TET3_MOUSE - dbPTM
TET3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TET3_MOUSE
UniProt AC Q8BG87
Protein Name Methylcytosine dioxygenase TET3
Gene Name Tet3
Organism Mus musculus (Mouse).
Sequence Length 1668
Subcellular Localization Nucleus . Chromosome . Cytoplasm . At the zygotic stage, localizes in the male pronucleus, while it localizes to the cytoplasm at other preimplantation stages (PubMed:21892189). Binds to the promoter of target genes, close to the transcription start
Protein Description Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in DNA demethylation in the paternal pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of maternal pronucleus because of the presence of DPPA3/PGC7 on maternal chromatin that prevents TET3-binding to chromatin. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT.; Isoform 3: Has higher affinity for DNA and lower catalytic activity than isoform 1, probably due to the N-terminal CXXC-type zinc-finger domain that mediates high-affinity binding to DNA and that is not present in isoform 1..
Protein Sequence MDSGPVYHGDSRQLSTSGAPVNGAREPAGPGLLGAAGPWRVDQKPDWEAASGPTHAARLEDAHDLVAFSAVAEAVSSYGALSTRLYETFNREMSREAGSNGRGPRPESCSEGSEDLDTLQTALALARHGMKPPNCTCDGPECPDFLEWLEGKIKSMAMEGGQGRPRLPGALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTSQASCPLPEALSPSAPFRSPQSYLRAPSWPVVPPEEHPSFAPDSPAFPPATPRPEFSEAWGTDTPPATPRNSWPVPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPVPSPISQREAPLLSSEPDTHQKAQTALQQHLHHKRNLFLEQAQDASFPTSTEPQAPGWWAPPGSPAPRPPDKPPKEKKKKPPTPAGGPVGAEKTTPGIKTSVRKPIQIKKSRSRDMQPLFLPVRQIVLEGLKPQASEGQAPLPAQLSVPPPASQGAASQSCATPLTPEPSLALFAPSPSGDSLLPPTQEMRSPSPMVALQSGSTGGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQEPENQSTCLPAPESPFATRSPKKIKIESSGAVTVLSTTCFHSEEGGQEATPTKAENPLTPTLSGFLESPLKYLDTPTKSLLDTPAKKAQSEFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFPREVRRLPEPAKSCRQRQLEARKAAAEKKKLQKEKLSTPEKIKQEALELAGVTTDPGLSLKGGLSQQSLKPSLKVEPQNHFSSFKYSGNAVVESYSVLGSCRPSDPYSMSSVYSYHSRYAQPGLASVNGFHSKYTLPSFGYYGFPSSNPVFPSQFLGPSAWGHGGSGGSFEKKPDLHALHNSLNPAYGGAEFAELPGQAVATDNHHPIPHHQQPAYPGPKEYLLPKVPQLHPASRDPSPFAQSSSCYNRSIKQEPIDPLTQAESIPRDSAKMSRTPLPEASQNGGPSHLWGQYSGGPSMSPKRTNSVGGNWGVFPPGESPTIVPDKLNSFGASCLTPSHFPESQWGLFTGEGQQSAPHAGARLRGKPWSPCKFGNGTSALTGPSLTEKPWGMGTGDFNPALKGGPGFQDKLWNPVKVEEGRIPTPGANPLDKAWQAFGMPLSSNEKLFGALKSEEKLWDPFSLEEGTAEEPPSKGVVKEEKSGPTVEEDEEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARQRQEEAARLGLGQQEAKLYGKKRKWGGAMVAEPQHKEKKGAIPTRQALAMPTDSAVTVSSYAYTKVTGPYSRWI
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
51O-linked_GlycosylationKPDWEAASGPTHAAR
CCCHHHCCCCCCHHH		52.97105050833
121 (in isoform 4)Phosphorylation-27.1030635358
123 (in isoform 4)Phosphorylation-4.5730635358
126 (in isoform 4)Phosphorylation-8.8730635358
320PhosphorylationSWPVPRPSPDPMAEL
CCCCCCCCCCHHHHH		43.12-
360O-linked_GlycosylationKVKVEAPSSSPAPVP
CEEEECCCCCCCCCC		50.9677070287
360PhosphorylationKVKVEAPSSSPAPVP
CEEEECCCCCCCCCC		50.96-
361PhosphorylationVKVEAPSSSPAPVPS
EEEECCCCCCCCCCC		39.00-
362PhosphorylationKVEAPSSSPAPVPSP
EEECCCCCCCCCCCC		29.4426370283
362O-linked_GlycosylationKVEAPSSSPAPVPSP
EEECCCCCCCCCCCC		29.4477070291
368PhosphorylationSSPAPVPSPISQREA
CCCCCCCCCCCCCCC		34.7928066266
371O-linked_GlycosylationAPVPSPISQREAPLL
CCCCCCCCCCCCCCC		26.94105050835
371PhosphorylationAPVPSPISQREAPLL
CCCCCCCCCCCCCCC		26.9428066266
478PhosphorylationIQIKKSRSRDMQPLF
EEEECCCCCCCCCCE		39.46-
557O-linked_GlycosylationPPTQEMRSPSPMVAL
CCCCCCCCCCCCEEC		28.5577070297
557PhosphorylationPPTQEMRSPSPMVAL
CCCCCCCCCCCCEEC		28.55-
579UbiquitinationPLPPADDKLEELIRQ
CCCCCHHHHHHHHHH		59.34-
665PhosphorylationTKAENPLTPTLSGFL
CCCCCCCCCCCCHHH		18.5825159016
667PhosphorylationAENPLTPTLSGFLES
CCCCCCCCCCHHHCC		28.4625159016
669PhosphorylationNPLTPTLSGFLESPL
CCCCCCCCHHHCCHH		29.9421743459
674PhosphorylationTLSGFLESPLKYLDT
CCCHHHCCHHHHCCC		37.3725159016
674O-linked_GlycosylationTLSGFLESPLKYLDT
CCCHHHCCHHHHCCC		37.3772258545
681PhosphorylationSPLKYLDTPTKSLLD
CHHHHCCCCCHHHCC		30.2030482847
689PhosphorylationPTKSLLDTPAKKAQS
CCHHHCCCHHHHHHC		25.7229109428
772PhosphorylationKWVIRRHTLEEKLLC
HHHHHHCCHHHHHHH		33.77-
918O-linked_GlycosylationQAYQNQVTNEDVAID
HHHHHCCCCCCHHHH		24.11105050829
1008O-linked_GlycosylationENQNAKVSSGAIQVL
HHHCCCCCCHHHHHH		23.5077070301
1071O-linked_GlycosylationALELAGVTTDPGLSL
HHHHCCCCCCCCCCC		25.2777070303
1072O-linked_GlycosylationLELAGVTTDPGLSLK
HHHCCCCCCCCCCCC		37.4877070299
1077O-linked_GlycosylationVTTDPGLSLKGGLSQ
CCCCCCCCCCCCCCC		33.6777070311
1083O-linked_GlycosylationLSLKGGLSQQSLKPS
CCCCCCCCCCCCCCC		29.4655414245
1090PhosphorylationSQQSLKPSLKVEPQN
CCCCCCCCCCCCCCC		38.9521454597
1105O-linked_GlycosylationHFSSFKYSGNAVVES
CCCCCEECCCEEEEE		26.5977070309
1136MethylationSVYSYHSRYAQPGLA
HHEEEHHHCCCCCCE		19.9324129315
1136Asymmetric dimethylarginineSVYSYHSRYAQPGLA
HHEEEHHHCCCCCCE		19.93-
1252O-linked_GlycosylationVPQLHPASRDPSPFA
CCCCCCCCCCCCCCC		41.4955414237
1252PhosphorylationVPQLHPASRDPSPFA
CCCCCCCCCCCCCCC		41.4926643407
1256PhosphorylationHPASRDPSPFAQSSS
CCCCCCCCCCCCCCC		36.6226643407
1256O-linked_GlycosylationHPASRDPSPFAQSSS
CCCCCCCCCCCCCCC		36.6246304085
1263PhosphorylationSPFAQSSSCYNRSIK
CCCCCCCCCCCCCCC		26.35-
1263O-linked_GlycosylationSPFAQSSSCYNRSIK
CCCCCCCCCCCCCCC		26.3551512199
1265PhosphorylationFAQSSSCYNRSIKQE
CCCCCCCCCCCCCCC		18.63-
1271MethylationCYNRSIKQEPIDPLT
CCCCCCCCCCCCHHH		61.0924129315
1282O-linked_GlycosylationDPLTQAESIPRDSAK
CHHHCCHHCCCCCCC		40.6977070317
1293O-linked_GlycosylationDSAKMSRTPLPEASQ
CCCCCCCCCCCHHHH		23.1346304097
1318PhosphorylationYSGGPSMSPKRTNSV
CCCCCCCCCCCCCCC		31.44-
1351PhosphorylationKLNSFGASCLTPSHF
CCCCCCCCCCCCCCC		15.27-
1387PhosphorylationRLRGKPWSPCKFGNG
CCCCCCCCCCCCCCC		29.0225159016
1404O-linked_GlycosylationALTGPSLTEKPWGMG
CCCCCCCCCCCCCCC		46.4277070315
1412O-linked_GlycosylationEKPWGMGTGDFNPAL
CCCCCCCCCCCCHHH		25.3777070305
1442PhosphorylationVEEGRIPTPGANPLD
CCCCCCCCCCCCHHH		31.8026643407
1485PhosphorylationPFSLEEGTAEEPPSK
CCCCCCCCCCCCCCC		33.8928285833
1491PhosphorylationGTAEEPPSKGVVKEE
CCCCCCCCCCCCCCC		53.4028285833
1648PhosphorylationALAMPTDSAVTVSSY
HHCCCCCCCEEEEEE		27.4128059163
1651O-linked_GlycosylationMPTDSAVTVSSYAYT
CCCCCCEEEEEEEEE		17.8777070329
1653O-linked_GlycosylationTDSAVTVSSYAYTKV
CCCCEEEEEEEEEEE		14.3177070323
1654O-linked_GlycosylationDSAVTVSSYAYTKVT
CCCEEEEEEEEEEEC		14.9477070327
1655PhosphorylationSAVTVSSYAYTKVTG
CCEEEEEEEEEEECC		8.9828059163
1658O-linked_GlycosylationTVSSYAYTKVTGPYS
EEEEEEEEEECCCCC		15.7477070331
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 TET3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TET3_MOUSE !!
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 TET3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TET3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TET3_MOUSE

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Related Literatures of Post-Translational Modification

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