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Q8NFU7

- TET1_HUMAN

UniProt

Q8NFU7 - TET1_HUMAN

Protein

Methylcytosine dioxygenase TET1

Gene

TET1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (03 Oct 2006)
      Previous versions | rss
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    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.
    DNA 5-hydroxymethylcytosine + 2-oxoglutarate + O2 = DNA 5-formylcytosine + succinate + CO2.
    DNA 5-formylcytosine + 2-oxoglutarate + O2 = DNA 5-carboxylcytosine + succinate + CO2.

    Cofactori

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

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri584 – 62542CXXC-typePROSITE-ProRule annotationAdd
    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. chromatin modification Source: UniProtKB-KW
    2. DNA demethylation Source: UniProtKB
    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

    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 Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    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 TET1PRO_0000251949Add
    BLAST

    Post-translational modificationi

    Glycosylated. Interaction with OGT leads to GlcNAcylation By similarity.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.By similarity1 Publication

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni528 – 674147Sufficient for binding to genomic CpG islandsAdd
    BLAST
    Regioni1580 – 159314Interaction with DNABy similarityAdd
    BLAST
    Regioni2043 – 204532-oxoglutarate bindingBy similarity
    Regioni2049 – 20513Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the TET family.Curated
    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri584 – 62542CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    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

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    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2001 – 20011F → L in CAD28467. (PubMed:17974005)Curated

    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 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

    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: October 1, 2014
    This is version 91 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 (PubMed:21496894). 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.1 Publication

    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