TET1_HUMAN - dbPTM
TET1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TET1_HUMAN
UniProt AC Q8NFU7
Protein Name Methylcytosine dioxygenase TET1
Gene Name TET1
Organism Homo sapiens (Human).
Sequence Length 2136
Subcellular Localization Nucleus .
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 active DNA demethylation. 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. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, plays a more general role in chromatin regulation. Preferentially binds to CpG-rich sequences at promoters of both transcriptionally active and Polycomb-repressed genes. 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. Also involved in transcription repression of a subset of genes through recruitment of transcriptional repressors to promoters. Involved in the balance between pluripotency and lineage commitment of cells it plays a role in embryonic stem cells maintenance and inner cell mass cell specification. Plays an important role in the tumorigenicity of glioblastoma cells. TET1-mediated production of 5hmC acts as a recruitment signal for the CHTOP-methylosome complex to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis. [PubMed: 25284789]
Protein Sequence MSRSRHARPSRLVRKEDVNKKKKNSQLRKTTKGANKNVASVKTLSPGKLKQLIQERDVKKKTEPKPPVPVRSLLTRAGAARMNLDRTEVLFQNPESLTCNGFTMALRSTSLSRRLSQPPLVVAKSKKVPLSKGLEKQHDCDYKILPALGVKHSENDSVPMQDTQVLPDIETLIGVQNPSLLKGKSQETTQFWSQRVEDSKINIPTHSGPAAEILPGPLEGTRCGEGLFSEETLNDTSGSPKMFAQDTVCAPFPQRATPKVTSQGNPSIQLEELGSRVESLKLSDSYLDPIKSEHDCYPTSSLNKVIPDLNLRNCLALGGSTSPTSVIKFLLAGSKQATLGAKPDHQEAFEATANQQEVSDTTSFLGQAFGAIPHQWELPGADPVHGEALGETPDLPEIPGAIPVQGEVFGTILDQQETLGMSGSVVPDLPVFLPVPPNPIATFNAPSKWPEPQSTVSYGLAVQGAIQILPLGSGHTPQSSSNSEKNSLPPVMAISNVENEKQVHISFLPANTQGFPLAPERGLFHASLGIAQLSQAGPSKSDRGSSQVSVTSTVHVVNTTVVTMPVPMVSTSSSSYTTLLPTLEKKKRKRCGVCEPCQQKTNCGECTYCKNRKNSHQICKKRKCEELKKKPSVVVPLEVIKENKRPQREKKPKVLKADFDNKPVNGPKSESMDYSRCGHGEEQKLELNPHTVENVTKNEDSMTGIEVEKWTQNKKSQLTDHVKGDFSANVPEAEKSKNSEVDKKRTKSPKLFVQTVRNGIKHVHCLPAETNVSFKKFNIEEFGKTLENNSYKFLKDTANHKNAMSSVATDMSCDHLKGRSNVLVFQQPGFNCSSIPHSSHSIINHHASIHNEGDQPKTPENIPSKEPKDGSPVQPSLLSLMKDRRLTLEQVVAIEALTQLSEAPSENSSPSKSEKDEESEQRTASLLNSCKAILYTVRKDLQDPNLQGEPPKLNHCPSLEKQSSCNTVVFNGQTTTLSNSHINSATNQASTKSHEYSKVTNSLSLFIPKSNSSKIDTNKSIAQGIITLDNCSNDLHQLPPRNNEVEYCNQLLDSSKKLDSDDLSCQDATHTQIEEDVATQLTQLASIIKINYIKPEDKKVESTPTSLVTCNVQQKYNQEKGTIQQKPPSSVHNNHGSSLTKQKNPTQKKTKSTPSRDRRKKKPTVVSYQENDRQKWEKLSYMYGTICDIWIASKFQNFGQFCPHDFPTVFGKISSSTKIWKPLAQTRSIMQPKTVFPPLTQIKLQRYPESAEEKVKVEPLDSLSLFHLKTESNGKAFTDKAYNSQVQLTVNANQKAHPLTQPSSPPNQCANVMAGDDQIRFQQVVKEQLMHQRLPTLPGISHETPLPESALTLRNVNVVCSGGITVVSTKSEEEVCSSSFGTSEFSTVDSAQKNFNDYAMNFFTNPTKNLVSITKDSELPTCSCLDRVIQKDKGPYYTHLGAGPSVAAVREIMENRYGQKGNAIRIEIVVYTGKEGKSSHGCPIAKWVLRRSSDEEKVLCLVRQRTGHHCPTAVMVVLIMVWDGIPLPMADRLYTELTENLKSYNGHPTDRRCTLNENRTCTCQGIDPETCGASFSFGCSWSMYFNGCKFGRSPSPRRFRIDPSSPLHEKNLEDNLQSLATRLAPIYKQYAPVAYQNQVEYENVARECRLGSKEGRPFSGVTACLDFCAHPHRDIHNMNNGSTVVCTLTREDNRSLGVIPQDEQLHVLPLYKLSDTDEFGSKEGMEAKIKSGAIEVLAPRRKKRTCFTQPVPRSGKKRAAMMTEVLAHKIRAVEKKPIPRIKRKNNSTTTNNSKPSSLPTLGSNTETVQPEVKSETEPHFILKSSDNTKTYSLMPSAPHPVKEASPGFSWSPKTASATPAPLKNDATASCGFSERSSTPHCTMPSGRLSGANAAAADGPGISQLGEVAPLPTLSAPVMEPLINSEPSTGVTEPLTPHQPNHQPSFLTSPQDLASSPMEEDEQHSEADEPPSDEPLSDDPLSPAEEKLPHIDEYWSDSEHIFLDANIGGVAIAPAHGSVLIECARRELHATTPVEHPNRNHPTRLSLVFYQHKNLNKPQHGFELNKIKFEAKEAKNKKMKASEQKDQAANEGPEQSSEVNELNQIPSHKALTLTHDNVVTVSPYALTHVAGPYNHWV
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
10PhosphorylationRSRHARPSRLVRKED
CCCCCCHHHCCCHHH
32.4717081983
30PhosphorylationKNSQLRKTTKGANKN
HHHHHHHHHCCCCCC
27.57-
31PhosphorylationNSQLRKTTKGANKNV
HHHHHHHHCCCCCCC
30.43-
43PhosphorylationKNVASVKTLSPGKLK
CCCEECEECCHHHHH
30.2526699800
45PhosphorylationVASVKTLSPGKLKQL
CEECEECCHHHHHHH
36.5224719451
48AcetylationVKTLSPGKLKQLIQE
CEECCHHHHHHHHHH
56.7625953088
72PhosphorylationKPPVPVRSLLTRAGA
CCCCCHHHHHHHHCH
28.1524719451
87PhosphorylationARMNLDRTEVLFQNP
HHCCCCCCEEEECCH
30.0622210691
96PhosphorylationVLFQNPESLTCNGFT
EEECCHHHCCCCCCH
30.1822210691
98PhosphorylationFQNPESLTCNGFTMA
ECCHHHCCCCCCHHH
17.1329759185
108PhosphorylationGFTMALRSTSLSRRL
CCHHHHHHHCHHHHH
24.1722210691
112PhosphorylationALRSTSLSRRLSQPP
HHHHHCHHHHHCCCC
18.3429759185
116PhosphorylationTSLSRRLSQPPLVVA
HCHHHHHCCCCEEEE
38.5424719451
179PhosphorylationLIGVQNPSLLKGKSQ
HHCCCCHHHHCCCCH
54.6124719451
185PhosphorylationPSLLKGKSQETTQFW
HHHHCCCCHHHHHHH
41.7529970186
188PhosphorylationLKGKSQETTQFWSQR
HCCCCHHHHHHHHHH
20.4729970186
189PhosphorylationKGKSQETTQFWSQRV
CCCCHHHHHHHHHHH
22.48-
193PhosphorylationQETTQFWSQRVEDSK
HHHHHHHHHHHHHCC
14.92-
232PhosphorylationEGLFSEETLNDTSGS
CCCCCCCCCCCCCCC
27.1529449344
236PhosphorylationSEETLNDTSGSPKMF
CCCCCCCCCCCCCCC
33.6329449344
237PhosphorylationEETLNDTSGSPKMFA
CCCCCCCCCCCCCCC
39.8929449344
239PhosphorylationTLNDTSGSPKMFAQD
CCCCCCCCCCCCCCC
22.5528165663
285PhosphorylationESLKLSDSYLDPIKS
HEECCCHHHCCCCCC
24.9928787133
292PhosphorylationSYLDPIKSEHDCYPT
HHCCCCCCCCCCCCC
40.6628787133
320PhosphorylationNCLALGGSTSPTSVI
CCHHCCCCCCCHHHH
24.7429978859
321PhosphorylationCLALGGSTSPTSVIK
CHHCCCCCCCHHHHH
41.8429978859
322PhosphorylationLALGGSTSPTSVIKF
HHCCCCCCCHHHHHH
28.0729978859
324PhosphorylationLGGSTSPTSVIKFLL
CCCCCCCHHHHHHHH
35.0829978859
325PhosphorylationGGSTSPTSVIKFLLA
CCCCCCHHHHHHHHC
25.8129978859
582PhosphorylationSYTTLLPTLEKKKRK
CCCCCHHHHHHHCCC
47.7424173317
669PhosphorylationKPVNGPKSESMDYSR
CCCCCCCCCCCCCCC
37.73-
691PhosphorylationKLELNPHTVENVTKN
CCCCCCCCCCCCCCC
30.6722468782
701PhosphorylationNVTKNEDSMTGIEVE
CCCCCCCCCCCCEEE
16.4428509920
703PhosphorylationTKNEDSMTGIEVEKW
CCCCCCCCCCEEEHH
38.6727732954
746PhosphorylationSEVDKKRTKSPKLFV
CHHHHCCCCCCHHHH
44.7624719451
805PhosphorylationANHKNAMSSVATDMS
HCCHHHHHHHHHHCC
21.17-
806PhosphorylationNHKNAMSSVATDMSC
CCHHHHHHHHHHCCC
11.59-
858O-linked_GlycosylationNEGDQPKTPENIPSK
CCCCCCCCCCCCCCC
42.3828411811
858PhosphorylationNEGDQPKTPENIPSK
CCCCCCCCCCCCCCC
42.3830576142
864O-linked_GlycosylationKTPENIPSKEPKDGS
CCCCCCCCCCCCCCC
45.9428411811
864PhosphorylationKTPENIPSKEPKDGS
CCCCCCCCCCCCCCC
45.9424719451
871PhosphorylationSKEPKDGSPVQPSLL
CCCCCCCCCCCHHHH
31.8412124344
905PhosphorylationTQLSEAPSENSSPSK
HHHHCCCCCCCCCCC
57.3624173317
908PhosphorylationSEAPSENSSPSKSEK
HCCCCCCCCCCCCCC
39.3024173317
909PhosphorylationEAPSENSSPSKSEKD
CCCCCCCCCCCCCCC
44.7824173317
935PhosphorylationNSCKAILYTVRKDLQ
HHHHHHHHHHHHHCC
9.33-
1086PhosphorylationTQLTQLASIIKINYI
HHHHHHHHHHEEEEC
33.1824719451
1129PhosphorylationTIQQKPPSSVHNNHG
CCCCCCCCCCCCCCC
54.2229978859
1130PhosphorylationIQQKPPSSVHNNHGS
CCCCCCCCCCCCCCC
32.9229978859
1137PhosphorylationSVHNNHGSSLTKQKN
CCCCCCCCCCCCCCC
18.0229978859
1138PhosphorylationVHNNHGSSLTKQKNP
CCCCCCCCCCCCCCC
44.6529978859
1140PhosphorylationNNHGSSLTKQKNPTQ
CCCCCCCCCCCCCCC
33.1229978859
1146PhosphorylationLTKQKNPTQKKTKST
CCCCCCCCCCCCCCC
63.5129978859
1150PhosphorylationKNPTQKKTKSTPSRD
CCCCCCCCCCCCCCC
36.9420363803
1155PhosphorylationKKTKSTPSRDRRKKK
CCCCCCCCCCCCCCC
47.0720363803
1161AcetylationPSRDRRKKKPTVVSY
CCCCCCCCCCEEEEC
63.27130749
1215PhosphorylationTVFGKISSSTKIWKP
CCCCCCCCCCCCCHH
45.5623898821
1216PhosphorylationVFGKISSSTKIWKPL
CCCCCCCCCCCCHHH
27.2529449344
1217PhosphorylationFGKISSSTKIWKPLA
CCCCCCCCCCCHHHC
28.6229449344
1228PhosphorylationKPLAQTRSIMQPKTV
HHHCCCCCCCCCCCC
26.29-
1234PhosphorylationRSIMQPKTVFPPLTQ
CCCCCCCCCCCCCHH
33.78-
1282PhosphorylationKAFTDKAYNSQVQLT
CEECCHHHCCCEEEE
22.5325690035
1284PhosphorylationFTDKAYNSQVQLTVN
ECCHHHCCCEEEEEC
21.0325690035
1300PhosphorylationNQKAHPLTQPSSPPN
CCCCCCCCCCCCCCC
42.7730377224
1303PhosphorylationAHPLTQPSSPPNQCA
CCCCCCCCCCCCCCC
45.7330624053
1304PhosphorylationHPLTQPSSPPNQCAN
CCCCCCCCCCCCCCC
51.5730624053
1361PhosphorylationRNVNVVCSGGITVVS
CCCEEEECCCEEEEC
28.5722199227
1365PhosphorylationVVCSGGITVVSTKSE
EEECCCEEEECCCCH
20.3822199227
1368PhosphorylationSGGITVVSTKSEEEV
CCCEEEECCCCHHHH
26.2822199227
1369PhosphorylationGGITVVSTKSEEEVC
CCEEEECCCCHHHHH
27.2922199227
1382PhosphorylationVCSSSFGTSEFSTVD
HHHCCCCCCCCCCHH
24.07-
1492O-linked_GlycosylationAKWVLRRSSDEEKVL
HHHHHHCCCCHHHEE
35.3928411811
1589UbiquitinationSMYFNGCKFGRSPSP
EEEECCCCCCCCCCC
52.86-
1593PhosphorylationNGCKFGRSPSPRRFR
CCCCCCCCCCCCCCC
30.0624173317
1595PhosphorylationCKFGRSPSPRRFRID
CCCCCCCCCCCCCCC
32.0817081983
1604PhosphorylationRRFRIDPSSPLHEKN
CCCCCCCCCCHHHCC
40.6222210691
1605PhosphorylationRFRIDPSSPLHEKNL
CCCCCCCCCHHHCCH
36.5522210691
1641PhosphorylationAYQNQVEYENVAREC
CCCCCCCCHHHHHHH
17.5919835603
1662PhosphorylationGRPFSGVTACLDFCA
CCCCCCCCHHHHHHC
18.3822210691
1682PhosphorylationIHNMNNGSTVVCTLT
CCCCCCCCEEEEEEE
21.8322210691
1731PhosphorylationGMEAKIKSGAIEVLA
HHHHHHHCCCEEEEC
36.6124505115
1745PhosphorylationAPRRKKRTCFTQPVP
CCCCCCCCCCCCCCC
22.3526699800
1748PhosphorylationRKKRTCFTQPVPRSG
CCCCCCCCCCCCCCC
33.8226699800
1769UbiquitinationMTEVLAHKIRAVEKK
HHHHHHHHHHHHHCC
28.42-
1789PhosphorylationKRKNNSTTTNNSKPS
CCCCCCCCCCCCCCC
27.6122210691
1797PhosphorylationTNNSKPSSLPTLGSN
CCCCCCCCCCCCCCC
47.0622210691
1800PhosphorylationSKPSSLPTLGSNTET
CCCCCCCCCCCCCCC
49.3922210691
1805PhosphorylationLPTLGSNTETVQPEV
CCCCCCCCCCCCCCC
34.4325003641
1845PhosphorylationPHPVKEASPGFSWSP
CCCCCCCCCCCCCCC
27.0127732954
1849PhosphorylationKEASPGFSWSPKTAS
CCCCCCCCCCCCCCC
32.3427732954
1851PhosphorylationASPGFSWSPKTASAT
CCCCCCCCCCCCCCC
18.4729978859
1867PhosphorylationAPLKNDATASCGFSE
CCCCCCCCCCCCCCC
23.20-

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 TET1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TET1_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 TET1_HUMAN !!

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

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 TET1_HUMAN

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Related Literatures of Post-Translational Modification

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