TDRD3_HUMAN
ID TDRD3_HUMAN Reviewed; 651 AA.
AC Q9H7E2; B2MWP9; Q53XA6; Q6P992;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=TDRD3;
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] (ISOFORM 3), ALTERNATIVE SPLICING, FUNCTION,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-598, AND INTERACTION WITH EWSR1;
RP FMR1; FUS; SERBP1; EEF1A1 AND DDX3X OR DDX3Y.
RX PubMed=18632687; DOI=10.1093/hmg/ddn203;
RA Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
RT "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic
RT stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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 FUNCTION, AND INTERACTION WITH SNRPB AND SNRPN.
RX PubMed=15955813; DOI=10.1074/jbc.m414328200;
RA Cote J., Richard S.;
RT "Tudor domains bind symmetrical dimethylated arginines.";
RL J. Biol. Chem. 280:28476-28483(2005).
RN [8]
RP INTERACTION WITH LYS-48-LINKED TETRA-UBIQUITIN; FMR1; FXR1 AND FXR2,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18664458; DOI=10.1093/hmg/ddn219;
RA Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B.,
RA Meister G., Keidel E., Fischer U.;
RT "Tdrd3 is a novel stress granule-associated protein interacting with the
RT Fragile-X syndrome protein FMRP.";
RL Hum. Mol. Genet. 17:3236-3246(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP INTERACTION WITH THE EXON JUNCTION COMPLEX, AND MUTAGENESIS OF
RP 638-ARG--TYR-644.
RX PubMed=20930030; DOI=10.1101/gad.604610;
RA Kashima I., Jonas S., Jayachandran U., Buchwald G., Conti E., Lupas A.N.,
RA Izaurralde E.;
RT "SMG6 interacts with the exon junction complex via two conserved EJC-
RT binding motifs (EBMs) required for nonsense-mediated mRNA decay.";
RL Genes Dev. 24:2440-2450(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN TUDOR.
RX PubMed=21172665; DOI=10.1016/j.molcel.2010.11.024;
RA Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T.;
RT "TDRD3 is an effector molecule for arginine-methylated histone marks.";
RL Mol. Cell 40:1016-1023(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH POLR2A.
RX PubMed=26700805; DOI=10.1038/nature16469;
RA Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z., Schmitges F.W.,
RA Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J., Pawson T.J.,
RA Blencowe B.J., Greenblatt J.F.;
RT "SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal
RT domain control termination.";
RL Nature 529:48-53(2016).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-470, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP STRUCTURE BY NMR OF 194-243.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UBA domain of human Tudor domain containing
RT protein 3.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Scaffolding protein that specifically recognizes and binds
CC dimethylarginine-containing proteins. In nucleus, acts as a
CC coactivator: recognizes and binds asymmetric dimethylation on the core
CC histone tails associated with transcriptional activation (H3R17me2a and
CC H4R3me2a) and recruits proteins at these arginine-methylated loci. In
CC cytoplasm, may play a role in the assembly and/or disassembly of mRNA
CC stress granules and in the regulation of translation of target mRNAs by
CC binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing
CC proteins. {ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:21172665}.
CC -!- SUBUNIT: Component of mRNA stress granules. Interacts with FMR1, FXR1,
CC FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small
CC nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN.
CC Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with
CC monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with
CC the exon junction complex (EJC) composed at least of CASC3, EIF4A3,
CC MAGOH and RBM8A. Interacts with POLR2A (via the C-terminal domain
CC (CTD)). {ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:20930030,
CC ECO:0000269|PubMed:26700805}.
CC -!- INTERACTION:
CC Q9H7E2; P24928: POLR2A; NbExp=6; IntAct=EBI-3938232, EBI-295301;
CC Q9H7E2-3; O95985: TOP3B; NbExp=4; IntAct=EBI-10969939, EBI-373403;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18632687}. Nucleus
CC {ECO:0000269|PubMed:21172665}. Note=Predominantly cytoplasmic.
CC Associated with actively translating polyribosomes and with mRNA stress
CC granules. {ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H7E2-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q9H7E2-2; Sequence=VSP_037053;
CC Name=3;
CC IsoId=Q9H7E2-3; Sequence=VSP_037052;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:18664458}.
CC -!- DOMAIN: The Tudor domain specifically recognizes and binds asymmetric
CC dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg-
CC 3', 2 tags for epigenetic transcriptional activation.
CC {ECO:0000269|PubMed:21172665}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU643838; ACC94142.1; -; mRNA.
DR EMBL; AK024660; BAB14950.1; -; mRNA.
DR EMBL; BX537910; CAD97894.1; -; mRNA.
DR EMBL; AL354764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471124; EAW52079.1; -; Genomic_DNA.
DR EMBL; BC030514; AAH30514.1; -; mRNA.
DR EMBL; BC060876; AAH60876.1; -; mRNA.
DR CCDS; CCDS53872.1; -. [Q9H7E2-3]
DR CCDS; CCDS9441.1; -. [Q9H7E2-1]
DR RefSeq; NP_001139542.1; NM_001146070.1. [Q9H7E2-3]
DR RefSeq; NP_001139543.1; NM_001146071.1. [Q9H7E2-1]
DR RefSeq; NP_110421.1; NM_030794.2. [Q9H7E2-1]
DR RefSeq; XP_016876266.1; XM_017020777.1. [Q9H7E2-3]
DR PDB; 1WJI; NMR; -; A=194-243.
DR PDB; 2LTO; NMR; -; A=554-608.
DR PDB; 3PMT; X-ray; 1.80 A; A=553-611.
DR PDB; 3PNW; X-ray; 2.05 A; C/F/I/L/O/R/U/X=540-615.
DR PDB; 3S6W; X-ray; 1.78 A; A=555-608.
DR PDB; 5GVD; X-ray; 1.62 A; A/B=1-68.
DR PDB; 5GVE; X-ray; 3.61 A; B=1-68.
DR PDB; 5YJ8; X-ray; 1.76 A; A=555-608.
DR PDB; 6V9T; X-ray; 2.15 A; AAA/BBB=554-611.
DR PDBsum; 1WJI; -.
DR PDBsum; 2LTO; -.
DR PDBsum; 3PMT; -.
DR PDBsum; 3PNW; -.
DR PDBsum; 3S6W; -.
DR PDBsum; 5GVD; -.
DR PDBsum; 5GVE; -.
DR PDBsum; 5YJ8; -.
DR PDBsum; 6V9T; -.
DR AlphaFoldDB; Q9H7E2; -.
DR BMRB; Q9H7E2; -.
DR SMR; Q9H7E2; -.
DR BioGRID; 123514; 203.
DR ComplexPortal; CPX-1621; TDRD3-TOP3B type IA topoisomerase complex. [Q9H7E2-3]
DR CORUM; Q9H7E2; -.
DR DIP; DIP-61935N; -.
DR IntAct; Q9H7E2; 29.
DR MINT; Q9H7E2; -.
DR STRING; 9606.ENSP00000440190; -.
DR ChEMBL; CHEMBL3879852; -.
DR iPTMnet; Q9H7E2; -.
DR MetOSite; Q9H7E2; -.
DR PhosphoSitePlus; Q9H7E2; -.
DR BioMuta; TDRD3; -.
DR DMDM; 29337133; -.
DR EPD; Q9H7E2; -.
DR jPOST; Q9H7E2; -.
DR MassIVE; Q9H7E2; -.
DR MaxQB; Q9H7E2; -.
DR PaxDb; Q9H7E2; -.
DR PeptideAtlas; Q9H7E2; -.
DR PRIDE; Q9H7E2; -.
DR ProteomicsDB; 81113; -. [Q9H7E2-1]
DR ProteomicsDB; 81114; -. [Q9H7E2-2]
DR ProteomicsDB; 81115; -. [Q9H7E2-3]
DR ABCD; Q9H7E2; 3 sequenced antibodies.
DR Antibodypedia; 24335; 148 antibodies from 23 providers.
DR DNASU; 81550; -.
DR Ensembl; ENST00000196169.7; ENSP00000196169.3; ENSG00000083544.16. [Q9H7E2-1]
DR Ensembl; ENST00000377881.8; ENSP00000367113.2; ENSG00000083544.16. [Q9H7E2-3]
DR Ensembl; ENST00000377894.6; ENSP00000367126.2; ENSG00000083544.16. [Q9H7E2-1]
DR Ensembl; ENST00000621840.4; ENSP00000477993.1; ENSG00000083544.16. [Q9H7E2-2]
DR Ensembl; ENST00000648252.1; ENSP00000498191.1; ENSG00000083544.16. [Q9H7E2-1]
DR GeneID; 81550; -.
DR KEGG; hsa:81550; -.
DR MANE-Select; ENST00000377881.8; ENSP00000367113.2; NM_001146070.2; NP_001139542.1. [Q9H7E2-3]
DR UCSC; uc001vhz.5; human. [Q9H7E2-1]
DR CTD; 81550; -.
DR DisGeNET; 81550; -.
DR GeneCards; TDRD3; -.
DR HGNC; HGNC:20612; TDRD3.
DR HPA; ENSG00000083544; Low tissue specificity.
DR MIM; 614392; gene.
DR neXtProt; NX_Q9H7E2; -.
DR OpenTargets; ENSG00000083544; -.
DR PharmGKB; PA134962690; -.
DR VEuPathDB; HostDB:ENSG00000083544; -.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000155487; -.
DR HOGENOM; CLU_022646_0_0_1; -.
DR InParanoid; Q9H7E2; -.
DR OMA; IHNSENF; -.
DR OrthoDB; 914913at2759; -.
DR PhylomeDB; Q9H7E2; -.
DR TreeFam; TF316491; -.
DR PathwayCommons; Q9H7E2; -.
DR SignaLink; Q9H7E2; -.
DR SIGNOR; Q9H7E2; -.
DR BioGRID-ORCS; 81550; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; TDRD3; human.
DR EvolutionaryTrace; Q9H7E2; -.
DR GeneWiki; TDRD3; -.
DR GenomeRNAi; 81550; -.
DR Pharos; Q9H7E2; Tbio.
DR PRO; PR:Q9H7E2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9H7E2; protein.
DR Bgee; ENSG00000083544; Expressed in calcaneal tendon and 195 other tissues.
DR ExpressionAtlas; Q9H7E2; baseline and differential.
DR Genevisible; Q9H7E2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0140225; C:DNA topoisomerase III-beta-TDRD3 complex; IPI:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IC:ComplexPortal.
DR CDD; cd04508; TUDOR; 1.
DR CDD; cd14282; UBA_TDRD3; 1.
DR Gene3D; 2.40.50.770; -; 1.
DR IDEAL; IID00499; -.
DR InterPro; IPR013894; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041915; UBA_TDRD3.
DR Pfam; PF08585; RMI1_N; 1.
DR Pfam; PF00567; TUDOR; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00333; TUDOR; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..651
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000183163"
FT DOMAIN 193..233
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 555..615
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 234..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..651
FT /note="EBM motif; may mediate interaction with the EJC"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MAQVAGAALSQAGWYLSDEGIEACTSSPDKVNVNDIILIALNTDLRT
FT IGKKFLPSDINSGKVEKLEGPCVLQIQKIRNVAAPKDNEESQAAPRM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:18632687"
FT /id="VSP_037052"
FT VAR_SEQ 97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037053"
FT MUTAGEN 598
FT /note="E->K: Abolishes interaction with dimethylarginine-
FT containing protein motifs and reduces association with mRNA
FT stress granules."
FT /evidence="ECO:0000269|PubMed:18632687"
FT MUTAGEN 638..644
FT /note="RPTQQFY->EPTQQFE: Loss of interaction with the EJC."
FT /evidence="ECO:0000269|PubMed:20930030"
FT CONFLICT 101
FT /note="H -> R (in Ref. 6; AAH60876)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="P -> H (in Ref. 6; AAH60876)"
FT /evidence="ECO:0000305"
FT STRAND 1..21
FT /evidence="ECO:0007829|PDB:5GVD"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5GVD"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5GVD"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5GVD"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5GVD"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5GVD"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1WJI"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1WJI"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:1WJI"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:1WJI"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:3PNW"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:5YJ8"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:5YJ8"
FT STRAND 572..581
FT /evidence="ECO:0007829|PDB:5YJ8"
FT TURN 582..585
FT /evidence="ECO:0007829|PDB:5YJ8"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:5YJ8"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:5YJ8"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:5YJ8"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:5YJ8"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:5YJ8"
SQ SEQUENCE 651 AA; 73185 MW; 1D82F323F6EF4B05 CRC64;
MLRLQMTDGH ISCTAVEFSY MSKISLNTPP GTKVKLSGIV DIKNGFLLLN DSNTTVLGGE
VEHLIEKWEL QRSLSKHNRS NIGTEGGPPP FVPFGQKCVS HVQVDSRELD RRKTLQVTMP
VKPTNDNDEF EKQRTAAIAE VAKSKETKTF GGGGGGARSN LNMNAAGNRN REVLQKEKST
KSEGKHEGVY RELVDEKALK HITEMGFSKE ASRQALMDNG NNLEAALNVL LTSNKQKPVM
GPPLRGRGKG RGRIRSEDEE DLGNARPSAP STLFDFLESK MGTLNVEEPK SQPQQLHQGQ
YRSSNTEQNG VKDNNHLRHP PRNDTRQPRN EKPPRFQRDS QNSKSVLEGS GLPRNRGSER
PSTSSVSEVW AEDRIKCDRP YSRYDRTKDT SYPLGSQHSD GAFKKRDNSM QSRSGKGPSF
AEAKENPLPQ GSVDYNNQKR GKRESQTSIP DYFYDRKSQT INNEAFSGIK IEKHFNVNTD
YQNPVRSNSF IGVPNGEVEM PLKGRRIGPI KPAGPVTAVP CDDKIFYNSG PKRRSGPIKP
EKILESSIPM EYAKMWKPGD ECFALYWEDN KFYRAEVEAL HSSGMTAVVK FIDYGNYEEV
LLSNIKPIQT EAWEEEGTYD QTLEFRRGGD GQPRRSTRPT QQFYQPPRAR N
