExp=16; IntAct=EBI-528269, EBI-2269715;
Q9UPQ9:TNRC6B; NbExp=13; IntAct=EBI-528269, EBI-947158;
Q9UPQ9-2:TNRC6B; NbExp=4; IntAct=EBI-528269, EBI-6514011;
Q9HCJ0:TNRC6C; NbExp=4; IntAct=EBI-528269, EBI-6507625;
Q9HA38:ZMAT3; NbExp=5; IntAct=EBI-528269, EBI-2548480;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:23125361}. Nucleus
{ECO:0000269|PubMed:23125361}. Note=Translational repression of
mRNAs results in their recruitment to P-bodies. Translocation to
the nucleus requires IMP8.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UKV8-1; Sequence=Displayed;
Name=2;
IsoId=Q9UKV8-2; Sequence=VSP_037001;
Note=No experimental confirmation available.;
-!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism
similar to that of RNase H. However, while RNase H utilizes a
triad of Asp-Asp-Glu (DDE) for metal ion coordination, this
protein appears to utilize a triad of Asp-Asp-His (DDH).
-!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein
stability but is not required for miRNA-binding or endonuclease
activity. {ECO:0000255|HAMAP-Rule:MF_03031,
ECO:0000269|PubMed:18690212}.
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03031}.
-!- SEQUENCE CAUTION:
Sequence=AAH07633.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL76093.1; Type=Miscellaneous discrepancy; Note=cDNA contains a duplication of an internal sequence at the 5' end.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC067931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007633; AAH07633.1; ALT_INIT; mRNA.
EMBL; BC018727; AAH18727.2; -; mRNA.
EMBL; BC125214; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY077717; AAL76093.1; ALT_SEQ; mRNA.
EMBL; BT007229; AAP35893.1; -; mRNA.
EMBL; AF121255; AAF13034.2; -; mRNA.
CCDS; CCDS55279.1; -. [Q9UKV8-2]
CCDS; CCDS6380.1; -. [Q9UKV8-1]
RefSeq; NP_001158095.1; NM_001164623.2. [Q9UKV8-2]
RefSeq; NP_036286.2; NM_012154.4. [Q9UKV8-1]
UniGene; Hs.660189; -.
UniGene; Hs.743313; -.
PDB; 3LUC; X-ray; 1.69 A; A/B/C=439-575.
PDB; 3LUD; X-ray; 2.10 A; A/B/C=439-575.
PDB; 3LUG; X-ray; 1.85 A; A/B/C=439-575.
PDB; 3LUH; X-ray; 2.00 A; A/B/C=439-575.
PDB; 3LUJ; X-ray; 1.80 A; A/B/C=439-575.
PDB; 3LUK; X-ray; 1.70 A; A/B/C=439-575.
PDB; 3QX8; X-ray; 2.30 A; A/B/C=439-575.
PDB; 3QX9; X-ray; 2.00 A; A/B/C=439-575.
PDB; 4F3T; X-ray; 2.25 A; A=1-859.
PDB; 4OLA; X-ray; 2.30 A; A=1-859.
PDB; 4OLB; X-ray; 2.90 A; A=1-859.
PDB; 4W5N; X-ray; 2.90 A; A=1-859.
PDB; 4W5O; X-ray; 1.80 A; A=1-859.
PDB; 4W5Q; X-ray; 3.10 A; A=1-859.
PDB; 4W5R; X-ray; 2.50 A; A=1-859.
PDB; 4W5T; X-ray; 2.50 A; A=1-859.
PDB; 4Z4C; X-ray; 2.30 A; A=1-859.
PDB; 4Z4D; X-ray; 1.60 A; A=1-859.
PDB; 4Z4E; X-ray; 1.80 A; A=1-859.
PDB; 4Z4F; X-ray; 2.80 A; A=1-859.
PDB; 4Z4G; X-ray; 2.70 A; A=1-859.
PDB; 4Z4H; X-ray; 2.50 A; A=1-859.
PDB; 4Z4I; X-ray; 2.80 A; A=1-859.
PDB; 5JS1; X-ray; 2.50 A; A=1-859.
PDB; 5JS2; X-ray; 2.95 A; A=1-859.
PDB; 5KI6; X-ray; 2.15 A; A=1-859.
PDB; 5T7B; X-ray; 2.53 A; A=1-859.
PDBsum; 3LUC; -.
PDBsum; 3LUD; -.
PDBsum; 3LUG; -.
PDBsum; 3LUH; -.
PDBsum; 3LUJ; -.
PDBsum; 3LUK; -.
PDBsum; 3QX8; -.
PDBsum; 3QX9; -.
PDBsum; 4F3T; -.
PDBsum; 4OLA; -.
PDBsum; 4OLB; -.
PDBsum; 4W5N; -.
PDBsum; 4W5O; -.
PDBsum; 4W5Q; -.
PDBsum; 4W5R; -.
PDBsum; 4W5T; -.
PDBsum; 4Z4C; -.
PDBsum; 4Z4D; -.
PDBsum; 4Z4E; -.
PDBsum; 4Z4F; -.
PDBsum; 4Z4G; -.
PDBsum; 4Z4H; -.
PDBsum; 4Z4I; -.
PDBsum; 5JS1; -.
PDBsum; 5JS2; -.
PDBsum; 5KI6; -.
PDBsum; 5T7B; -.
DisProt; DP00736; -.
ProteinModelPortal; Q9UKV8; -.
SMR; Q9UKV8; -.
BioGrid; 118041; 97.
CORUM; Q9UKV8; -.
DIP; DIP-29194N; -.
IntAct; Q9UKV8; 195.
MINT; MINT-1957975; -.
STRING; 9606.ENSP00000220592; -.
iPTMnet; Q9UKV8; -.
PhosphoSitePlus; Q9UKV8; -.
SwissPalm; Q9UKV8; -.
BioMuta; AGO2; -.
DMDM; 229463006; -.
EPD; Q9UKV8; -.
PaxDb; Q9UKV8; -.
PeptideAtlas; Q9UKV8; -.
PRIDE; Q9UKV8; -.
DNASU; 27161; -.
Ensembl; ENST00000220592; ENSP00000220592; ENSG00000123908. [Q9UKV8-1]
Ensembl; ENST00000519980; ENSP00000430176; ENSG00000123908. [Q9UKV8-2]
GeneID; 27161; -.
KEGG; hsa:27161; -.
UCSC; uc003yvm.5; human. [Q9UKV8-1]
CTD; 27161; -.
DisGeNET; 27161; -.
EuPathDB; HostDB:ENSG00000123908.11; -.
GeneCards; AGO2; -.
HGNC; HGNC:3263; AGO2.
HPA; CAB019309; -.
HPA; HPA058075; -.
MIM; 606229; gene.
neXtProt; NX_Q9UKV8; -.
OpenTargets; ENSG00000123908; -.
PharmGKB; PA27694; -.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
InParanoid; Q9UKV8; -.
KO; K11593; -.
OMA; SPDGYYH; -.
OrthoDB; EOG091G020J; -.
PhylomeDB; Q9UKV8; -.
TreeFam; TF101510; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
SIGNOR; Q9UKV8; -.
EvolutionaryTrace; Q9UKV8; -.
GeneWiki; EIF2C2; -.
GenomeRNAi; 27161; -.
PRO; PR:Q9UKV8; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000123908; -.
CleanEx; HS_EIF2C2; -.
ExpressionAtlas; Q9UKV8; baseline and differential.
Genevisible; Q9UKV8; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IC:BHF-UCL.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IMP:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0004521; F:endoribonuclease activity; IDA:BHF-UCL.
GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; IDA:BHF-UCL.
GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
GO; GO:0098808; F:mRNA cap binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:BHF-UCL.
GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; NAS:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0090625; P:mRNA cleavage involved in gene silencing by siRNA; IDA:BHF-UCL.
GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:1905618; P:positive regulation of miRNA mediated inhibition of translation; IDA:ParkinsonsUK-UCL.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0030422; P:production of siRNA involved in RNA interference; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006412; P:translation; NAS:UniProtKB.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03031; AGO2; 1.
InterPro; IPR028602; AGO2.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Endonuclease; Hydrolase; Hydroxylation; Magnesium; Manganese;
Metal-binding; Nitration; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Transcription; Transcription regulation;
Translation regulation.
CHAIN 1 859 Protein argonaute-2.
/FTId=PRO_0000194057.
DOMAIN 235 348 PAZ. {ECO:0000255|HAMAP-Rule:MF_03031}.
DOMAIN 517 818 Piwi. {ECO:0000255|HAMAP-Rule:MF_03031}.
REGION 311 316 Interaction with guide RNA.
REGION 524 566 Interaction with guide RNA.
REGION 587 590 Interaction with GW182 family members.
{ECO:0000255}.
REGION 650 660 Interaction with GW182 family members.
{ECO:0000255}.
REGION 709 710 Interaction with guide RNA.
REGION 753 761 Interaction with guide RNA.
REGION 790 812 Interaction with guide RNA.
METAL 597 597 Divalent metal cation. {ECO:0000305}.
METAL 669 669 Divalent metal cation. {ECO:0000305}.
METAL 807 807 Divalent metal cation. {ECO:0000305}.
MOD_RES 2 2 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q8CJG0,
ECO:0000255|HAMAP-Rule:MF_03031}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 700 700 4-hydroxyproline. {ECO:0000255|HAMAP-
Rule:MF_03031,
ECO:0000269|PubMed:18690212}.
MOD_RES 828 828 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 724 757 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037001.
MUTAGEN 140 140 L->W: No effect.
{ECO:0000269|PubMed:15284456}.
MUTAGEN 470 470 F->V: No effect on miRNA-binding or
target mRNA cleavage. Abrogates binding
to the 7-methylguanosine cap of mRNA and
prevents inhibition of translation.
Abolishes interaction with TNRC6C; when
associated with V-505.
{ECO:0000269|PubMed:17524464,
ECO:0000269|PubMed:21981923}.
MUTAGEN 470 470 F->W: No effect on binding to the 7-
methylguanosine cap of mRNA or inhibition
of translation.
{ECO:0000269|PubMed:17524464,
ECO:0000269|PubMed:21981923}.
MUTAGEN 505 505 F->V: No effect on miRNA-binding or
target mRNA cleavage. Abrogates binding
to the 7-methylguanosine cap of mRNA and
prevents inhibition of translation and
abolishes interaction with TNRC6C; when
associated with V-470.
{ECO:0000269|PubMed:17524464,
ECO:0000269|PubMed:21981923}.
MUTAGEN 505 505 F->W: No effect on binding to the 7-
methylguanosine cap of mRNA or inhibition
of translation.
{ECO:0000269|PubMed:17524464,
ECO:0000269|PubMed:21981923}.
MUTAGEN 533 533 K->A: Impairs RNA cleavage.
{ECO:0000269|PubMed:15800629}.
MUTAGEN 545 545 Q->A: Impairs RNA cleavage.
{ECO:0000269|PubMed:15800629}.
MUTAGEN 570 570 K->A: Impairs RNA cleavage.
{ECO:0000269|PubMed:15800629}.
MUTAGEN 597 597 D->A: Abrogates RNA cleavage but does not
affect binding to siRNA or translational
repression. {ECO:0000269|PubMed:15284456,
ECO:0000269|PubMed:15800637,
ECO:0000269|PubMed:18771919}.
MUTAGEN 633 633 Q->A: No effect.
{ECO:0000269|PubMed:15284456}.
MUTAGEN 633 633 Q->R: Abrogates RNA cleavage. Binds
siRNA. {ECO:0000269|PubMed:15284456}.
MUTAGEN 634 634 H->P,A: Abrogates RNA cleavage. Binds
siRNA. {ECO:0000269|PubMed:15284456}.
MUTAGEN 669 669 D->A: Abrogates RNA cleavage but does not
affect binding to siRNA.
{ECO:0000269|PubMed:15284456,
ECO:0000269|PubMed:15800637,
ECO:0000269|PubMed:16357216}.
MUTAGEN 673 673 E->A: Impairs RNA cleavage.
{ECO:0000269|PubMed:15800637,
ECO:0000269|PubMed:23746446}.
MUTAGEN 673 673 E->G: No effect on RNA cleavage.
{ECO:0000269|PubMed:15800637,
ECO:0000269|PubMed:23746446}.
MUTAGEN 676 676 F->A,I,M,R,Y: Impairs RNA cleavage.
{ECO:0000269|PubMed:23746446}.
MUTAGEN 676 676 F->V: Abrogates RNA cleavage.
{ECO:0000269|PubMed:23746446}.
MUTAGEN 682 682 H->Y: No effect.
{ECO:0000269|PubMed:15284456}.
MUTAGEN 683 683 E->G: No effect on RNA cleavage.
{ECO:0000269|PubMed:15800637}.
MUTAGEN 700 700 P->A: Reduced protein stability.
{ECO:0000269|PubMed:18690212}.
MUTAGEN 704 704 F->Y: No effect.
{ECO:0000269|PubMed:15284456}.
MUTAGEN 744 744 T->Y: No effect.
{ECO:0000269|PubMed:15284456}.
MUTAGEN 807 807 H->A,R: Abrogates RNA cleavage.
{ECO:0000269|PubMed:15800637,
ECO:0000269|PubMed:23746446}.
CONFLICT 564 564 C -> W (in Ref. 5; AAF13034).
{ECO:0000305}.
CONFLICT 589 589 Q -> E (in Ref. 5; AAF13034).
{ECO:0000305}.
CONFLICT 617 617 S -> R (in Ref. 5; AAF13034).
{ECO:0000305}.
CONFLICT 637 637 E -> K (in Ref. 3; AAL76093).
{ECO:0000305}.
STRAND 35 48 {ECO:0000244|PDB:4Z4D}.
STRAND 53 63 {ECO:0000244|PDB:4Z4D}.
HELIX 68 81 {ECO:0000244|PDB:4Z4D}.
TURN 82 86 {ECO:0000244|PDB:4Z4D}.
STRAND 96 104 {ECO:0000244|PDB:4Z4D}.
TURN 107 110 {ECO:0000244|PDB:4Z4D}.
STRAND 113 117 {ECO:0000244|PDB:4Z4D}.
STRAND 122 124 {ECO:0000244|PDB:4W5N}.
STRAND 128 139 {ECO:0000244|PDB:4Z4D}.
HELIX 140 147 {ECO:0000244|PDB:4Z4D}.
STRAND 150 153 {ECO:0000244|PDB:4Z4D}.
HELIX 156 167 {ECO:0000244|PDB:4Z4D}.
HELIX 170 173 {ECO:0000244|PDB:4Z4D}.
STRAND 174 177 {ECO:0000244|PDB:4Z4D}.
STRAND 180 183 {ECO:0000244|PDB:4Z4D}.
STRAND 191 193 {ECO:0000244|PDB:4Z4D}.
STRAND 196 207 {ECO:0000244|PDB:4Z4D}.
STRAND 210 225 {ECO:0000244|PDB:4Z4D}.
HELIX 230 238 {ECO:0000244|PDB:4Z4D}.
HELIX 243 245 {ECO:0000244|PDB:4Z4D}.
HELIX 252 262 {ECO:0000244|PDB:4Z4D}.
STRAND 266 268 {ECO:0000244|PDB:4Z4D}.
STRAND 278 288 {ECO:0000244|PDB:4Z4D}.
TURN 289 291 {ECO:0000244|PDB:4Z4D}.
STRAND 293 297 {ECO:0000244|PDB:5KI6}.
STRAND 299 301 {ECO:0000244|PDB:4F3T}.
STRAND 303 307 {ECO:0000244|PDB:5KI6}.
HELIX 308 316 {ECO:0000244|PDB:4Z4D}.
STRAND 325 331 {ECO:0000244|PDB:4Z4D}.
TURN 333 336 {ECO:0000244|PDB:4F3T}.
STRAND 337 340 {ECO:0000244|PDB:4Z4D}.
HELIX 341 343 {ECO:0000244|PDB:4Z4D}.
STRAND 344 346 {ECO:0000244|PDB:5KI6}.
STRAND 348 351 {ECO:0000244|PDB:4OLB}.
HELIX 358 368 {ECO:0000244|PDB:4Z4D}.
HELIX 372 386 {ECO:0000244|PDB:4Z4D}.
HELIX 388 390 {ECO:0000244|PDB:4Z4D}.
HELIX 392 396 {ECO:0000244|PDB:4Z4D}.
STRAND 406 412 {ECO:0000244|PDB:4Z4D}.
TURN 422 425 {ECO:0000244|PDB:4Z4D}.
STRAND 450 455 {ECO:0000244|PDB:4Z4D}.
TURN 459 461 {ECO:0000244|PDB:4Z4D}.
HELIX 464 480 {ECO:0000244|PDB:4Z4D}.
STRAND 490 494 {ECO:0000244|PDB:4Z4D}.
HELIX 498 500 {ECO:0000244|PDB:4Z4D}.
HELIX 501 511 {ECO:0000244|PDB:4Z4D}.
STRAND 517 522 {ECO:0000244|PDB:4Z4D}.
HELIX 528 537 {ECO:0000244|PDB:4Z4D}.
TURN 538 540 {ECO:0000244|PDB:4Z4D}.
STRAND 544 548 {ECO:0000244|PDB:4Z4D}.
HELIX 550 553 {ECO:0000244|PDB:4Z4D}.
HELIX 557 570 {ECO:0000244|PDB:4Z4D}.
HELIX 580 582 {ECO:0000244|PDB:4Z4D}.
HELIX 585 588 {ECO:0000244|PDB:4Z4D}.
STRAND 591 599 {ECO:0000244|PDB:4Z4D}.
TURN 603 605 {ECO:0000244|PDB:5KI6}.
STRAND 610 617 {ECO:0000244|PDB:4Z4D}.
STRAND 619 622 {ECO:0000244|PDB:4Z4D}.
STRAND 625 633 {ECO:0000244|PDB:4Z4D}.
HELIX 642 657 {ECO:0000244|PDB:4Z4D}.
STRAND 662 669 {ECO:0000244|PDB:4Z4D}.
HELIX 673 675 {ECO:0000244|PDB:4Z4D}.
HELIX 676 694 {ECO:0000244|PDB:4Z4D}.
STRAND 701 709 {ECO:0000244|PDB:4Z4D}.
STRAND 710 712 {ECO:0000244|PDB:4W5Q}.
STRAND 715 719 {ECO:0000244|PDB:4Z4D}.
HELIX 720 722 {ECO:0000244|PDB:4Z4D}.
TURN 725 728 {ECO:0000244|PDB:4Z4D}.
STRAND 734 736 {ECO:0000244|PDB:4Z4D}.
STRAND 738 741 {ECO:0000244|PDB:4Z4D}.
STRAND 743 745 {ECO:0000244|PDB:4Z4D}.
STRAND 747 751 {ECO:0000244|PDB:4Z4D}.
STRAND 757 759 {ECO:0000244|PDB:5JS1}.
STRAND 763 770 {ECO:0000244|PDB:4Z4D}.
HELIX 776 786 {ECO:0000244|PDB:4Z4D}.
STRAND 793 795 {ECO:0000244|PDB:5KI6}.
HELIX 801 816 {ECO:0000244|PDB:4Z4D}.
TURN 817 820 {ECO:0000244|PDB:4Z4D}.
HELIX 837 846 {ECO:0000244|PDB:4Z4D}.
TURN 850 854 {ECO:0000244|PDB:4Z4D}.
SEQUENCE 859 AA; 97208 MW; 5C8552C43FC81345 CRC64;
MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP KIDIYHYELD
IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL YTAMPLPIGR DKVELEVTLP
GEGKDRIFKV SIKWVSCVSL QALHDALSGR LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS
FFTASEGCSN PLGGGREVWF GFHQSVRPSL WKMMLNIDVS ATAFYKAQPV IEFVCEVLDF
KSIEEQQKPL TDSQRVKFTK EIKGLKVEIT HCGQMKRKYR VCNVTRRPAS HQTFPLQQES
GQTVECTVAQ YFKDRHKLVL RYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ
TSTMIRATAR SAPDRQEEIS KLMRSASFNT DPYVREFGIM VKDEMTDVTG RVLQPPSILY
GGRNKAIATP VQGVWDMRNK QFHTGIEIKV WAIACFAPQR QCTEVHLKSF TEQLRKISRD
AGMPIQGQPC FCKYAQGADS VEPMFRHLKN TYAGLQLVVV ILPGKTPVYA EVKRVGDTVL
GMATQCVQMK NVQRTTPQTL SNLCLKINVK LGGVNNILLP QGRPPVFQQP VIFLGADVTH
PPAGDGKKPS IAAVVGSMDA HPNRYCATVR VQQHRQEIIQ DLAAMVRELL IQFYKSTRFK
PTRIIFYRDG VSEGQFQQVL HHELLAIREA CIKLEKDYQP GITFIVVQKR HHTRLFCTDK
NERVGKSGNI PAGTTVDTKI THPTEFDFYL CSHAGIQGTS RPSHYHVLWD DNRFSSDELQ
ILTYQLCHTY VRCTRSVSIP APAYYAHLVA FRARYHLVDK EHDSAEGSHT SGQSNGRDHQ
ALAKAVQVHQ DTLRTMYFA


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