CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
83IRNVAAPKDNEESQAubiquitination[1]
128TPPGTKVKLSGIVDIubiquitination[1]
190PFVPFGQKCVSHVQVubiquitination[1]
225NDNDEFEKQRTAAIAubiquitination[1]
532SVDYNNQKRGKRESQubiquitination[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
 IPR002999; Tudor.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 
Pfam
 PF00567; TUDOR
 PF00627; UBA 
SMART
 SM00333; TUDOR
 SM00165; UBA 
PROSITE
 PS50304; TUDOR
 PS50030; UBA 
PRINTS