Tet2
entrez
214133
canonical
uniprot
Q4JK59
canonical
ensembl
ENSMUSG00000040943
resolver
ensp
ENSMUSP00000096203
resolver
ensp
ENSMUSP00000143029
resolver
ensp
ENSMUSP00000223137
resolver
ensp
ENSMUSP00000340190
resolver
ensp
ENSMUSP00000340192
resolver
ensp
ENSMUSP00000340195
resolver
enst
ENSMUST00000196398
resolver
genesymbol
Tet2
resolver
genesymbol_syn
Kiaa1546
resolver
uniprot
A0A0G2JF55
resolver
uniprot
Q3U5R5
resolver
uniprot
Q3U633
resolver
uniprot
Q3UAI0
resolver
uniprot
Q6ZPN2
resolver
uniprot
Q8K2K3
resolver
uniprot_entry
A0A0G2JF55_MOUSE
resolver
uniprot_entry
TET2_MOUSE
resolver
uniprot_sec
Q3U5R5
resolver
uniprot_sec
Q3U633
resolver
uniprot_sec
Q3UAI0
resolver
uniprot_sec
Q6ZPN2
resolver
uniprot_sec
Q8K2K3
resolver
amino_acid_sequence
MEQDRTTHAEGTRLSPFLIAPPSPISHTEPLAVKLQNGSPLAERPHPEVNGDTKWQSSQSCYGISHMKGSQSSHESPHEDRGYSRCLQNGGIKRTVSEPSLSGLHPNKILKLDQKAKGESNIFEESQERNHGKSSRQPNVSGLSDNGEPVTSTTQESSGADAFPTRNYNGVEIQVLNEQEGEKGRSVTLLKNKIVLMPNGATVSAHSEENTRGELLEKTQCYPDCVSIAVQSTASHVNTPSSQAAIELSHEIPQPSLTSAQINFSQTSSLQLPPEPAAMVTKACDADNASKPAIVPGTCPFQKAEHQQKSALDIGPSRAENKTIQGSMELFAEEYYPSSDRNLQASHGSSEQYSKQKETNGAYFRQSSKFPKDSISPTTVTPPSQSLLAPRLVLQPPLEGKGALNDVALEEHHDYPNRSNRTLLREGKIDHQPKTSSSQSLNPSVHTPNPPLMLPEQHQNDCGSPSPEKSRKMSEYLMYYLPNHGHSGGLQEHSQYLMGHREQEIPKDANGKQTQGSVQAAPGWIELKAPNLHEALHQTKRKDISLHSVLHSQTGPVNQMSSKQSTGNVNMPGGFQRLPYLQKTAQPEQKAQMYQVQVNQGPSPGMGDQHLQFQKALYQECIPRTDPSSEAHPQAPSVPQYHFQQRVNPSSDKHLSQQATETQRLSGFLQHTPQTQASQTPASQNSNFPQICQQQQQQQLQRKNKEQMPQTFSHLQGSNDKQREGSCFGQIKVEESFCVGNQYSKSSNFQTHNNTQGGLEQVQNINKNFPYSKILTPNSSNLQILPSNDTHPACEREQALHPVGSKTSNLQNMQYFPNNVTPNQDVHRCFQEQAQKPQQASSLQGLKDRSQGESPAPPAEAAQQRYLVHNEAKALPVPEQGGSQTQTPPQKDTQKHAALRWLLLQKQEQQQTQQSQPGHNQMLRPIKTEPVSKPSSYRYPLSPPQENMSSRIKQEISSPSRDNGQPKSIIETMEQHLKQFQLKSLCDYKALTLKSQKHVKVPTDIQAAESENHARAAEPQATKSTDCSVLDDVSESDTPGEQSQNGKCEGCNPDKDEAPYYTHLGAGPDVAAIRTLMEERYGEKGKAIRIEKVIYTGKEGKSSQGCPIAKWVYRRSSEEEKLLCLVRVRPNHTCETAVMVIAIMLWDGIPKLLASELYSELTDILGKCGICTNRRCSQNETRNCCCQGENPETCGASFSFGCSWSMYYNGCKFARSKKPRKFRLHGAEPKEEERLGSHLQNLATVIAPIYKKLAPDAYNNQVEFEHQAPDCCLGLKEGRPFSGVTACLDFSAHSHRDQQNMPNGSTVVVTLNREDNREVGAKPEDEQFHVLPMYIIAPEDEFGSTEGQEKKIRMGSIEVLQSFRRRRVIRIGELPKSCKKKAEPKKAKTKKAARKRSSLENCSSRTEKGKSSSHTKLMENASHMKQMTAQPQLSGPVIRQPPTLQRHLQQGQRPQQPQPPQPQPQTTPQPQPQPQHIMPGNSQSVGSHCSGSTSVYTRQPTPHSPYPSSAHTSDIYGDTNHVNFYPTSSHASGSYLNPSNYMNPYLGLLNQNNQYAPFPYNGSVPVDNGSPFLGSYSPQAQSRDLHRYPNQDHLTNQNLPPIHTLHQQTFGDSPSKYLSYGNQNMQRDAFTTNSTLKPNVHHLATFSPYPTPKMDSHFMGAASRSPYSHPHTDYKTSEHHLPSHTIYSYTAAASGSSSSHAFHNKENDNIANGLSRVLPGFNHDRTASAQELLYSLTGSSQEKQPEVSGQDAAAVQEIEYWSDSEHNFQDPCIGGVAIAPTHGSILIECAKCEVHATTKVNDPDRNHPTRISLVLYRHKNLFLPKHCLALWEAKMAEKARKEEECGKNGSDHVSQKNHGKQEKREPTGPQEPSYLRFIQSLAENTGSVTTDSTVTTSPYAFTQVTGPYNTFV
uniprot
proteins
ec_number
1.14.11.80
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21057493, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:23352454, ECO:0000269|PubMed:23353889}.
uniprot
proteins
mass_dalton
212130
uniprot
proteins
mutagenesis
MUTAGEN 1200; /note="F->L: No effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1204; /note="W->R: Loss of 5-methylcytosine demethylase activity in vivo. No effect on interaction with DCAF1, nor on monoubiquitination."; /evidence="ECO:0000269|PubMed:21057493"; MUTAGEN 1205; /note="S->R: No effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1211; /note="C->Y: Loss of monoubiquitination and of 5-methylcytosine demethylase activity in vivo. No effect on interaction with DCAF1."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1212; /note="K->E: Strongly reduces ubiquitination, loss of DNA-binding, loss of 5-methylcytosine demethylase activity in vivo. Does not affect nuclear localization, nor interaction with DCAF1."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1212; /note="K->N: Strongly reduces ubiquitination, loss of DNA-binding, loss of 5-methylcytosine demethylase activity in vivo. Does not affect nuclear localization, nor interaction with DCAF1."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1212; /note="K->R: Strongly reduces ubiquitination."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1213; /note="F->S: Loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1215; /note="R->G: Loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1231; /note="E->G: No effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo."; /evidence="ECO:0000269|PubMed:25557551"; MUTAGEN 1280; /note="P->S: Impairs enzyme activity."; /evidence="ECO:0000269|PubMed:21057493"; MUTAGEN 1295; /note="H->Y: Loss of enzyme activity, no effect on interaction with DCAF1; when associated with A-1297."; /evidence="ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:25557551"; MUTAGEN 1297; /note="D->A: Loss of enzyme activity, no effect on interaction with DCAF1; when associated with Y-1295."; /evidence="ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:25557551"; MUTAGEN 1795; /note="H->R,Q: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:21057493"; MUTAGEN 1810; /note="R->S,M: Impairs enzyme activity."; /evidence="ECO:0000269|PubMed:21057493"; MUTAGEN 1827; /note="C->D: Impairs enzyme activity."; /evidence="ECO:0000269|PubMed:21057493
uniprot
proteins
post_translational_modification
PTM: May be glycosylated. It is unclear whether interaction with OGT leads to GlcNAcylation. According to a report, it is GlcNAcylated by OGT (PubMed:23352454). In contrast, another group reports no GlcNAcylation by OGT in human ortholog. {ECO:0000269|PubMed:23352454}.; PTM: Monoubiquitinated at Lys-1212 by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex; this modification promotes binding to DNA. {ECO:0000269|PubMed:25557551}.; PTM: Acetylated. {ECO:0000250|UniProtKB:Q6N021}.
uniprot
proteins
protein_family
TET family
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16722336
uniprot
proteins
pubmed
20639862
uniprot
proteins
pubmed
21057493
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21723200
uniprot
proteins
pubmed
21778364
uniprot
proteins
pubmed
21803851
uniprot
proteins
pubmed
21817016
uniprot
proteins
pubmed
23151479
uniprot
proteins
pubmed
23352454
uniprot
proteins
pubmed
23352810
uniprot
proteins
pubmed
23353889
uniprot
proteins
pubmed
24357321
uniprot
proteins
pubmed
25557551
uniprot
proteins
sequence_length
1912
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6N021}. Chromosome {ECO:0000250|UniProtKB:Q6N021}. Note=Localization to chromatin depends upon monoubiquitination at Lys-1212. {ECO:0000250|UniProtKB:Q6N021}.
uniprot
proteins