| Tag | Content |
|---|
| CPLM ID | CPLM-021472 |
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 | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 83 | IRNVAAPKDNEESQA | ubiquitination | [1] | | 128 | TPPGTKVKLSGIVDI | ubiquitination | [1] | | 190 | PFVPFGQKCVSHVQV | ubiquitination | [1] | | 225 | NDNDEFEKQRTAAIA | ubiquitination | [1] | | 532 | SVDYNNQKRGKRESQ | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
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. |
Sequence Annotation | DOMAIN 193 233 UBA.
DOMAIN 555 615 Tudor.
MOD_RES 256 256 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 651 AA |
Protein Sequence | MAQVAGAALS QAGWYLSDEG IEACTSSPDK VNVNDIILIA LNTDLRTIGK KFLPSDINSG 60
KVEKLEGPCV LQIQKIRNVA APKDNEESQA APRMLRLQMT DGHISCTAVE FSYMSKISLN 120
TPPGTKVKLS GIVDIKNGFL LLNDSNTTVL GGEVEHLIEK WELQRSLSKH NRSNIGTEGG 180
PPPFVPFGQK CVSHVQVDSR ELDRRKTLQV TMPVKPTNDN DEFEKQRTAA IAEVAKSKET 240
KTFGGGGGGA RSNLNMNAAG NRNREVLQKE KSTKSEGKHE GVYRELVDEK ALKHITEMGF 300
SKEASRQALM DNGNNLEAAL NVLLTSNKQK PVMGPPLRGR GKGRGRIRSE DEEDLGNARP 360
SAPSTLFDFL ESKMGTLNVE EPKSQPQQLH QGQYRSSNTE QNGVKDNNHL RHPPRNDTRQ 420
PRNEKPPRFQ RDSQNSKSVL EGSGLPRNRG SERPSTSSVS EVWAEDRIKC DRPYSRYDRT 480
KDTSYPLGSQ HSDGAFKKRD NSMQSRSGKG PSFAEAKENP LPQGSVDYNN QKRGKRESQT 540
SIPDYFYDRK SQTINNEAFS GIKIEKHFNV NTDYQNPVRS NSFIGVPNGE VEMPLKGRRI 600
GPIKPAGPVT AVPCDDKIFY NSGPKRRSGP IKPEKILESS IPMEYAKMWK PGDECFALYW 660
EDNKFYRAEV EALHSSGMTA VVKFIDYGNY EEVLLSNIKP IQTEAWEEEG TYDQTLEFRR 720
GGDGQPRRST RPTQQFYQPP RARN 744 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0003682; F:chromatin binding; IDA:UniProtKB. GO:0035064; F:methylated histone residue binding; IDA:UniProtKB. GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |