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Protein

Tudor domain-containing protein 3

Gene

Tdrd3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Names & Taxonomyi

Protein namesi
Recommended name:
Tudor domain-containing protein 3
Gene namesi
Name:Tdrd3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310126. Tdrd3.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Tudor domain-containing protein 3PRO_0000342365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ66HC1.
PRIDEiQ66HC1.

PTM databases

iPTMnetiQ66HC1.
PhosphoSiteiQ66HC1.

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. Interacts with POLR2A (via the C-terminal domain (CTD)).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi258345. 1 interaction.
STRINGi10116.ENSRNOP00000012440.

Structurei

3D structure databases

ProteinModelPortaliQ66HC1.
SMRiQ66HC1. Positions 194-243, 553-613.
ModBaseiSearch...
MobiDBiSearch...

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 EJCBy similarityAdd
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.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3683. Eukaryota.
ENOG4111KPK. LUCA.
HOGENOMiHOG000154539.
HOVERGENiHBG059153.
InParanoidiQ66HC1.
KOiK18404.
PhylomeDBiQ66HC1.

Family and domain databases

InterProiIPR013894. RMI1_N.
IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF08585. RMI1_N. 1 hit.
PF06003. SMN. 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]

Sequencei

Sequence statusi: Complete.

Q66HC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVQMTDGH TSCTAVEFSY ISKISLNTPP GTKVKLSGTV DIKNGFLLLS
60 70 80 90 100
DSNTTVLGGE VEHLIDKWAL QRSLLKHNRS NIGAEGGPPP FLPFGQKCAS
110 120 130 140 150
TVQVDSRELD RRKTLQVSLP AKPTNDNDEF EKQRTAAIAE VAKSKETKTF
160 170 180 190 200
GGGGGGVRSH LNIGAGGHRN REVSQKEKAS KSESKNEGVY RELVDEKALK
210 220 230 240 250
HITEMGFSKE ASRQALMDNA NNLEAALNVL LNSSKQKPVV GPPPRGRGKG
260 270 280 290 300
RGRVRSEDEE DLGNARPSAP STLFDFLESK MGTLNMEEPR SQPQHLYQGQ
310 320 330 340 350
HRVSNTEQNG IKDGNQSRHL PRNDPRQPRN EKPPRFQRDT PNLKSALENS
360 370 380 390 400
VLSRNRGSER PSSSSGSDVW AEERIKCDRP YSRYDRTKDA SYPLGFQHND
410 420 430 440 450
GAFKRRDNSM QNRSGRGPLY AEAKENPHPS EFVDYNNQKR GKRENQTSNP
460 470 480 490 500
DHFYDRKSRT MNSEAFSGLK IEKHFSANTD YQNPVQSNSF VGVPNGETDM
510 520 530 540 550
PMKGRRVGPI KPAGPVTAVP YDDKIFYNSG PKRRSGPIKP EKVIESSIPV
560 570 580 590 600
EYAKMWKPGD ECFALYWEDN KFYRAEVEAL HSSGMTAVVK FTDYGNYEEV
610 620 630 640 650
LLSNIKPVQT EAWEEEGTYD HTIEFRRGGD GQPRRSTRPT QQFYQPPRAR

N
Length:651
Mass (Da):73,028
Last modified:October 11, 2004 - v1
Checksum:i226109C2519D3D59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081929 mRNA. Translation: AAH81929.1.
RefSeqiNP_001012043.1. NM_001012043.1.
UniGeneiRn.18991.

Genome annotation databases

GeneIDi306066.
KEGGirno:306066.
UCSCiRGD:1310126. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081929 mRNA. Translation: AAH81929.1.
RefSeqiNP_001012043.1. NM_001012043.1.
UniGeneiRn.18991.

3D structure databases

ProteinModelPortaliQ66HC1.
SMRiQ66HC1. Positions 194-243, 553-613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi258345. 1 interaction.
STRINGi10116.ENSRNOP00000012440.

PTM databases

iPTMnetiQ66HC1.
PhosphoSiteiQ66HC1.

Proteomic databases

PaxDbiQ66HC1.
PRIDEiQ66HC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi306066.
KEGGirno:306066.
UCSCiRGD:1310126. rat.

Organism-specific databases

CTDi81550.
RGDi1310126. Tdrd3.

Phylogenomic databases

eggNOGiKOG3683. Eukaryota.
ENOG4111KPK. LUCA.
HOGENOMiHOG000154539.
HOVERGENiHBG059153.
InParanoidiQ66HC1.
KOiK18404.
PhylomeDBiQ66HC1.

Miscellaneous databases

PROiQ66HC1.

Family and domain databases

InterProiIPR013894. RMI1_N.
IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF08585. RMI1_N. 1 hit.
PF06003. SMN. 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]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTDRD3_RAT
AccessioniPrimary (citable) accession number: Q66HC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.