| Tag | Content |
|---|
| CPLM ID | CPLM-018478 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tudor domain-containing protein 3 |
Protein Synonyms/Alias | |
Gene Name | Tdrd3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 405 | NAEQNGMKDGTQSRH | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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). |
Sequence Annotation | DOMAIN 286 326 UBA.
DOMAIN 647 707 Tudor.
MOD_RES 349 349 Phosphoserine (By similarity). |
Keyword | 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 743 AA |
Protein Sequence | MAEVSGAALS QAGWYLSDEG VEACTSSPGK GSINDIILIA LNTDLRTIGK KFLPSDINGG 60
KVEKLEGPCV LQIQKVRNVA APKDNEESQA APRMLRVQMT DGHTSCTAVE FSYISKISLN 120
TPPGTKVKLS GTVDIKNGFL LLSDSNTTVL GGEVEHLIDK WALQRSLLKH NRSNIGAEGG 180
PPPFLPFGQK CASNVQVDSR ELDRRKTLQV SLPAKPANDN DEFEKQRTAA IAEVAKSKET 240
KTFGGGGGGA RSNLNIGAAG HRNREVLQKE KASKSESKNE GVYRELVDEK ALKHITEMGF 300
SKEASRQALM DNANNLEAAL NVLLNSSKQK PAVGPPARGR GKGRGRGRSE DEEDLGTARP 360
SAPSTLFDFL ESKMGTLNVE EPKSQPQHLH QGQHRGWNAE QNGMKDGTQS RHLPRNDTRQ 420
PRNERPPRFQ KDTPTSKSTV ENSVLSRNRG SERPSSSSGS DVWAEERIKC DRPYSRYDRT 480
KDASHPLGLQ HNDGAFKKRE NSMQNRPGRG PLYAEAKENP LPPEFVDYNN QRRGRRENQT 540
GHPDHCYERK PRTMNSEAVS GLKIEKHFSV NTDYPRPVQS NSLGVPNGET APPLKGRRVG 600
PIKSAGPVTA VPYDDKIFYN SGPKRRSGPI KPEKVIESSI PVEYAKVWKP GDECFALYWE 660
DNKFYRAEVE ALHSSGMTAV VKFTDYGNYE EVLLSNIKPV QTEAWEEEGT YDHTIEFRRG 720
GDGQPRRSTR PTQQFYQPPR ARN 743 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0003682; F:chromatin binding; ISS:UniProtKB. GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. GO:0003723; F:RNA binding; IEA:InterPro. GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0006397; P:mRNA processing; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |