Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8NFU7 (TET1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TET1
Synonyms:CXXC6, KIAA1676, LCX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11

Catalytic activity

DNA 5-methylcytosine + 2-oxoglutarate + O2 = DNA 5-hydroxymethylcytosine + succinate + CO2. Ref.8 Ref.9

DNA 5-hydroxymethylcytosine + 2-oxoglutarate + O2 = DNA 5-formylcytosine + succinate + CO2. Ref.8 Ref.9

DNA 5-formylcytosine + 2-oxoglutarate + O2 = DNA 5-carboxylcytosine + succinate + CO2. Ref.8 Ref.9

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.8

Binds 3 zinc ions per subunit. The zinc ions have a structural role By similarity. Ref.8

Subunit structure

Interacts with HCFC1 and OGT By similarity. Interacts with SIN3A; recruits the transcriptional corepressor SIN3A to gene promoters. Ref.10

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in fetal heart, lung and brain, and in adult skeletal muscle, thymus and ovary. Not detected in adult heart, lung or brain. Ref.1 Ref.6

Post-translational modification

Glycosylated. Interaction with OGT leads to GlcNAcylation By similarity.

Involvement in disease

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'.

Sequence similarities

Belongs to the TET family.

Contains 1 CXXC-type zinc finger.

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 (Ref.9). 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.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Iron
Metal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Dioxygenase
Oxidoreductase
Repressor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA demethylation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

inner cell mass cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of methylation-dependent chromatin silencing

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

protein O-linked glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA methylation

Inferred from electronic annotation. Source: Ensembl

stem cell maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred by curator Ref.8. Source: UniProtKB

   Molecular_functioniron ion binding

Inferred from direct assay Ref.8. Source: UniProtKB

methylcytosine dioxygenase activity

Inferred from direct assay Ref.8. Source: UniProtKB

structure-specific DNA binding

Inferred from direct assay Ref.8. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21362136Methylcytosine dioxygenase TET1
PRO_0000251949

Regions

Zinc finger584 – 62542CXXC-type
Region528 – 674147Sufficient for binding to genomic CpG islands
Region1580 – 159314Interaction with DNA By similarity
Region2043 – 204532-oxoglutarate binding By similarity
Region2049 – 20513Substrate binding By similarity

Sites

Metal binding14221Zinc 1 By similarity
Metal binding14241Zinc 1 By similarity
Metal binding14821Zinc 2 By similarity
Metal binding15081Zinc 1; via pros nitrogen By similarity
Metal binding15101Zinc 1 By similarity
Metal binding15611Zinc 2 By similarity
Metal binding15631Zinc 2 By similarity
Metal binding15791Zinc 3 By similarity
Metal binding15881Zinc 3 By similarity
Metal binding16481Zinc 3 By similarity
Metal binding16701Zinc 2; via tele nitrogen By similarity
Metal binding16721Iron; catalytic
Metal binding16741Iron; catalytic
Metal binding20281Iron; catalytic By similarity
Metal binding20591Zinc 3; via pros nitrogen By similarity
Binding site155112-oxoglutarate By similarity
Binding site166412-oxoglutarate By similarity
Binding site16771Substrate By similarity
Binding site170612-oxoglutarate By similarity
Site1608 – 16092Breakpoint for translocation to form KMT2A/MLL1-TET1 oncogene

Natural variations

Natural variant1621D → G.
Corresponds to variant rs10823229 [ dbSNP | Ensembl ].
VAR_027734
Natural variant1931S → T.
Corresponds to variant rs12773594 [ dbSNP | Ensembl ].
VAR_027735
Natural variant2561A → V.
Corresponds to variant rs12221107 [ dbSNP | Ensembl ].
VAR_027736
Natural variant10181N → S.
Corresponds to variant rs16925541 [ dbSNP | Ensembl ].
VAR_027737
Natural variant11231I → M. Ref.1
Corresponds to variant rs3998860 [ dbSNP | Ensembl ].
VAR_027738

Experimental info

Mutagenesis16721H → Y: Loss of catalytic activity and loss of the ability to induce DNA demethylation. Ref.8 Ref.9
Mutagenesis16741D → A: Loss of catalytic activity and loss of the ability to induce DNA demethylation. Ref.8 Ref.9
Sequence conflict20011F → L in CAD28467. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8NFU7 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 66E24EF0594A964C

FASTA2,136235,309
        10         20         30         40         50         60 
MSRSRHARPS RLVRKEDVNK KKKNSQLRKT TKGANKNVAS VKTLSPGKLK QLIQERDVKK 

        70         80         90        100        110        120 
KTEPKPPVPV RSLLTRAGAA RMNLDRTEVL FQNPESLTCN GFTMALRSTS LSRRLSQPPL 

       130        140        150        160        170        180 
VVAKSKKVPL SKGLEKQHDC DYKILPALGV KHSENDSVPM QDTQVLPDIE TLIGVQNPSL 

       190        200        210        220        230        240 
LKGKSQETTQ FWSQRVEDSK INIPTHSGPA AEILPGPLEG TRCGEGLFSE ETLNDTSGSP 

       250        260        270        280        290        300 
KMFAQDTVCA PFPQRATPKV TSQGNPSIQL EELGSRVESL KLSDSYLDPI KSEHDCYPTS 

       310        320        330        340        350        360 
SLNKVIPDLN LRNCLALGGS TSPTSVIKFL LAGSKQATLG AKPDHQEAFE ATANQQEVSD 

       370        380        390        400        410        420 
TTSFLGQAFG AIPHQWELPG ADPVHGEALG ETPDLPEIPG AIPVQGEVFG TILDQQETLG 

       430        440        450        460        470        480 
MSGSVVPDLP VFLPVPPNPI ATFNAPSKWP EPQSTVSYGL AVQGAIQILP LGSGHTPQSS 

       490        500        510        520        530        540 
SNSEKNSLPP VMAISNVENE KQVHISFLPA NTQGFPLAPE RGLFHASLGI AQLSQAGPSK 

       550        560        570        580        590        600 
SDRGSSQVSV TSTVHVVNTT VVTMPVPMVS TSSSSYTTLL PTLEKKKRKR CGVCEPCQQK 

       610        620        630        640        650        660 
TNCGECTYCK NRKNSHQICK KRKCEELKKK PSVVVPLEVI KENKRPQREK KPKVLKADFD 

       670        680        690        700        710        720 
NKPVNGPKSE SMDYSRCGHG EEQKLELNPH TVENVTKNED SMTGIEVEKW TQNKKSQLTD 

       730        740        750        760        770        780 
HVKGDFSANV PEAEKSKNSE VDKKRTKSPK LFVQTVRNGI KHVHCLPAET NVSFKKFNIE 

       790        800        810        820        830        840 
EFGKTLENNS YKFLKDTANH KNAMSSVATD MSCDHLKGRS NVLVFQQPGF NCSSIPHSSH 

       850        860        870        880        890        900 
SIINHHASIH NEGDQPKTPE NIPSKEPKDG SPVQPSLLSL MKDRRLTLEQ VVAIEALTQL 

       910        920        930        940        950        960 
SEAPSENSSP SKSEKDEESE QRTASLLNSC KAILYTVRKD LQDPNLQGEP PKLNHCPSLE 

       970        980        990       1000       1010       1020 
KQSSCNTVVF NGQTTTLSNS HINSATNQAS TKSHEYSKVT NSLSLFIPKS NSSKIDTNKS 

      1030       1040       1050       1060       1070       1080 
IAQGIITLDN CSNDLHQLPP RNNEVEYCNQ LLDSSKKLDS DDLSCQDATH TQIEEDVATQ 

      1090       1100       1110       1120       1130       1140 
LTQLASIIKI NYIKPEDKKV ESTPTSLVTC NVQQKYNQEK GTIQQKPPSS VHNNHGSSLT 

      1150       1160       1170       1180       1190       1200 
KQKNPTQKKT KSTPSRDRRK KKPTVVSYQE NDRQKWEKLS YMYGTICDIW IASKFQNFGQ 

      1210       1220       1230       1240       1250       1260 
FCPHDFPTVF GKISSSTKIW KPLAQTRSIM QPKTVFPPLT QIKLQRYPES AEEKVKVEPL 

      1270       1280       1290       1300       1310       1320 
DSLSLFHLKT ESNGKAFTDK AYNSQVQLTV NANQKAHPLT QPSSPPNQCA NVMAGDDQIR 

      1330       1340       1350       1360       1370       1380 
FQQVVKEQLM HQRLPTLPGI SHETPLPESA LTLRNVNVVC SGGITVVSTK SEEEVCSSSF 

      1390       1400       1410       1420       1430       1440 
GTSEFSTVDS AQKNFNDYAM NFFTNPTKNL VSITKDSELP TCSCLDRVIQ KDKGPYYTHL 

      1450       1460       1470       1480       1490       1500 
GAGPSVAAVR EIMENRYGQK GNAIRIEIVV YTGKEGKSSH GCPIAKWVLR RSSDEEKVLC 

      1510       1520       1530       1540       1550       1560 
LVRQRTGHHC PTAVMVVLIM VWDGIPLPMA DRLYTELTEN LKSYNGHPTD RRCTLNENRT 

      1570       1580       1590       1600       1610       1620 
CTCQGIDPET CGASFSFGCS WSMYFNGCKF GRSPSPRRFR IDPSSPLHEK NLEDNLQSLA 

      1630       1640       1650       1660       1670       1680 
TRLAPIYKQY APVAYQNQVE YENVARECRL GSKEGRPFSG VTACLDFCAH PHRDIHNMNN 

      1690       1700       1710       1720       1730       1740 
GSTVVCTLTR EDNRSLGVIP QDEQLHVLPL YKLSDTDEFG SKEGMEAKIK SGAIEVLAPR 

      1750       1760       1770       1780       1790       1800 
RKKRTCFTQP VPRSGKKRAA MMTEVLAHKI RAVEKKPIPR IKRKNNSTTT NNSKPSSLPT 

      1810       1820       1830       1840       1850       1860 
LGSNTETVQP EVKSETEPHF ILKSSDNTKT YSLMPSAPHP VKEASPGFSW SPKTASATPA 

      1870       1880       1890       1900       1910       1920 
PLKNDATASC GFSERSSTPH CTMPSGRLSG ANAAAADGPG ISQLGEVAPL PTLSAPVMEP 

      1930       1940       1950       1960       1970       1980 
LINSEPSTGV TEPLTPHQPN HQPSFLTSPQ DLASSPMEED EQHSEADEPP SDEPLSDDPL 

      1990       2000       2010       2020       2030       2040 
SPAEEKLPHI DEYWSDSEHI FLDANIGGVA IAPAHGSVLI ECARRELHAT TPVEHPNRNH 

      2050       2060       2070       2080       2090       2100 
PTRLSLVFYQ HKNLNKPQHG FELNKIKFEA KEAKNKKMKA SEQKDQAANE GPEQSSEVNE 

      2110       2120       2130 
LNQIPSHKAL TLTHDNVVTV SPYALTHVAG PYNHWV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_085128.2. NM_030625.2.
UniGeneHs.567594.
Hs.708977.

3D structure databases

ProteinModelPortalQ8NFU7.
SMRQ8NFU7. Positions 586-679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123225. 1 interaction.
STRING9606.ENSP00000362748.

PTM databases

PhosphoSiteQ8NFU7.

Polymorphism databases

DMDM115502139.

Proteomic databases

PaxDbQ8NFU7.
PRIDEQ8NFU7.

Protocols and materials databases

DNASU80312.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373644; ENSP00000362748; ENSG00000138336.
GeneID80312.
KEGGhsa:80312.
UCSCuc001jok.4. human.

Organism-specific databases

CTD80312.
GeneCardsGC10P070320.
HGNCHGNC:29484. TET1.
HPACAB014886.
HPA019032.
MIM607790. gene.
neXtProtNX_Q8NFU7.
PharmGKBPA162405605.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76473.
HOGENOMHOG000154549.
InParanoidQ8NFU7.
KOK13097.
OMAPHCTMPS.
OrthoDBEOG7DVD94.
PhylomeDBQ8NFU7.
TreeFamTF324004.

Gene expression databases

BgeeQ8NFU7.
CleanExHS_TET1.
GenevestigatorQ8NFU7.

Family and domain databases

InterProIPR024779. 2OGFeDO_nucleic_acid_mod.
IPR002857. Znf_CXXC.
[Graphical view]
PfamPF12851. Tet_JBP. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PROSITEPS51058. ZF_CXXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTET1. human.
GeneWikiTet_methylcytosine_dioxygenase_1.
GenomeRNAi80312.
NextBio70802.
PROQ8NFU7.
SOURCESearch...

Entry information

Entry nameTET1_HUMAN
AccessionPrimary (citable) accession number: Q8NFU7
Secondary accession number(s): Q5VUP7 expand/collapse secondary AC list , Q7Z6B6, Q8TCR1, Q9C0I7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: March 19, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM