TET3_HUMAN - dbPTM
TET3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TET3_HUMAN
UniProt AC O43151
Protein Name Methylcytosine dioxygenase TET3
Gene Name TET3
Organism Homo sapiens (Human).
Sequence Length 1660
Subcellular Localization Nucleus . Cytoplasm . Chromosome . At the zygotic stage, localizes in the male pronucleus, while it localizes to the cytoplasm at other preimplantation stages. Binds to the promoter of target genes, close to the transcription start site.
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 (By similarity). Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes. [PubMed: 23217707 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 (By similarity 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]
Protein Sequence MDSGPVYHGDSRQLSASGVPVNGAREPAGPSLLGTGGPWRVDQKPDWEAAPGPAHTARLEDAHDLVAFSAVAEAVSSYGALSTRLYETFNREMSREAGNNSRGPRPGPEGCSAGSEDLDTLQTALALARHGMKPPNCNCDGPECPDYLEWLEGKIKSVVMEGGEERPRLPGPLPPGEAGLPAPSTRPLLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSPMTALQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATRSPKQIKIESSGAVTVLSTTCFHSEEGGQEATPTKAENPLTPTLSGFLESPLKYLDTPTKSLLDTPAKRAQAEFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQNAKVGSGAIQVLTAFPREVRRLPEPAKSCRQRQLEARKAAAEKKKIQKEKLSTPEKIKQEALELAGITSDPGLSLKGGLSQQGLKPSLKVEPQNHFSSFKYSGNAVVESYSVLGNCRPSDPYSMNSVYSYHSYYAQPSLTSVNGFHSKYALPSFSYYGFPSSNPVFPSQFLGPGAWGHSGSSGSFEKKPDLHALHNSLSPAYGGAEFAELPSQAVPTDAHHPTPHHQQPAYPGPKEYLLPKAPLLHSVSRDPSPFAQSSNCYNRSIKQEPVDPLTQAEPVPRDAGKMGKTPLSEVSQNGGPSHLWGQYSGGPSMSPKRTNGVGGSWGVFSSGESPAIVPDKLSSFGASCLAPSHFTDGQWGLFPGEGQQAASHSGGRLRGKPWSPCKFGNSTSALAGPSLTEKPWALGAGDFNSALKGSPGFQDKLWNPMKGEEGRIPAAGASQLDRAWQSFGLPLGSSEKLFGALKSEEKLWDPFSLEEGPAEEPPSKGAVKEEKGGGGAEEEEEELWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARARQEEAARLGLGQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTRQALAVPTDSAVTVSSYAYTKVTGPYSRWI
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
3Phosphorylation-----MDSGPVYHGD
-----CCCCCCCCCC
57.78-
7Phosphorylation-MDSGPVYHGDSRQL
-CCCCCCCCCCCCCC
11.83-
28PhosphorylationVNGAREPAGPSLLGT
CCCCCCCCCCCCCCC
37.4627732954
30PhosphorylationGAREPAGPSLLGTGG
CCCCCCCCCCCCCCC
24.7427732954
33PhosphorylationEPAGPSLLGTGGPWR
CCCCCCCCCCCCCCC
7.2825849741
44UbiquitinationGPWRVDQKPDWEAAP
CCCCCCCCCCCCCCC
40.24-
76PhosphorylationSAVAEAVSSYGALST
HHHHHHHHHHCHHHH
25.5328122231
77PhosphorylationAVAEAVSSYGALSTR
HHHHHHHHHCHHHHH
22.4628122231
78PhosphorylationVAEAVSSYGALSTRL
HHHHHHHHCHHHHHH
10.0228122231
82PhosphorylationVSSYGALSTRLYETF
HHHHCHHHHHHHHHH
15.7928122231
83PhosphorylationSSYGALSTRLYETFN
HHHCHHHHHHHHHHC
26.0828122231
86UbiquitinationGALSTRLYETFNREM
CHHHHHHHHHHCHHH
15.05-
86PhosphorylationGALSTRLYETFNREM
CHHHHHHHHHHCHHH
15.0527642862
101PhosphorylationSREAGNNSRGPRPGP
HHHCCCCCCCCCCCC
42.4832142685
121 (in isoform 4)Phosphorylation-4.2027732954
123 (in isoform 4)Phosphorylation-27.1027732954
126 (in isoform 4)Phosphorylation-9.1925849741
156UbiquitinationEWLEGKIKSVVMEGG
HHHHHHHEEEEECCC
40.46-
179UbiquitinationPLPPGEAGLPAPSTR
CCCCCCCCCCCCCCC
28.08-
198UbiquitinationSEVPQISPQEGLPLS
CCCCCCCCCCCCCCC
37.56-
264PhosphorylationAPFRSPQSYLRAPSW
CCCCCCCCCCCCCCC
29.5324719451
291UbiquitinationPDSSAFPPATPRTEF
CCCCCCCCCCCCCCC
42.17-
304PhosphorylationEFPEAWGTDTPPATP
CCCCHHCCCCCCCCC
26.4628348404
306PhosphorylationPEAWGTDTPPATPRS
CCHHCCCCCCCCCCC
30.8927251275
310PhosphorylationGTDTPPATPRSSWPM
CCCCCCCCCCCCCCC
25.63-
313PhosphorylationTPPATPRSSWPMPRP
CCCCCCCCCCCCCCC
37.6522210691
314PhosphorylationPPATPRSSWPMPRPS
CCCCCCCCCCCCCCC
36.1622210691
352AcetylationRPEALPTKPKVKVEA
CCCCCCCCCCEEEEC
40.6825953088
356SumoylationLPTKPKVKVEAPSSS
CCCCCCEEEECCCCC
40.25-
356SumoylationLPTKPKVKVEAPSSS
CCCCCCEEEECCCCC
40.2528112733
361PhosphorylationKVKVEAPSSSPAPAP
CEEEECCCCCCCCCC
50.9629255136
362PhosphorylationVKVEAPSSSPAPAPS
EEEECCCCCCCCCCC
39.0029255136
363PhosphorylationKVEAPSSSPAPAPSP
EEECCCCCCCCCCCC
29.4429255136
369PhosphorylationSSPAPAPSPVLQREA
CCCCCCCCCCCCCCC
29.7329255136
381O-linked_GlycosylationREAPTPSSEPDTHQK
CCCCCCCCCCCHHHH
55.1130379171
429PhosphorylationPGWWPPPSSPVPRLP
CCCCCCCCCCCCCCC
53.7124719451
465AcetylationEKAAPGIKPSVRKPI
CCCCCCCCCCCCCCC
36.8426051181
491SumoylationPLFPPVRQIVLEGLR
CCCCCHHHHHHHCCC
30.31-
504PhosphorylationLRSPASQEVQAHPPA
CCCCCCCCHHCCCCC
33.82-
535UbiquitinationSLALFAPSPSRDSLL
CEEEECCCCCCCCCC
31.8829967540
545PhosphorylationRDSLLPPTQEMRSPS
CCCCCCCCCCCCCCC
34.91-
550PhosphorylationPPTQEMRSPSPMTAL
CCCCCCCCCCCCCCC
28.5528450419
552PhosphorylationTQEMRSPSPMTALQP
CCCCCCCCCCCCCCC
28.6628450419
555PhosphorylationMRSPSPMTALQPGST
CCCCCCCCCCCCCCC
27.8328450419
561PhosphorylationMTALQPGSTGPLPPA
CCCCCCCCCCCCCCC
36.5528450419
605PhosphorylationQDPENQQTCLPAPES
CCCCCCCCCCCCCCC
13.2726074081
612PhosphorylationTCLPAPESPFATRSP
CCCCCCCCCCCCCCC
25.0226074081
616PhosphorylationAPESPFATRSPKQIK
CCCCCCCCCCCCCEE
31.8726074081
618PhosphorylationESPFATRSPKQIKIE
CCCCCCCCCCCEEEE
31.9026074081
648PhosphorylationEEGGQEATPTKAENP
CCCCCCCCCCCCCCC
30.6430576142
650PhosphorylationGGQEATPTKAENPLT
CCCCCCCCCCCCCCC
38.2330576142
657PhosphorylationTKAENPLTPTLSGFL
CCCCCCCCCCCCHHH
18.5825159151
659PhosphorylationAENPLTPTLSGFLES
CCCCCCCCCCHHHCC
28.4625850435
661PhosphorylationNPLTPTLSGFLESPL
CCCCCCCCHHHCCHH
29.9428450419
666PhosphorylationTLSGFLESPLKYLDT
CCCHHHCCHHHHCCC
37.3729255136
673PhosphorylationSPLKYLDTPTKSLLD
CHHHHCCCCCHHHCC
30.2021712546
676UbiquitinationKYLDTPTKSLLDTPA
HHCCCCCHHHCCCHH
40.07-
677PhosphorylationYLDTPTKSLLDTPAK
HCCCCCHHHCCCHHH
36.3221712546
681PhosphorylationPTKSLLDTPAKRAQA
CCHHHCCCHHHHHHC
25.7221712546
684AcetylationSLLDTPAKRAQAEFP
HHCCCHHHHHHCCCC
49.8525953088
690PhosphorylationAKRAQAEFPTCDCVE
HHHHHCCCCCCCHHH
7.32-
718UbiquitinationLGSGPTVASIRELME
CCCCCCHHHHHHHHH
11.17-
747PhosphorylationVIYTGKEGKSSRGCP
EEEECCCCCCCCCCC
38.33-
792PhosphorylationVIVILILAWEGIPRS
HHHHHHHHHCCCCHH
8.69-
801PhosphorylationEGIPRSLGDTLYQEL
CCCCHHHHHHHHHHH
27.40-
808PhosphorylationGDTLYQELTDTLRKY
HHHHHHHHHHHHHHH
2.87-
811UbiquitinationLYQELTDTLRKYGNP
HHHHHHHHHHHHCCC
24.1929967540
812PhosphorylationYQELTDTLRKYGNPT
HHHHHHHHHHHCCCC
5.04-
816PhosphorylationTDTLRKYGNPTSRRC
HHHHHHHCCCCCCCC
36.35-
819UbiquitinationLRKYGNPTSRRCGLN
HHHHCCCCCCCCCCC
38.5729967540
859UbiquitinationSMYFNGCKYARSKTP
EEEECCCCCCCCCCC
43.26-
884UbiquitinationKEEEVLRKSFQDLAT
HHHHHHHHHHHHHHH
52.00-
898UbiquitinationTEVAPLYKRLAPQAY
HHHHHHHHHHCCHHH
48.93-
994UbiquitinationDEFGSEENQNAKVGS
CCCCCHHHCCCCCCC
36.03-
1019UbiquitinationREVRRLPEPAKSCRQ
HHHHCCCHHHHHHHH
63.5829967540
1033UbiquitinationQRQLEARKAAAEKKK
HHHHHHHHHHHHHHH
49.8029967540
1040AcetylationKAAAEKKKIQKEKLS
HHHHHHHHHHHHHCC
62.5319828831
1047PhosphorylationKIQKEKLSTPEKIKQ
HHHHHHCCCHHHHHH
53.6422210691
1048PhosphorylationIQKEKLSTPEKIKQE
HHHHHCCCHHHHHHH
46.0022210691
1053SumoylationLSTPEKIKQEALELA
CCCHHHHHHHHHHHC
53.83-
1053SumoylationLSTPEKIKQEALELA
CCCHHHHHHHHHHHC
53.8328112733
1069PhosphorylationITSDPGLSLKGGLSQ
CCCCCCCCCCCCCCC
33.6724719451
1080UbiquitinationGLSQQGLKPSLKVEP
CCCCCCCCCCCCCCC
39.11-
1084SumoylationQGLKPSLKVEPQNHF
CCCCCCCCCCCCCCC
49.2228112733
1183PhosphorylationSSGSFEKKPDLHALH
CCCCCCCCCCHHHHC
36.24-
1188SumoylationEKKPDLHALHNSLSP
CCCCCHHHHCCCCCC
20.15-
1188UbiquitinationEKKPDLHALHNSLSP
CCCCCHHHHCCCCCC
20.1529967540
1215UbiquitinationQAVPTDAHHPTPHHQ
CCCCCCCCCCCCCCC
30.21-
1242PhosphorylationPKAPLLHSVSRDPSP
CCCCCCCCCCCCCCC
23.0424719451
1244PhosphorylationAPLLHSVSRDPSPFA
CCCCCCCCCCCCCCC
33.7023898821
1248PhosphorylationHSVSRDPSPFAQSSN
CCCCCCCCCCCCCCC
36.6223898821
1262SumoylationNCYNRSIKQEPVDPL
CCCCCCCCCCCCCCC
50.27-
1262SumoylationNCYNRSIKQEPVDPL
CCCCCCCCCCCCCCC
50.2728112733
1285PhosphorylationDAGKMGKTPLSEVSQ
CCCCCCCCCHHHHHH
24.59-
1288PhosphorylationKMGKTPLSEVSQNGG
CCCCCCHHHHHHCCC
36.8422210691
1297PhosphorylationVSQNGGPSHLWGQYS
HHHCCCCCCCCCCCC
34.19-
1303PhosphorylationPSHLWGQYSGGPSMS
CCCCCCCCCCCCCCC
12.8228450419
1304PhosphorylationSHLWGQYSGGPSMSP
CCCCCCCCCCCCCCC
29.4128450419
1308PhosphorylationGQYSGGPSMSPKRTN
CCCCCCCCCCCCCCC
34.8622210691
1310PhosphorylationYSGGPSMSPKRTNGV
CCCCCCCCCCCCCCC
31.4424719451
1376AcetylationSGGRLRGKPWSPCKF
CCCCCCCCCCCCCCC
36.5626051181
1379PhosphorylationRLRGKPWSPCKFGNS
CCCCCCCCCCCCCCC
29.0223898821
1383PhosphorylationKPWSPCKFGNSTSAL
CCCCCCCCCCCCCCC
16.64-
1397SumoylationLAGPSLTEKPWALGA
CCCCCCCCCCCCCCC
63.52-
1397UbiquitinationLAGPSLTEKPWALGA
CCCCCCCCCCCCCCC
63.5229967540
1409PhosphorylationLGAGDFNSALKGSPG
CCCCCHHHHHCCCCC
34.66-
1414PhosphorylationFNSALKGSPGFQDKL
HHHHHCCCCCHHHCC
21.9128348404
1426SumoylationDKLWNPMKGEEGRIP
HCCCCCCCCCCCCCC
65.5128112733
1453PhosphorylationSFGLPLGSSEKLFGA
HHCCCCCCHHHHHHH
42.9028348404
1454PhosphorylationFGLPLGSSEKLFGAL
HCCCCCCHHHHHHHH
36.6328348404
1456UbiquitinationLPLGSSEKLFGALKS
CCCCCHHHHHHHHCC
51.57-
1505PhosphorylationEEEEELWSDSEHNFL
HHHHHHHCCCCCCCC
43.8328348404
1507PhosphorylationEEELWSDSEHNFLDE
HHHHHCCCCCCCCCC
34.9328348404
1514PhosphorylationSEHNFLDENIGGVAV
CCCCCCCCCCCCEEE
53.55-
1544PhosphorylationLHATTPLKKPNRCHP
HHCCCCCCCCCCCCC
68.35-
1597UbiquitinationEEAARLGLGQQEAKL
HHHHHHCCCHHHHHH
7.1029967540
1601UbiquitinationRLGLGQQEAKLYGKK
HHCCCHHHHHHHCCC
39.6229967540
1603SumoylationGLGQQEAKLYGKKRK
CCCHHHHHHHCCCCC
41.30-
1630PhosphorylationEKKGVVPTRQALAVP
CCCCCCCCHHHEECC
24.6521964256
1638PhosphorylationRQALAVPTDSAVTVS
HHHEECCCCCCCEEE
35.67-
1640PhosphorylationALAVPTDSAVTVSSY
HEECCCCCCCEEEEE
27.41-
1679Ubiquitination--------------------------
--------------------------
29967540
1712Ubiquitination-----------------------------------------------------------
-----------------------------------------------------------
29967540
1738Sumoylation-------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------
-
1738Ubiquitination-------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------
29967540
1745Ubiquitination--------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------
29967540

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TET3_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 TET3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DCAF1_HUMANVPRBPphysical
25557551
DDB1_HUMANDDB1physical
25557551

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TET3_HUMAN

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Related Literatures of Post-Translational Modification

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