TRBP2_HUMAN
ID TRBP2_HUMAN Reviewed; 366 AA.
AC Q15633; Q12878; Q8WY32; Q8WY33; Q9BRY2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
DE AltName: Full=TAR RNA-binding protein 2;
DE AltName: Full=Trans-activation-responsive RNA-binding protein;
GN Name=TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034}; Synonyms=TRBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION (MICROBIAL
RP INFECTION), AND VARIANT PHE-251.
RX PubMed=2011739; DOI=10.1126/science.2011739;
RA Gatignol A., Buckler-White A.J., Berkhout B., Jeang K.T.;
RT "Characterization of a human TAR RNA-binding protein that activates the
RT HIV-1 LTR.";
RL Science 251:1597-1600(1991).
RN [2]
RP SEQUENCE REVISION.
RA Gatignol A., Duarte M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-251.
RX PubMed=7774957; DOI=10.1016/0888-7543(95)80110-8;
RA Kozak C.A., Gatignol A., Graham K., Jeang K.T., McBride O.W.;
RT "Genetic mapping in human and mouse of the locus encoding TRBP, a protein
RT that binds the TAR region of the human immunodeficiency virus (HIV-1).";
RL Genomics 25:66-72(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74, AND ALTERNATIVE PROMOTER USAGE.
RX PubMed=11641396; DOI=10.1074/jbc.m104645200;
RA Bannwarth S., Talakoub L., Letourneur F., Duarte M., Purcell D.F.,
RA Hiscott J., Gatignol A.;
RT "Organization of the human tarbp2 gene reveals two promoters that are
RT repressed in an astrocytic cell line.";
RL J. Biol. Chem. 276:48803-48813(2001).
RN [8]
RP CHARACTERIZATION OF RNA-BINDING.
RX PubMed=8455607; DOI=10.1128/mcb.13.4.2193-2202.1993;
RA Gatignol A., Buckler C., Jeang K.T.;
RT "Relatedness of an RNA-binding motif in human immunodeficiency virus type 1
RT TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila
RT staufen.";
RL Mol. Cell. Biol. 13:2193-2202(1993).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), SELF-ASSOCIATION, AND INTERACTION WITH
RP EIF2AK2.
RX PubMed=11438532; DOI=10.1074/jbc.m103584200;
RA Daher A., Longuet M., Dorin D., Bois F., Segeral E., Bannwarth S.,
RA Battisti P.-L., Purcell D.F., Benarous R., Vaquero C., Meurs E.F.,
RA Gatignol A.;
RT "Two dimerization domains in the trans-activation response RNA-binding
RT protein (TRBP) individually reverse the protein kinase R inhibition of HIV-
RT 1 long terminal repeat expression.";
RL J. Biol. Chem. 276:33899-33905(2001).
RN [10]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=12475984; DOI=10.1074/jbc.m208954200;
RA Dorin D., Bonnet M.C., Bannwarth S., Gatignol A., Meurs E.F., Vaquero C.;
RT "The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-
RT containing RNAs in vitro and in vivo independently of its ability to
RT inhibit the dsRNA-dependent kinase PKR.";
RL J. Biol. Chem. 278:4440-4448(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH DICER1 AND AGO2.
RX PubMed=16271387; DOI=10.1016/j.cell.2005.10.022;
RA Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.;
RT "Human RISC couples microRNA biogenesis and posttranscriptional gene
RT silencing.";
RL Cell 123:631-640(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SELF-ASSOCIATION, AND
RP INTERACTION WITH DICER1.
RX PubMed=16142218; DOI=10.1038/sj.embor.7400509;
RA Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
RA Filipowicz W.;
RT "TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts
RT with Dicer and functions in RNA silencing.";
RL EMBO Rep. 6:961-967(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH DICER1 AND AGO2.
RX PubMed=16357216; DOI=10.1101/gad.1384005;
RA Maniataki E., Mourelatos Z.;
RT "A human, ATP-independent, RISC assembly machine fueled by pre-miRNA.";
RL Genes Dev. 19:2979-2990(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1 AND
RP AGO2, AND RNA-BINDING.
RX PubMed=15973356; DOI=10.1038/nature03868;
RA Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N.,
RA Nishikura K., Shiekhattar R.;
RT "TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene
RT silencing.";
RL Nature 436:740-744(2005).
RN [15]
RP FUNCTION, INTERACTION WITH DICER1; AGO2 AND PRKRA, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16424907; DOI=10.1038/sj.emboj.7600942;
RA Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.;
RT "The role of PACT in the RNA silencing pathway.";
RL EMBO J. 25:522-532(2006).
RN [16]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1 AND PRKRA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17452327; DOI=10.1074/jbc.m611768200;
RA Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.;
RT "Human TRBP and PACT directly interact with each other and associate with
RT dicer to facilitate the production of small interfering RNA.";
RL J. Biol. Chem. 282:17649-17657(2007).
RN [17]
RP INTERACTION WITH DHX9.
RX PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016;
RA Robb G.B., Rana T.M.;
RT "RNA helicase A interacts with RISC in human cells and functions in RISC
RT loading.";
RL Mol. Cell 26:523-537(2007).
RN [18]
RP INTERACTION WITH DICER1; AGO2; EIF6; RPL7A AND MOV10, AND ASSOCIATION WITH
RP THE 60S RIBOSOME.
RX PubMed=17507929; DOI=10.1038/nature05841;
RA Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
RA Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
RT "MicroRNA silencing through RISC recruitment of eIF6.";
RL Nature 447:823-828(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH DICER1
RP AND AGO2.
RX PubMed=18178619; DOI=10.1073/pnas.0710869105;
RA MacRae I.J., Ma E., Zhou M., Robinson C.V., Doudna J.A.;
RT "In vitro reconstitution of the human RISC-loading complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:512-517(2008).
RN [21]
RP SELF-ASSOCIATION, INTERACTION WITH EIF2AK2 AND PRKRA, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18421256; DOI=10.4161/rna.5.2.6069;
RA Laraki G., Clerzius G., Daher A., Melendez-Pena C., Daniels S.,
RA Gatignol A.;
RT "Interactions between the double-stranded RNA-binding proteins TRBP and
RT PACT define the Medipal domain that mediates protein-protein
RT interactions.";
RL RNA Biol. 5:92-103(2008).
RN [22]
RP RETRACTED PAPER.
RX PubMed=19219043; DOI=10.1038/ng.317;
RA Melo S.A., Ropero S., Moutinho C., Aaltonen L.A., Yamamoto H., Calin G.A.,
RA Rossi S., Fernandez A.F., Carneiro F., Oliveira C., Ferreira B., Liu C.-G.,
RA Villanueva A., Capella G., Schwartz S. Jr., Shiekhattar R., Esteller M.;
RT "A TARBP2 mutation in human cancer impairs microRNA processing and DICER1
RT function.";
RL Nat. Genet. 41:365-370(2009).
RN [23]
RP RETRACTION NOTICE OF PUBMED:19219043 NOTICE FOR PUBMED:19219043.
RX PubMed=26813765; DOI=10.1038/ng0216-221;
RA Melo S.A., Ropero S., Moutinho C., Aaltonen L.A., Yamamoto H., Calin G.A.,
RA Rossi S., Fernandez A.F., Carneiro F., Oliveira C., Ferreira B., Liu C.-G.,
RA Villanueva A., Capella G., Schwartz S. Jr., Shiekhattar R., Esteller M.;
RT "Retraction: A TARBP2 mutation in human cancer impairs microRNA processing
RT and DICER1 function.";
RL Nat. Genet. 48:221-221(2016).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP INTERACTION WITH EBOLAVIRUS VP30 (MICROBIAL INFECTION), AND INTERACTION
RP WITH EBOLAVIRUS VP35 (MICROBIAL INFECTION).
RX PubMed=21228243; DOI=10.1128/jvi.01160-10;
RA Fabozzi G., Nabel C.S., Dolan M.A., Sullivan N.J.;
RT "Ebolavirus proteins suppress the effects of small interfering RNA by
RT direct interaction with the mammalian RNA interference pathway.";
RL J. Virol. 85:2512-2523(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=30626973; DOI=10.1038/s41586-018-0841-4;
RA Ringeard M., Marchand V., Decroly E., Motorin Y., Bennasser Y.;
RT "FTSJ3 is an RNA 2'-O-methyltransferase recruited by HIV to avoid innate
RT immune sensing.";
RL Nature 565:500-504(2019).
RN [28]
RP STRUCTURE BY NMR OF 150-225.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second DSRBD of TAR RNA-binding protein 2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Required for formation of the RNA induced silencing complex
CC (RISC). Component of the RISC loading complex (RLC), also known as the
CC micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1,
CC AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required
CC to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load
CC them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal
CC RISC and may subsequently dissociate from DICER1 and TARBP2. May also
CC play a role in the production of short interfering RNAs (siRNAs) from
CC double-stranded RNA (dsRNA) by DICER1. {ECO:0000255|HAMAP-
CC Rule:MF_03034, ECO:0000269|PubMed:15973356,
CC ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
CC ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907,
CC ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619}.
CC -!- FUNCTION: (Microbial infection) Binds to the HIV-1 TAR RNA which is
CC located in the long terminal repeat (LTR) of HIV-1, and stimulates
CC translation of TAR-containing RNAs (PubMed:2011739, PubMed:11438532,
CC PubMed:12475984). This is achieved in part at least by binding to and
CC inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition
CC of EIF2S1/eIF-2-alpha (PubMed:11438532). May also promote translation
CC of TAR-containing RNAs independently of EIF2AK2/PKR (PubMed:12475984).
CC Mediates recruitment of FTSJ3 methyltransferase to HIV-1 RNA, leading
CC to 2'-O-methylation of the viral genome, allowing HIV-1 to escape the
CC innate immune system (PubMed:30626973). {ECO:0000269|PubMed:11438532,
CC ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:2011739,
CC ECO:0000269|PubMed:30626973}.
CC -!- SUBUNIT: Self-associates. Component of the RISC loading complex (RLC),
CC or micro-RNA (miRNA) loading complex (miRLC), which is composed of
CC DICER1, AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also
CC referred to as RISC. Interacts with EIF2AK2/PKR and inhibits its
CC protein kinase activity. Interacts with DHX9 and PRKRA. Interacts with
CC DICER1, AGO2, MOV10, EIF6 and RPL7A (60S ribosome subunit); they form a
CC large RNA-induced silencing complex (RISC) (PubMed:17507929).
CC {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:11438532,
CC ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218,
CC ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16357216,
CC ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327,
CC ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:17531811,
CC ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:18421256}.
CC -!- SUBUNIT: (Microbial infection) Interacts with FTSJ3; forms a complex
CC with FTSJ3 and HIV-1 TAR RNA. {ECO:0000269|PubMed:30626973}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus VP30; this
CC interaction, which occurs only in the presence of siRNA, prevents
CC TARBP2 binding to DICER1 and thus allows the virus to counteract host
CC RNA silencing. {ECO:0000269|PubMed:21228243}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus VP35; this
CC interaction prevents TARBP2 binding to DICER1 and thus allows the virus
CC to counteract host RNA silencing. {ECO:0000269|PubMed:21228243}.
CC -!- INTERACTION:
CC Q15633; P55265-1: ADAR; NbExp=2; IntAct=EBI-978581, EBI-6913056;
CC Q15633; P55265-5: ADAR; NbExp=3; IntAct=EBI-978581, EBI-6913210;
CC Q15633; P78563-4: ADARB1; NbExp=3; IntAct=EBI-978581, EBI-12002366;
CC Q15633; Q9UKV8: AGO2; NbExp=12; IntAct=EBI-978581, EBI-528269;
CC Q15633; Q9UPY3: DICER1; NbExp=25; IntAct=EBI-978581, EBI-395506;
CC Q15633; Q9UPY3-1: DICER1; NbExp=5; IntAct=EBI-978581, EBI-15569571;
CC Q15633; P19525: EIF2AK2; NbExp=2; IntAct=EBI-978581, EBI-640775;
CC Q15633; Q96T60: PNKP; NbExp=3; IntAct=EBI-978581, EBI-1045072;
CC Q15633; O75569: PRKRA; NbExp=13; IntAct=EBI-978581, EBI-713955;
CC Q15633; Q96SI9: STRBP; NbExp=3; IntAct=EBI-978581, EBI-740355;
CC Q15633; Q15633: TARBP2; NbExp=5; IntAct=EBI-978581, EBI-978581;
CC Q15633; Q15560: TCEA2; NbExp=3; IntAct=EBI-978581, EBI-710310;
CC Q15633; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-978581, EBI-954696;
CC Q15633; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-978581, EBI-11955057;
CC Q15633; Q9HA38: ZMAT3; NbExp=3; IntAct=EBI-978581, EBI-2548480;
CC Q15633; Q9H898-2: ZMAT4; NbExp=3; IntAct=EBI-978581, EBI-11529334;
CC Q15633; Q9UL40: ZNF346; NbExp=6; IntAct=EBI-978581, EBI-2462313;
CC Q15633; P0DTC9: N; Xeno; NbExp=5; IntAct=EBI-978581, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=TRBP2;
CC IsoId=Q15633-1; Sequence=Displayed;
CC Name=2; Synonyms=TRBP1;
CC IsoId=Q15633-2; Sequence=VSP_035584;
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
CC -!- CAUTION: A paper describing truncating mutations of TARBP2 in tumor
CC cells and resultant effects on DICER1 stability and miRNA processing
CC has been retracted, due to concerns of image duplication in some of the
CC figures. {ECO:0000305|PubMed:19219043, ECO:0000305|PubMed:26813765}.
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DR EMBL; M60801; AAA36765.1; -; mRNA.
DR EMBL; U08998; AAB50581.2; -; mRNA.
DR EMBL; BT007140; AAP35804.1; -; mRNA.
DR EMBL; CH471054; EAW96720.1; -; Genomic_DNA.
DR EMBL; BC005860; AAH05860.1; -; mRNA.
DR EMBL; AF281068; AAL55730.1; -; Genomic_DNA.
DR EMBL; AF281068; AAL55731.1; -; Genomic_DNA.
DR CCDS; CCDS41791.1; -. [Q15633-2]
DR CCDS; CCDS8861.1; -. [Q15633-1]
DR PIR; G01420; G01420.
DR RefSeq; NP_004169.3; NM_004178.4. [Q15633-2]
DR RefSeq; NP_599150.1; NM_134323.1. [Q15633-1]
DR RefSeq; NP_599151.2; NM_134324.2. [Q15633-2]
DR RefSeq; XP_005269171.1; XM_005269114.1. [Q15633-2]
DR RefSeq; XP_005269172.1; XM_005269115.2. [Q15633-2]
DR PDB; 2CPN; NMR; -; A=150-225.
DR PDB; 3ADL; X-ray; 2.20 A; A=161-231.
DR PDB; 3LLH; X-ray; 2.14 A; A/B=22-105.
DR PDB; 4WYQ; X-ray; 3.20 A; B/E=289-363.
DR PDB; 5N8L; NMR; -; A=16-227.
DR PDB; 5N8M; NMR; -; A=16-227.
DR PDB; 5ZAK; EM; 4.40 A; B=1-366.
DR PDB; 5ZAL; EM; 4.70 A; B=1-366.
DR PDB; 5ZAM; EM; 5.70 A; B=1-366.
DR PDB; 6ZBK; X-ray; 1.49 A; B=262-366.
DR PDBsum; 2CPN; -.
DR PDBsum; 3ADL; -.
DR PDBsum; 3LLH; -.
DR PDBsum; 4WYQ; -.
DR PDBsum; 5N8L; -.
DR PDBsum; 5N8M; -.
DR PDBsum; 5ZAK; -.
DR PDBsum; 5ZAL; -.
DR PDBsum; 5ZAM; -.
DR PDBsum; 6ZBK; -.
DR AlphaFoldDB; Q15633; -.
DR BMRB; Q15633; -.
DR SMR; Q15633; -.
DR BioGRID; 112758; 148.
DR ComplexPortal; CPX-134; RISC-loading complex, TARBP2 variant.
DR CORUM; Q15633; -.
DR DIP; DIP-29665N; -.
DR IntAct; Q15633; 60.
DR MINT; Q15633; -.
DR STRING; 9606.ENSP00000266987; -.
DR BindingDB; Q15633; -.
DR ChEMBL; CHEMBL2098; -.
DR GlyGen; Q15633; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15633; -.
DR PhosphoSitePlus; Q15633; -.
DR BioMuta; TARBP2; -.
DR DMDM; 209572714; -.
DR EPD; Q15633; -.
DR jPOST; Q15633; -.
DR MassIVE; Q15633; -.
DR MaxQB; Q15633; -.
DR PaxDb; Q15633; -.
DR PeptideAtlas; Q15633; -.
DR PRIDE; Q15633; -.
DR ProteomicsDB; 60666; -. [Q15633-1]
DR ProteomicsDB; 60667; -. [Q15633-2]
DR Antibodypedia; 15253; 422 antibodies from 35 providers.
DR DNASU; 6895; -.
DR Ensembl; ENST00000266987.7; ENSP00000266987.2; ENSG00000139546.11. [Q15633-1]
DR Ensembl; ENST00000394357.6; ENSP00000377885.2; ENSG00000139546.11. [Q15633-2]
DR Ensembl; ENST00000456234.6; ENSP00000416077.2; ENSG00000139546.11. [Q15633-2]
DR GeneID; 6895; -.
DR KEGG; hsa:6895; -.
DR MANE-Select; ENST00000266987.7; ENSP00000266987.2; NM_134323.2; NP_599150.1.
DR UCSC; uc001sdo.4; human. [Q15633-1]
DR CTD; 6895; -.
DR DisGeNET; 6895; -.
DR GeneCards; TARBP2; -.
DR HGNC; HGNC:11569; TARBP2.
DR HPA; ENSG00000139546; Low tissue specificity.
DR MIM; 605053; gene.
DR neXtProt; NX_Q15633; -.
DR OpenTargets; ENSG00000139546; -.
DR PharmGKB; PA36334; -.
DR VEuPathDB; HostDB:ENSG00000139546; -.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000157748; -.
DR HOGENOM; CLU_048292_2_0_1; -.
DR InParanoid; Q15633; -.
DR OMA; GYSCTWD; -.
DR OrthoDB; 1093169at2759; -.
DR PhylomeDB; Q15633; -.
DR TreeFam; TF315953; -.
DR PathwayCommons; Q15633; -.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
DR SignaLink; Q15633; -.
DR SIGNOR; Q15633; -.
DR BioGRID-ORCS; 6895; 13 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q15633; -.
DR GeneWiki; TARBP2; -.
DR GenomeRNAi; 6895; -.
DR Pharos; Q15633; Tbio.
DR PRO; PR:Q15633; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15633; protein.
DR Bgee; ENSG00000139546; Expressed in right hemisphere of cerebellum and 132 other tissues.
DR ExpressionAtlas; Q15633; baseline and differential.
DR Genevisible; Q15633; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:BHF-UCL.
DR GO; GO:0036002; F:pre-mRNA binding; TAS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:BHF-UCL.
DR GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; IMP:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; IDA:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0050689; P:negative regulation of defense response to virus by host; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
DR GO; GO:1903798; P:regulation of miRNA maturation; IEA:Ensembl.
DR GO; GO:0070920; P:regulation of production of small RNA involved in gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0046782; P:regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0030422; P:siRNA processing; IDA:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR CDD; cd19890; DSRM_TARBP2_rpt1; 1.
DR CDD; cd10844; DSRM_TARBP2_rpt2; 1.
DR CDD; cd19893; DSRM_TARBP2_rpt3; 1.
DR HAMAP; MF_03034; TRBP2; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR028605; TRBP2.
DR InterPro; IPR044469; TRBP2_DSRM_1.
DR InterPro; IPR044470; TRBP2_DSRM_2.
DR InterPro; IPR044471; TRBP2_DSRM_3.
DR PANTHER; PTHR46205:SF1; PTHR46205:SF1; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..366
FT /note="RISC-loading complex subunit TARBP2"
FT /id="PRO_0000065622"
FT DOMAIN 30..97
FT /note="DRBM 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 159..227
FT /note="DRBM 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 293..361
FT /note="DRBM 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 22..105
FT /note="Sufficient for interaction with PRKRA"
FT REGION 152..234
FT /note="Sufficient for interaction with PRKRA"
FT REGION 228..366
FT /note="Sufficient for interaction with DICER1"
FT REGION 287..366
FT /note="Sufficient for interaction with PRKRA"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2011739"
FT /id="VSP_035584"
FT VARIANT 251
FT /note="S -> F (in dbSNP:rs1126500)"
FT /evidence="ECO:0000269|PubMed:2011739,
FT ECO:0000269|PubMed:7774957"
FT /id="VAR_046992"
FT CONFLICT 144
FT /note="P -> A (in Ref. 1; AAA36765)"
FT /evidence="ECO:0000305"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:5N8L"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:3LLH"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3LLH"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5N8L"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3LLH"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:3LLH"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:3LLH"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:3ADL"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3ADL"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2CPN"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3ADL"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3ADL"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3ADL"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:6ZBK"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:6ZBK"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6ZBK"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4WYQ"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 344..364
FT /evidence="ECO:0007829|PDB:6ZBK"
SQ SEQUENCE 366 AA; 39039 MW; 768BA11751DA4912 CRC64;
MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE
DIPVFTAAAA ATPVPSVVLT RSPPMELQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV
TQESGPAHRK EFTMTCRVER FIEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEVEP
DDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCRVLSE
LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS ATTREAARGE AARRALQYLK
IMAGSK
