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Protein

Transcription factor 20

Gene

Tcf20

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1565 – 157915A.T hookAdd
BLAST
Zinc fingeri1911 – 196252PHD-type; atypicalAdd
BLAST

GO - Molecular functioni

  • poly(A) RNA binding Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription regulatory region DNA binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor 20
Short name:
TCF-20
Alternative name(s):
Nuclear factor SPBP
Stromelysin-1 PDGF-responsive element-binding protein
Short name:
SPRE-binding protein
Gene namesi
Name:Tcf20
Synonyms:Spbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:108399. Tcf20.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1629 – 16291A → T: Loss of interaction with RNF4; when associated with S-1702; R-1736 and V-1737. 1 Publication
Mutagenesisi1702 – 17021P → S: Loss of interaction with RNF4; when associated with T-1629; R-1736 and V-1737. 1 Publication
Mutagenesisi1736 – 17372CG → RV: Loss of interaction with RNF4; when associated with T-1629 and S-1702. 1 Publication
Mutagenesisi1926 – 19261C → A: Reduces the inhibitory effect of the atypical PHD domain. 1 Publication
Mutagenesisi1931 – 19311C → A: Reduces the inhibitory effect of the atypical PHD domain. 1 Publication
Mutagenesisi1936 – 19361H → L: Reduces the inhibitory effect of the atypical PHD domain. 1 Publication
Mutagenesisi1939 – 19391C → A: Reduces the inhibitory effect of the atypical PHD domain. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19871987Transcription factor 20PRO_0000072449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471PhosphoserineBy similarity
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei603 – 6031PhosphoserineBy similarity
Modified residuei612 – 6121PhosphoserineCombined sources
Modified residuei631 – 6311N6-acetyllysineCombined sources
Cross-linki739 – 739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki852 – 852Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki873 – 873Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei900 – 9001PhosphoserineBy similarity
Cross-linki958 – 958Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki985 – 985Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei994 – 9941PhosphoserineBy similarity
Modified residuei1081 – 10811PhosphoserineBy similarity
Cross-linki1165 – 1165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1363 – 13631PhosphoserineBy similarity
Modified residuei1389 – 13891PhosphoserineBy similarity
Cross-linki1474 – 1474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1550 – 15501PhosphoserineBy similarity
Modified residuei1697 – 16971PhosphoserineBy similarity
Modified residuei1699 – 16991PhosphothreonineBy similarity
Modified residuei1790 – 17901PhosphothreonineCombined sources
Modified residuei1792 – 17921PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9EPQ8.
MaxQBiQ9EPQ8.
PaxDbiQ9EPQ8.
PRIDEiQ9EPQ8.

PTM databases

iPTMnetiQ9EPQ8.
PhosphoSiteiQ9EPQ8.

Expressioni

Tissue specificityi

Expressed in brain, lung, liver, kidney and testes.1 Publication

Developmental stagei

Isoform 2 is exclusively expressed at 7-11 days of development. Isoform 1 is found only at low levels in 15-17 days embryos.

Gene expression databases

CleanExiMM_TCF20.
GenevisibleiQ9EPQ8. MM.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with RNF4 and JUN. Binds to the regulatory region of MMP3.Curated2 Publications

Protein-protein interaction databases

IntActiQ9EPQ8. 1 interaction.
MINTiMINT-4137206.
STRINGi10090.ENSMUSP00000105136.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1198 – 121922Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1282 – 129514Nuclear localization signalAdd
BLAST
Motifi1604 – 162825Nuclear localization signalAdd
BLAST
Motifi1812 – 18198Nuclear localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 698Poly-Ala
Compositional biasi173 – 19523Poly-GlnAdd
BLAST
Compositional biasi249 – 27729Ser-richAdd
BLAST
Compositional biasi322 – 35029Poly-GlnAdd
BLAST
Compositional biasi1585 – 15928Poly-Pro
Compositional biasi1681 – 16844Poly-Glu
Compositional biasi1793 – 17975Poly-Glu

Domaini

The atypical PHD domain functions as a negative modulator of cofactor binding.

Sequence similaritiesi

Contains 1 A.T hook DNA-binding domain.Curated
Contains 1 PHD-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1911 – 196252PHD-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPTF. Eukaryota.
ENOG410ZTQQ. LUCA.
GeneTreeiENSGT00530000063684.
HOGENOMiHOG000026801.
HOVERGENiHBG079232.
InParanoidiQ9EPQ8.
OMAiEVLQGYH.
TreeFamiTF331317.

Family and domain databases

InterProiIPR001965. Znf_PHD.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EPQ8-1) [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
MQSFREQSSY HGNQQSYPQE VHSSSRIEEF SPRQAQMFQN FGGAGGGSSG
60 70 80 90 100
TGSSSSGRRG TAAAAAAMAS ETSGHQGYQG FRKEAGDFYY MAGNKDTVAA
110 120 130 140 150
GTPQPPQRRP SGPVQSYGPP QGSSFGNQYA SEGHVSQFQA QHSALGGVSH
160 170 180 190 200
YQQDYTGPFS PGSAQYQQQA SSQQQQQQQQ QQQQQQQQQQ QQVQQLRQQL
210 220 230 240 250
YQSHQPLPQT TGQPASGSSH LQPMQRPSTL PSSAGYQLRV GQFGQHYQSS
260 270 280 290 300
ASSSSSSSFP SPQRFSQSGQ SYDGSYSVNA GSQYEGHNVG SNAQAYGTQS
310 320 330 340 350
NYSYQPQSMK NFEQAKIPPG NQQGQQQQQQ QPQPQQQQPQ QQQQQQQQQQ
360 370 380 390 400
HPPQHVMQYT NAATKMPLQS QVGQYNQPEV PVRSPMQFHQ NFSPISNPSP
410 420 430 440 450
AASVVQSPSC SSTPSPLMQS GENLQCGQGN VPMSSRNRIL QLMPQLSPTP
460 470 480 490 500
SMMPSPNSHA AGFKGFGLEG VPEKRLTDPG LSSLSALSSQ VANLPNTVQH
510 520 530 540 550
MLLSDALTPQ KKTSKRPSSS SKKADSCTNS EGSSQPEEQL KSPMAESLDG
560 570 580 590 600
GCSSSSEDQG ERVRQLSGQS TSSDTTYKCG ASEKAGSSPT QGAQNEAPRL
610 620 630 640 650
STSPATRDEA ASPGAKDTSL SSEGNTKVNE KTVGVIVSRE AMTGRVEKSG
660 670 680 690 700
GQDKGSQEDD PAASQRPPSN SGVKEISHTS LPQPDPPGGG SKGNKNGDNN
710 720 730 740 750
SSNHNGEGNG PSSHSAVGPS FTGRTEPSKS PGSLRYSYKE SFGSAVPRNV
760 770 780 790 800
SGYPQYPSGQ EKGDFGSHGE RKGRNEKFPS LLQEVLQGYH HHPDRRYPRS
810 820 830 840 850
AQEHQGMASG LEGTARPNIL VSQTNELASR GLLNKSIGSL LENPHWGPWE
860 870 880 890 900
RKSSSTAPEM KQINLSDYPI PRKFEIEPPS SAHEPGGSLS ERRSVICDIS
910 920 930 940 950
PLRQIVRDPG AHSLGHMGTD ARIGRNERLN PSLSQSVILP GGLVSMETKL
960 970 980 990 1000
KSQSGQIKEE DFEQSKSQAS FNKKSGDHCH PTSIKHETYR GNASPGAAAH
1010 1020 1030 1040 1050
DSISDYGPQD SRSTPMRRVP GRVGSRETMR GRSSSQYHDF AEKLKMSPGR
1060 1070 1080 1090 1100
SRGPGGDPHH MNPHMTFSER ANRSSLHAPF SPNSESLASA YHTNTRAHAY
1110 1120 1130 1140 1150
GDPNTGLNSQ LHYKRQMYQQ QQEEYKDWAS SSAQGVIAAA QHRQEGPRKS
1160 1170 1180 1190 1200
PRQQQFLDRV RSPLKNDKDG MMYGPPVGTY HDPSTQEAGR CLMSSDGLPA
1210 1220 1230 1240 1250
KSMELKHSSQ KLQESCWDLS RQTSPAKSSG PPGMSNQKRY GPPHEPDGHG
1260 1270 1280 1290 1300
LAESAQSSKP SNVMLRLPGQ EDHSSQNPLI MRRRVRSFIS PIPSKRQSQD
1310 1320 1330 1340 1350
VKNSNADDKG RLLHPSKEGA DKAYNSYSHL SHSQDIKSIP KRDSSKDLPN
1360 1370 1380 1390 1400
PDNRNCPAVT LTSPAKTKIL PPRKGRGLKL EAIVQKITSP NIRRSASANS
1410 1420 1430 1440 1450
AEAGGDTVTL DDILSLKSGP PEGGTVATQE AEMEKRKCEV VSDLVSVTNQ
1460 1470 1480 1490 1500
ESNVEKPLPG PSEEWRGSGD DKVKTEAHVE TASTGKEPSG TMTSTASQKP
1510 1520 1530 1540 1550
GGNQGRPDGS LGGAAPLIFP DSKNVAPVGI LAPEANPKAE EKENDTVMIS
1560 1570 1580 1590 1600
PKQESFPPKG YFPSGKKKGR PIGSVNKQKK QQQQPPPPPQ PPQMPEGSAD
1610 1620 1630 1640 1650
GEPKPKKQRQ RRERRKPGAQ PRKRKTKQAV PIVEPQEPEI KLKYATQPLD
1660 1670 1680 1690 1700
KTDAKNKSFF PYIHVVNKCE LGAVCTIINA EEEEQTKLVR SRKGQRSLTP
1710 1720 1730 1740 1750
PPSSTESKVL PASSFMLQGP VVTESSVMGH LVCCLCGKWA SYRNMGDLFG
1760 1770 1780 1790 1800
PFYPQDYAAT LPKNPPPKRS SEMQSKVKVR HKSASNGSKT DTEEEEEQQQ
1810 1820 1830 1840 1850
QKEQRSLAAH PRFKRRHRSE DCGGGPRSLS RGLPCKKAAT EGSSEKTVSD
1860 1870 1880 1890 1900
TKPSVPTTSE GGPELELQIP ELPLDSNEFW VHEGCILWAN GIYLVCGRLY
1910 1920 1930 1940 1950
GLQEALEIAR EMKCSHCQEA GATLGCYNKG CSFRYHYPCA IDADCLLHEE
1960 1970 1980
NFSVRCPKHK PPLPCPLPPL QNKTAKGSLS TEQSERG
Length:1,987
Mass (Da):215,683
Last modified:October 16, 2013 - v3
Checksum:iDB6EE205C311DB59
GO
Isoform 2 (identifier: Q9EPQ8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1961-1987: PPLPCPLPPLQNKTAKGSLSTEQSERG → VRLWR

Show »
Length:1,965
Mass (Da):213,566
Checksum:i1B21452F2D195BE2
GO

Sequence cautioni

The sequence AAA86495.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551H → R in AAG28929 (PubMed:10995766).Curated
Sequence conflicti366 – 3661M → I in AAG28929 (PubMed:10995766).Curated
Sequence conflicti443 – 4431M → L in AAG28929 (PubMed:10995766).Curated
Sequence conflicti954 – 9541S → G in AAG28929 (PubMed:10995766).Curated
Sequence conflicti1022 – 10221R → I in AAA86495 (PubMed:7760812).Curated
Sequence conflicti1082 – 10821P → R in AAA86495 (PubMed:7760812).Curated
Sequence conflicti1161 – 11611R → G in AAA86495 (PubMed:7760812).Curated
Sequence conflicti1201 – 12011K → Q in AAG28929 (PubMed:10995766).Curated
Sequence conflicti1216 – 12161C → R in AAG28929 (PubMed:10995766).Curated
Sequence conflicti1297 – 12971Q → R in AAA86495 (PubMed:7760812).Curated
Sequence conflicti1418 – 14181S → G in AAA86495 (PubMed:7760812).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1961 – 198727PPLPC…QSERG → VRLWR in isoform 2. 2 PublicationsVSP_003986Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007594 mRNA. Translation: AAG28929.1.
AC087902 Genomic DNA. No translation available.
AC129563 Genomic DNA. No translation available.
BC138038 mRNA. Translation: AAI38039.1.
U20284 mRNA. Translation: AAA86495.1. Frameshift.
CCDSiCCDS27693.1. [Q9EPQ8-2]
CCDS49681.1. [Q9EPQ8-1]
RefSeqiNP_001107612.1. NM_001114140.1. [Q9EPQ8-1]
XP_006520795.1. XM_006520732.1. [Q9EPQ8-1]
XP_006520796.1. XM_006520733.1. [Q9EPQ8-1]
XP_011243853.1. XM_011245551.1. [Q9EPQ8-1]
XP_011243855.1. XM_011245553.1. [Q9EPQ8-2]
UniGeneiMm.252156.

Genome annotation databases

EnsembliENSMUST00000048966; ENSMUSP00000048486; ENSMUSG00000041852. [Q9EPQ8-2]
ENSMUST00000109510; ENSMUSP00000105136; ENSMUSG00000041852. [Q9EPQ8-1]
GeneIDi21411.
KEGGimmu:21411.
UCSCiuc007wzo.3. mouse. [Q9EPQ8-1]
uc007wzp.3. mouse. [Q9EPQ8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007594 mRNA. Translation: AAG28929.1.
AC087902 Genomic DNA. No translation available.
AC129563 Genomic DNA. No translation available.
BC138038 mRNA. Translation: AAI38039.1.
U20284 mRNA. Translation: AAA86495.1. Frameshift.
CCDSiCCDS27693.1. [Q9EPQ8-2]
CCDS49681.1. [Q9EPQ8-1]
RefSeqiNP_001107612.1. NM_001114140.1. [Q9EPQ8-1]
XP_006520795.1. XM_006520732.1. [Q9EPQ8-1]
XP_006520796.1. XM_006520733.1. [Q9EPQ8-1]
XP_011243853.1. XM_011245551.1. [Q9EPQ8-1]
XP_011243855.1. XM_011245553.1. [Q9EPQ8-2]
UniGeneiMm.252156.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EPQ8. 1 interaction.
MINTiMINT-4137206.
STRINGi10090.ENSMUSP00000105136.

PTM databases

iPTMnetiQ9EPQ8.
PhosphoSiteiQ9EPQ8.

Proteomic databases

EPDiQ9EPQ8.
MaxQBiQ9EPQ8.
PaxDbiQ9EPQ8.
PRIDEiQ9EPQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048966; ENSMUSP00000048486; ENSMUSG00000041852. [Q9EPQ8-2]
ENSMUST00000109510; ENSMUSP00000105136; ENSMUSG00000041852. [Q9EPQ8-1]
GeneIDi21411.
KEGGimmu:21411.
UCSCiuc007wzo.3. mouse. [Q9EPQ8-1]
uc007wzp.3. mouse. [Q9EPQ8-2]

Organism-specific databases

CTDi6942.
MGIiMGI:108399. Tcf20.

Phylogenomic databases

eggNOGiENOG410IPTF. Eukaryota.
ENOG410ZTQQ. LUCA.
GeneTreeiENSGT00530000063684.
HOGENOMiHOG000026801.
HOVERGENiHBG079232.
InParanoidiQ9EPQ8.
OMAiEVLQGYH.
TreeFamiTF331317.

Miscellaneous databases

ChiTaRSiTcf20. mouse.
NextBioi300692.
PROiQ9EPQ8.
SOURCEiSearch...

Gene expression databases

CleanExiMM_TCF20.
GenevisibleiQ9EPQ8. MM.

Family and domain databases

InterProiIPR001965. Znf_PHD.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nuclear factor SPBP contains different functional domains and stimulates the activity of various transcriptional activators."
    Rekdal C., Sjoettem E., Johansen T.
    J. Biol. Chem. 275:40288-40300(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, ALTERNATIVE SPLICING.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORM 1).
    Tissue: Brain.
  4. "Molecular characterization of a novel transcription factor that controls stromelysin expression."
    Sanz L., Moscat J., Diaz-Meco M.T.
    Mol. Cell. Biol. 15:3164-3170(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 774-1965 (ISOFORM 2).
    Tissue: Fibroblast.
  5. "Cross-talk between different enhancer elements during mitogenic induction of the human stromelysin-1 gene."
    Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.
    J. Biol. Chem. 271:18231-18236(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JUN.
  6. "Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers."
    Lyngsoe C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S., Noerby P.L., Bonven B.J., Joergensen P.
    J. Biol. Chem. 275:26144-26149(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF4, TISSUE SPECIFICITY, MUTAGENESIS.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; THR-1790 AND THR-1792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTCF20_MOUSE
AccessioniPrimary (citable) accession number: Q9EPQ8
Secondary accession number(s): B9EHJ7, Q60792
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 16, 2013
Last modified: March 16, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.