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Trinucleotide repeat-containing gene 6A protein (CAG repeat protein 26) (EMSY interactor protein) (GW182 autoantigen) (Protein GW1) (Glycine-tryptophan protein of 182 kDa)

 TNR6A_HUMAN             Reviewed;        1962 AA.
Q8NDV7; C9JAR8; O15408; Q658L5; Q6NVB5; Q8NEZ0; Q8TBT8; Q8TCR0;
Q9NV59; Q9P268;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
25-OCT-2017, entry version 158.
RecName: Full=Trinucleotide repeat-containing gene 6A protein;
AltName: Full=CAG repeat protein 26;
AltName: Full=EMSY interactor protein;
AltName: Full=GW182 autoantigen;
Short=Protein GW1;
AltName: Full=Glycine-tryptophan protein of 182 kDa;
Name=TNRC6A; Synonyms=CAGH26, KIAA1460, TNRC6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), RNA-BINDING, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
TISSUE=Cervix carcinoma;
PubMed=11950943; DOI=10.1091/mbc.01-11-0544;
Eystathioy T., Chan E.K.L., Tenenbaum S.A., Keene J.D., Griffith K.,
Fritzler M.J.;
"A phosphorylated cytoplasmic autoantigen, GW182, associates with a
unique population of human mRNAs within novel cytoplasmic speckles.";
Mol. Biol. Cell 13:1338-1351(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hughes-Davies L.;
"Candidate EMSY interactor protein.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 861-1962 (ISOFORM 6).
TISSUE=Kidney, and Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1515-1962.
TISSUE=Kidney, and PNS;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-157 (ISOFORM 5).
TISSUE=Brain;
PubMed=9225980; DOI=10.1007/s004390050476;
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
"cDNAs with long CAG trinucleotide repeats from human brain.";
Hum. Genet. 100:114-122(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1962.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-1962.
TISSUE=Ovarian carcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
AUTOANTIGENIC EPITOPE MAPPING.
PubMed=14598044; DOI=10.1007/s00109-003-0495-y;
Eystathioy T., Chan E.K.L., Takeuchi K., Mahler M., Luft L.M.,
Zochodne D.W., Fritzler M.J.;
"Clinical and serological associations of autoantibodies to GW bodies
and a novel cytoplasmic autoantigen GW182.";
J. Mol. Med. 81:811-818(2003).
[10]
SUBCELLULAR LOCATION.
PubMed=13130130; DOI=10.1261/rna.5810203;
Eystathioy T., Jakymiw A., Chan E.K.L., Seraphin B., Cougot N.,
Fritzler M.J.;
"The GW182 protein colocalizes with mRNA degradation associated
proteins hDcp1 and hLSm4 in cytoplasmic GW bodies.";
RNA 9:1171-1173(2003).
[11]
SUBCELLULAR LOCATION.
PubMed=15494374; DOI=10.1242/jcs.01477;
Yang Z., Jakymiw A., Wood M.R., Eystathioy T., Rubin R.L.,
Fritzler M.J., Chan E.K.L.;
"GW182 is critical for the stability of GW bodies expressed during the
cell cycle and cell proliferation.";
J. Cell Sci. 117:5567-5578(2004).
[12]
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).
[13]
FUNCTION, INTERACTION WITH AGO2, AND SUBCELLULAR LOCATION.
PubMed=16284623; DOI=10.1038/ncb1333;
Liu J., Rivas F.V., Wohlschlegel J., Yates J.R. III, Parker R.,
Hannon G.J.;
"A role for the P-body component GW182 in microRNA function.";
Nat. Cell Biol. 7:1261-1266(2005).
[14]
FUNCTION, INTERACTION WITH AGO2, ASSOCIATION WITH SIRNA, AND
SUBCELLULAR LOCATION.
PubMed=16284622; DOI=10.1038/ncb1334;
Jakymiw A., Lian S.L., Eystathioy T., Li S., Satoh M., Hamel J.C.,
Fritzler M.J., Chan E.K.L.;
"Disruption of GW bodies impairs mammalian RNA interference.";
Nat. Cell Biol. 7:1267-1274(2005).
[15]
ERRATUM.
Jakymiw A., Lian S.L., Eystathioy T., Li S., Satoh M., Hamel J.C.,
Fritzler M.J., Chan E.K.L.;
Nat. Cell Biol. 8:100-100(2006).
[16]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICRORNA.
PubMed=16906129; DOI=10.1038/sj.embor.7400783;
Pauley K.M., Eystathioy T., Jakymiw A., Hamel J.C., Fritzler M.J.,
Chan E.K.L.;
"Formation of GW bodies is a consequence of microRNA genesis.";
EMBO Rep. 7:904-910(2006).
[17]
FUNCTION.
PubMed=17671087; DOI=10.1101/gad.1566707;
Wakiyama M., Takimoto K., Ohara O., Yokoyama S.;
"Let-7 microRNA-mediated mRNA deadenylation and translational
repression in a mammalian cell-free system.";
Genes Dev. 21:1857-1862(2007).
[18]
ERRATUM.
Wakiyama M., Takimoto K., Ohara O., Yokoyama S.;
Genes Dev. 21:2509-2509(2007).
[19]
FUNCTION.
PubMed=17596515; DOI=10.1091/mbc.E07-01-0070;
Lian S.L., Fritzler M.J., Katz J., Hamazaki T., Terada N., Satoh M.,
Chan E.K.L.;
"Small interfering RNA-mediated silencing induces target-dependent
assembly of GW/P bodies.";
Mol. Biol. Cell 18:3375-3387(2007).
[20]
ERRATUM.
Lian S.L., Fritzler M.J., Katz J., Hamazaki T., Terada N., Satoh M.,
Chan E.K.L.;
Mol. Biol. Cell 18:4200-4200(2007).
[21]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19056672; DOI=10.1242/jcs.036905;
Li S., Lian S.L., Moser J.J., Fritzler M.L., Fritzler M.J., Satoh M.,
Chan E.K.L.;
"Identification of GW182 and its novel isoform TNGW1 as translational
repressors in Ago2-mediated silencing.";
J. Cell Sci. 121:4134-4144(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH AGO2.
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1470, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18946079; DOI=10.1091/mbc.E08-08-0796;
Jagannath A., Wood M.J.A.;
"Localization of double-stranded small interfering RNA to cytoplasmic
processing bodies is Ago2 dependent and results in up-regulation of
GW182 and Argonaute-2.";
Mol. Biol. Cell 20:521-529(2009).
[25]
FUNCTION, AND INTERACTION WITH AGO2.
PubMed=19304925; DOI=10.1261/rna.1448009;
Zipprich J.T., Bhattacharyya S., Mathys H., Filipowicz W.;
"Importance of the C-terminal domain of the human GW182 protein TNRC6C
for translational repression.";
RNA 15:781-793(2009).
[26]
INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF TRP-313; TRP-345; TRP-370; TRP-420 AND TRP-483.
PubMed=19324964; DOI=10.1261/rna.1229409;
Lian S.L., Li S., Abadal G.X., Pauley B.A., Fritzler M.J.,
Chan E.K.L.;
"The C-terminal half of human Ago2 binds to multiple GW-rich regions
of GW182 and requires GW182 to mediate silencing.";
RNA 15:804-813(2009).
[27]
INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4.
PubMed=19383768; DOI=10.1261/rna.1606309;
Lazzaretti D., Tournier I., Izaurralde E.;
"The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence
bound transcripts independently of Argonaute proteins.";
RNA 15:1059-1066(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1869, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
INTERACTION WITH CNOT1.
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-878; SER-991;
SER-1212; SER-1270 AND SER-1890, 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).
[32]
INTERACTION WITH ZC3H12A.
PubMed=26134560; DOI=10.1074/jbc.M114.635870;
Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G.,
Fu M.;
"Monocyte chemotactic protein-induced protein 1 and 4 form a complex
but act independently in regulation of interleukin-6 mRNA
degradation.";
J. Biol. Chem. 290:20782-20792(2015).
-!- FUNCTION: Plays a role in RNA-mediated gene silencing by both
micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required
for miRNA-dependent repression of translation and for siRNA-
dependent endonucleolytic cleavage of complementary mRNAs by
argonaute family proteins. As scaffoldng protein associates with
argonaute proteins bound to partially complementary mRNAs and
simultaneously can recruit CCR4-NOT and PAN deadenylase complexes.
{ECO:0000269|PubMed:16284622, ECO:0000269|PubMed:16284623,
ECO:0000269|PubMed:17596515, ECO:0000269|PubMed:17671087,
ECO:0000269|PubMed:19056672, ECO:0000269|PubMed:19304925}.
-!- SUBUNIT: Interacts with AGO2 (PubMed:16284623, PubMed:16284622,
PubMed:18690212, PubMed:19304925, PubMed:19324964,
PubMed:19383768). Interacts with AGO1, AGO3 and AGO4
(PubMed:19324964, PubMed:19383768). Interacts with CNOT1; the
interaction is direct and mediates the association with the CCR4-
NOT complex (PubMed:21981923). Interacts with ZC3H12A
(PubMed:26134560). {ECO:0000269|PubMed:16284622,
ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:18690212,
ECO:0000269|PubMed:19304925, ECO:0000269|PubMed:19324964,
ECO:0000269|PubMed:19383768, ECO:0000269|PubMed:21981923,
ECO:0000269|PubMed:26134560}.
-!- INTERACTION:
Q9UL18:AGO1; NbExp=5; IntAct=EBI-2269715, EBI-527363;
Q9UKV8:AGO2; NbExp=16; IntAct=EBI-2269715, EBI-528269;
Q9H9G7:AGO3; NbExp=3; IntAct=EBI-2269715, EBI-2267883;
Q9HCK5:AGO4; NbExp=4; IntAct=EBI-2269715, EBI-2269696;
A5YKK6:CNOT1; NbExp=2; IntAct=EBI-2269715, EBI-1222758;
O75603:GCM2; NbExp=4; IntAct=EBI-12822025, EBI-10188645;
P11940:PABPC1; NbExp=3; IntAct=EBI-2269715, EBI-81531;
Q58A45:PAN3; NbExp=2; IntAct=EBI-2269715, EBI-2513054;
Q9BXF9:TEKT3; NbExp=4; IntAct=EBI-12822025, EBI-8644516;
Q15645:TRIP13; NbExp=3; IntAct=EBI-2269715, EBI-358993;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:11950943, ECO:0000269|PubMed:13130130,
ECO:0000269|PubMed:15494374, ECO:0000269|PubMed:15908945,
ECO:0000269|PubMed:16284622, ECO:0000269|PubMed:16284623,
ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:18946079,
ECO:0000269|PubMed:19056672, ECO:0000269|PubMed:19324964}.
Note=Mammalian P-bodies are also known as GW bodies (GWBs).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=TNGW1;
IsoId=Q8NDV7-1; Sequence=Displayed;
Name=2;
IsoId=Q8NDV7-2; Sequence=VSP_013294;
Name=3;
IsoId=Q8NDV7-3; Sequence=VSP_037287, VSP_037288, VSP_037289;
Name=4;
IsoId=Q8NDV7-4; Sequence=VSP_013292;
Name=5;
IsoId=Q8NDV7-5; Sequence=VSP_013295;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q8NDV7-6; Sequence=VSP_037288;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11950943}.
-!- INDUCTION: By exogenous short interfering RNA (siRNA).
{ECO:0000269|PubMed:18946079}.
-!- MISCELLANEOUS: Antibodies against TNRC6A are found in sera from
patients with Sjoegren syndrome (SS), ataxia and sensor neuropathy
diseases that developed autoantibodies against protein of the GWB
structure. Autoantibodies were mapped to the GW-rich mid-part, the
non-GW-rich region and the C-terminus of the protein.
-!- SIMILARITY: Belongs to the GW182 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91899.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD28525.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY035864; AAK62026.1; -; mRNA.
EMBL; AJ492221; CAD37348.1; -; mRNA.
EMBL; AL713750; CAD28525.2; ALT_INIT; mRNA.
EMBL; AL833757; CAH56236.1; -; mRNA.
EMBL; AC002565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC024324; AAH24324.2; -; mRNA.
EMBL; BC068209; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U80739; AAB91438.1; -; mRNA.
EMBL; AB040893; BAA95984.1; -; mRNA.
EMBL; AK001773; BAA91899.1; ALT_INIT; mRNA.
CCDS; CCDS10624.2; -. [Q8NDV7-1]
CCDS; CCDS81959.1; -. [Q8NDV7-6]
RefSeq; NP_001317449.1; NM_001330520.1. [Q8NDV7-6]
RefSeq; NP_055309.2; NM_014494.2. [Q8NDV7-1]
RefSeq; XP_005255314.1; XM_005255257.4. [Q8NDV7-2]
RefSeq; XP_016878642.1; XM_017023153.1. [Q8NDV7-2]
UniGene; Hs.655057; -.
PDB; 5W6V; X-ray; 2.83 A; B=1073-1094.
PDBsum; 5W6V; -.
ProteinModelPortal; Q8NDV7; -.
SMR; Q8NDV7; -.
BioGrid; 118141; 47.
DIP; DIP-54489N; -.
ELM; Q8NDV7; -.
IntAct; Q8NDV7; 80.
MINT; MINT-4535204; -.
STRING; 9606.ENSP00000379144; -.
iPTMnet; Q8NDV7; -.
PhosphoSitePlus; Q8NDV7; -.
BioMuta; TNRC6A; -.
DMDM; 296452846; -.
EPD; Q8NDV7; -.
MaxQB; Q8NDV7; -.
PaxDb; Q8NDV7; -.
PeptideAtlas; Q8NDV7; -.
PRIDE; Q8NDV7; -.
Ensembl; ENST00000315183; ENSP00000326900; ENSG00000090905. [Q8NDV7-6]
Ensembl; ENST00000395799; ENSP00000379144; ENSG00000090905. [Q8NDV7-1]
GeneID; 27327; -.
KEGG; hsa:27327; -.
UCSC; uc002dmm.4; human. [Q8NDV7-1]
CTD; 27327; -.
DisGeNET; 27327; -.
EuPathDB; HostDB:ENSG00000090905.17; -.
GeneCards; TNRC6A; -.
H-InvDB; HIX0012904; -.
H-InvDB; HIX0173209; -.
HGNC; HGNC:11969; TNRC6A.
HPA; HPA015305; -.
HPA; HPA017869; -.
MIM; 610739; gene.
neXtProt; NX_Q8NDV7; -.
OpenTargets; ENSG00000090905; -.
PharmGKB; PA36656; -.
eggNOG; ENOG410IF5S; Eukaryota.
eggNOG; ENOG41110AX; LUCA.
GeneTree; ENSGT00410000025966; -.
HOVERGEN; HBG062594; -.
InParanoid; Q8NDV7; -.
KO; K18412; -.
OMA; NLNSVRQ; -.
OrthoDB; EOG091G00G6; -.
PhylomeDB; Q8NDV7; -.
TreeFam; TF329702; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-4086398; Ca2+ pathway.
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-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
ChiTaRS; TNRC6A; human.
GeneWiki; TNRC6A; -.
GenomeRNAi; 27327; -.
PRO; PR:Q8NDV7; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000090905; -.
ExpressionAtlas; Q8NDV7; baseline and differential.
Genevisible; Q8NDV7; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035195; P:gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
CDD; cd12711; RRM_TNRC6A; 1.
InterPro; IPR019486; Argonaute_hook_dom.
InterPro; IPR026805; GW182_M_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR032226; TNRC6_PABC-bd.
InterPro; IPR033501; TNRC6A.
InterPro; IPR034924; TNRC6A_RRM.
PANTHER; PTHR13020:SF28; PTHR13020:SF28; 1.
Pfam; PF10427; Ago_hook; 1.
Pfam; PF12938; M_domain; 1.
Pfam; PF16608; TNRC6-PABC_bdg; 1.
SUPFAM; SSF54928; SSF54928; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome;
RNA-binding; RNA-mediated gene silencing; Translation regulation.
CHAIN 1 1962 Trinucleotide repeat-containing gene 6A
protein.
/FTId=PRO_0000081980.
DOMAIN 1781 1853 RRM.
REGION 1 932 Interaction with argonaute family
proteins.
REGION 254 503 Sufficient for interaction with AGO1,
AGO3 and AGO4.
REGION 270 346 Sufficient for interaction with AGO2.
REGION 318 399 Sufficient for interaction with AGO2.
REGION 340 439 Sufficient for interaction with AGO2.
REGION 409 495 Sufficient for interaction with AGO2.
REGION 502 751 Sufficient for interaction with AGO2.
REGION 566 1343 Sufficient for interaction with AGO1 and
AGO4.
REGION 1074 1144 Sufficient for interaction with AGO2.
REGION 1604 1622 PABPC1-interacting motif-2 (PAM2).
REGION 1670 1962 Sufficient for interaction with AGO2.
COILED 7 54 {ECO:0000255}.
COMPBIAS 93 127 Gln-rich.
COMPBIAS 192 365 Ser-rich.
MOD_RES 739 739 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 878 878 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1212 1212 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1270 1270 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1470 1470 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1585 1585 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1869 1869 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1890 1890 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1801 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013292.
VAR_SEQ 1 1232 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037287.
VAR_SEQ 1 253 Missing (in isoform 2).
{ECO:0000303|PubMed:11950943}.
/FTId=VSP_013294.
VAR_SEQ 1 54 MRELEAKATKDVERNLSRDLVQEEEQLMEEKKKKKDDKKKK
EAAQKKATEQKIK -> MAYFGGTLYWLIFSTPFLLLGL
(in isoform 5).
{ECO:0000303|PubMed:9225980}.
/FTId=VSP_013295.
VAR_SEQ 1280 1328 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037288.
VAR_SEQ 1611 1962 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037289.
VARIANT 185 185 N -> K (in dbSNP:rs11639856).
/FTId=VAR_057251.
VARIANT 592 592 A -> T (in dbSNP:rs6497759).
/FTId=VAR_057252.
VARIANT 788 788 P -> S (in dbSNP:rs3803716).
/FTId=VAR_057253.
VARIANT 1268 1268 E -> K (in dbSNP:rs2112782).
/FTId=VAR_057254.
MUTAGEN 313 313 W->A: Does not impair interaction with
AGO2; when associated with A-345; A-370;
A-420 and A-483.
{ECO:0000269|PubMed:19324964}.
MUTAGEN 345 345 W->A: Does not impair interaction with
AGO2; when associated with A-313; A-370;
A-420 and A-483.
{ECO:0000269|PubMed:19324964}.
MUTAGEN 370 370 W->A: Does not impair interaction with
AGO2; when associated with A-313; A-345;
A-420 and A-483.
{ECO:0000269|PubMed:19324964}.
MUTAGEN 420 420 W->A: Does not impair interaction with
AGO2; when associated with A-313; A-345;
A-370 and A-483.
{ECO:0000269|PubMed:19324964}.
MUTAGEN 483 483 W->A: Does not impair interaction with
AGO2; when associated with A-313; A-345;
A-370 and A-420.
{ECO:0000269|PubMed:19324964}.
CONFLICT 31 34 KKKK -> TEKE (in Ref. 2; CAD37348).
{ECO:0000305}.
CONFLICT 1375 1375 V -> VV (in Ref. 3; CAD28525).
{ECO:0000305}.
CONFLICT 1704 1704 S -> F (in Ref. 8; BAA91899).
{ECO:0000305}.
SEQUENCE 1962 AA; 210297 MW; 963C054628E18592 CRC64;
MRELEAKATK DVERNLSRDL VQEEEQLMEE KKKKKDDKKK KEAAQKKATE QKIKVPEQIK
PSVSQPQPAN SNNGTSTATS TNNNAKRATA NNQQPQQQQQ QQQPQQQQPQ QQPQPQPQQQ
QPQQQPQALP RYPREVPPRF RHQEHKQLLK RGQHFPVIAA NLGSAVKVLN SQSESSALTN
QQPQNNGEVQ NSKNQSDINH STSGSHYENS QRGPVSSTSD SSTNCKNAVV SDLSEKEAWP
SAPGSDPELA SECMDADSAS SSESERNITI MASGNTGGEK DGLRNSTGLG SQNKFVVGSS
SNNVGHGSST GPWGFSHGAI ISTCQVSVDA PESKSESSNN RMNAWGTVSS SSNGGLNPST
LNSASNHGAW PVLENNGLAL KGPVGSGSSG INIQCSTIGQ MPNNQSINSK VSGGSTHGTW
GSLQETCESE VSGTQKVSFS GQPQNITTEM TGPNNTTNFM TSSLPNSGSV QNNELPSSNT
GAWRVSTMNH PQMQAPSGMN GTSLSHLSNG ESKSGGSYGT TWGAYGSNYS GDKCSGPNGQ
ANGDTVNATL MQPGVNGPMG TNFQVNTNKG GGVWESGAAN SQSTSWGSGN GANSGGSRRG
WGTPAQNTGT NLPSVEWNKL PSNQHSNDSA NGNGKTFTNG WKSTEEEDQG SATSQTNEQS
SVWAKTGGTV ESDGSTESTG RLEEKGTGES QSRDRRKIDQ HTLLQSIVNR TDLDPRVLSN
SGWGQTPIKQ NTAWDTETSP RGERKTDNGT EAWGSSATQT FNSGACIDKT SPNGNDTSSV
SGWGDPKPAL RWGDSKGSNC QGGWEDDSAA TGMVKSNQWG NCKEEKAAWN DSQKNKQGWG
DGQKSSQGWS VSASDNWGET SRNNHWGEAN KKSSSGGSDS DRSVSGWNEL GKTSSFTWGN
NINPNNSSGW DESSKPTPSQ GWGDPPKSNQ SLGWGDSSKP VSSPDWNKQQ DIVGSWGIPP
ATGKPPGTGW LGGPIPAPAK EEEPTGWEEP SPESIRRKME IDDGTSAWGD PSKYNYKNVN
MWNKNVPNGN SRSDQQAQVH QLLTPASAIS NKEASSGSGW GEPWGEPSTP ATTVDNGTSA
WGKPIDSGPS WGEPIAAASS TSTWGSSSVG PQALSKSGPK SMQDGWCGDD MPLPGNRPTG
WEEEEDVEIG MWNSNSSQEL NSSLNWPPYT KKMSSKGLSG KKRRRERGMM KGGNKQEEAW
INPFVKQFSN ISFSRDSPEE NVQSNKMDLS GGMLQDKRME IDKHSLNIGD YNRTVGKGPG
SRPQISKESS MERNPYFDKD GIVADESQNM QFMSSQSMKL PPSNSALPNQ ALGSIAGLGM
QNLNSVRQNG NPSMFGVGNT AAQPRGMQQP PAQPLSSSQP NLRAQVPPPL LSPQVPVSLL
KYAPNNGGLN PLFGPQQVAM LNQLSQLNQL SQISQLQRLL AQQQRAQSQR SVPSGNRPQQ
DQQGRPLSVQ QQMMQQSRQL DPNLLVKQQT PPSQQQPLHQ PAMKSFLDNV MPHTTPELQK
GPSPINAFSN FPIGLNSNLN VNMDMNSIKE PQSRLRKWTT VDSISVNTSL DQNSSKHGAI
SSGFRLEESP FVPYDFMNSS TSPASPPGSI GDGWPRAKSP NGSSSVNWPP EFRPGEPWKG
YPNIDPETDP YVTPGSVINN LSINTVREVD HLRDRNSGSS SSLNTTLPST SAWSSIRASN
YNVPLSSTAQ STSARNSDSK LTWSPGSVTN TSLAHELWKV PLPPKNITAP SRPPPGLTGQ
KPPLSTWDNS PLRIGGGWGN SDARYTPGSS WGESSSGRIT NWLVLKNLTP QIDGSTLRTL
CMQHGPLITF HLNLPHGNAL VRYSSKEEVV KAQKSLHMCV LGNTTILAEF ASEEEISRFF
AQSQSLTPSP GWQSLGSSQS RLGSLDCSHS FSSRTDLNHW NGAGLSGTNC GDLHGTSLWG
TPHYSTSLWG PPSSSDPRGI SSPSPINAFL SVDHLGGGGE SM


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