TDRD3_HUMAN - dbPTM
TDRD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDRD3_HUMAN
UniProt AC Q9H7E2
Protein Name Tudor domain-containing protein 3
Gene Name TDRD3
Organism Homo sapiens (Human).
Sequence Length 651
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules.
Protein 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..
Protein Sequence MLRLQMTDGHISCTAVEFSYMSKISLNTPPGTKVKLSGIVDIKNGFLLLNDSNTTVLGGEVEHLIEKWELQRSLSKHNRSNIGTEGGPPPFVPFGQKCVSHVQVDSRELDRRKTLQVTMPVKPTNDNDEFEKQRTAAIAEVAKSKETKTFGGGGGGARSNLNMNAAGNRNREVLQKEKSTKSEGKHEGVYRELVDEKALKHITEMGFSKEASRQALMDNGNNLEAALNVLLTSNKQKPVMGPPLRGRGKGRGRIRSEDEEDLGNARPSAPSTLFDFLESKMGTLNVEEPKSQPQQLHQGQYRSSNTEQNGVKDNNHLRHPPRNDTRQPRNEKPPRFQRDSQNSKSVLEGSGLPRNRGSERPSTSSVSEVWAEDRIKCDRPYSRYDRTKDTSYPLGSQHSDGAFKKRDNSMQSRSGKGPSFAEAKENPLPQGSVDYNNQKRGKRESQTSIPDYFYDRKSQTINNEAFSGIKIEKHFNVNTDYQNPVRSNSFIGVPNGEVEMPLKGRRIGPIKPAGPVTAVPCDDKIFYNSGPKRRSGPIKPEKILESSIPMEYAKMWKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFIDYGNYEEVLLSNIKPIQTEAWEEEGTYDQTLEFRRGGDGQPRRSTRPTQQFYQPPRARN
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
27 (in isoform 3)Phosphorylation-43.6924719451
80PhosphorylationSLSKHNRSNIGTEGG
HHHHCCHHCCCCCCC		37.8120068231
83 (in isoform 3)Ubiquitination-23.20-
84PhosphorylationHNRSNIGTEGGPPPF
CCHHCCCCCCCCCCC		27.8820068231
97UbiquitinationPFVPFGQKCVSHVQV
CCCCCCHHHEEEEEE		36.66-
114PhosphorylationRELDRRKTLQVTMPV
CCCCCCCEEEEEECC		22.1728555341
122UbiquitinationLQVTMPVKPTNDNDE
EEEEECCCCCCCCHH		40.01-
128 (in isoform 3)Ubiquitination-65.90-
132UbiquitinationNDNDEFEKQRTAAIA
CCCHHHHHHHHHHHH		50.86-
147PhosphorylationEVAKSKETKTFGGGG
HHHHCCCCCCCCCCC		38.84-
148UbiquitinationVAKSKETKTFGGGGG
HHHCCCCCCCCCCCC		42.84-
149PhosphorylationAKSKETKTFGGGGGG
HHCCCCCCCCCCCCC		34.63-
159PhosphorylationGGGGGARSNLNMNAA
CCCCCHHHCCCCCCC		45.17-
182PhosphorylationQKEKSTKSEGKHEGV
HHHHCCCCCCCCHHH		52.2321945579
190PhosphorylationEGKHEGVYRELVDEK
CCCCHHHHHHHCCHH		14.8221945579
190 (in isoform 3)Ubiquitination-14.82-
209AcetylationITEMGFSKEASRQAL
HHHCCCCHHHHHHHH		55.8526051181
209UbiquitinationITEMGFSKEASRQAL
HHHCCCCHHHHHHHH		55.85-
225 (in isoform 3)Ubiquitination-22.03-
245MethylationPVMGPPLRGRGKGRG
CCCCCCCCCCCCCCC		38.2454559919
247MethylationMGPPLRGRGKGRGRI
CCCCCCCCCCCCCCC		36.9054559927
256PhosphorylationKGRGRIRSEDEEDLG
CCCCCCCCCCHHHHC		47.2130266825
268PhosphorylationDLGNARPSAPSTLFD
HHCCCCCCCCHHHHH		47.4630266825
271PhosphorylationNARPSAPSTLFDFLE
CCCCCCCHHHHHHHH		37.1429978859
272PhosphorylationARPSAPSTLFDFLES
CCCCCCHHHHHHHHH		30.3129978859
279PhosphorylationTLFDFLESKMGTLNV
HHHHHHHHCCCCCCC		30.0423927012
280UbiquitinationLFDFLESKMGTLNVE
HHHHHHHCCCCCCCC		31.79-
281SulfoxidationFDFLESKMGTLNVEE
HHHHHHCCCCCCCCC		7.4521406390
283PhosphorylationFLESKMGTLNVEEPK
HHHHCCCCCCCCCCC		16.2027642862
290UbiquitinationTLNVEEPKSQPQQLH
CCCCCCCCCCCCCCC		66.07-
291PhosphorylationLNVEEPKSQPQQLHQ
CCCCCCCCCCCCCCC		58.7828348404
301PhosphorylationQQLHQGQYRSSNTEQ
CCCCCCCCCCCCCCC		21.20-
312UbiquitinationNTEQNGVKDNNHLRH
CCCCCCCCCCCCCCC		57.02-
325PhosphorylationRHPPRNDTRQPRNEK
CCCCCCCCCCCCCCC		34.4524719451
340PhosphorylationPPRFQRDSQNSKSVL
CCCCCCCCCCCCHHH		33.1923401153
343PhosphorylationFQRDSQNSKSVLEGS
CCCCCCCCCHHHCCC		20.7628857561
345PhosphorylationRDSQNSKSVLEGSGL
CCCCCCCHHHCCCCC		31.5818632687
349PhosphorylationNSKSVLEGSGLPRNR
CCCHHHCCCCCCCCC		23.8924719451
362PhosphorylationNRGSERPSTSSVSEV
CCCCCCCCCCCHHHH		47.3327251275
363PhosphorylationRGSERPSTSSVSEVW
CCCCCCCCCCHHHHH		27.9227251275
364PhosphorylationGSERPSTSSVSEVWA
CCCCCCCCCHHHHHH		32.8328555341
365PhosphorylationSERPSTSSVSEVWAE
CCCCCCCCHHHHHHH		29.7428555341
384PhosphorylationCDRPYSRYDRTKDTS
CCCCCCCCCCCCCCC		12.1127251275
388UbiquitinationYSRYDRTKDTSYPLG
CCCCCCCCCCCCCCC		60.96-
390PhosphorylationRYDRTKDTSYPLGSQ
CCCCCCCCCCCCCCC		31.54-
391PhosphorylationYDRTKDTSYPLGSQH
CCCCCCCCCCCCCCC		34.5828555341
394PhosphorylationTKDTSYPLGSQHSDG
CCCCCCCCCCCCCCC		8.6127642862
396PhosphorylationDTSYPLGSQHSDGAF
CCCCCCCCCCCCCCC		32.1923312004
399PhosphorylationYPLGSQHSDGAFKKR
CCCCCCCCCCCCCCC		30.0628555341
409PhosphorylationAFKKRDNSMQSRSGK
CCCCCCCCCCCCCCC		23.6130576142
412PhosphorylationKRDNSMQSRSGKGPS
CCCCCCCCCCCCCCC		21.55-
414PhosphorylationDNSMQSRSGKGPSFA
CCCCCCCCCCCCCHH		50.53-
418PhosphorylationQSRSGKGPSFAEAKE
CCCCCCCCCHHHHHC		29.7424719451
424UbiquitinationGPSFAEAKENPLPQG
CCCHHHHHCCCCCCC		49.91-
432PhosphorylationENPLPQGSVDYNNQK
CCCCCCCCCCCCCCC		13.4329507054
435PhosphorylationLPQGSVDYNNQKRGK
CCCCCCCCCCCCCCC		17.5428634298
438PhosphorylationGSVDYNNQKRGKRES
CCCCCCCCCCCCCCC		32.9327251275
439UbiquitinationSVDYNNQKRGKRESQ
CCCCCCCCCCCCCCC		66.30-
445PhosphorylationQKRGKRESQTSIPDY
CCCCCCCCCCCCCCH		42.6725159151
447PhosphorylationRGKRESQTSIPDYFY
CCCCCCCCCCCCHHH		37.5928102081
448PhosphorylationGKRESQTSIPDYFYD
CCCCCCCCCCCHHHC		25.2029978859
452PhosphorylationSQTSIPDYFYDRKSQ
CCCCCCCHHHCCCCC		9.9320873877
454PhosphorylationTSIPDYFYDRKSQTI
CCCCCHHHCCCCCEE		14.4920873877
455PhosphorylationSIPDYFYDRKSQTIN
CCCCHHHCCCCCEEC		41.4527251275
457UbiquitinationPDYFYDRKSQTINNE
CCHHHCCCCCEECCC		43.98-
458PhosphorylationDYFYDRKSQTINNEA
CHHHCCCCCEECCCC		33.1925159151
460PhosphorylationFYDRKSQTINNEAFS
HHCCCCCEECCCCCC		32.5329802988
470SumoylationNEAFSGIKIEKHFNV
CCCCCCEEEEEEECC		48.6228112733
470UbiquitinationNEAFSGIKIEKHFNV
CCCCCCEEEEEEECC		48.62-
473AcetylationFSGIKIEKHFNVNTD
CCCEEEEEEECCCCC		57.9026051181
473UbiquitinationFSGIKIEKHFNVNTD
CCCEEEEEEECCCCC		57.90-
479PhosphorylationEKHFNVNTDYQNPVR
EEEECCCCCCCCCCC		31.6221945579
481PhosphorylationHFNVNTDYQNPVRSN
EECCCCCCCCCCCCC		14.2521945579
487PhosphorylationDYQNPVRSNSFIGVP
CCCCCCCCCCEECCC		36.7425159151
489PhosphorylationQNPVRSNSFIGVPNG
CCCCCCCCEECCCCC		21.3525159151
524AcetylationTAVPCDDKIFYNSGP
EEEECCCEEEECCCC		22.8226051181
524UbiquitinationTAVPCDDKIFYNSGP
EEEECCCEEEECCCC		22.82-
525PhosphorylationAVPCDDKIFYNSGPK
EEECCCEEEECCCCC		5.9524719451
527PhosphorylationPCDDKIFYNSGPKRR
ECCCEEEECCCCCCC		16.3425159151
529PhosphorylationDDKIFYNSGPKRRSG
CCEEEECCCCCCCCC		45.1328555341
532UbiquitinationIFYNSGPKRRSGPIK
EEECCCCCCCCCCCC		65.06-
532 (in isoform 3)Ubiquitination-65.06-
535PhosphorylationNSGPKRRSGPIKPEK
CCCCCCCCCCCCHHH		53.6126657352
538PhosphorylationPKRRSGPIKPEKILE
CCCCCCCCCHHHHHH		15.4127251275
540PhosphorylationRRSGPIKPEKILESS
CCCCCCCHHHHHHCC		49.1624719451
541PhosphorylationRSGPIKPEKILESSI
CCCCCCHHHHHHCCC		47.9627251275
546PhosphorylationKPEKILESSIPMEYA
CHHHHHHCCCCHHHH		30.0729978859
547PhosphorylationPEKILESSIPMEYAK
HHHHHHCCCCHHHHH		22.7229978859
551PhosphorylationLESSIPMEYAKMWKP
HHCCCCHHHHHCCCC		36.6627251275
552PhosphorylationESSIPMEYAKMWKPG
HCCCCHHHHHCCCCC		12.7929978859
553PhosphorylationSSIPMEYAKMWKPGD
CCCCHHHHHCCCCCC		5.0724719451
572PhosphorylationLYWEDNKFYRAEVEA
EEECCCCEEHHHHHH		6.6427642862
574PhosphorylationWEDNKFYRAEVEALH
ECCCCEEHHHHHHHH		27.6627642862
582PhosphorylationAEVEALHSSGMTAVV
HHHHHHHHCCCEEEE		29.4527251275
618PhosphorylationEAWEEEGTYDQTLEF
CHHCCCCCCCCEEEE		27.49-
619PhosphorylationAWEEEGTYDQTLEFR
HHCCCCCCCCEEEEE		19.5322817900
622PhosphorylationEEGTYDQTLEFRRGG
CCCCCCCEEEEECCC		25.92-
628PhosphorylationQTLEFRRGGDGQPRR
CEEEEECCCCCCCCC		34.0024719451
636PhosphorylationGDGQPRRSTRPTQQF
CCCCCCCCCCCCCCC		30.0128555341
637PhosphorylationDGQPRRSTRPTQQFY
CCCCCCCCCCCCCCC		38.5728555341
640PhosphorylationPRRSTRPTQQFYQPP
CCCCCCCCCCCCCCC		31.5428555341
644PhosphorylationTRPTQQFYQPPRARN
CCCCCCCCCCCCCCC		18.7721945579
645PhosphorylationRPTQQFYQPPRARN-
CCCCCCCCCCCCCC-		42.6927642862
737Phosphorylation---------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------		27642862
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 TDRD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDRD3_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 TDRD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FMR1_HUMANFMR1physical
18664458
FXR1_HUMANFXR1physical
18664458
FXR2_HUMANFXR2physical
18664458
FMR1_HUMANFMR1physical
18632687
RL28_HUMANRPL28physical
18632687
RS6_HUMANRPS6physical
18632687
EWS_HUMANEWSR1physical
18632687
DDX3X_HUMANDDX3Xphysical
18632687
EF1A1_HUMANEEF1A1physical
18632687
FUS_HUMANFUSphysical
18632687
PAIRB_HUMANSERBP1physical
18632687
FXR1_HUMANFXR1physical
24778252
FXR2_HUMANFXR2physical
24778252
FMR1_HUMANFMR1physical
24778252
KCTD2_HUMANKCTD2physical
24778252
PABP1_HUMANPABPC1physical
20930030
MGN_HUMANMAGOHphysical
20930030
RBM8A_HUMANRBM8Aphysical
20930030
RPB1_HUMANPOLR2Aphysical
26700805
USP9X_HUMANUSP9Xphysical
28101374
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 TDRD3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory