TDRKH_HUMAN - dbPTM
TDRKH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDRKH_HUMAN
UniProt AC Q9Y2W6
Protein Name Tudor and KH domain-containing protein
Gene Name TDRKH
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Cytoplasm . Mitochondrion . Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Colocalizes with pi- and piP-bodies, a subset of the nuage which contain
Protein 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..
Protein Sequence MSTERTSWTSLSTIQKIALGLGIPASATVAYILYRRYRESREERLTFVGEDDIEIEMRVPQEAVKLIIGRQGANIKQLRKQTGARIDVDTEDVGDERVLLISGFPVQVCKAKAAIHQILTENTPVSEQLSVPQRSVGRIIGRGGETIRSICKASGAKITCDKESEGTLLLSRLIKISGTQKEVAAAKHLILEKVSEDEELRKRIAHSAETRVPRKQPISVRREDMTEPGGAGEPALWKNTSSSMEPTAPLVTPPPKGGGDMAVVVSKEGSWEKPSDDSFQKSEAQAIPEMPMFEIPSPDFSFHADEYLEVYVSASEHPNHFWIQIVGSRSLQLDKLVNEMTQHYENSVPEDLTVHVGDIVAAPLPTNGSWYRARVLGTLENGNLDLYFVDFGDNGDCPLKDLRALRSDFLSLPFQAIECSLARIAPSGDQWEEEALDEFDRLTHCADWKPLVAKISSYVQTGISTWPKIYLYDTSNGKKLDIGLELVHKGYAIELPEDIEENRAVPDMLKDMATETDASLSTLLTETKKSSGEITHTLSCLSLSEAASMSGDDNLEDDYLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MSTERTSWTSLSTI
-CCCCCCCCCCHHHH		34.2824719451
26PhosphorylationLGLGIPASATVAYIL
HCCCCCHHHHHHHHH		21.0824719451
31PhosphorylationPASATVAYILYRRYR
CHHHHHHHHHHHHHH		6.26-
65UbiquitinationRVPQEAVKLIIGRQG
ECCHHHHHHHHCCCC		40.8025621951
76UbiquitinationGRQGANIKQLRKQTG
CCCCCCHHHHHHHHC		42.9925621951
90PhosphorylationGARIDVDTEDVGDER
CCCCCCCCCCCCCCE		33.65-
110UbiquitinationGFPVQVCKAKAAIHQ
CCCHHHHHHHHHHHH		54.8125621951
112UbiquitinationPVQVCKAKAAIHQIL
CHHHHHHHHHHHHHH		24.6825621951
114 (in isoform 3)Phosphorylation-10.0917322306
142MethylationSVGRIIGRGGETIRS
HHHHHHCCCHHHHHH		39.26115918353
146PhosphorylationIIGRGGETIRSICKA
HHCCCHHHHHHHHHH		25.6023403867
152UbiquitinationETIRSICKASGAKIT
HHHHHHHHHCCCEEE		43.8725621951
159PhosphorylationKASGAKITCDKESEG
HHCCCEEEECCCCCH		17.5917322306
162UbiquitinationGAKITCDKESEGTLL
CCEEEECCCCCHHEH		66.35-
164PhosphorylationKITCDKESEGTLLLS
EEEECCCCCHHEHHH		47.2522817900
171PhosphorylationSEGTLLLSRLIKISG
CCHHEHHHHHHHHCC		25.6321712546
175UbiquitinationLLLSRLIKISGTQKE
EHHHHHHHHCCCHHH		35.1025621951
181UbiquitinationIKISGTQKEVAAAKH
HHHCCCHHHHHHHHH		54.7325621951
187UbiquitinationQKEVAAAKHLILEKV
HHHHHHHHHHHHHHC		33.9325621951
193UbiquitinationAKHLILEKVSEDEEL
HHHHHHHHCCCCHHH		47.8425621951
201MethylationVSEDEELRKRIAHSA
CCCCHHHHHHHHHHC		29.50115918357
240PhosphorylationEPALWKNTSSSMEPT
CCCCCCCCCCCCCCC		26.6822199227
241PhosphorylationPALWKNTSSSMEPTA
CCCCCCCCCCCCCCC		29.7922199227
242PhosphorylationALWKNTSSSMEPTAP
CCCCCCCCCCCCCCC		31.5022199227
243PhosphorylationLWKNTSSSMEPTAPL
CCCCCCCCCCCCCCC		27.2522199227
247PhosphorylationTSSSMEPTAPLVTPP
CCCCCCCCCCCCCCC		27.8327251275
252PhosphorylationEPTAPLVTPPPKGGG
CCCCCCCCCCCCCCC		37.4522199227
256UbiquitinationPLVTPPPKGGGDMAV
CCCCCCCCCCCCEEE		75.7825621951
267UbiquitinationDMAVVVSKEGSWEKP
CEEEEEECCCCCCCC		55.2625621951
270PhosphorylationVVVSKEGSWEKPSDD
EEEECCCCCCCCCCC		32.9030108239
275PhosphorylationEGSWEKPSDDSFQKS
CCCCCCCCCCCCCHH		66.1823663014
278PhosphorylationWEKPSDDSFQKSEAQ
CCCCCCCCCCHHHHH		34.2723898821
282PhosphorylationSDDSFQKSEAQAIPE
CCCCCCHHHHHHCCC		27.64-
456PhosphorylationKPLVAKISSYVQTGI
HHHHHHHHHHHHHCC		18.2128348404
457PhosphorylationPLVAKISSYVQTGIS
HHHHHHHHHHHHCCC		32.5624719451
458PhosphorylationLVAKISSYVQTGIST
HHHHHHHHHHHCCCC		6.9826471730
461PhosphorylationKISSYVQTGISTWPK
HHHHHHHHCCCCCCE		26.8328348404
470PhosphorylationISTWPKIYLYDTSNG
CCCCCEEEEEECCCC		12.82-
478AcetylationLYDTSNGKKLDIGLE
EEECCCCEEEEEEEE		55.1825953088
479UbiquitinationYDTSNGKKLDIGLEL
EECCCCEEEEEEEEE		53.4425621951
510UbiquitinationRAVPDMLKDMATETD
CCCCHHHHHHHHHCC		38.5325621951
519PhosphorylationMATETDASLSTLLTE
HHHHCCHHHHHHHHH		26.1827251275
529UbiquitinationTLLTETKKSSGEITH
HHHHHCCCCCCCCEE		58.2225621951
537PhosphorylationSSGEITHTLSCLSLS
CCCCCEEEEEEEEHH		16.2426074081
539PhosphorylationGEITHTLSCLSLSEA
CCCEEEEEEEEHHHH		17.7326074081
542PhosphorylationTHTLSCLSLSEAASM
EEEEEEEEHHHHHHH		33.8926074081
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TDRKH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDRKH_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TDRKH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TDRKH_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TDRKH_HUMAN

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Related Literatures of Post-Translational Modification

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