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Entry version 129 (08 May 2019)
Sequence version 3 (16 Jun 2009)
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Protein

Methylcytosine dioxygenase TET2

Gene

TET2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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.6 Publications

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. According to another model, cytosine demethylation is rather mediated via conversion of 5hmC into 5fC and 5caC, followed by excision by TDG (PubMed:21817016).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1133Zinc 11 Publication1
Metal bindingi1135Zinc 11 Publication1
Metal bindingi1193Zinc 21 Publication1
Metal bindingi1219Zinc 1; via pros nitrogen1 Publication1
Metal bindingi1221Zinc 11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei12612-oxoglutarate1
Metal bindingi1271Zinc 21 Publication1
Metal bindingi1273Zinc 21 Publication1
Metal bindingi1289Zinc 31 Publication1
Metal bindingi1298Zinc 31 Publication1
Metal bindingi1358Zinc 31 Publication1
Binding sitei13742-oxoglutarate1
Metal bindingi1380Zinc 2; via tele nitrogen1 Publication1
Metal bindingi1382Iron; catalytic1 Publication1
Metal bindingi1384Iron; catalytic1 Publication1
Binding sitei1387Substrate1
Binding sitei14162-oxoglutarate1
Metal bindingi1881Iron; catalytic1 Publication1
Metal bindingi1912Zinc 3; via pros nitrogen1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • ferrous iron binding Source: UniProtKB
  • iron ion binding Source: GO_Central
  • methylcytosine dioxygenase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Dioxygenase, DNA-binding, Oxidoreductase
Biological processCell cycle
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5221030 TET1,2,3 and TDG demethylate DNA

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q6N021

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Methylcytosine dioxygenase TET2 (EC:1.14.11.n21 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TET2
Synonyms:KIAA1546
ORF Names:Nbla00191
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:25941 TET2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
612839 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q6N021

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

TET2 is frequently mutated in myeloproliferative disorders (MPD). These constitute a heterogeneous group of disorders, also known as myeloproliferative diseases or myeloproliferative neoplasms (MPN), characterized by cellular proliferation of one or more hematologic cell lines in the peripheral blood, distinct from acute leukemia. Included diseases are: essential thrombocythemia, polycythemia vera, primary myelofibrosis (chronic idiopathic myelofibrosis). Bone marrow samples from patients display uniformly low levels of hmC in genomic DNA compared to bone marrow samples from healthy controls as well as hypomethylation relative to controls at the majority of differentially methylated CpG sites.
Polycythemia vera (PV)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA myeloproliferative disorder characterized by abnormal proliferation of all hematopoietic bone marrow elements, erythroid hyperplasia, an absolute increase in total blood volume, but also by myeloid leukocytosis, thrombocytosis and splenomegaly.
Related information in OMIM
TET2 is frequently mutated in systemic mastocytosis; also known as systemic mast cell disease. A condition with features in common with myeloproliferative diseases. It is a clonal disorder of the mast cell and its precursor cells. The clinical symptoms and signs of systemic mastocytosis are due to accumulation of clonally derived mast cells in different tissues, including bone marrow, skin, the gastrointestinal tract, the liver, and the spleen.
Myelodysplastic syndrome (MDS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. Bone marrow samples from patients display uniformly low levels of hmC in genomic DNA compared to bone marrow samples from healthy controls as well as hypomethylation relative to controls at the majority of differentially methylated CpG sites.
Disease descriptionA heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML).
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1261R → G: Loss of enzyme activity. 1 Publication1
Mutagenesisi1262R → A: Slightly reduces enzyme activity. 1 Publication1
Mutagenesisi1290S → A: Reduces enzyme activity; when associated with A-1295. 1 Publication1
Mutagenesisi1291 – 1296WSMYYN → GGSGGS: Loss of enzyme activity. 1 Publication6
Mutagenesisi1293 – 1294MY → AA: Strongly reduced enzyme activity. Slightly decreased affinity for DNA. 1 Publication2
Mutagenesisi1295Y → A: Reduces enzyme activity; when associated with A-1290. 1 Publication1
Mutagenesisi1303S → N: Loss of enzyme activity; when associated with E-1299. 1 Publication1
Mutagenesisi1382H → Y: Loss of enzyme activity. Still able to enhance histone H2B GlcNAcylation by OGT; when associated with A-1384. Loss of enzyme activity; when associated with V-1384. 2 Publications1
Mutagenesisi1384D → A: Loss of enzyme activity. Still able to enhance histone H2B GlcNAcylation by OGT; when associated with Y-1382. 2 Publications1
Mutagenesisi1384D → V: Loss of enzyme activity; when associated with Y-1382. 2 Publications1
Mutagenesisi1387N → A: Near loss of enzyme activity. 1 Publication1
Mutagenesisi1902Y → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi1904H → R: Loss of enzyme activity. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
54790

MalaCards human disease database

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MalaCardsi
TET2
MIMi263300 phenotype
614286 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000168769

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
75564 Acquired idiopathic sideroblastic anemia
86845 Acute myeloid leukaemia with myelodysplasia-related features
3318 Essential thrombocythemia
729 Polycythemia vera
824 Primary myelofibrosis
98826 Refractory anemia
86839 Refractory anemia with excess blasts

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA162405634

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TET2

Domain mapping of disease mutations (DMDM)

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DMDMi
239938839

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003245881 – 2002Methylcytosine dioxygenase TET2Add BLAST2002

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei15PhosphoserineBy similarity1
Modified residuei75PhosphoserineCombined sources1
Modified residuei99PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1109PhosphoserineCombined sources1
Modified residuei1682Asymmetric dimethylarginineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

May be glycosylated. It is unclear whether interaction with OGT leads to GlcNAcylation. According to a report, it is not GlcNAcylated by OGT (PubMed:23353889). In contrast, another group reports GlcNAcylation by OGT in mouse ortholog.1 Publication

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q6N021

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q6N021

MaxQB - The MaxQuant DataBase

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MaxQBi
Q6N021

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q6N021

PeptideAtlas

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PeptideAtlasi
Q6N021

PRoteomics IDEntifications database

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PRIDEi
Q6N021

ProteomicsDB human proteome resource

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ProteomicsDBi
66598
66599 [Q6N021-2]
66600 [Q6N021-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6N021

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q6N021

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Broadly expressed. Highly expressed in hematopoietic cells; highest expression observed in granulocytes. Expression is reduced in granulocytes from peripheral blood of patients affected by myelodysplastic syndromes.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000168769 Expressed in 192 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q6N021 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q6N021 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA043135

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with HCFC1 and OGT.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
120151, 12 interactors

Protein interaction database and analysis system

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IntActi
Q6N021, 12 interactors

Molecular INTeraction database

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MINTi
Q6N021

STRING: functional protein association networks

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STRINGi
9606.ENSP00000442788

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12002
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q6N021

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1290 – 1303Interaction with DNAAdd BLAST14
Regioni1896 – 18982-oxoglutarate binding3
Regioni1902 – 1904Substrate binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi398 – 419Pro-richAdd BLAST22
Compositional biasi591 – 969Gln-richAdd BLAST379
Compositional biasi1523 – 1553Gln-richAdd BLAST31

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TET family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IE22 Eukaryota
ENOG410XPWW LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160003

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6N021

Database of Orthologous Groups

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OrthoDBi
704215at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q6N021

TreeFam database of animal gene trees

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TreeFami
TF337563

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024779 2OGFeDO_noxygenase_dom
IPR040175 TET1/2/3

The PANTHER Classification System

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PANTHERi
PTHR23358 PTHR23358, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12851 Tet_JBP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01333 Tet_JBP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q6N021-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEQDRTNHVE GNRLSPFLIP SPPICQTEPL ATKLQNGSPL PERAHPEVNG
60 70 80 90 100
DTKWHSFKSY YGIPCMKGSQ NSRVSPDFTQ ESRGYSKCLQ NGGIKRTVSE
110 120 130 140 150
PSLSGLLQIK KLKQDQKANG ERRNFGVSQE RNPGESSQPN VSDLSDKKES
160 170 180 190 200
VSSVAQENAV KDFTSFSTHN CSGPENPELQ ILNEQEGKSA NYHDKNIVLL
210 220 230 240 250
KNKAVLMPNG ATVSASSVEH THGELLEKTL SQYYPDCVSI AVQKTTSHIN
260 270 280 290 300
AINSQATNEL SCEITHPSHT SGQINSAQTS NSELPPKPAA VVSEACDADD
310 320 330 340 350
ADNASKLAAM LNTCSFQKPE QLQQQKSVFE ICPSPAENNI QGTTKLASGE
360 370 380 390 400
EFCSGSSSNL QAPGGSSERY LKQNEMNGAY FKQSSVFTKD SFSATTTPPP
410 420 430 440 450
PSQLLLSPPP PLPQVPQLPS EGKSTLNGGV LEEHHHYPNQ SNTTLLREVK
460 470 480 490 500
IEGKPEAPPS QSPNPSTHVC SPSPMLSERP QNNCVNRNDI QTAGTMTVPL
510 520 530 540 550
CSEKTRPMSE HLKHNPPIFG SSGELQDNCQ QLMRNKEQEI LKGRDKEQTR
560 570 580 590 600
DLVPPTQHYL KPGWIELKAP RFHQAESHLK RNEASLPSIL QYQPNLSNQM
610 620 630 640 650
TSKQYTGNSN MPGGLPRQAY TQKTTQLEHK SQMYQVEMNQ GQSQGTVDQH
660 670 680 690 700
LQFQKPSHQV HFSKTDHLPK AHVQSLCGTR FHFQQRADSQ TEKLMSPVLK
710 720 730 740 750
QHLNQQASET EPFSNSHLLQ HKPHKQAAQT QPSQSSHLPQ NQQQQQKLQI
760 770 780 790 800
KNKEEILQTF PHPQSNNDQQ REGSFFGQTK VEECFHGENQ YSKSSEFETH
810 820 830 840 850
NVQMGLEEVQ NINRRNSPYS QTMKSSACKI QVSCSNNTHL VSENKEQTTH
860 870 880 890 900
PELFAGNKTQ NLHHMQYFPN NVIPKQDLLH RCFQEQEQKS QQASVLQGYK
910 920 930 940 950
NRNQDMSGQQ AAQLAQQRYL IHNHANVFPV PDQGGSHTQT PPQKDTQKHA
960 970 980 990 1000
ALRWHLLQKQ EQQQTQQPQT ESCHSQMHRP IKVEPGCKPH ACMHTAPPEN
1010 1020 1030 1040 1050
KTWKKVTKQE NPPASCDNVQ QKSIIETMEQ HLKQFHAKSL FDHKALTLKS
1060 1070 1080 1090 1100
QKQVKVEMSG PVTVLTRQTT AAELDSHTPA LEQQTTSSEK TPTKRTAASV
1110 1120 1130 1140 1150
LNNFIESPSK LLDTPIKNLL DTPVKTQYDF PSCRCVEQII EKDEGPFYTH
1160 1170 1180 1190 1200
LGAGPNVAAI REIMEERFGQ KGKAIRIERV IYTGKEGKSS QGCPIAKWVV
1210 1220 1230 1240 1250
RRSSSEEKLL CLVRERAGHT CEAAVIVILI LVWEGIPLSL ADKLYSELTE
1260 1270 1280 1290 1300
TLRKYGTLTN RRCALNEERT CACQGLDPET CGASFSFGCS WSMYYNGCKF
1310 1320 1330 1340 1350
ARSKIPRKFK LLGDDPKEEE KLESHLQNLS TLMAPTYKKL APDAYNNQIE
1360 1370 1380 1390 1400
YEHRAPECRL GLKEGRPFSG VTACLDFCAH AHRDLHNMQN GSTLVCTLTR
1410 1420 1430 1440 1450
EDNREFGGKP EDEQLHVLPL YKVSDVDEFG SVEAQEEKKR SGAIQVLSSF
1460 1470 1480 1490 1500
RRKVRMLAEP VKTCRQRKLE AKKAAAEKLS SLENSSNKNE KEKSAPSRTK
1510 1520 1530 1540 1550
QTENASQAKQ LAELLRLSGP VMQQSQQPQP LQKQPPQPQQ QQRPQQQQPH
1560 1570 1580 1590 1600
HPQTESVNSY SASGSTNPYM RRPNPVSPYP NSSHTSDIYG STSPMNFYST
1610 1620 1630 1640 1650
SSQAAGSYLN SSNPMNPYPG LLNQNTQYPS YQCNGNLSVD NCSPYLGSYS
1660 1670 1680 1690 1700
PQSQPMDLYR YPSQDPLSKL SLPPIHTLYQ PRFGNSQSFT SKYLGYGNQN
1710 1720 1730 1740 1750
MQGDGFSSCT IRPNVHHVGK LPPYPTHEMD GHFMGATSRL PPNLSNPNMD
1760 1770 1780 1790 1800
YKNGEHHSPS HIIHNYSAAP GMFNSSLHAL HLQNKENDML SHTANGLSKM
1810 1820 1830 1840 1850
LPALNHDRTA CVQGGLHKLS DANGQEKQPL ALVQGVASGA EDNDEVWSDS
1860 1870 1880 1890 1900
EQSFLDPDIG GVAVAPTHGS ILIECAKREL HATTPLKNPN RNHPTRISLV
1910 1920 1930 1940 1950
FYQHKSMNEP KHGLALWEAK MAEKAREKEE ECEKYGPDYV PQKSHGKKVK
1960 1970 1980 1990 2000
REPAEPHETS EPTYLRFIKS LAERTMSVTT DSTVTTSPYA FTRVTGPYNR

YI
Length:2,002
Mass (Da):223,811
Last modified:June 16, 2009 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6D740305EE2A8D46
GO
Isoform 2 (identifier: Q6N021-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1137-1165: EQIIEKDEGPFYTHLGAGPNVAAIREIME → GKCQKCTETHGVYPELANLSSDMGFSFFF
     1166-2002: Missing.

Show »
Length:1,165
Mass (Da):130,254
Checksum:i95546FBB1F6FE0FD
GO
Isoform 3 (identifier: Q6N021-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1137-1194: EQIIEKDEGP...KEGKSSQGCP → GLDRRVKLLG...SELATPVRLQ
     1195-2002: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:1,194
Mass (Da):133,481
Checksum:iFDA110D6E8FB7790
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EQS8E7EQS8_HUMAN
Methylcytosine dioxygenase TET2
TET2
2,023Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EPB1E7EPB1_HUMAN
Methylcytosine dioxygenase TET2
TET2
1,167Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RE87D6RE87_HUMAN
Methylcytosine dioxygenase TET2
TET2
110Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA90898 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA90898 differs from that shown. Reason: Frameshift at position 323.Curated
The sequence BAA90898 differs from that shown. Reason: Erroneous termination at position 325. Translated as Gln.Curated
The sequence BAB55391 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti599Q → R in BAA90898 (PubMed:14702039).Curated1
Sequence conflicti702H → Q in CAE45851 (PubMed:17974005).Curated1
Sequence conflicti878L → S in BAE45750 (PubMed:12880961).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03984129P → R1 PublicationCorresponds to variant dbSNP:rs12498609EnsemblClinVar.1
Natural variantiVAR_05817134L → F2 PublicationsCorresponds to variant dbSNP:rs111948941EnsemblClinVar.1
Natural variantiVAR_058130123R → H1 PublicationCorresponds to variant dbSNP:rs773565437Ensembl.1
Natural variantiVAR_058172145S → N in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs114619974EnsemblClinVar.1
Natural variantiVAR_058173174P → H1 PublicationCorresponds to variant dbSNP:rs146031219EnsemblClinVar.1
Natural variantiVAR_039842218V → M2 PublicationsCorresponds to variant dbSNP:rs6843141EnsemblClinVar.1
Natural variantiVAR_058131308A → T in chronic myelomonocytic leukemia and acute myeloid leukemia samples. 1 PublicationCorresponds to variant dbSNP:rs569067880Ensembl.1
Natural variantiVAR_058174312N → S in an acute myeloid leukemia sample; somatic mutation. 1 Publication1
Natural variantiVAR_058132355G → D1 PublicationCorresponds to variant dbSNP:rs61744960EnsemblClinVar.1
Natural variantiVAR_039843363P → L1 PublicationCorresponds to variant dbSNP:rs17253672EnsemblClinVar.1
Natural variantiVAR_058133399P → L in myelodysplastic/myeloproliferative disorders; a patient positive for mutation F-617 in JAK2. 1 Publication1
Natural variantiVAR_058134429G → R1 PublicationCorresponds to variant dbSNP:rs201642693EnsemblClinVar.1
Natural variantiVAR_058175460S → F in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs376570662EnsemblClinVar.1
Natural variantiVAR_058176666D → G in a chronic myelomonocytic leukemia sample; somatic mutation. 1 Publication1
Natural variantiVAR_058135817S → T in myelodysplastic/myeloproliferative disorders. 1 PublicationCorresponds to variant dbSNP:rs753786455Ensembl.1
Natural variantiVAR_058177867Y → H3 PublicationsCorresponds to variant dbSNP:rs144386291EnsemblClinVar.1
Natural variantiVAR_039844912A → G. Corresponds to variant dbSNP:rs4145756Ensembl.1
Natural variantiVAR_058136924H → R1 PublicationCorresponds to variant dbSNP:rs34485921EnsemblClinVar.1
Natural variantiVAR_058178941P → S in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs532738858Ensembl.1
Natural variantiVAR_058137949H → R1 PublicationCorresponds to variant dbSNP:rs778464072Ensembl.1
Natural variantiVAR_0581791073E → V1 Publication1
Natural variantiVAR_0581801084Q → P3 PublicationsCorresponds to variant dbSNP:rs75056899EnsemblClinVar.1
Natural variantiVAR_0581811135C → Y in a myeloproliferative disorder; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs769422572Ensembl.1
Natural variantiVAR_0581381167R → T in a myelodysplatic/myeloproliferative disorder and a chronic myelomonocytic leukemia sample. 1 Publication1
Natural variantiVAR_0581391175I → V in a refractory anemia with ringed sideroblasts sample. 1 Publication1
Natural variantiVAR_0581821204S → C in a myeloproliferative disorder; somatic mutation. 1 Publication1
Natural variantiVAR_0581831214R → W in a myelodysplastic syndrome; somatic mutation in a chronic myelomonocytic leukemia sample. 2 PublicationsCorresponds to variant dbSNP:rs761811530Ensembl.1
Natural variantiVAR_0581401237 – 1239Missing in a polycythemia vera sample; somatic mutation. 1 Publication3
Natural variantiVAR_0581981242D → R Requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_0581841242D → V in myeloproliferative disorders. 1 Publication1
Natural variantiVAR_0581851245Y → S in a myeloproliferative disorder; somatic mutation. 1 Publication1
Natural variantiVAR_0581861261R → C in a myeloproliferative disorder; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs898441677Ensembl.1
Natural variantiVAR_0581871261R → H in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs771761785Ensembl.1
Natural variantiVAR_0581411261R → L in a myelodysplastic syndrome. 1 Publication1
Natural variantiVAR_0581421285Missing in a myelodysplastic syndrome; somatic mutation. 1 Publication1
Natural variantiVAR_0581431287F → L in myelodysplastic/myeloproliferative disorders. 1 Publication1
Natural variantiVAR_0581441291W → R in a myelodysplastic syndrome; somatic mutation; abolishes enzyme activity. 2 Publications1
Natural variantiVAR_0581451299K → E in a refractory anemia sample. 2 Publications1
Natural variantiVAR_0581461299K → N in chronic myelomonocytic leukemia samples. 1 Publication1
Natural variantiVAR_0581471302R → G in primary myelofibrosis and chronic myelomonocytic leukemia samples. 2 Publications1
Natural variantiVAR_0581481318E → G in chronic myelomonocytic leukemia samples. 1 Publication1
Natural variantiVAR_0581491367P → S in a chronic myelomonocytic leukemia sample. 1
Natural variantiVAR_0581501396C → W in a myelodysplastic syndrome. 1 Publication1
Natural variantiVAR_0581511398L → R in a myelodysplastic syndrome; somatic mutation. 1 Publication1
Natural variantiVAR_0581881417V → F in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs749210253Ensembl.1
Natural variantiVAR_0581891701M → I1 PublicationCorresponds to variant dbSNP:rs62623390EnsemblClinVar.1
Natural variantiVAR_0581901718V → L in refractory anemia with ringed sideroblasts; somatic mutation in an acute myeloid leukemia sample. 2 PublicationsCorresponds to variant dbSNP:rs142312318EnsemblClinVar.1
Natural variantiVAR_0581911721L → W1 PublicationCorresponds to variant dbSNP:rs34402524EnsemblClinVar.1
Natural variantiVAR_0581921723P → S2 PublicationsCorresponds to variant dbSNP:rs146348065EnsemblClinVar.1
Natural variantiVAR_0581521757H → D in a chronic myelomonocytic leukemia sample; somatic mutation. 1 Publication1
Natural variantiVAR_0581931762I → V2 PublicationsCorresponds to variant dbSNP:rs2454206EnsemblClinVar.1
Natural variantiVAR_0581941778H → R1 PublicationCorresponds to variant dbSNP:rs62621450EnsemblClinVar.1
Natural variantiVAR_0581531811C → R in a chronic myelomonocytic leukemia sample; somatic mutation. 1 Publication1
Natural variantiVAR_0581541828Q → L in a myeloproliferative disorder; somatic mutation. 1 Publication1
Natural variantiVAR_0581551869G → W in an essential thrombocythemia sample. 1 PublicationCorresponds to variant dbSNP:rs1453845082Ensembl.1
Natural variantiVAR_0581561872L → P in a refractory anemia with excess blasts sample. 1 Publication1
Natural variantiVAR_0581571873I → T in myelodysplastic syndromes, myeloproliferative disorders and chronic myelomonocytic leukemia; somatic mutation in acute myeloid leukemia and chronic myelomonocytic leukemia samples. 5 PublicationsCorresponds to variant dbSNP:rs116519313Ensembl.1
Natural variantiVAR_0581951875C → R in a myelodysplastic syndrome; somatic mutation. 1 Publication1
Natural variantiVAR_0581961881H → Q in a myelodysplastic syndrome; somatic mutation. 1 Publication1
Natural variantiVAR_0581581881H → R in a myeloproliferative disorder; somatic mutation; also in a patient with systemic mastocytosis associated with chronic myelomonocytic leukemia. 2 PublicationsCorresponds to variant dbSNP:rs1417392445Ensembl.1
Natural variantiVAR_0581591896R → M in a primary acute myeloid leukemia sample; somatic mutation; reduces enzyme activity. 2 Publications1
Natural variantiVAR_0581971896R → S in a myeloproliferative disorder; somatic mutation. 1 Publication1
Natural variantiVAR_0581601898S → F in a secondary acute myeloid leukemia sample; somatic mutation; loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs767475870Ensembl.1
Natural variantiVAR_0581611900V → A1 Publication1
Natural variantiVAR_0581621911 – 1916Missing in a myelodysplastic syndrome; somatic mutation. 1 Publication6
Natural variantiVAR_0581631913G → D in myelodysplastic syndromes; refractory cytopenia with multilineage dysplasia and ringed sideroblasts; somatic mutation in a patient. 2 Publications1
Natural variantiVAR_0581641919A → V in a myeloproliferative disorder; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1163887807Ensembl.1
Natural variantiVAR_0581651926R → H in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1316795626Ensembl.1
Natural variantiVAR_0581661941P → S in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1283441077Ensembl.1
Natural variantiVAR_0581671962P → L in a myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs200971953EnsemblClinVar.1
Natural variantiVAR_0581681966R → H in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs754215085Ensembl.1
Natural variantiVAR_0581691974R → M in a chronic myelomonocytic leukemia sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1406914931Ensembl.1
Natural variantiVAR_0581702000R → K1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0322821137 – 1194EQIIE…SQGCP → GLDRRVKLLGLKESSILVKK AKVLRDVLLLSGWFAEAAVK RSYCVWCGSELATPVRLQ in isoform 3. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_0322831137 – 1165EQIIE…REIME → GKCQKCTETHGVYPELANLS SDMGFSFFF in isoform 2. 2 PublicationsAdd BLAST29
Alternative sequenceiVSP_0322841166 – 2002Missing in isoform 2. 2 PublicationsAdd BLAST837
Alternative sequenceiVSP_0322851195 – 2002Missing in isoform 3. 1 PublicationAdd BLAST808

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BX640738 mRNA Translation: CAE45851.1
AC004069 Genomic DNA No translation available.
AC026029 Genomic DNA No translation available.
AK000039 mRNA Translation: BAA90898.1 Sequence problems.
AK027819 mRNA Translation: BAB55391.1 Different initiation.
AB075496 mRNA Translation: BAE45750.1
BC110509 mRNA Translation: AAI10510.1
BC110510 mRNA Translation: AAI10511.2
AB046766 mRNA Translation: BAB13372.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3666.1 [Q6N021-2]
CCDS47120.1 [Q6N021-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001120680.1, NM_001127208.2 [Q6N021-1]
NP_060098.3, NM_017628.4 [Q6N021-2]
XP_005263139.1, XM_005263082.2 [Q6N021-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265149; ENSP00000265149; ENSG00000168769 [Q6N021-3]
ENST00000305737; ENSP00000306705; ENSG00000168769 [Q6N021-2]
ENST00000380013; ENSP00000369351; ENSG00000168769 [Q6N021-1]
ENST00000540549; ENSP00000442788; ENSG00000168769 [Q6N021-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
54790

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:54790

UCSC genome browser

More...
UCSCi
uc003hxj.3 human [Q6N021-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640738 mRNA Translation: CAE45851.1
AC004069 Genomic DNA No translation available.
AC026029 Genomic DNA No translation available.
AK000039 mRNA Translation: BAA90898.1 Sequence problems.
AK027819 mRNA Translation: BAB55391.1 Different initiation.
AB075496 mRNA Translation: BAE45750.1
BC110509 mRNA Translation: AAI10510.1
BC110510 mRNA Translation: AAI10511.2
AB046766 mRNA Translation: BAB13372.1
CCDSiCCDS3666.1 [Q6N021-2]
CCDS47120.1 [Q6N021-1]
RefSeqiNP_001120680.1, NM_001127208.2 [Q6N021-1]
NP_060098.3, NM_017628.4 [Q6N021-2]
XP_005263139.1, XM_005263082.2 [Q6N021-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NM6X-ray2.03A1129-1480[»]
A1844-1936[»]
5D9YX-ray1.97A1129-1480[»]
A1844-1936[»]
5DEUX-ray1.80A1129-1480[»]
A1844-1935[»]
SMRiQ6N021
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120151, 12 interactors
IntActiQ6N021, 12 interactors
MINTiQ6N021
STRINGi9606.ENSP00000442788

PTM databases

iPTMnetiQ6N021
PhosphoSitePlusiQ6N021

Polymorphism and mutation databases

BioMutaiTET2
DMDMi239938839

Proteomic databases

EPDiQ6N021
jPOSTiQ6N021
MaxQBiQ6N021
PaxDbiQ6N021
PeptideAtlasiQ6N021
PRIDEiQ6N021
ProteomicsDBi66598
66599 [Q6N021-2]
66600 [Q6N021-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265149; ENSP00000265149; ENSG00000168769 [Q6N021-3]
ENST00000305737; ENSP00000306705; ENSG00000168769 [Q6N021-2]
ENST00000380013; ENSP00000369351; ENSG00000168769 [Q6N021-1]
ENST00000540549; ENSP00000442788; ENSG00000168769 [Q6N021-1]
GeneIDi54790
KEGGihsa:54790
UCSCiuc003hxj.3 human [Q6N021-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
54790
DisGeNETi54790

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TET2
HGNCiHGNC:25941 TET2
HPAiHPA043135
MalaCardsiTET2
MIMi263300 phenotype
612839 gene
614286 phenotype
neXtProtiNX_Q6N021
OpenTargetsiENSG00000168769
Orphaneti75564 Acquired idiopathic sideroblastic anemia
86845 Acute myeloid leukaemia with myelodysplasia-related features
3318 Essential thrombocythemia
729 Polycythemia vera
824 Primary myelofibrosis
98826 Refractory anemia
86839 Refractory anemia with excess blasts
PharmGKBiPA162405634

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IE22 Eukaryota
ENOG410XPWW LUCA
GeneTreeiENSGT00940000160003
InParanoidiQ6N021
OrthoDBi704215at2759
PhylomeDBiQ6N021
TreeFamiTF337563

Enzyme and pathway databases

ReactomeiR-HSA-5221030 TET1,2,3 and TDG demethylate DNA
SIGNORiQ6N021

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
TET2 human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
54790

Protein Ontology

More...
PROi
PR:Q6N021

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168769 Expressed in 192 organ(s), highest expression level in blood
ExpressionAtlasiQ6N021 baseline and differential
GenevisibleiQ6N021 HS

Family and domain databases

InterProiView protein in InterPro
IPR024779 2OGFeDO_noxygenase_dom
IPR040175 TET1/2/3
PANTHERiPTHR23358 PTHR23358, 1 hit
PfamiView protein in Pfam
PF12851 Tet_JBP, 1 hit
SMARTiView protein in SMART
SM01333 Tet_JBP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTET2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6N021
Secondary accession number(s): B5MDU0
, Q2TB88, Q3LIB8, Q96JX5, Q9HCM6, Q9NXW0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 16, 2009
Last modified: May 8, 2019
This is version 129 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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