TDRD9_HUMAN - dbPTM
TDRD9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDRD9_HUMAN
UniProt AC Q8NDG6
Protein Name ATP-dependent RNA helicase TDRD9 {ECO:0000305}
Gene Name TDRD9 {ECO:0000312|HGNC:HGNC:20122}
Organism Homo sapiens (Human).
Sequence Length 1382
Subcellular Localization Cytoplasm . Nucleus . Component of the nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs. PI
Protein Description ATP-binding RNA helicase required during spermatogenesis. [PubMed: 28536242 Required to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Acts downstream of piRNA biogenesis: exclusively required for transposon silencing in the nucleus, suggesting that it acts as a nuclear effector in the nucleus together with PIWIL4.]
Protein Sequence MLRKLTIEQINDWFTIGKTVTNVELLGAPPAFPAGAAREEVQRQDVAPGAGPAAQAPALAQAPARPAAAFERSLSQRSSEVEYINKYRQLEAQELDVCRSVQPTSGPGPRPSLAKLSSVTCIPGTTYKYPDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATISCKEFADYFAVPVQNKMNPAYIFEVEGKPHSVEEYYLNDLEHIHHSKLSPHLLEEPVITKDIYEVAVSLIQMFDDLDMKESGNKAWSGAQFVLERSSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLVHKDFWDNSIPDHVVPEMLRCPLGSTILKVKLLDMGEPRALLATALSPPGLSDIERTILLLKEVGALAVSGQREDENPHDGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPFRQHLDGYRNKVNFSGSSKSDCIALVEAFKTWKACRQTGELRYPKDELNWGRLNYIQIKRIREVAELYEELKTRISQFNMHVDSRRPVMDQEYIYKQRFILQVVLAGAFYPNYFTFGQPDEEMAVRELAGKDPKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKAFVEFSRNPTERFKTLPAVYMAIKMSQLKVSLELSVHSAEEIEGKVQGMNVSKLRNTRVNVDFQKQTVDPMQVSFNTSDRSQTVTDLLLTIDVTEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPSAKSLVCGKHWSDGASQWFASLVSGCTLLVKVFSVVHSVLHVDVYQYSGVQDAINIRDVLIQQGYAELTEESYESKQSHEVLKGLFSKSVENMTDGSVPFPMKDDEKYLIRILLESFSTNKLGTPNCKAELHGPFNPYELKCHSLTRISKFRCVWIEKESINSVIISDAPEDLHQRMLVAASLSINATGSTMLLRETSLMPHIPGLPALLSMLFAPVIELRIDQNGKYYTGVLCGLGWNPATGASILPEHDMELAFDVQFSVEDVVEVNILRAAINKLVCDGPNGCKCLGPERVAQLQDIARQKLLGLFCQSKPREKIVPKWHEKPYEWNQVDPKLVMEQADRESSRGKNTFLYQLHKLVVLGT
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
86UbiquitinationSEVEYINKYRQLEAQ
HHHHHHHHHHHHHHH		32.05-
115UbiquitinationGPRPSLAKLSSVTCI
CCCCCHHHHCCCEEC		54.95-
117PhosphorylationRPSLAKLSSVTCIPG
CCCHHHHCCCEECCC		23.27-
120PhosphorylationLAKLSSVTCIPGTTY
HHHHCCCEECCCCCC		13.4829116813
128UbiquitinationCIPGTTYKYPDLPIS
ECCCCCCCCCCCCHH		48.49-
129PhosphorylationIPGTTYKYPDLPISR
CCCCCCCCCCCCHHH		7.4929116813
135PhosphorylationKYPDLPISRYKEEVV
CCCCCCHHHCCHHHH		27.8429116813
137PhosphorylationPDLPISRYKEEVVSL
CCCCHHHCCHHHHHH		18.8929116813
189UbiquitinationIVVTQPRKIGASSIA
EEECCCCCCCCHHHH		52.77-
232PhosphorylationTRLIYMTTGVLLQKI
CCHHHHHHHHHHHHH		14.57-
318UbiquitinationYIFEVEGKPHSVEEY
EEEEECCCCCCCEEE		26.50-
337UbiquitinationLEHIHHSKLSPHLLE
HHHHCCCCCCHHHHC		48.94-
440UbiquitinationSPVPGYRKIILSTNI
ECCCCCCEEEEECCC		26.14-
477PhosphorylationVCDEDTNYQSLRLSW
ECCCCCCCEEEEEEE		11.1127642862
487UbiquitinationLRLSWASKTSCNQRK
EEEEECCCCCCCCCC		36.39-
511UbiquitinationYCYRLVHKDFWDNSI
CHHHEECCCCCCCCC		47.33-
537UbiquitinationPLGSTILKVKLLDMG
CCCCCEEEEEEECCC		33.21-
539UbiquitinationGSTILKVKLLDMGEP
CCCEEEEEEECCCCC		41.57-
570UbiquitinationERTILLLKEVGALAV
HHHHHHHHHHCCEEE		50.77-
631PhosphorylationLIIAAALSLKNFFAM
HHHHHHHCCCCHHHC		32.3524719451
650UbiquitinationHLDGYRNKVNFSGSS
HHCCCCCCCCCCCCC		29.56-
658UbiquitinationVNFSGSSKSDCIALV
CCCCCCCHHHHHHHH		52.60-
669UbiquitinationIALVEAFKTWKACRQ
HHHHHHHHHHHHHHH		61.60-
684UbiquitinationTGELRYPKDELNWGR
HCCCCCCHHHCCCCC		55.70-
694PhosphorylationLNWGRLNYIQIKRIR
CCCCCCCHHHHHHHH		9.97-
698UbiquitinationRLNYIQIKRIREVAE
CCCHHHHHHHHHHHH		25.95-
707PhosphorylationIREVAELYEELKTRI
HHHHHHHHHHHHHHH		10.00-
711UbiquitinationAELYEELKTRISQFN
HHHHHHHHHHHHHHC		38.75-
735UbiquitinationMDQEYIYKQRFILQV
CCHHHHHHHHHHHHH		25.99-
803UbiquitinationFRQCGQVKSIVFDGA
HHHHCCCEEEEEECC		26.95-
811UbiquitinationSIVFDGAKAFVEFSR
EEEEECCHHHEEECC		48.14-
835AcetylationPAVYMAIKMSQLKVS
HHHHHHHHHHHCEEE		23.987338421
837PhosphorylationVYMAIKMSQLKVSLE
HHHHHHHHHCEEEEE		27.62-
842PhosphorylationKMSQLKVSLELSVHS
HHHHCEEEEEEEECC		17.9724719451
863PhosphorylationKVQGMNVSKLRNTRV
EECCCCHHHHCCCEE		22.4422210691
864UbiquitinationVQGMNVSKLRNTRVN
ECCCCHHHHCCCEEE		47.38-
876UbiquitinationRVNVDFQKQTVDPMQ
EEECEECCCCCCCEE		48.18-
878PhosphorylationNVDFQKQTVDPMQVS
ECEECCCCCCCEEEE		33.6324043423
885PhosphorylationTVDPMQVSFNTSDRS
CCCCEEEEECCCCCC		8.9024043423
888PhosphorylationPMQVSFNTSDRSQTV
CEEEEECCCCCCCCH		29.9624043423
889PhosphorylationMQVSFNTSDRSQTVT
EEEEECCCCCCCCHH		31.9324043423
1101UbiquitinationKQSHEVLKGLFSKSV
HHHHHHHHHHHHCCC		59.76-
1105PhosphorylationEVLKGLFSKSVENMT
HHHHHHHHCCCCCCC		29.1224719451
1106UbiquitinationVLKGLFSKSVENMTD
HHHHHHHCCCCCCCC		51.71-
1146UbiquitinationKLGTPNCKAELHGPF
CCCCCCCEEECCCCC		52.08-
1159UbiquitinationPFNPYELKCHSLTRI
CCCHHHCCCCCCCEE		20.26-
1168MethylationHSLTRISKFRCVWIE
CCCCEEEEEEEEEEE		34.1623644510
1168"N6,N6-dimethyllysine"HSLTRISKFRCVWIE
CCCCEEEEEEEEEEE		34.16-
1200PhosphorylationQRMLVAASLSINATG
HHHHHHHHCEECCCC		16.9522210691
1206PhosphorylationASLSINATGSTMLLR
HHCEECCCCCCEEEE		27.4622210691
1208PhosphorylationLSINATGSTMLLRET
CEECCCCCCEEEECC		13.2922210691
1295UbiquitinationILRAAINKLVCDGPN
HHHHHHHHHHCCCCC		35.86-
1305UbiquitinationCDGPNGCKCLGPERV
CCCCCCCCCCCHHHH		33.61-
1322UbiquitinationLQDIARQKLLGLFCQ
HHHHHHHHHHHHHCC		39.88-
1331UbiquitinationLGLFCQSKPREKIVP
HHHHCCCCCHHHCCC		23.40-
1339UbiquitinationPREKIVPKWHEKPYE
CHHHCCCCCCCCCCC		50.73-
1343UbiquitinationIVPKWHEKPYEWNQV
CCCCCCCCCCCHHCC		39.76-
1345PhosphorylationPKWHEKPYEWNQVDP
CCCCCCCCCHHCCCH		44.6527642862
1353UbiquitinationEWNQVDPKLVMEQAD
CHHCCCHHHHHHHHH		49.61-
1367UbiquitinationDRESSRGKNTFLYQL
HHHHHCCCCCHHHHE		52.26-
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 TDRD9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDRD9_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 TDRD9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TDRD9_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TDRD9_HUMAN

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Related Literatures of Post-Translational Modification

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