TET1_MOUSE - dbPTM
TET1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TET1_MOUSE
UniProt AC Q3URK3
Protein Name Methylcytosine dioxygenase TET1
Gene Name Tet1
Organism Mus musculus (Mouse).
Sequence Length 2007
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 essential 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 MSRSRPAKPSKSVKTKLQKKKDIQMKTKTSKQAVRHGASAKAVNPGKPKQLIKRRDGKKETEDKTPTPAPSFLTRAGAARMNRDRNQVLFQNPDSLTCNGFTMALRRTSLSWRLSQRPVVTPKPKKVPPSKKQCTHNIQDEPGVKHSENDSVPSQHATVSPGTENGEQNRCLVEGESQEITQSCPVFEERIEDTQSCISASGNLEAEISWPLEGTHCEELLSHQTSDNECTSPQECAPLPQRSTSEVTSQKNTSNQLADLSSQVESIKLSDPSPNPTGSDHNGFPDSSFRIVPELDLKTCMPLDESVYPTALIRFILAGSQPDVFDTKPQEKTLITTPEQVGSHPNQVLDATSVLGQAFSTLPLQWGFSGANLVQVEALGKGSDSPEDLGAITMLNQQETVAMDMDRNATPDLPIFLPKPPNTVATYSSPLLGPEPHSSTSCGLEVQGATPILTLDSGHTPQLPPNPESSSVPLVIAANGTRAEKQFGTSLFPAVPQGFTVAAENEVQHAPLDLTQGSQAAPSKLEGEISRVSITGSADVKATAMSMPVTQASTSSPPCNSTPPMVERRKRKACGVCEPCQQKANCGECTYCKNRKNSHQICKKRKCEVLKKKPEATSQAQVTKENKRPQREKKPKVLKTDFNNKPVNGPKSESMDCSRRGHGEEEQRLDLITHPLENVRKNAGGMTGIEVEKWAPNKKSHLAEGQVKGSCDANLTGVENPQPSEDDKQQTNPSPTFAQTIRNGMKNVHCLPTDTHLPLNKLNHEEFSKALGNNSSKLLTDPSNCKDAMSVTTSGGECDHLKGPRNTLLFQKPGLNCRSGAEPTIFNNHPNTHSAGSRPHPPEKVPNKEPKDGSPVQPSLLSLMKDRRLTLEQVVAIEALTQLSEAPSESSSPSKPEKDEEAHQKTASLLNSCKAILHSVRKDLQDPNVQGKGLHHDTVVFNGQNRTFKSPDSFATNQALIKSQGYPSSPTAEKKGAAGGRAPFDGFENSHPLPIESHNLENCSQVLSCDQNLSSHDPSCQDAPYSQIEEDVAAQLTQLASTINHINAEVRNAESTPESLVAKNTKQKHSQEKRMVHQKPPSSTQTKPSVPSAKPKKAQKKARATPHANKRKKKPPARSSQENDQKKQEQLAIEYSKMHDIWMSSKFQRFGQSSPRSFPVLLRNIPVFNQILKPVTQSKTPSQHNELFPPINQIKFTRNPELAKEKVKVEPSDSLPTCQFKTESGGQTFAEPADNSQGQPMVSVNQEAHPLPQSPPSNQCANIMAGAAQTQFHLGAQENLVHQIPPPTLPGTSPDTLLPDPASILRKGKVLHFDGITVVTEKREAQTSSNGPLGPTTDSAQSEFKESIMDLLSKPAKNLIAGLKEQEAAPCDCDGGTQKEKGPYYTHLGAGPSVAAVRELMETRFGQKGKAIRIEKIVFTGKEGKSSQGCPVAKWVIRRSGPEEKLICLVRERVDHHCSTAVIVVLILLWEGIPRLMADRLYKELTENLRSYSGHPTDRRCTLNKKRTCTCQGIDPKTCGASFSFGCSWSMYFNGCKFGRSENPRKFRLAPNYPLHEKQLEKNLQELATVLAPLYKQMAPVAYQNQVEYEEVAGDCRLGNEEGRPFSGVTCCMDFCAHSHKDIHNMHNGSTVVCTLIRADGRDTNCPEDEQLHVLPLYRLADTDEFGSVEGMKAKIKSGAIQVNGPTRKRRLRFTEPVPRCGKRAKMKQNHNKSGSHNTKSFSSASSTSHLVKDESTDFCPLQASSAETSTCTYSKTASGGFAETSSILHCTMPSGAHSGANAAAGECTGTVQPAEVAAHPHQSLPTADSPVHAEPLTSPSEQLTSNQSNQQLPLLSNSQKLASCQVEDERHPEADEPQHPEDDNLPQLDEFWSDSEEIYADPSFGGVAIAPIHGSVLIECARKELHATTSLRSPKRGVPFRVSLVFYQHKSLNKPNHGFDINKIKCKCKKVTKKKPADRECPDVSPEANLSHQIPSRVASTLTRDNVVTVSPYSLTHVAGPYNRWV
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
10PhosphorylationRSRPAKPSKSVKTKL
CCCCCCCCHHHHHHH		36.5320139300
12PhosphorylationRPAKPSKSVKTKLQK
CCCCCCHHHHHHHHH		32.9320139300
115PhosphorylationTSLSWRLSQRPVVTP
HCCCCHHHCCCCCCC		18.64-
121PhosphorylationLSQRPVVTPKPKKVP
HHCCCCCCCCCCCCC		26.31-
160PhosphorylationPSQHATVSPGTENGE
CCCCEEECCCCCCCC		17.1729895711
177PhosphorylationRCLVEGESQEITQSC
CEEEECCCHHHHHCC		43.92-
253O-linked_GlycosylationEVTSQKNTSNQLADL
HHHCCCCCHHHHHHH		35.7725568311
270O-linked_GlycosylationQVESIKLSDPSPNPT
HHEEEECCCCCCCCC		42.3477070227
273O-linked_GlycosylationSIKLSDPSPNPTGSD
EEECCCCCCCCCCCC		42.1525568311
277O-linked_GlycosylationSDPSPNPTGSDHNGF
CCCCCCCCCCCCCCC		56.8325568311
298UbiquitinationIVPELDLKTCMPLDE
ECCCCCCCCCCCCCC		39.07-
299PhosphorylationVPELDLKTCMPLDES
CCCCCCCCCCCCCCC		22.72-
320PhosphorylationIRFILAGSQPDVFDT
HHHHHHCCCCCCCCC		32.69-
327O-linked_GlycosylationSQPDVFDTKPQEKTL
CCCCCCCCCCCCCEE		32.9125568311
327PhosphorylationSQPDVFDTKPQEKTL
CCCCCCCCCCCCCEE		32.91-
328UbiquitinationQPDVFDTKPQEKTLI
CCCCCCCCCCCCEEE		46.69-
535O-linked_GlycosylationEISRVSITGSADVKA
EEEEEEEECCCCCEE		19.9951588499
556PhosphorylationVTQASTSSPPCNSTP
CEECCCCCCCCCCCC		32.7122006019
561PhosphorylationTSSPPCNSTPPMVER
CCCCCCCCCCCCHHH		49.35-
687PhosphorylationRKNAGGMTGIEVEKW
HHHCCCCCCEEEEEE		37.9825619855
724O-linked_GlycosylationGVENPQPSEDDKQQT
CCCCCCCCCCCCCCC		48.70105050871
731O-linked_GlycosylationSEDDKQQTNPSPTFA
CCCCCCCCCCCHHHH		46.7525568311
734PhosphorylationDKQQTNPSPTFAQTI
CCCCCCCCHHHHHHH		38.3522006019
736PhosphorylationQQTNPSPTFAQTIRN
CCCCCCHHHHHHHHH		35.62-
740O-linked_GlycosylationPSPTFAQTIRNGMKN
CCHHHHHHHHHCCCC		20.6225568311
792O-linked_GlycosylationCKDAMSVTTSGGECD
CCCCEEEECCCCCCC		14.1325568311
793O-linked_GlycosylationKDAMSVTTSGGECDH
CCCEEEECCCCCCCC		24.1825568311
794O-linked_GlycosylationDAMSVTTSGGECDHL
CCEEEECCCCCCCCC		35.1225568311
854PhosphorylationNKEPKDGSPVQPSLL
CCCCCCCCCCCHHHH		31.8429895711
892PhosphorylationEAPSESSSPSKPEKD
CCCCCCCCCCCCCCC		42.33-
947PhosphorylationVFNGQNRTFKSPDSF
EECCCCCEECCCCCC		42.8630635358
950PhosphorylationGQNRTFKSPDSFATN
CCCCEECCCCCCHHC		29.7330635358
953O-linked_GlycosylationRTFKSPDSFATNQAL
CEECCCCCCHHCHHH		21.8425568311
953PhosphorylationRTFKSPDSFATNQAL
CEECCCCCCHHCHHH		21.8430635358
956O-linked_GlycosylationKSPDSFATNQALIKS
CCCCCCHHCHHHHHH		26.3425568311
956PhosphorylationKSPDSFATNQALIKS
CCCCCCHHCHHHHHH		26.3430635358
963PhosphorylationTNQALIKSQGYPSSP
HCHHHHHHCCCCCCC		23.1130635358
966PhosphorylationALIKSQGYPSSPTAE
HHHHHCCCCCCCHHH		7.7230635358
968PhosphorylationIKSQGYPSSPTAEKK
HHHCCCCCCCHHHHC		40.2330635358
969PhosphorylationKSQGYPSSPTAEKKG
HHCCCCCCCHHHHCC		23.0529895711
971PhosphorylationQGYPSSPTAEKKGAA
CCCCCCCHHHHCCCC		49.7730635358
1180PhosphorylationKPVTQSKTPSQHNEL
CCCCCCCCCCCCCCC		33.1625159016
1182PhosphorylationVTQSKTPSQHNELFP
CCCCCCCCCCCCCCC		49.6725159016
1327O-linked_GlycosylationTEKREAQTSSNGPLG
EECCCCCCCCCCCCC		40.9625568311
1342O-linked_GlycosylationPTTDSAQSEFKESIM
CCCHHHHHHHHHHHH		44.7225568311
1668PhosphorylationADTDEFGSVEGMKAK
CCCCCCCCCCHHHHE		23.4729899451
1721O-linked_GlycosylationSGSHNTKSFSSASST
CCCCCCCCCCCCCCC		28.4625568311
1728O-linked_GlycosylationSFSSASSTSHLVKDE
CCCCCCCCCCCCCCC		20.0525568311
1729O-linked_GlycosylationFSSASSTSHLVKDES
CCCCCCCCCCCCCCC		19.4425568311
1746PhosphorylationFCPLQASSAETSTCT
CCCCCCCCCCCCCCE		32.8929895711
1751PhosphorylationASSAETSTCTYSKTA
CCCCCCCCCEEEECC		19.1129895711
1753PhosphorylationSAETSTCTYSKTASG
CCCCCCCEEEECCCC		30.8029895711
1754PhosphorylationAETSTCTYSKTASGG
CCCCCCEEEECCCCC		15.4329895711
1755PhosphorylationETSTCTYSKTASGGF
CCCCCEEEECCCCCC		12.8429895711
1914PhosphorylationHATTSLRSPKRGVPF
HCCCCCCCCCCCCCE		39.81-
1966O-linked_GlycosylationDRECPDVSPEANLSH
CCCCCCCCCCCCHHH		25.1425568311
1966PhosphorylationDRECPDVSPEANLSH
CCCCCCCCCCCCHHH		25.14-
1981O-linked_GlycosylationQIPSRVASTLTRDNV
CCCHHHHHCCCCCCE		22.5425568311
1982O-linked_GlycosylationIPSRVASTLTRDNVV
CCHHHHHCCCCCCEE		23.5525568311
1984O-linked_GlycosylationSRVASTLTRDNVVTV
HHHHHCCCCCCEEEE		35.7425568311
1992PhosphorylationRDNVVTVSPYSLTHV
CCCEEEECCCCCCCC		14.57-
1995O-linked_GlycosylationVVTVSPYSLTHVAGP
EEEECCCCCCCCCCC		30.1225568311
1997O-linked_GlycosylationTVSPYSLTHVAGPYN
EECCCCCCCCCCCCC		14.3625568311
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TET1_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 TET1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_MOUSESin3aphysical
21490601
SAP30_MOUSESap30physical
21490601
SDS3_MOUSESuds3physical
21490601
SP130_MOUSESap130physical
21490601
HDAC2_MOUSEHdac2physical
21490601
RBBP7_MOUSERbbp7physical
21490601
HDAC1_MOUSEHdac1physical
21490601
ARI4B_MOUSEArid4bphysical
21490601
NANOG_MOUSENanogphysical
23395962
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TET1_MOUSE

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Related Literatures of Post-Translational Modification

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