TDRD7_HUMAN - dbPTM
TDRD7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDRD7_HUMAN
UniProt AC Q8NHU6
Protein Name Tudor domain-containing protein 7
Gene Name TDRD7
Organism Homo sapiens (Human).
Sequence Length 1098
Subcellular Localization Cytoplasm . Localizes to cytoplasmic RNA granules. Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. De
Protein Description Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis..
Protein Sequence MLEGDLVSKMLRAVLQSHKNGVALPRLQGEYRSLTGDWIPFKQLGFPTLEAYLRSVPAVVRIETSRSGEITCYAMACTETARIAQLVARQRSSKRKTGRQVNCQMRVKKTMPFFLEGKPKATLRQPGFASNFSVGKKPNPAPLRDKGNSVGVKPDAEMSPYMLHTTLGNEAFKDIPVQRHVTMSTNNRFSPKASLQPPLQMHLSRTSTKEMSDNLNQTVEKPNVKPPASYTYKMDEVQNRIKEILNKHNNGIWISKLPHFYKELYKEDLNQGILQQFEHWPHICTVEKPCSGGQDLLLYPAKRKQLLRSELDTEKVPLSPLPGPKQTPPLKGCPTVMAGDFKEKVADLLVKYTSGLWASALPKAFEEMYKVKFPEDALKNLASLSDVCSIDYISGNPQKAILYAKLPLPTDKIQKDAGQAHGDNDIKAMVEQEYLQVEESIAESANTFMEDITVPPLMIPTEASPSVLVVELSNTNEVVIRYVGKDYSAAQELMEDEMKEYYSKNPKITPVQAVNVGQLLAVNAEEDAWLRAQVISTEENKIKVCYVDYGFSENVEKSKAYKLNPKFCSLSFQATKCKLAGLEVLSDDPDLVKVVESLTCGKIFAVEILDKADIPLVVLYDTSGEDDININATCLKAICDKSLEVHLQVDAMYTNVKVTNICSDGTLYCQVPCKGLNKLSDLLRKIEDYFHCKHMTSECFVSLPFCGKICLFHCKGKWLRVEITNVHSSRALDVQFLDSGTVTSVKVSELREIPPRFLQEMIAIPPQAIKCCLADLPQSIGMWTPDAVLWLRDSVLNCSDCSIKVTKVDETRGIAHVYLFTPKNFPDPHRSINRQITNADLWKHQKDVFLSAISSGADSPNSKNGNMPMSGNTGENFRKNLTDVIKKSMVDHTSAFSTEELPPPVHLSKPGEHMDVYVPVACHPGYFVIQPWQEIHKLEVLMEEMILYYSVSEERHIAVEKDQVYAAKVENKWHRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPLVDMFRKLPFQAVTAQLAGVKCNQWSEEASMVFRNHVEKKPLVALVQTVIENANPWDRKVVVYLVDTSLPDTDTWIHDFMSEYLIELSKVN
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
8PhosphorylationMLEGDLVSKMLRAVL
CCCHHHHHHHHHHHH		21.46-
19UbiquitinationRAVLQSHKNGVALPR
HHHHHHCCCCCCCCC		61.7229967540
35UbiquitinationQGEYRSLTGDWIPFK
CCCHHHCCCCCCCHH		34.0529967540
55PhosphorylationTLEAYLRSVPAVVRI
CHHHHHHHCCEEEEE		29.8323403867
62UbiquitinationSVPAVVRIETSRSGE
HCCEEEEEEECCCCC		4.5929967540
109UbiquitinationNCQMRVKKTMPFFLE
CCEEEEEECCCCEEC		47.3929967540
110PhosphorylationCQMRVKKTMPFFLEG
CEEEEEECCCCEECC		25.10-
118AcetylationMPFFLEGKPKATLRQ
CCCEECCCCCCCCCC		33.6925953088
133PhosphorylationPGFASNFSVGKKPNP
CCCCCCCCCCCCCCC		33.9228857561
136UbiquitinationASNFSVGKKPNPAPL
CCCCCCCCCCCCCCC		64.0029967540
159PhosphorylationVKPDAEMSPYMLHTT
CCCCCCCCCCEEEEE		12.3728450419
161PhosphorylationPDAEMSPYMLHTTLG
CCCCCCCCEEEEECC		12.6627642862
165PhosphorylationMSPYMLHTTLGNEAF
CCCCEEEEECCCHHH		21.5428450419
166PhosphorylationSPYMLHTTLGNEAFK
CCCEEEEECCCHHHC		23.1728450419
168UbiquitinationYMLHTTLGNEAFKDI
CEEEEECCCHHHCCC		28.0429967540
173UbiquitinationTLGNEAFKDIPVQRH
ECCCHHHCCCCEEEE		62.8929967540
184PhosphorylationVQRHVTMSTNNRFSP
EEEEEECCCCCCCCC		20.7223403867
190PhosphorylationMSTNNRFSPKASLQP
CCCCCCCCCCHHCCC		23.4323403867
204PhosphorylationPPLQMHLSRTSTKEM
CCCEEHHCCCCHHHH		20.8723882029
206PhosphorylationLQMHLSRTSTKEMSD
CEEHHCCCCHHHHHH		37.0523882029
207PhosphorylationQMHLSRTSTKEMSDN
EEHHCCCCHHHHHHH		36.0523882029
208PhosphorylationMHLSRTSTKEMSDNL
EHHCCCCHHHHHHHH		30.3423882029
214UbiquitinationSTKEMSDNLNQTVEK
CHHHHHHHHHHCCCC		33.3229967540
241UbiquitinationMDEVQNRIKEILNKH
HHHHHHHHHHHHHHH		6.5229967540
242UbiquitinationDEVQNRIKEILNKHN
HHHHHHHHHHHHHHC		35.1529967540
2422-HydroxyisobutyrylationDEVQNRIKEILNKHN
HHHHHHHHHHHHHHC		35.15-
245PhosphorylationQNRIKEILNKHNNGI
HHHHHHHHHHHCCCE		7.9732142685
247UbiquitinationRIKEILNKHNNGIWI
HHHHHHHHHCCCEEH		44.2429967540
251UbiquitinationILNKHNNGIWISKLP
HHHHHCCCEEHHCCH		23.1729967540
261PhosphorylationISKLPHFYKELYKED
HHCCHHHHHHHHHHH		10.6626270265
288UbiquitinationPHICTVEKPCSGGQD
CEEEEEECCCCCCCC		47.1629967540
299PhosphorylationGGQDLLLYPAKRKQL
CCCCEEECCHHHHHH		10.9122817900
313PhosphorylationLLRSELDTEKVPLSP
HHHCCCCCCCCCCCC		50.7823403867
315UbiquitinationRSELDTEKVPLSPLP
HCCCCCCCCCCCCCC		51.7729967540
319PhosphorylationDTEKVPLSPLPGPKQ
CCCCCCCCCCCCCCC		20.5130266825
325UbiquitinationLSPLPGPKQTPPLKG
CCCCCCCCCCCCCCC		73.1229967540
327PhosphorylationPLPGPKQTPPLKGCP
CCCCCCCCCCCCCCC		32.7629496963
399UbiquitinationYISGNPQKAILYAKL
ECCCCCCEEEEEEEC		38.3629967540
403PhosphorylationNPQKAILYAKLPLPT
CCCEEEEEEECCCCC		8.7928674419
467UbiquitinationPTEASPSVLVVELSN
CCCCCCCEEEEECCC		5.5129967540
482PhosphorylationTNEVVIRYVGKDYSA
CCEEEEEEECCCCHH		11.48-
501PhosphorylationMEDEMKEYYSKNPKI
HHHHHHHHHHHCCCC		13.92-
502PhosphorylationEDEMKEYYSKNPKIT
HHHHHHHHHHCCCCC		17.79-
504UbiquitinationEMKEYYSKNPKITPV
HHHHHHHHCCCCCCC		62.2329967540
519UbiquitinationQAVNVGQLLAVNAEE
EECCHHHEEEECCCC		2.4629967540
541UbiquitinationVISTEENKIKVCYVD
EEECCCCEEEEEEEE		47.3829967540
559UbiquitinationSENVEKSKAYKLNPK
CCCHHHCHHHCCCCC		67.8024816145
576UbiquitinationSLSFQATKCKLAGLE
CCEEEECCCHHCCCE		32.18-
578UbiquitinationSFQATKCKLAGLEVL
EEEECCCHHCCCEEE		42.8229967540
586PhosphorylationLAGLEVLSDDPDLVK
HCCCEEECCCCCHHH		45.1828857561
593UbiquitinationSDDPDLVKVVESLTC
CCCCCHHHHHHHCCC		48.1129967540
600UbiquitinationKVVESLTCGKIFAVE
HHHHHCCCCCEEEEE		6.7429967540
642PhosphorylationLKAICDKSLEVHLQV
HHHHHCCCCEEEEEE		19.2628509920
659O-linked_GlycosylationMYTNVKVTNICSDGT
EECCEEEEEEECCCE		17.1031492838
666O-linked_GlycosylationTNICSDGTLYCQVPC
EEEECCCEEEEECCC		21.3931492838
674UbiquitinationLYCQVPCKGLNKLSD
EEEECCCCCHHHHHH		61.4329967540
772UbiquitinationPPQAIKCCLADLPQS
CHHHHHHHHCCCCHH		2.7429967540
805UbiquitinationCSDCSIKVTKVDETR
CCCCEEEEEEEECCC		6.2929967540
806PhosphorylationSDCSIKVTKVDETRG
CCCEEEEEEEECCCC		21.98-
831PhosphorylationNFPDPHRSINRQITN
CCCCCCCCCCHHCCC		22.60-
846UbiquitinationADLWKHQKDVFLSAI
HHHHHCHHHHHHHHH		56.4229967540
851PhosphorylationHQKDVFLSAISSGAD
CHHHHHHHHHCCCCC		16.4623403867
854PhosphorylationDVFLSAISSGADSPN
HHHHHHHCCCCCCCC		23.5723403867
855PhosphorylationVFLSAISSGADSPNS
HHHHHHCCCCCCCCC		31.7123403867
859PhosphorylationAISSGADSPNSKNGN
HHCCCCCCCCCCCCC		26.0029255136
862PhosphorylationSGADSPNSKNGNMPM
CCCCCCCCCCCCCCC		30.7729255136
879UbiquitinationNTGENFRKNLTDVIK
CCHHHHHHHHHHHHH		52.7729967540
886AcetylationKNLTDVIKKSMVDHT
HHHHHHHHHHHCCCC		38.3525953088
894UbiquitinationKSMVDHTSAFSTEEL
HHHCCCCCCCCCCCC		24.7329967540
930UbiquitinationHPGYFVIQPWQEIHK
CCCEEEECCHHHHHH		28.0724816145
968UbiquitinationKDQVYAAKVENKWHR
CHHEEEEEECCCHHH		41.7429967540
1004UbiquitinationHELVNIRKVQPLVDM
CEEEEEEECHHHHHH		41.2324816145
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 TDRD7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDRD7_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 TDRD7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TACC1_HUMANTACC1physical
14603251
CDK17_HUMANCDK17physical
14603251
TDRD7_HUMANTDRD7physical
25416956
MAGA8_HUMANMAGEA8physical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613887Cataract 36 (CTRCT36)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TDRD7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-862, ANDMASS SPECTROMETRY.

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