Q91W18 (TDRD3_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tudor domain-containing protein 3 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 743 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. |
| Subunit structure | 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 By similarity. |
| Subcellular location | Cytoplasm By similarity. Nucleus By similarity. Note: Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules By similarity. |
| Domain | 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 similarities | Contains 1 Tudor domain. Contains 1 UBA domain. |
| Sequence caution | The sequence AAH05670.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH66144.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC26033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC28263.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Chromatin regulator |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW mRNA processingInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | RNA binding Inferred from electronic annotation. Source: InterPro chromatin bindingInferred from sequence or structural similarity. Source: UniProtKB methylated histone residue bindingInferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q91W18-1) 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. | ||||||
| Isoform 2 (identifier: Q91W18-2) The sequence of this isoform differs from the canonical sequence as follows: 706-743: EEEGTYDHTIEFRRGGDGQPRRSTRPTQQFYQPPRARN → VRDPNSVQRLL | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q91W18-3) The sequence of this isoform differs from the canonical sequence as follows: 1-14: MAEVSGAALSQAGW → MLFILFNR | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||
Molecule processing | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 743 | 743 | Tudor domain-containing protein 3 | PRO_0000183164 | |||||||||||||||||
Regions | |||||||||||||||||||||
| Domain | 286 – 326 | 41 | UBA | ||||||||||||||||||
| Domain | 647 – 707 | 61 | Tudor | ||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||
| Modified residue | 349 | 1 | Phosphoserine By similarity | ||||||||||||||||||
Natural variations | |||||||||||||||||||||
| Alternative sequence | 1 – 14 | 14 | MAEVS…SQAGW → MLFILFNR in isoform 3. | VSP_037054 | |||||||||||||||||
| Alternative sequence | 706 – 743 | 38 | EEEGT…PRARN → VRDPNSVQRLL in isoform 2. | VSP_034485 | |||||||||||||||||
Experimental info | |||||||||||||||||||||
| Sequence conflict | 8 | 1 | A → G in BAC28263. Ref.1 | ||||||||||||||||||
| Sequence conflict | 57 | 1 | I → V in AAH66144. Ref.3 | ||||||||||||||||||
| Sequence conflict | 350 | 1 | E → V in BAC28263. Ref.1 | ||||||||||||||||||
| Sequence conflict | 365 | 1 | T → M in AAH66144. Ref.3 | ||||||||||||||||||
| Sequence conflict | 375 | 1 | G → R in AAH66144. Ref.3 | ||||||||||||||||||
| Sequence conflict | 408 | 1 | T → S in AAH05670. Ref.3 | ||||||||||||||||||
| Sequence conflict | 469 | 1 | K → R in AAH05670. Ref.3 | ||||||||||||||||||
| Sequence conflict | 489 | 1 | L → F in AAH05670. Ref.3 | ||||||||||||||||||
| Sequence conflict | 559 | 1 | V → F in AAH05670. Ref.3 | ||||||||||||||||||
| Sequence conflict | 576 | 1 | R → S in AAH05670. Ref.3 | ||||||||||||||||||
| Sequence conflict | 679 | 1 | A → E in BAC28263. Ref.1 | ||||||||||||||||||
| Sequence conflict | 717 | 1 | F → L in AAH66144. Ref.3 | ||||||||||||||||||
Secondary structure | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| Beta strand | 653 – 657 | 5 | |||||||||||||||||||
| Turn | 659 – 661 | 3 | |||||||||||||||||||
| Beta strand | 664 – 672 | 9 | |||||||||||||||||||
| Beta strand | 678 – 683 | 6 | |||||||||||||||||||
| Beta strand | 689 – 693 | 5 | |||||||||||||||||||
| Helix | 694 – 696 | 3 | |||||||||||||||||||
| Beta strand | 697 – 699 | 3 | |||||||||||||||||||
Sequences
| ||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-743 (ISOFORM 2). Strain: C57BL/6J. Tissue: Lung and Skin. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. |
| [3] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6J. Tissue: Embryo and Mammary tumor. |
| [4] | "Solution structure of the Tudor domain of Tudor domain containing protein 3 from mouse." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 646-699. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AK028617 mRNA. Translation: BAC26033.1. Different initiation. AK033390 mRNA. Translation: BAC28263.1. Different initiation. AC154562 Genomic DNA. No translation available. CT010453 Genomic DNA. No translation available. BC005670 mRNA. Translation: AAH05670.3. Different initiation. BC066144 mRNA. Translation: AAH66144.1. Different initiation. | ||||||||||||
| IPI | IPI00227152. IPI00896611. IPI01008137. | ||||||||||||
| RefSeq | NP_766193.3. NM_172605.3. | ||||||||||||
| UniGene | Mm.35168. Mm.474717. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q91W18. | ||||||||||||
| SMR | Q91W18. Positions 2-164, 287-337, 645-705. | ||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q91W18. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q91W18. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000168275; ENSMUSP00000129019; ENSMUSG00000022019. ENSMUST00000169504; ENSMUSP00000131542; ENSMUSG00000022019. ENSMUST00000170865; ENSMUSP00000126189; ENSMUSG00000022019. | ||||||||||||
| GeneID | 219249. | ||||||||||||
| KEGG | mmu:219249. | ||||||||||||
| UCSC | uc007uuf.2. mouse. uc007uug.2. mouse. uc011zpb.1. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 81550. | ||||||||||||
| MGI | MGI:2444023. Tdrd3. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | roNOG11489. | ||||||||||||
| GeneTree | ENSGT00440000038925. | ||||||||||||
| HOGENOM | HBG402882. | ||||||||||||
| HOVERGEN | HBG059153. | ||||||||||||
| InParanoid | Q91W18. | ||||||||||||
| OrthoDB | EOG4WM4T9. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q91W18. | ||||||||||||
| Bgee | Q91W18. | ||||||||||||
| CleanEx | MM_TDRD3. | ||||||||||||
| Genevestigator | Q91W18. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR013894. DUF1767. IPR010304. Survival_motor_neuron. IPR002999. Tudor. IPR018351. Tudor_subgr. IPR009060. UBA-like. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view] | ||||||||||||
| Pfam | PF08585. DUF1767. 1 hit. PF06003. SMN. 1 hit. PF00627. UBA. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00333. TUDOR. 1 hit. SM00165. UBA. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF46934. UBA_like. 1 hit. | ||||||||||||
| PROSITE | PS50304. TUDOR. 1 hit. PS50030. UBA. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 376651. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | TDRD3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q91W18 Secondary accession number(s): E9Q2Q4 Q8C1A4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with