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Q9H7E2

- TDRD3_HUMAN

UniProt

Q9H7E2 - TDRD3_HUMAN

Protein

Tudor domain-containing protein 3

Gene

TDRD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. methylated histone binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. regulation of RNA biosynthetic process Source: GOC

    Keywords - Molecular functioni

    Chromatin regulator

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tudor domain-containing protein 3
    Gene namesi
    Name:TDRD3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:20612. TDRD3.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi598 – 5981E → K: Abolishes interaction with dimethylarginine-containing protein motifs and reduces association with mRNA stress granules. 2 Publications
    Mutagenesisi638 – 6447RPTQQFY → EPTQQFE: Loss of interaction with the EJC. 1 Publication

    Organism-specific databases

    PharmGKBiPA134962690.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Tudor domain-containing protein 3PRO_0000183163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei256 – 2561Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H7E2.
    PaxDbiQ9H7E2.
    PRIDEiQ9H7E2.

    PTM databases

    PhosphoSiteiQ9H7E2.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9H7E2.
    BgeeiQ9H7E2.
    CleanExiHS_TDRD3.
    GenevestigatoriQ9H7E2.

    Organism-specific databases

    HPAiCAB034925.

    Interactioni

    Subunit structurei

    Component of mRNA stress granules. Interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN. Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A.4 Publications

    Protein-protein interaction databases

    BioGridi123514. 14 interactions.
    IntActiQ9H7E2. 1 interaction.
    STRINGi9606.ENSP00000196169.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi196 – 2038
    Turni204 – 2063
    Helixi209 – 21810
    Helixi223 – 23311
    Helixi550 – 5534
    Beta strandi561 – 5666
    Turni567 – 5704
    Beta strandi571 – 5799
    Beta strandi585 – 5917
    Turni592 – 5943
    Beta strandi597 – 6015
    Helixi602 – 6043
    Beta strandi605 – 6073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WJINMR-A194-243[»]
    2LTONMR-A554-608[»]
    3PMTX-ray1.80A553-611[»]
    3PNWX-ray2.05C/F/I/L/O/R/U/X540-615[»]
    3S6WX-ray1.78A555-608[»]
    ProteinModelPortaliQ9H7E2.
    SMRiQ9H7E2. Positions 1-68, 194-243, 548-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H7E2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini193 – 23341UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini555 – 61561TudorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni631 – 65121EBM motif; may mediate interaction with the EJCAdd
    BLAST

    Domaini

    The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg-3', 2 tags for epigenetic transcriptional activation.1 Publication

    Sequence similaritiesi

    Contains 1 Tudor domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG300229.
    HOGENOMiHOG000154539.
    HOVERGENiHBG059153.
    InParanoidiQ9H7E2.
    OMAiCVLQIQK.
    OrthoDBiEOG7F7W8R.
    PhylomeDBiQ9H7E2.
    TreeFamiTF316491.

    Family and domain databases

    InterProiIPR002999. Tudor.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PfamiPF00567. TUDOR. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00333. TUDOR. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50304. TUDOR. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H7E2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLRLQMTDGH ISCTAVEFSY MSKISLNTPP GTKVKLSGIV DIKNGFLLLN    50
    DSNTTVLGGE VEHLIEKWEL QRSLSKHNRS NIGTEGGPPP FVPFGQKCVS 100
    HVQVDSRELD RRKTLQVTMP VKPTNDNDEF EKQRTAAIAE VAKSKETKTF 150
    GGGGGGARSN LNMNAAGNRN REVLQKEKST KSEGKHEGVY RELVDEKALK 200
    HITEMGFSKE ASRQALMDNG NNLEAALNVL LTSNKQKPVM GPPLRGRGKG 250
    RGRIRSEDEE DLGNARPSAP STLFDFLESK MGTLNVEEPK SQPQQLHQGQ 300
    YRSSNTEQNG VKDNNHLRHP PRNDTRQPRN EKPPRFQRDS QNSKSVLEGS 350
    GLPRNRGSER PSTSSVSEVW AEDRIKCDRP YSRYDRTKDT SYPLGSQHSD 400
    GAFKKRDNSM QSRSGKGPSF AEAKENPLPQ GSVDYNNQKR GKRESQTSIP 450
    DYFYDRKSQT INNEAFSGIK IEKHFNVNTD YQNPVRSNSF IGVPNGEVEM 500
    PLKGRRIGPI KPAGPVTAVP CDDKIFYNSG PKRRSGPIKP EKILESSIPM 550
    EYAKMWKPGD ECFALYWEDN KFYRAEVEAL HSSGMTAVVK FIDYGNYEEV 600
    LLSNIKPIQT EAWEEEGTYD QTLEFRRGGD GQPRRSTRPT QQFYQPPRAR 650
    N 651
    Length:651
    Mass (Da):73,185
    Last modified:March 1, 2001 - v1
    Checksum:i1D82F323F6EF4B05
    GO
    Isoform 2 (identifier: Q9H7E2-2) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         97-97: Missing.

    Show »
    Length:650
    Mass (Da):73,057
    Checksum:i997FB4382F678469
    GO
    Isoform 3 (identifier: Q9H7E2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAQVAGAALS...NEESQAAPRM

    Show »
    Length:744
    Mass (Da):83,103
    Checksum:iCF27720025EFBD81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011H → R in AAH60876. (PubMed:15489334)Curated
    Sequence conflicti509 – 5091P → H in AAH60876. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAQVAGAALSQAGWYLSDEG IEACTSSPDKVNVNDIILIA LNTDLRTIGKKFLPSDINSG KVEKLEGPCVLQIQKIRNVA APKDNEESQAAPRM in isoform 3. 1 PublicationVSP_037052
    Alternative sequencei97 – 971Missing in isoform 2. 1 PublicationVSP_037053

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU643838 mRNA. Translation: ACC94142.1.
    AK024660 mRNA. Translation: BAB14950.1.
    BX537910 mRNA. Translation: CAD97894.1.
    AL354764, AL512666 Genomic DNA. Translation: CAH72281.1.
    AL512666, AL354764 Genomic DNA. Translation: CAH74000.1.
    CH471124 Genomic DNA. Translation: EAW52079.1.
    BC030514 mRNA. Translation: AAH30514.1.
    BC060876 mRNA. Translation: AAH60876.1.
    CCDSiCCDS53872.1. [Q9H7E2-3]
    CCDS9441.1. [Q9H7E2-1]
    RefSeqiNP_001139542.1. NM_001146070.1. [Q9H7E2-3]
    NP_001139543.1. NM_001146071.1. [Q9H7E2-1]
    NP_110421.1. NM_030794.2. [Q9H7E2-1]
    XP_005266615.1. XM_005266558.2. [Q9H7E2-3]
    UniGeneiHs.525061.

    Genome annotation databases

    EnsembliENST00000196169; ENSP00000196169; ENSG00000083544. [Q9H7E2-1]
    ENST00000377881; ENSP00000367113; ENSG00000083544. [Q9H7E2-1]
    ENST00000377894; ENSP00000367126; ENSG00000083544. [Q9H7E2-1]
    ENST00000535286; ENSP00000440190; ENSG00000083544. [Q9H7E2-3]
    GeneIDi81550.
    KEGGihsa:81550.
    UCSCiuc001vhz.4. human. [Q9H7E2-1]
    uc001vib.4. human. [Q9H7E2-2]
    uc010aeg.3. human. [Q9H7E2-3]

    Polymorphism databases

    DMDMi29337133.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU643838 mRNA. Translation: ACC94142.1 .
    AK024660 mRNA. Translation: BAB14950.1 .
    BX537910 mRNA. Translation: CAD97894.1 .
    AL354764 , AL512666 Genomic DNA. Translation: CAH72281.1 .
    AL512666 , AL354764 Genomic DNA. Translation: CAH74000.1 .
    CH471124 Genomic DNA. Translation: EAW52079.1 .
    BC030514 mRNA. Translation: AAH30514.1 .
    BC060876 mRNA. Translation: AAH60876.1 .
    CCDSi CCDS53872.1. [Q9H7E2-3 ]
    CCDS9441.1. [Q9H7E2-1 ]
    RefSeqi NP_001139542.1. NM_001146070.1. [Q9H7E2-3 ]
    NP_001139543.1. NM_001146071.1. [Q9H7E2-1 ]
    NP_110421.1. NM_030794.2. [Q9H7E2-1 ]
    XP_005266615.1. XM_005266558.2. [Q9H7E2-3 ]
    UniGenei Hs.525061.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WJI NMR - A 194-243 [» ]
    2LTO NMR - A 554-608 [» ]
    3PMT X-ray 1.80 A 553-611 [» ]
    3PNW X-ray 2.05 C/F/I/L/O/R/U/X 540-615 [» ]
    3S6W X-ray 1.78 A 555-608 [» ]
    ProteinModelPortali Q9H7E2.
    SMRi Q9H7E2. Positions 1-68, 194-243, 548-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123514. 14 interactions.
    IntActi Q9H7E2. 1 interaction.
    STRINGi 9606.ENSP00000196169.

    PTM databases

    PhosphoSitei Q9H7E2.

    Polymorphism databases

    DMDMi 29337133.

    Proteomic databases

    MaxQBi Q9H7E2.
    PaxDbi Q9H7E2.
    PRIDEi Q9H7E2.

    Protocols and materials databases

    DNASUi 81550.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000196169 ; ENSP00000196169 ; ENSG00000083544 . [Q9H7E2-1 ]
    ENST00000377881 ; ENSP00000367113 ; ENSG00000083544 . [Q9H7E2-1 ]
    ENST00000377894 ; ENSP00000367126 ; ENSG00000083544 . [Q9H7E2-1 ]
    ENST00000535286 ; ENSP00000440190 ; ENSG00000083544 . [Q9H7E2-3 ]
    GeneIDi 81550.
    KEGGi hsa:81550.
    UCSCi uc001vhz.4. human. [Q9H7E2-1 ]
    uc001vib.4. human. [Q9H7E2-2 ]
    uc010aeg.3. human. [Q9H7E2-3 ]

    Organism-specific databases

    CTDi 81550.
    GeneCardsi GC13P060970.
    HGNCi HGNC:20612. TDRD3.
    HPAi CAB034925.
    MIMi 614392. gene.
    neXtProti NX_Q9H7E2.
    PharmGKBi PA134962690.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300229.
    HOGENOMi HOG000154539.
    HOVERGENi HBG059153.
    InParanoidi Q9H7E2.
    OMAi CVLQIQK.
    OrthoDBi EOG7F7W8R.
    PhylomeDBi Q9H7E2.
    TreeFami TF316491.

    Miscellaneous databases

    ChiTaRSi TDRD3. human.
    EvolutionaryTracei Q9H7E2.
    GeneWikii TDRD3.
    GenomeRNAii 81550.
    NextBioi 71791.
    PROi Q9H7E2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H7E2.
    Bgeei Q9H7E2.
    CleanExi HS_TDRD3.
    Genevestigatori Q9H7E2.

    Family and domain databases

    InterProi IPR002999. Tudor.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    Pfami PF00567. TUDOR. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00333. TUDOR. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50304. TUDOR. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
      Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
      Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-598, INTERACTION WITH EWSR1; FMR1; FUS; SERBP1; EEF1A1 AND DDX3X OR DDX3Y.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal kidney.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Testis.
    7. "Tudor domains bind symmetrical dimethylated arginines."
      Cote J., Richard S.
      J. Biol. Chem. 280:28476-28483(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNRPB AND SNRPN.
    8. "Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP."
      Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., Meister G., Keidel E., Fischer U.
      Hum. Mol. Genet. 17:3236-3246(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYS-48-LINKED TETRA-UBIQUITIN; FMR1; FXR1 AND FXR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "SMG6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay."
      Kashima I., Jonas S., Jayachandran U., Buchwald G., Conti E., Lupas A.N., Izaurralde E.
      Genes Dev. 24:2440-2450(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE EXON JUNCTION COMPLEX, MUTAGENESIS OF 638-ARG--TYR-644.
    12. "TDRD3 is an effector molecule for arginine-methylated histone marks."
      Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T.
      Mol. Cell 40:1016-1023(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN TUDOR.
    13. "Solution structure of the UBA domain of human Tudor domain containing protein 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 194-243.

    Entry informationi

    Entry nameiTDRD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H7E2
    Secondary accession number(s): B2MWP9, Q53XA6, Q6P992
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3