TET2_HUMAN - dbPTM
TET2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TET2_HUMAN
UniProt AC Q6N021
Protein Name Methylcytosine dioxygenase TET2
Gene Name TET2
Organism Homo sapiens (Human).
Sequence Length 2002
Subcellular Localization
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. Has a preference for 5-hydroxymethylcytosine in CpG motifs. 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, 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 MEQDRTNHVEGNRLSPFLIPSPPICQTEPLATKLQNGSPLPERAHPEVNGDTKWHSFKSYYGIPCMKGSQNSRVSPDFTQESRGYSKCLQNGGIKRTVSEPSLSGLLQIKKLKQDQKANGERRNFGVSQERNPGESSQPNVSDLSDKKESVSSVAQENAVKDFTSFSTHNCSGPENPELQILNEQEGKSANYHDKNIVLLKNKAVLMPNGATVSASSVEHTHGELLEKTLSQYYPDCVSIAVQKTTSHINAINSQATNELSCEITHPSHTSGQINSAQTSNSELPPKPAAVVSEACDADDADNASKLAAMLNTCSFQKPEQLQQQKSVFEICPSPAENNIQGTTKLASGEEFCSGSSSNLQAPGGSSERYLKQNEMNGAYFKQSSVFTKDSFSATTTPPPPSQLLLSPPPPLPQVPQLPSEGKSTLNGGVLEEHHHYPNQSNTTLLREVKIEGKPEAPPSQSPNPSTHVCSPSPMLSERPQNNCVNRNDIQTAGTMTVPLCSEKTRPMSEHLKHNPPIFGSSGELQDNCQQLMRNKEQEILKGRDKEQTRDLVPPTQHYLKPGWIELKAPRFHQAESHLKRNEASLPSILQYQPNLSNQMTSKQYTGNSNMPGGLPRQAYTQKTTQLEHKSQMYQVEMNQGQSQGTVDQHLQFQKPSHQVHFSKTDHLPKAHVQSLCGTRFHFQQRADSQTEKLMSPVLKQHLNQQASETEPFSNSHLLQHKPHKQAAQTQPSQSSHLPQNQQQQQKLQIKNKEEILQTFPHPQSNNDQQREGSFFGQTKVEECFHGENQYSKSSEFETHNVQMGLEEVQNINRRNSPYSQTMKSSACKIQVSCSNNTHLVSENKEQTTHPELFAGNKTQNLHHMQYFPNNVIPKQDLLHRCFQEQEQKSQQASVLQGYKNRNQDMSGQQAAQLAQQRYLIHNHANVFPVPDQGGSHTQTPPQKDTQKHAALRWHLLQKQEQQQTQQPQTESCHSQMHRPIKVEPGCKPHACMHTAPPENKTWKKVTKQENPPASCDNVQQKSIIETMEQHLKQFHAKSLFDHKALTLKSQKQVKVEMSGPVTVLTRQTTAAELDSHTPALEQQTTSSEKTPTKRTAASVLNNFIESPSKLLDTPIKNLLDTPVKTQYDFPSCRCVEQIIEKDEGPFYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVVRRSSSEEKLLCLVRERAGHTCEAAVIVILILVWEGIPLSLADKLYSELTETLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFGCSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESHLQNLSTLMAPTYKKLAPDAYNNQIEYEHRAPECRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREFGGKPEDEQLHVLPLYKVSDVDEFGSVEAQEEKKRSGAIQVLSSFRRKVRMLAEPVKTCRQRKLEAKKAAAEKLSSLENSSNKNEKEKSAPSRTKQTENASQAKQLAELLRLSGPVMQQSQQPQPLQKQPPQPQQQQRPQQQQPHHPQTESVNSYSASGSTNPYMRRPNPVSPYPNSSHTSDIYGSTSPMNFYSTSSQAAGSYLNSSNPMNPYPGLLNQNTQYPSYQCNGNLSVDNCSPYLGSYSPQSQPMDLYRYPSQDPLSKLSLPPIHTLYQPRFGNSQSFTSKYLGYGNQNMQGDGFSSCTIRPNVHHVGKLPPYPTHEMDGHFMGATSRLPPNLSNPNMDYKNGEHHSPSHIIHNYSAAPGMFNSSLHALHLQNKENDMLSHTANGLSKMLPALNHDRTACVQGGLHKLSDANGQEKQPLALVQGVASGAEDNDEVWSDSEQSFLDPDIGGVAVAPTHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKMAEKAREKEEECEKYGPDYVPQKSHGKKVKREPAEPHETSEPTYLRFIKSLAERTMSVTTDSTVTTSPYAFTRVTGPYNRYI
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
6Phosphorylation--MEQDRTNHVEGNR
--CCCCCCCCCCCCC		37.6628450419
15PhosphorylationHVEGNRLSPFLIPSP
CCCCCCCCCCCCCCC		15.4628450419
21PhosphorylationLSPFLIPSPPICQTE
CCCCCCCCCCCCCCC		35.9928450419
27PhosphorylationPSPPICQTEPLATKL
CCCCCCCCCCCCHHC		34.8526074081
32PhosphorylationCQTEPLATKLQNGSP
CCCCCCCHHCCCCCC		39.7128450419
38PhosphorylationATKLQNGSPLPERAH
CHHCCCCCCCCCCCC		30.7129255136
53AcetylationPEVNGDTKWHSFKSY
CCCCCCCCCCCCCEE		47.8823954790
69PhosphorylationGIPCMKGSQNSRVSP
CCCCCCCCCCCCCCC		22.2223186163
72PhosphorylationCMKGSQNSRVSPDFT
CCCCCCCCCCCCCCC		26.8230108239
75PhosphorylationGSQNSRVSPDFTQES
CCCCCCCCCCCCHHH		20.0323401153
79PhosphorylationSRVSPDFTQESRGYS
CCCCCCCCHHHCCHH		38.5130266825
82PhosphorylationSPDFTQESRGYSKCL
CCCCCHHHCCHHHHH		22.6130266825
97PhosphorylationQNGGIKRTVSEPSLS
HCCCCCCCCCCCCHH		24.3125159151
99PhosphorylationGGIKRTVSEPSLSGL
CCCCCCCCCCCHHHH		43.0823401153
102PhosphorylationKRTVSEPSLSGLLQI
CCCCCCCCHHHHHHH		30.9928450419
104PhosphorylationTVSEPSLSGLLQIKK
CCCCCCHHHHHHHHH		31.5626074081
110AcetylationLSGLLQIKKLKQDQK
HHHHHHHHHHHHHHH		38.81126212603
111AcetylationSGLLQIKKLKQDQKA
HHHHHHHHHHHHHHH		63.65126212605
128PhosphorylationERRNFGVSQERNPGE
CCCCCCCCCCCCCCC		27.0630257219
152PhosphorylationSDKKESVSSVAQENA
CCCHHHHHHHHHHHH		28.5129083192
153PhosphorylationDKKESVSSVAQENAV
CCHHHHHHHHHHHHH		21.2229083192
305PhosphorylationADDADNASKLAAMLN
CCCCCHHHHHHHHHH		34.1626074081
313PhosphorylationKLAAMLNTCSFQKPE
HHHHHHHHCCCCCHH		12.9326074081
315PhosphorylationAAMLNTCSFQKPEQL
HHHHHHCCCCCHHHH		28.7726074081
318AcetylationLNTCSFQKPEQLQQQ
HHHCCCCCHHHHHHC		48.8126051181
327PhosphorylationEQLQQQKSVFEICPS
HHHHHCCCCCHHCCC		27.9226074081
334PhosphorylationSVFEICPSPAENNIQ
CCCHHCCCCCHHCCC		32.1225159151
343PhosphorylationAENNIQGTTKLASGE
CHHCCCCCEEECCCC		12.3729978859
344PhosphorylationENNIQGTTKLASGEE
HHCCCCCEEECCCCC		30.7729978859
369MethylationAPGGSSERYLKQNEM
CCCCCHHHHHHHHHC		43.99115387113
396PhosphorylationKDSFSATTTPPPPSQ
CCCCCCCCCCCCHHH		36.7028348404
397PhosphorylationDSFSATTTPPPPSQL
CCCCCCCCCCCHHHH		29.4628348404
402PhosphorylationTTTPPPPSQLLLSPP
CCCCCCHHHHCCCCC		38.9528348404
460PhosphorylationGKPEAPPSQSPNPST
CCCCCCCCCCCCCCC		42.0828348404
462PhosphorylationPEAPPSQSPNPSTHV
CCCCCCCCCCCCCCC		30.8628348404
466PhosphorylationPSQSPNPSTHVCSPS
CCCCCCCCCCCCCCC		37.4728348404
467PhosphorylationSQSPNPSTHVCSPSP
CCCCCCCCCCCCCCC		21.4228348404
471PhosphorylationNPSTHVCSPSPMLSE
CCCCCCCCCCCCCCC		27.5928348404
492PhosphorylationVNRNDIQTAGTMTVP
CCHHHCCCCCEEEEE		27.6522210691
495PhosphorylationNDIQTAGTMTVPLCS
HHCCCCCEEEEECCC		13.7522210691
497PhosphorylationIQTAGTMTVPLCSEK
CCCCCEEEEECCCCC		20.8622210691
561AcetylationPPTQHYLKPGWIELK
CCCCHHCCCCEEEEE		34.0326051181
585PhosphorylationHLKRNEASLPSILQY
HHHHCCCCCHHHHHH		34.33-
655AcetylationDQHLQFQKPSHQVHF
HHHHCCCCCCCEEEC		50.1826051181
655UbiquitinationDQHLQFQKPSHQVHF
HHHHCCCCCCCEEEC		50.18-
696PhosphorylationSQTEKLMSPVLKQHL
HHHHHHHHHHHHHHH		23.4621815630
747UbiquitinationQNQQQQQKLQIKNKE
HHHHHHHHHHHCCHH		37.71-
817PhosphorylationQNINRRNSPYSQTMK
HHHHHCCCCCHHHHC		24.3325849741
819PhosphorylationINRRNSPYSQTMKSS
HHHCCCCCHHHHCCC		17.15-
820PhosphorylationNRRNSPYSQTMKSSA
HHCCCCCHHHHCCCC		23.6627732954
822PhosphorylationRNSPYSQTMKSSACK
CCCCCHHHHCCCCCE		22.18-
859PhosphorylationELFAGNKTQNLHHMQ
HHHCCCCCCCCCCCC		27.04-
900UbiquitinationASVLQGYKNRNQDMS
HHHHHHHHCCCCCCC		57.14-
938PhosphorylationPDQGGSHTQTPPQKD
CCCCCCCCCCCCCCC		35.5228555341
940PhosphorylationQGGSHTQTPPQKDTQ
CCCCCCCCCCCCCHH		37.7828555341
1023PhosphorylationCDNVQQKSIIETMEQ
CCHHHHHHHHHHHHH		25.1828555341
1047PhosphorylationLFDHKALTLKSQKQV
HHCCCCHHCCCCCEE		36.6828258704
1076PhosphorylationTTAAELDSHTPALEQ
CCHHHHHCCCHHHHH		41.7123186163
1078PhosphorylationAAELDSHTPALEQQT
HHHHHCCCHHHHHCC		17.7623186163
1085PhosphorylationTPALEQQTTSSEKTP
CHHHHHCCCCCCCCC		28.4827732954
1086PhosphorylationPALEQQTTSSEKTPT
HHHHHCCCCCCCCCC		26.3927732954
1087PhosphorylationALEQQTTSSEKTPTK
HHHHCCCCCCCCCCH		39.6327732954
1088PhosphorylationLEQQTTSSEKTPTKR
HHHCCCCCCCCCCHH		40.8127732954
1091PhosphorylationQTTSSEKTPTKRTAA
CCCCCCCCCCHHHHH		31.9427050516
1093PhosphorylationTSSEKTPTKRTAASV
CCCCCCCCHHHHHHH		38.0927732954
1099PhosphorylationPTKRTAASVLNNFIE
CCHHHHHHHHHHHHH		25.3630108239
1107PhosphorylationVLNNFIESPSKLLDT
HHHHHHHCHHHHCCC		29.6519664994
1109PhosphorylationNNFIESPSKLLDTPI
HHHHHCHHHHCCCCH		45.2630278072
1114PhosphorylationSPSKLLDTPIKNLLD
CHHHHCCCCHHHHCC		27.2122199227
1117AcetylationKLLDTPIKNLLDTPV
HHCCCCHHHHCCCCC		42.62126212601
1122PhosphorylationPIKNLLDTPVKTQYD
CHHHHCCCCCCCCCC		29.9221712546
1126PhosphorylationLLDTPVKTQYDFPSC
HCCCCCCCCCCCCCC		32.3728450419
1299UbiquitinationSMYYNGCKFARSKIP
HHEECCCHHHHCCCC		43.38-
1317AcetylationKLLGDDPKEEEKLES
CCCCCCHHHHHHHHH		82.0811791449
1331PhosphorylationSHLQNLSTLMAPTYK
HHHHHHHHHHHHCHH		24.58-
1338UbiquitinationTLMAPTYKKLAPDAY
HHHHHCHHHHCCCHH		43.73-
1339UbiquitinationLMAPTYKKLAPDAYN
HHHHCHHHHCCCHHH		39.19-
1339AcetylationLMAPTYKKLAPDAYN
HHHHCHHHHCCCHHH		39.1911791459
1345PhosphorylationKKLAPDAYNNQIEYE
HHHCCCHHHCCCCEE		23.2517053785
1441PhosphorylationAQEEKKRSGAIQVLS
HHHHHHHHCHHHHHH		41.2628122231
1449PhosphorylationGAIQVLSSFRRKVRM
CHHHHHHHHHHHHHH		20.72-
1463PhosphorylationMLAEPVKTCRQRKLE
HHHHHHHHHHHHHHH		17.10-
1478AcetylationAKKAAAEKLSSLENS
HHHHHHHHHHHHHCC		49.2823954790
1481O-linked_GlycosylationAAAEKLSSLENSSNK
HHHHHHHHHHCCCCC		50.5730379171
1481PhosphorylationAAAEKLSSLENSSNK
HHHHHHHHHHCCCCC		50.5730576142
1485PhosphorylationKLSSLENSSNKNEKE
HHHHHHCCCCCCHHH		26.3930576142
1494PhosphorylationNKNEKEKSAPSRTKQ
CCCHHHCCCCCHHHH		46.64-
1497PhosphorylationEKEKSAPSRTKQTEN
HHHCCCCCHHHHCCC		52.91-
1502PhosphorylationAPSRTKQTENASQAK
CCCHHHHCCCHHHHH		32.53-
1506PhosphorylationTKQTENASQAKQLAE
HHHCCCHHHHHHHHH		42.10-
1518PhosphorylationLAELLRLSGPVMQQS
HHHHHHHHCHHHHCC		34.3225627689
1518O-linked_GlycosylationLAELLRLSGPVMQQS
HHHHHHHHCHHHHCC		34.3272255791
1559PhosphorylationPQTESVNSYSASGST
CCCCCCCCCCCCCCC		20.5024275569
1560PhosphorylationQTESVNSYSASGSTN
CCCCCCCCCCCCCCC		11.7624275569
1561PhosphorylationTESVNSYSASGSTNP
CCCCCCCCCCCCCCC		18.7724275569
1565PhosphorylationNSYSASGSTNPYMRR
CCCCCCCCCCCCCCC		23.6324275569
1682MethylationIHTLYQPRFGNSQSF
CCCCCCCCCCCCCCC		36.2624129315
1682Asymmetric dimethylarginineIHTLYQPRFGNSQSF
CCCCCCCCCCCCCCC		36.26-
1970PhosphorylationTYLRFIKSLAERTMS
HHHHHHHHHHHHCCC		28.1723403867
1975PhosphorylationIKSLAERTMSVTTDS
HHHHHHHCCCCCCCC		12.80-
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
99SPhosphorylationKinaseAMPKA1Q13131
PSP
1939YPhosphorylationKinaseJAK2O60674
PSP
1964YPhosphorylationKinaseJAK2O60674
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TET2_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 TET2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCAF1_HUMANVPRBPphysical
25557551
DDB1_HUMANDDB1physical
25557551
COE1_HUMANEBF1physical
23863747
SEMG1_HUMANSEMG1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
essential thrombocythemia, polycythemia vera, primary myelofibrosis (chronic idiopathic myelofibrosis). Bone marrow samples from patients display uniformly low levels of hmC in genomic DNA compared to bone marrow samples from healthy controls as well as hypomethylation relative to controls at the majority of differentially methylated CpG sites.Note=TET2 is frequently mutated in myeloproliferative disorders (MPD). These constitute a heterogeneous group of disorders, also known as myeloproliferative diseases or myeloproliferative neoplasms (MPN), characterized by cellular proliferation of one or more hematologic cell lines in the peripheral blood, distinct from acute leukemia. Included diseases are
263300
Note=TET2 is frequently mutated in systemic mastocytosis
also known as systemic mast cell disease. A condition with features in common with myeloproliferative diseases. It is a clonal disorder of the mast cell and its precursor cells. The clinical symptoms and signs of systemic mastocytosis are due to accumulation of clonally derived mast cells in different tissues, including bone marrow, skin, the gastrointestinal tract, the liver, and the spleen.
614286
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TET2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-1107, ANDMASS SPECTROMETRY.
"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 THR-97, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1345, AND MASSSPECTROMETRY.

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