CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023713
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tudor and KH domain-containing protein 
Protein Synonyms/Alias
 Tudor domain-containing protein 2 
Gene Name
 TDRKH 
Gene Synonyms/Alias
 TDRD2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65RVPQEAVKLIIGRQGubiquitination[1]
110GFPVQVCKAKAAIHQubiquitination[1]
112PVQVCKAKAAIHQILubiquitination[1, 2]
162GAKITCDKESEGTLLubiquitination[1]
181IKISGTQKEVAAAKHubiquitination[1]
187QKEVAAAKHLILEKVubiquitination[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]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules (By similarity). 
Sequence Annotation
 DOMAIN 52 115 KH 1.
 DOMAIN 124 190 KH 2.
 DOMAIN 353 412 Tudor.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Differentiation; Mitochondrion; Polymorphism; Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Spermatogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 561 AA 
Protein Sequence
MSTERTSWTS LSTIQKIALG LGIPASATVA YILYRRYRES REERLTFVGE DDIEIEMRVP 60
QEAVKLIIGR QGANIKQLRK QTGARIDVDT EDVGDERVLL ISGFPVQVCK AKAAIHQILT 120
ENTPVSEQLS VPQRSVGRII GRGGETIRSI CKASGAKITC DKESEGTLLL SRLIKISGTQ 180
KEVAAAKHLI LEKVSEDEEL RKRIAHSAET RVPRKQPISV RREDMTEPGG AGEPALWKNT 240
SSSMEPTAPL VTPPPKGGGD MAVVVSKEGS WEKPSDDSFQ KSEAQAIPEM PMFEIPSPDF 300
SFHADEYLEV YVSASEHPNH FWIQIVGSRS LQLDKLVNEM TQHYENSVPE DLTVHVGDIV 360
AAPLPTNGSW YRARVLGTLE NGNLDLYFVD FGDNGDCPLK DLRALRSDFL SLPFQAIECS 420
LARIAPSGDQ WEEEALDEFD RLTHCADWKP LVAKISSYVQ TGISTWPKIY LYDTSNGKKL 480
DIGLELVHKG YAIELPEDIE ENRAVPDMLK DMATETDASL STLLTETKKS SGEITHTLSC 540
LSLSEAASMS GDDNLEDDYL L 561 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1.
 IPR002999; Tudor. 
Pfam
 PF00013; KH_1
 PF00567; TUDOR 
SMART
 SM00322; KH
 SM00333; TUDOR 
PROSITE
 PS50084; KH_TYPE_1
 PS50304; TUDOR 
PRINTS