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Q8NFU7

- TET1_HUMAN

UniProt

Q8NFU7 - TET1_HUMAN

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Protein

Methylcytosine dioxygenase TET1

Gene

TET1

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.
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
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 Curated

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 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, 1433-1751, 1991-2071.
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.
GeneTreeiENSGT00510000046514.
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

        10         20         30         40         50
MSRSRHARPS RLVRKEDVNK KKKNSQLRKT TKGANKNVAS VKTLSPGKLK
60 70 80 90 100
QLIQERDVKK KTEPKPPVPV RSLLTRAGAA RMNLDRTEVL FQNPESLTCN
110 120 130 140 150
GFTMALRSTS LSRRLSQPPL VVAKSKKVPL SKGLEKQHDC DYKILPALGV
160 170 180 190 200
KHSENDSVPM QDTQVLPDIE TLIGVQNPSL LKGKSQETTQ FWSQRVEDSK
210 220 230 240 250
INIPTHSGPA AEILPGPLEG TRCGEGLFSE ETLNDTSGSP KMFAQDTVCA
260 270 280 290 300
PFPQRATPKV TSQGNPSIQL EELGSRVESL KLSDSYLDPI KSEHDCYPTS
310 320 330 340 350
SLNKVIPDLN LRNCLALGGS TSPTSVIKFL LAGSKQATLG AKPDHQEAFE
360 370 380 390 400
ATANQQEVSD TTSFLGQAFG AIPHQWELPG ADPVHGEALG ETPDLPEIPG
410 420 430 440 450
AIPVQGEVFG TILDQQETLG MSGSVVPDLP VFLPVPPNPI ATFNAPSKWP
460 470 480 490 500
EPQSTVSYGL AVQGAIQILP LGSGHTPQSS SNSEKNSLPP VMAISNVENE
510 520 530 540 550
KQVHISFLPA NTQGFPLAPE RGLFHASLGI AQLSQAGPSK SDRGSSQVSV
560 570 580 590 600
TSTVHVVNTT VVTMPVPMVS TSSSSYTTLL PTLEKKKRKR CGVCEPCQQK
610 620 630 640 650
TNCGECTYCK NRKNSHQICK KRKCEELKKK PSVVVPLEVI KENKRPQREK
660 670 680 690 700
KPKVLKADFD NKPVNGPKSE SMDYSRCGHG EEQKLELNPH TVENVTKNED
710 720 730 740 750
SMTGIEVEKW TQNKKSQLTD HVKGDFSANV PEAEKSKNSE VDKKRTKSPK
760 770 780 790 800
LFVQTVRNGI KHVHCLPAET NVSFKKFNIE EFGKTLENNS YKFLKDTANH
810 820 830 840 850
KNAMSSVATD MSCDHLKGRS NVLVFQQPGF NCSSIPHSSH SIINHHASIH
860 870 880 890 900
NEGDQPKTPE NIPSKEPKDG SPVQPSLLSL MKDRRLTLEQ VVAIEALTQL
910 920 930 940 950
SEAPSENSSP SKSEKDEESE QRTASLLNSC KAILYTVRKD LQDPNLQGEP
960 970 980 990 1000
PKLNHCPSLE KQSSCNTVVF NGQTTTLSNS HINSATNQAS TKSHEYSKVT
1010 1020 1030 1040 1050
NSLSLFIPKS NSSKIDTNKS IAQGIITLDN CSNDLHQLPP RNNEVEYCNQ
1060 1070 1080 1090 1100
LLDSSKKLDS DDLSCQDATH TQIEEDVATQ LTQLASIIKI NYIKPEDKKV
1110 1120 1130 1140 1150
ESTPTSLVTC NVQQKYNQEK GTIQQKPPSS VHNNHGSSLT KQKNPTQKKT
1160 1170 1180 1190 1200
KSTPSRDRRK KKPTVVSYQE NDRQKWEKLS YMYGTICDIW IASKFQNFGQ
1210 1220 1230 1240 1250
FCPHDFPTVF GKISSSTKIW KPLAQTRSIM QPKTVFPPLT QIKLQRYPES
1260 1270 1280 1290 1300
AEEKVKVEPL DSLSLFHLKT ESNGKAFTDK AYNSQVQLTV NANQKAHPLT
1310 1320 1330 1340 1350
QPSSPPNQCA NVMAGDDQIR FQQVVKEQLM HQRLPTLPGI SHETPLPESA
1360 1370 1380 1390 1400
LTLRNVNVVC SGGITVVSTK SEEEVCSSSF GTSEFSTVDS AQKNFNDYAM
1410 1420 1430 1440 1450
NFFTNPTKNL VSITKDSELP TCSCLDRVIQ KDKGPYYTHL GAGPSVAAVR
1460 1470 1480 1490 1500
EIMENRYGQK GNAIRIEIVV YTGKEGKSSH GCPIAKWVLR RSSDEEKVLC
1510 1520 1530 1540 1550
LVRQRTGHHC PTAVMVVLIM VWDGIPLPMA DRLYTELTEN LKSYNGHPTD
1560 1570 1580 1590 1600
RRCTLNENRT CTCQGIDPET CGASFSFGCS WSMYFNGCKF GRSPSPRRFR
1610 1620 1630 1640 1650
IDPSSPLHEK NLEDNLQSLA TRLAPIYKQY APVAYQNQVE YENVARECRL
1660 1670 1680 1690 1700
GSKEGRPFSG VTACLDFCAH PHRDIHNMNN GSTVVCTLTR EDNRSLGVIP
1710 1720 1730 1740 1750
QDEQLHVLPL YKLSDTDEFG SKEGMEAKIK SGAIEVLAPR RKKRTCFTQP
1760 1770 1780 1790 1800
VPRSGKKRAA MMTEVLAHKI RAVEKKPIPR IKRKNNSTTT NNSKPSSLPT
1810 1820 1830 1840 1850
LGSNTETVQP EVKSETEPHF ILKSSDNTKT YSLMPSAPHP VKEASPGFSW
1860 1870 1880 1890 1900
SPKTASATPA PLKNDATASC GFSERSSTPH CTMPSGRLSG ANAAAADGPG
1910 1920 1930 1940 1950
ISQLGEVAPL PTLSAPVMEP LINSEPSTGV TEPLTPHQPN HQPSFLTSPQ
1960 1970 1980 1990 2000
DLASSPMEED EQHSEADEPP SDEPLSDDPL SPAEEKLPHI DEYWSDSEHI
2010 2020 2030 2040 2050
FLDANIGGVA IAPAHGSVLI ECARRELHAT TPVEHPNRNH PTRLSLVFYQ
2060 2070 2080 2090 2100
HKNLNKPQHG FELNKIKFEA KEAKNKKMKA SEQKDQAANE GPEQSSEVNE
2110 2120 2130
LNQIPSHKAL TLTHDNVVTV SPYALTHVAG PYNHWV
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, 1433-1751, 1991-2071.
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.
GeneTreei ENSGT00510000046514.
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: October 29, 2014
This is version 92 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