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Q8NFU7

- TET1_HUMAN

UniProt

Q8NFU7 - TET1_HUMAN

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Protein
Methylcytosine dioxygenase TET1
Gene
TET1, CXXC6, KIAA1676, LCX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

DNA 5-methylcytosine + 2-oxoglutarate + O2 = DNA 5-hydroxymethylcytosine + succinate + CO2.2 Publications
DNA 5-hydroxymethylcytosine + 2-oxoglutarate + O2 = DNA 5-formylcytosine + succinate + CO2.2 Publications
DNA 5-formylcytosine + 2-oxoglutarate + O2 = DNA 5-carboxylcytosine + succinate + CO2.2 Publications

Cofactori

Binds 1 Fe2+ ion per subunit.1 Publication
Binds 3 zinc ions per subunit. The zinc ions have a structural role By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1422 – 14221Zinc 1 By similarity
Metal bindingi1424 – 14241Zinc 1 By similarity
Metal bindingi1482 – 14821Zinc 2 By similarity
Metal bindingi1508 – 15081Zinc 1; via pros nitrogen By similarity
Metal bindingi1510 – 15101Zinc 1 By similarity
Binding sitei1551 – 155112-oxoglutarate By similarity
Metal bindingi1561 – 15611Zinc 2 By similarity
Metal bindingi1563 – 15631Zinc 2 By similarity
Metal bindingi1579 – 15791Zinc 3 By similarity
Metal bindingi1588 – 15881Zinc 3 By similarity
Sitei1608 – 16092Breakpoint for translocation to form KMT2A/MLL1-TET1 oncogene
Metal bindingi1648 – 16481Zinc 3 By similarity
Binding sitei1664 – 166412-oxoglutarate By similarity
Metal bindingi1670 – 16701Zinc 2; via tele nitrogen By similarity
Metal bindingi1672 – 16721Iron; catalytic
Metal bindingi1674 – 16741Iron; catalytic
Binding sitei1677 – 16771Substrate By similarity
Binding sitei1706 – 170612-oxoglutarate By similarity
Metal bindingi2028 – 20281Iron; catalytic By similarity
Metal bindingi2059 – 20591Zinc 3; via pros nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri584 – 62542CXXC-type
Add
BLAST

GO - Molecular functioni

  1. iron ion binding Source: UniProtKB
  2. methylcytosine dioxygenase activity Source: UniProtKB
  3. structure-specific DNA binding Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA demethylation Source: UniProtKB
  2. chromatin modification Source: UniProtKB-KW
  3. inner cell mass cell differentiation Source: UniProtKB
  4. negative regulation of methylation-dependent chromatin silencing Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. protein O-linked glycosylation Source: UniProtKB
  7. regulation of DNA methylation Source: Ensembl
  8. stem cell maintenance Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200682. TET1,2,3 and TDG demethylate DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylcytosine dioxygenase TET1 (EC:1.14.11.n2)
Alternative name(s):
CXXC-type zinc finger protein 6
Leukemia-associated protein with a CXXC domain
Ten-eleven translocation 1 gene protein
Gene namesi
Name:TET1
Synonyms:CXXC6, KIAA1676, LCX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:29484. TET1.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TET1 may be a cause of acute leukemias. Translocation t(10;11)(q22;q23) with KMT2A/MLL1. This is a rare chromosomal translocation 5' KMT2A/MLL1-TET1 3'.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1672 – 16721H → Y: Loss of catalytic activity and loss of the ability to induce DNA demethylation. 2 Publications
Mutagenesisi1674 – 16741D → A: Loss of catalytic activity and loss of the ability to induce DNA demethylation. 2 Publications

Organism-specific databases

PharmGKBiPA162405605.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21362136Methylcytosine dioxygenase TET1
PRO_0000251949Add
BLAST

Post-translational modificationi

Glycosylated. Interaction with OGT leads to GlcNAcylation By similarity.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8NFU7.
PRIDEiQ8NFU7.

PTM databases

PhosphoSiteiQ8NFU7.

Expressioni

Tissue specificityi

Expressed in fetal heart, lung and brain, and in adult skeletal muscle, thymus and ovary. Not detected in adult heart, lung or brain.2 Publications

Gene expression databases

BgeeiQ8NFU7.
CleanExiHS_TET1.
GenevestigatoriQ8NFU7.

Organism-specific databases

HPAiCAB014886.
HPA019032.

Interactioni

Subunit structurei

Interacts with HCFC1 and OGT By similarity. Interacts with SIN3A; recruits the transcriptional corepressor SIN3A to gene promoters.1 Publication

Protein-protein interaction databases

BioGridi123225. 1 interaction.
IntActiQ8NFU7. 2 interactions.
STRINGi9606.ENSP00000362748.

Structurei

3D structure databases

ProteinModelPortaliQ8NFU7.
SMRiQ8NFU7. Positions 586-637, 1421-2071.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni528 – 674147Sufficient for binding to genomic CpG islands
Add
BLAST
Regioni1580 – 159314Interaction with DNA By similarity
Add
BLAST
Regioni2043 – 204532-oxoglutarate binding By similarity
Regioni2049 – 20513Substrate binding By similarity

Sequence similaritiesi

Belongs to the TET family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG76473.
HOGENOMiHOG000154549.
InParanoidiQ8NFU7.
KOiK13097.
OMAiPHCTMPS.
OrthoDBiEOG7DVD94.
PhylomeDBiQ8NFU7.
TreeFamiTF324004.

Family and domain databases

InterProiIPR024779. 2OGFeDO_nucleic_acid_mod.
IPR002857. Znf_CXXC.
[Graphical view]
PfamiPF12851. Tet_JBP. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PROSITEiPS51058. ZF_CXXC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NFU7-1 [UniParc]FASTAAdd to Basket

« Hide

MSRSRHARPS RLVRKEDVNK KKKNSQLRKT TKGANKNVAS VKTLSPGKLK     50
QLIQERDVKK KTEPKPPVPV RSLLTRAGAA RMNLDRTEVL FQNPESLTCN 100
GFTMALRSTS LSRRLSQPPL VVAKSKKVPL SKGLEKQHDC DYKILPALGV 150
KHSENDSVPM QDTQVLPDIE TLIGVQNPSL LKGKSQETTQ FWSQRVEDSK 200
INIPTHSGPA AEILPGPLEG TRCGEGLFSE ETLNDTSGSP KMFAQDTVCA 250
PFPQRATPKV TSQGNPSIQL EELGSRVESL KLSDSYLDPI KSEHDCYPTS 300
SLNKVIPDLN LRNCLALGGS TSPTSVIKFL LAGSKQATLG AKPDHQEAFE 350
ATANQQEVSD TTSFLGQAFG AIPHQWELPG ADPVHGEALG ETPDLPEIPG 400
AIPVQGEVFG TILDQQETLG MSGSVVPDLP VFLPVPPNPI ATFNAPSKWP 450
EPQSTVSYGL AVQGAIQILP LGSGHTPQSS SNSEKNSLPP VMAISNVENE 500
KQVHISFLPA NTQGFPLAPE RGLFHASLGI AQLSQAGPSK SDRGSSQVSV 550
TSTVHVVNTT VVTMPVPMVS TSSSSYTTLL PTLEKKKRKR CGVCEPCQQK 600
TNCGECTYCK NRKNSHQICK KRKCEELKKK PSVVVPLEVI KENKRPQREK 650
KPKVLKADFD NKPVNGPKSE SMDYSRCGHG EEQKLELNPH TVENVTKNED 700
SMTGIEVEKW TQNKKSQLTD HVKGDFSANV PEAEKSKNSE VDKKRTKSPK 750
LFVQTVRNGI KHVHCLPAET NVSFKKFNIE EFGKTLENNS YKFLKDTANH 800
KNAMSSVATD MSCDHLKGRS NVLVFQQPGF NCSSIPHSSH SIINHHASIH 850
NEGDQPKTPE NIPSKEPKDG SPVQPSLLSL MKDRRLTLEQ VVAIEALTQL 900
SEAPSENSSP SKSEKDEESE QRTASLLNSC KAILYTVRKD LQDPNLQGEP 950
PKLNHCPSLE KQSSCNTVVF NGQTTTLSNS HINSATNQAS TKSHEYSKVT 1000
NSLSLFIPKS NSSKIDTNKS IAQGIITLDN CSNDLHQLPP RNNEVEYCNQ 1050
LLDSSKKLDS DDLSCQDATH TQIEEDVATQ LTQLASIIKI NYIKPEDKKV 1100
ESTPTSLVTC NVQQKYNQEK GTIQQKPPSS VHNNHGSSLT KQKNPTQKKT 1150
KSTPSRDRRK KKPTVVSYQE NDRQKWEKLS YMYGTICDIW IASKFQNFGQ 1200
FCPHDFPTVF GKISSSTKIW KPLAQTRSIM QPKTVFPPLT QIKLQRYPES 1250
AEEKVKVEPL DSLSLFHLKT ESNGKAFTDK AYNSQVQLTV NANQKAHPLT 1300
QPSSPPNQCA NVMAGDDQIR FQQVVKEQLM HQRLPTLPGI SHETPLPESA 1350
LTLRNVNVVC SGGITVVSTK SEEEVCSSSF GTSEFSTVDS AQKNFNDYAM 1400
NFFTNPTKNL VSITKDSELP TCSCLDRVIQ KDKGPYYTHL GAGPSVAAVR 1450
EIMENRYGQK GNAIRIEIVV YTGKEGKSSH GCPIAKWVLR RSSDEEKVLC 1500
LVRQRTGHHC PTAVMVVLIM VWDGIPLPMA DRLYTELTEN LKSYNGHPTD 1550
RRCTLNENRT CTCQGIDPET CGASFSFGCS WSMYFNGCKF GRSPSPRRFR 1600
IDPSSPLHEK NLEDNLQSLA TRLAPIYKQY APVAYQNQVE YENVARECRL 1650
GSKEGRPFSG VTACLDFCAH PHRDIHNMNN GSTVVCTLTR EDNRSLGVIP 1700
QDEQLHVLPL YKLSDTDEFG SKEGMEAKIK SGAIEVLAPR RKKRTCFTQP 1750
VPRSGKKRAA MMTEVLAHKI RAVEKKPIPR IKRKNNSTTT NNSKPSSLPT 1800
LGSNTETVQP EVKSETEPHF ILKSSDNTKT YSLMPSAPHP VKEASPGFSW 1850
SPKTASATPA PLKNDATASC GFSERSSTPH CTMPSGRLSG ANAAAADGPG 1900
ISQLGEVAPL PTLSAPVMEP LINSEPSTGV TEPLTPHQPN HQPSFLTSPQ 1950
DLASSPMEED EQHSEADEPP SDEPLSDDPL SPAEEKLPHI DEYWSDSEHI 2000
FLDANIGGVA IAPAHGSVLI ECARRELHAT TPVEHPNRNH PTRLSLVFYQ 2050
HKNLNKPQHG FELNKIKFEA KEAKNKKMKA SEQKDQAANE GPEQSSEVNE 2100
LNQIPSHKAL TLTHDNVVTV SPYALTHVAG PYNHWV 2136
Length:2,136
Mass (Da):235,309
Last modified:October 3, 2006 - v2
Checksum:i66E24EF0594A964C
GO

Sequence cautioni

The sequence CAD28467.3 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621D → G.
Corresponds to variant rs10823229 [ dbSNP | Ensembl ].
VAR_027734
Natural varianti193 – 1931S → T.
Corresponds to variant rs12773594 [ dbSNP | Ensembl ].
VAR_027735
Natural varianti256 – 2561A → V.
Corresponds to variant rs12221107 [ dbSNP | Ensembl ].
VAR_027736
Natural varianti1018 – 10181N → S.
Corresponds to variant rs16925541 [ dbSNP | Ensembl ].
VAR_027737
Natural varianti1123 – 11231I → M.1 Publication
Corresponds to variant rs3998860 [ dbSNP | Ensembl ].
VAR_027738

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2001 – 20011F → L in CAD28467. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF430147 mRNA. Translation: AAM88301.1.
AL513534, AL713888 Genomic DNA. Translation: CAH70220.1.
AL713888, AL513534 Genomic DNA. Translation: CAI15118.1.
AB051463 mRNA. Translation: BAB21767.1.
AL713658 mRNA. Translation: CAD28467.3. Sequence problems.
BC053905 mRNA. Translation: AAH53905.1.
CCDSiCCDS7281.1.
RefSeqiNP_085128.2. NM_030625.2.
UniGeneiHs.567594.
Hs.708977.

Genome annotation databases

EnsembliENST00000373644; ENSP00000362748; ENSG00000138336.
GeneIDi80312.
KEGGihsa:80312.
UCSCiuc001jok.4. human.

Polymorphism databases

DMDMi115502139.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF430147 mRNA. Translation: AAM88301.1 .
AL513534 , AL713888 Genomic DNA. Translation: CAH70220.1 .
AL713888 , AL513534 Genomic DNA. Translation: CAI15118.1 .
AB051463 mRNA. Translation: BAB21767.1 .
AL713658 mRNA. Translation: CAD28467.3 . Sequence problems.
BC053905 mRNA. Translation: AAH53905.1 .
CCDSi CCDS7281.1.
RefSeqi NP_085128.2. NM_030625.2.
UniGenei Hs.567594.
Hs.708977.

3D structure databases

ProteinModelPortali Q8NFU7.
SMRi Q8NFU7. Positions 586-637, 1421-2071.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123225. 1 interaction.
IntActi Q8NFU7. 2 interactions.
STRINGi 9606.ENSP00000362748.

PTM databases

PhosphoSitei Q8NFU7.

Polymorphism databases

DMDMi 115502139.

Proteomic databases

PaxDbi Q8NFU7.
PRIDEi Q8NFU7.

Protocols and materials databases

DNASUi 80312.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373644 ; ENSP00000362748 ; ENSG00000138336 .
GeneIDi 80312.
KEGGi hsa:80312.
UCSCi uc001jok.4. human.

Organism-specific databases

CTDi 80312.
GeneCardsi GC10P070320.
HGNCi HGNC:29484. TET1.
HPAi CAB014886.
HPA019032.
MIMi 607790. gene.
neXtProti NX_Q8NFU7.
PharmGKBi PA162405605.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG76473.
HOGENOMi HOG000154549.
InParanoidi Q8NFU7.
KOi K13097.
OMAi PHCTMPS.
OrthoDBi EOG7DVD94.
PhylomeDBi Q8NFU7.
TreeFami TF324004.

Enzyme and pathway databases

Reactomei REACT_200682. TET1,2,3 and TDG demethylate DNA.

Miscellaneous databases

ChiTaRSi TET1. human.
GeneWikii Tet_methylcytosine_dioxygenase_1.
GenomeRNAii 80312.
NextBioi 70802.
PROi Q8NFU7.
SOURCEi Search...

Gene expression databases

Bgeei Q8NFU7.
CleanExi HS_TET1.
Genevestigatori Q8NFU7.

Family and domain databases

InterProi IPR024779. 2OGFeDO_nucleic_acid_mod.
IPR002857. Znf_CXXC.
[Graphical view ]
Pfami PF12851. Tet_JBP. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view ]
PROSITEi PS51058. ZF_CXXC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23)."
    Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y.
    Cancer Res. 62:4075-4080(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-1123, FUNCTION, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
    Tissue: Leukemia.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1402-2136.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1665-2074.
    Tissue: Brain.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1809-2136.
    Tissue: Uterus.
  6. "TET1, a member of a novel protein family, is fused to MLL in acute myeloid leukemia containing the t(10;11)(q22;q23)."
    Lorsbach R.B., Moore J., Mathew S., Raimondi S.C., Mukatira S.T., Downing J.R.
    Leukemia 17:637-641(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, TISSUE SPECIFICITY.
  7. "The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain."
    Kriaucionis S., Heintz N.
    Science 324:929-930(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by the MLL fusion partner TET1."
    Tahiliani M., Koh K.P., Shen Y., Pastor W.A., Bandukwala H., Brudno Y., Agarwal S., Iyer L.M., Liu D.R., Aravind L., Rao A.
    Science 324:930-935(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, COFACTOR, MUTAGENESIS OF HIS-1672 AND ASP-1674.
  9. "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain."
    Guo J.U., Su Y., Zhong C., Ming G.L., Song H.
    Cell 145:423-434(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA DEMETHYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-1672 AND ASP-1674.
  10. "TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity."
    Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A., Rappsilber J., Helin K.
    Nature 473:343-348(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIN3A.
  11. "Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine."
    Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C., Zhang Y.
    Science 333:1300-1303(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTET1_HUMAN
AccessioniPrimary (citable) accession number: Q8NFU7
Secondary accession number(s): Q5VUP7
, Q7Z6B6, Q8TCR1, Q9C0I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Subsequent steps in cytosine demethylation are subject to discussion. According to a first model cytosine demethylation occurs through deamination of 5hmC into 5-hydroxymethyluracil (5hmU) and subsequent replacement by unmethylated cytosine by the base excision repair system (1 Publication). According to another model, cytosine demethylation is rather mediated via conversion of 5hmC into 5fC and 5caC, followed by excision by TDG and replacement by unmethylated cytosine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi