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Protein

Methylcytosine dioxygenase TET2

Gene

Tet2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. 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

Catalytic activityi

DNA 5-methylcytosine + 2-oxoglutarate + O2 = DNA 5-hydroxymethylcytosine + succinate + CO2.4 Publications

Cofactori

Protein has several cofactor binding sites:
  • Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 3 zinc ions per subunit. The zinc ions have a structural role.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1048 – 10481Zinc 1By similarity
Metal bindingi1106 – 11061Zinc 2By similarity
Metal bindingi1132 – 11321Zinc 1; via pros nitrogenBy similarity
Metal bindingi1134 – 11341Zinc 1By similarity
Binding sitei1174 – 117412-oxoglutarateBy similarity
Metal bindingi1184 – 11841Zinc 2By similarity
Metal bindingi1186 – 11861Zinc 2By similarity
Metal bindingi1202 – 12021Zinc 3By similarity
Metal bindingi1211 – 12111Zinc 3By similarity
Metal bindingi1271 – 12711Zinc 3By similarity
Binding sitei1287 – 128712-oxoglutarateBy similarity
Metal bindingi1293 – 12931Zinc 2; via tele nitrogenBy similarity
Metal bindingi1295 – 12951Iron; catalyticBy similarity
Metal bindingi1297 – 12971Iron; catalyticBy similarity
Binding sitei1300 – 13001SubstrateBy similarity
Binding sitei1329 – 132912-oxoglutarateBy similarity
Metal bindingi1795 – 17951Iron; catalyticBy similarity
Metal bindingi1826 – 18261Zinc 3; via pros nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

  • 5-methylcytosine catabolic process Source: UniProtKB
  • 5-methylcytosine metabolic process Source: MGI
  • cell cycle Source: UniProtKB-KW
  • cytosine metabolic process Source: MGI
  • DNA demethylation Source: UniProtKB
  • hematopoietic stem cell homeostasis Source: MGI
  • hemoglobin metabolic process Source: MGI
  • hemopoiesis Source: MGI
  • histone H3-K4 trimethylation Source: UniProtKB
  • homeostasis of number of cells Source: MGI
  • kidney development Source: MGI
  • liver morphogenesis Source: MGI
  • myeloid cell differentiation Source: UniProtKB
  • myeloid progenitor cell differentiation Source: MGI
  • oxidative DNA demethylation Source: Reactome
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • post-embryonic development Source: MGI
  • protein O-linked glycosylation Source: UniProtKB
  • response to organic cyclic compound Source: Ensembl
  • spleen development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

DNA-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5221030. TET1,2,3 and TDG demethylate DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylcytosine dioxygenase TET2 (EC:1.14.11.n24 Publications)
Alternative name(s):
Protein Ayu17-449
Gene namesi
Name:Tet2
Synonyms:Kiaa1546
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2443298. Tet2.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile but develop chronic myelomonocytic leukemia probably caused by dysregulation of hematopoietic stem cells. Mice lacking both Tet1 and Tet2 are fertile, with females having smaller ovaries and reduced fertility. They display decreased 5-hydroxymethylcytosine (5hmC) and abnormal methylation at various imprinted loci. Embryonic stem cells lacking both Tet1 and Tet2 remain pluripotent but lack 5hmC, leading to developmental defects in chimeric embryos.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1204 – 12041W → R: Impairs enzyme activity. 1 Publication
Mutagenesisi1280 – 12801P → S: Impairs enzyme activity. 1 Publication
Mutagenesisi1295 – 12951H → Y: Loss of enzyme activity; when associated with A-1297. 3 Publications
Mutagenesisi1297 – 12971D → A: Loss of enzyme activity; when associated with Y-1295. 3 Publications
Mutagenesisi1795 – 17951H → R or Q: Loss of enzyme activity. 1 Publication
Mutagenesisi1810 – 18101R → S or M: Impairs enzyme activity. 1 Publication
Mutagenesisi1827 – 18271C → D: Impairs enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19121912Methylcytosine dioxygenase TET2PRO_0000324589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei1036 – 10361PhosphoserineBy similarity

Post-translational modificationi

May be glycosylated. It is unclear whether interaction with OGT leads to GlcNAcylation. According to a report, it is GlcNAcylated by OGT (PubMed:23352454). In contrast, another group reports no GlcNAcylation by OGT in human ortholog.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ4JK59.
MaxQBiQ4JK59.
PaxDbiQ4JK59.
PeptideAtlasiQ4JK59.
PRIDEiQ4JK59.

PTM databases

iPTMnetiQ4JK59.
PhosphoSiteiQ4JK59.
SwissPalmiQ4JK59.

Expressioni

Tissue specificityi

Highly expressed in the brain, kidney, heart, lung, muscle and stomach. Present in embryonic stem cells (ES cells).2 Publications

Gene expression databases

BgeeiENSMUSG00000040943.
CleanExiMM_TET2.
ExpressionAtlasiQ4JK59. baseline and differential.
GenevisibleiQ4JK59. MM.

Interactioni

Subunit structurei

Interacts with HCFC1 (By similarity). Interacts with OGT.By similarity1 Publication

Protein-protein interaction databases

BioGridi229496. 9 interactions.
IntActiQ4JK59. 1 interaction.
STRINGi10090.ENSMUSP00000096203.

Structurei

3D structure databases

ProteinModelPortaliQ4JK59.
SMRiQ4JK59. Positions 1057-1366, 1759-1838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1203 – 121614Interaction with DNABy similarityAdd
BLAST
Regioni1810 – 181232-oxoglutarate bindingBy similarity
Regioni1816 – 18183Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 921346Gln-richAdd
BLAST
Compositional biasi1364 – 13674Poly-Arg
Compositional biasi1426 – 147550Gln-richAdd
BLAST
Compositional biasi1694 – 16996Poly-Ser

Sequence similaritiesi

Belongs to the TET family.Curated

Phylogenomic databases

eggNOGiENOG410IE22. Eukaryota.
ENOG410XPWW. LUCA.
GeneTreeiENSGT00510000046514.
HOGENOMiHOG000168510.
HOVERGENiHBG108562.
InParanoidiQ4JK59.
PhylomeDBiQ4JK59.
TreeFamiTF337563.

Family and domain databases

InterProiIPR024779. 2OGFeDO_noxygenase_dom.
[Graphical view]
PfamiPF12851. Tet_JBP. 1 hit.
[Graphical view]
SMARTiSM01333. Tet_JBP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4JK59-1) [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
MEQDRTTHAE GTRLSPFLIA PPSPISHTEP LAVKLQNGSP LAERPHPEVN
60 70 80 90 100
GDTKWQSSQS CYGISHMKGS QSSHESPHED RGYSRCLQNG GIKRTVSEPS
110 120 130 140 150
LSGLHPNKIL KLDQKAKGES NIFEESQERN HGKSSRQPNV SGLSDNGEPV
160 170 180 190 200
TSTTQESSGA DAFPTRNYNG VEIQVLNEQE GEKGRSVTLL KNKIVLMPNG
210 220 230 240 250
ATVSAHSEEN TRGELLEKTQ CYPDCVSIAV QSTASHVNTP SSQAAIELSH
260 270 280 290 300
EIPQPSLTSA QINFSQTSSL QLPPEPAAMV TKACDADNAS KPAIVPGTCP
310 320 330 340 350
FQKAEHQQKS ALDIGPSRAE NKTIQGSMEL FAEEYYPSSD RNLQASHGSS
360 370 380 390 400
EQYSKQKETN GAYFRQSSKF PKDSISPTTV TPPSQSLLAP RLVLQPPLEG
410 420 430 440 450
KGALNDVALE EHHDYPNRSN RTLLREGKID HQPKTSSSQS LNPSVHTPNP
460 470 480 490 500
PLMLPEQHQN DCGSPSPEKS RKMSEYLMYY LPNHGHSGGL QEHSQYLMGH
510 520 530 540 550
REQEIPKDAN GKQTQGSVQA APGWIELKAP NLHEALHQTK RKDISLHSVL
560 570 580 590 600
HSQTGPVNQM SSKQSTGNVN MPGGFQRLPY LQKTAQPEQK AQMYQVQVNQ
610 620 630 640 650
GPSPGMGDQH LQFQKALYQE CIPRTDPSSE AHPQAPSVPQ YHFQQRVNPS
660 670 680 690 700
SDKHLSQQAT ETQRLSGFLQ HTPQTQASQT PASQNSNFPQ ICQQQQQQQL
710 720 730 740 750
QRKNKEQMPQ TFSHLQGSND KQREGSCFGQ IKVEESFCVG NQYSKSSNFQ
760 770 780 790 800
THNNTQGGLE QVQNINKNFP YSKILTPNSS NLQILPSNDT HPACEREQAL
810 820 830 840 850
HPVGSKTSNL QNMQYFPNNV TPNQDVHRCF QEQAQKPQQA SSLQGLKDRS
860 870 880 890 900
QGESPAPPAE AAQQRYLVHN EAKALPVPEQ GGSQTQTPPQ KDTQKHAALR
910 920 930 940 950
WLLLQKQEQQ QTQQSQPGHN QMLRPIKTEP VSKPSSYRYP LSPPQENMSS
960 970 980 990 1000
RIKQEISSPS RDNGQPKSII ETMEQHLKQF QLKSLCDYKA LTLKSQKHVK
1010 1020 1030 1040 1050
VPTDIQAAES ENHARAAEPQ ATKSTDCSVL DDVSESDTPG EQSQNGKCEG
1060 1070 1080 1090 1100
CNPDKDEAPY YTHLGAGPDV AAIRTLMEER YGEKGKAIRI EKVIYTGKEG
1110 1120 1130 1140 1150
KSSQGCPIAK WVYRRSSEEE KLLCLVRVRP NHTCETAVMV IAIMLWDGIP
1160 1170 1180 1190 1200
KLLASELYSE LTDILGKCGI CTNRRCSQNE TRNCCCQGEN PETCGASFSF
1210 1220 1230 1240 1250
GCSWSMYYNG CKFARSKKPR KFRLHGAEPK EEERLGSHLQ NLATVIAPIY
1260 1270 1280 1290 1300
KKLAPDAYNN QVEFEHQAPD CCLGLKEGRP FSGVTACLDF SAHSHRDQQN
1310 1320 1330 1340 1350
MPNGSTVVVT LNREDNREVG AKPEDEQFHV LPMYIIAPED EFGSTEGQEK
1360 1370 1380 1390 1400
KIRMGSIEVL QSFRRRRVIR IGELPKSCKK KAEPKKAKTK KAARKRSSLE
1410 1420 1430 1440 1450
NCSSRTEKGK SSSHTKLMEN ASHMKQMTAQ PQLSGPVIRQ PPTLQRHLQQ
1460 1470 1480 1490 1500
GQRPQQPQPP QPQPQTTPQP QPQPQHIMPG NSQSVGSHCS GSTSVYTRQP
1510 1520 1530 1540 1550
TPHSPYPSSA HTSDIYGDTN HVNFYPTSSH ASGSYLNPSN YMNPYLGLLN
1560 1570 1580 1590 1600
QNNQYAPFPY NGSVPVDNGS PFLGSYSPQA QSRDLHRYPN QDHLTNQNLP
1610 1620 1630 1640 1650
PIHTLHQQTF GDSPSKYLSY GNQNMQRDAF TTNSTLKPNV HHLATFSPYP
1660 1670 1680 1690 1700
TPKMDSHFMG AASRSPYSHP HTDYKTSEHH LPSHTIYSYT AAASGSSSSH
1710 1720 1730 1740 1750
AFHNKENDNI ANGLSRVLPG FNHDRTASAQ ELLYSLTGSS QEKQPEVSGQ
1760 1770 1780 1790 1800
DAAAVQEIEY WSDSEHNFQD PCIGGVAIAP THGSILIECA KCEVHATTKV
1810 1820 1830 1840 1850
NDPDRNHPTR ISLVLYRHKN LFLPKHCLAL WEAKMAEKAR KEEECGKNGS
1860 1870 1880 1890 1900
DHVSQKNHGK QEKREPTGPQ EPSYLRFIQS LAENTGSVTT DSTVTTSPYA
1910
FTQVTGPYNT FV
Length:1,912
Mass (Da):212,130
Last modified:June 16, 2009 - v3
Checksum:iF49DEE206CD05670
GO
Isoform 2 (identifier: Q4JK59-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1300: Missing.

Note: No experimental confirmation available.
Show »
Length:612
Mass (Da):68,060
Checksum:i09D5192CD8860AF5
GO
Isoform 3 (identifier: Q4JK59-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1332: Missing.

Note: No experimental confirmation available.
Show »
Length:580
Mass (Da):64,499
Checksum:i4B40A59555161AE5
GO

Sequence cautioni

The sequence AAY90126 differs from that shown. Reason: Frameshift at positions 1143 and 1182. Curated
The sequence BAC98199 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE30334 differs from that shown. Reason: Frameshift at positions 1749 and 1760. Curated
The sequence BAE30334 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE31106 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE31842 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE31892 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE32012 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1225 – 12251H → R in AAY90126 (PubMed:16722336).Curated
Sequence conflicti1626 – 16261Q → R in BAE32012 (PubMed:16141072).Curated
Sequence conflicti1626 – 16261Q → R in BAE31842 (PubMed:16141072).Curated
Sequence conflicti1736 – 17361L → V in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1737 – 17371T → A in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1743 – 17431K → E in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1767 – 17671N → T in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1772 – 17721C → A in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1773 – 17731I → F in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1795 – 17951H → N in BAE30334 (PubMed:16141072).Curated
Sequence conflicti1795 – 17951H → N in BAE31106 (PubMed:16141072).Curated
Sequence conflicti1795 – 17951H → N in BAE31892 (PubMed:16141072).Curated
Sequence conflicti1795 – 17951H → N in BAE31842 (PubMed:16141072).Curated
Sequence conflicti1795 – 17951H → N in BAE32012 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 13321332Missing in isoform 3. 1 PublicationVSP_032286Add
BLAST
Alternative sequencei1 – 13001300Missing in isoform 2. 2 PublicationsVSP_032287Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ079067 mRNA. Translation: AAY90126.1. Frameshift.
AK129389 mRNA. Translation: BAC98199.1. Different initiation.
BC031159 mRNA. Translation: AAH31159.1.
BC040785 mRNA. Translation: AAH40785.1.
AK151359 mRNA. Translation: BAE30334.1. Sequence problems.
AK152297 mRNA. Translation: BAE31106.1. Different initiation.
AK153251 mRNA. Translation: BAE31842.1. Different initiation.
AK153311 mRNA. Translation: BAE31892.1. Different initiation.
AK153460 mRNA. Translation: BAE32012.1. Different initiation.
CCDSiCCDS51071.1. [Q4JK59-1]
RefSeqiNP_001035490.2. NM_001040400.2. [Q4JK59-1]
UniGeneiMm.347816.

Genome annotation databases

EnsembliENSMUST00000098603; ENSMUSP00000096203; ENSMUSG00000040943. [Q4JK59-1]
GeneIDi214133.
KEGGimmu:214133.
UCSCiuc008rko.2. mouse. [Q4JK59-2]
uc008rkp.2. mouse. [Q4JK59-3]
uc008rkq.2. mouse. [Q4JK59-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ079067 mRNA. Translation: AAY90126.1. Frameshift.
AK129389 mRNA. Translation: BAC98199.1. Different initiation.
BC031159 mRNA. Translation: AAH31159.1.
BC040785 mRNA. Translation: AAH40785.1.
AK151359 mRNA. Translation: BAE30334.1. Sequence problems.
AK152297 mRNA. Translation: BAE31106.1. Different initiation.
AK153251 mRNA. Translation: BAE31842.1. Different initiation.
AK153311 mRNA. Translation: BAE31892.1. Different initiation.
AK153460 mRNA. Translation: BAE32012.1. Different initiation.
CCDSiCCDS51071.1. [Q4JK59-1]
RefSeqiNP_001035490.2. NM_001040400.2. [Q4JK59-1]
UniGeneiMm.347816.

3D structure databases

ProteinModelPortaliQ4JK59.
SMRiQ4JK59. Positions 1057-1366, 1759-1838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229496. 9 interactions.
IntActiQ4JK59. 1 interaction.
STRINGi10090.ENSMUSP00000096203.

PTM databases

iPTMnetiQ4JK59.
PhosphoSiteiQ4JK59.
SwissPalmiQ4JK59.

Proteomic databases

EPDiQ4JK59.
MaxQBiQ4JK59.
PaxDbiQ4JK59.
PeptideAtlasiQ4JK59.
PRIDEiQ4JK59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098603; ENSMUSP00000096203; ENSMUSG00000040943. [Q4JK59-1]
GeneIDi214133.
KEGGimmu:214133.
UCSCiuc008rko.2. mouse. [Q4JK59-2]
uc008rkp.2. mouse. [Q4JK59-3]
uc008rkq.2. mouse. [Q4JK59-1]

Organism-specific databases

CTDi54790.
MGIiMGI:2443298. Tet2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IE22. Eukaryota.
ENOG410XPWW. LUCA.
GeneTreeiENSGT00510000046514.
HOGENOMiHOG000168510.
HOVERGENiHBG108562.
InParanoidiQ4JK59.
PhylomeDBiQ4JK59.
TreeFamiTF337563.

Enzyme and pathway databases

ReactomeiR-MMU-5221030. TET1,2,3 and TDG demethylate DNA.

Miscellaneous databases

ChiTaRSiTet2. mouse.
PROiQ4JK59.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000040943.
CleanExiMM_TET2.
ExpressionAtlasiQ4JK59. baseline and differential.
GenevisibleiQ4JK59. MM.

Family and domain databases

InterProiIPR024779. 2OGFeDO_noxygenase_dom.
[Graphical view]
PfamiPF12851. Tet_JBP. 1 hit.
[Graphical view]
SMARTiSM01333. Tet_JBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTET2_MOUSE
AccessioniPrimary (citable) accession number: Q4JK59
Secondary accession number(s): Q3U5R5
, Q3U633, Q3UAI0, Q6ZPN2, Q8K2K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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. 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.