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Q9H7E2

- TDRD3_HUMAN

UniProt

Q9H7E2 - TDRD3_HUMAN

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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

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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB
Complete GO annotation...

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. 1 Publication
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 3
PRO_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. 13 interactions.
IntActiQ9H7E2. 1 interaction.
STRINGi9606.ENSP00000196169.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9H7E2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini193 – 23341UBA
Add
BLAST
Domaini555 – 61561Tudor
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni631 – 65121EBM motif; may mediate interaction with the EJC
Add
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.
Contains 1 UBA domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAQVAGAALSQAGWYLSDEG IEACTSSPDKVNVNDIILIA LNTDLRTIGKKFLPSDINSG KVEKLEGPCVLQIQKIRNVA APKDNEESQAAPRM in isoform 3.
VSP_037052
Alternative sequencei97 – 971Missing in isoform 2.
VSP_037053

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011H → R in AAH60876. 1 Publication
Sequence conflicti509 – 5091P → H in AAH60876. 1 Publication

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. 13 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 105 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

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