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Lymphoid enhancer-binding factor 1 (LEF-1) (T cell-specific transcription factor 1-alpha) (TCF1-alpha)

 LEF1_HUMAN              Reviewed;         399 AA.
Q9UJU2; B4DG38; B7Z8E2; E9PDK3; Q3ZCU4; Q9HAZ0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 171.
RecName: Full=Lymphoid enhancer-binding factor 1;
Short=LEF-1;
AltName: Full=T cell-specific transcription factor 1-alpha;
Short=TCF1-alpha;
Name=LEF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
FUNCTION.
PubMed=2010090; DOI=10.1101/gad.5.4.656;
Waterman M.L., Fischer W.H., Jones K.A.;
"A thymus-specific member of the HMG protein family regulates the
human T cell receptor C alpha enhancer.";
Genes Dev. 5:656-669(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=10756202; DOI=10.1093/nar/28.9.1994;
Hovanes K., Li T.W., Waterman M.L.;
"The human LEF-1 gene contains a promoter preferentially active in
lymphocytes and encodes multiple isoforms derived from alternative
splicing.";
Nucleic Acids Res. 28:1994-2003(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), ALTERNATIVE SPLICING,
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19653274; DOI=10.1002/ijc.24802;
Jesse S., Koenig A., Ellenrieder V., Menke A.;
"Lef-1 isoforms regulate different target genes and reduce cellular
adhesion.";
Int. J. Cancer 126:1109-1120(2010).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Kobielak A., Kobielak K., Trzeciak W.H.;
"New transcript isoform of the human LEF-1 devoid of HMG domain,
derived from alternative splicing of exon 8.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
TISSUE=Amygdala, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
TISSUE=Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH ALYREF/THOC4.
PubMed=9119228; DOI=10.1101/gad.11.5.640;
Bruhn L., Munnerlyn A., Grosschedl R.;
"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required
for TCRalpha enhancer function.";
Genes Dev. 11:640-653(1997).
[10]
INTERACTION WITH CTNNB1.
PubMed=9488439; DOI=10.1128/MCB.18.3.1248;
Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G.,
Markman M., Lamers W., Destree O., Clevers H.;
"Two members of the Tcf family implicated in Wnt/b-catenin signaling
during embryogenesis in the mouse.";
Mol. Cell. Biol. 18:1248-1256(1998).
[11]
INTERACTION WITH TLE1, AND INHIBITION OF TRANSCRIPTIONAL ACTIVATION BY
TLE1.
PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
Stifani S., Paroush Z., Groner Y.;
"Transcriptional repression by AML1 and LEF-1 is mediated by the
TLE/Groucho corepressors.";
Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
[12]
IDENTIFICATION (ISOFORM 3), AND EXPRESSION IN COLON CANCER.
PubMed=11326276; DOI=10.1038/88264;
Hovanes K., Li T.W.H., Munguia J.E., Truong T., Milovanovic T.,
Lawrence Marsh J., Holcombe R.F., Waterman M.L.;
"Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are
selectively expressed in colon cancer.";
Nat. Genet. 28:53-57(2001).
[13]
FUNCTIONAL INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
PubMed=11266540; DOI=10.1093/nar/29.7.1410;
Brantjes H., Roose J., van De Wetering M., Clevers H.;
"All Tcf HMG box transcription factors interact with Groucho-related
co-repressors.";
Nucleic Acids Res. 29:1410-1419(2001).
[14]
INTERACTION WITH MDFI AND MDFIC.
PubMed=12192039; DOI=10.1128/MCB.22.18.6393-6405.2002;
Kusano S., Raab-Traub N.;
"I-mfa domain proteins interact with Axin and affect its regulation of
the Wnt and c-Jun N-terminal kinase signaling pathways.";
Mol. Cell. Biol. 22:6393-6405(2002).
[15]
INTERACTION WITH NLK, PHOSPHORYLATION AT THR-155 AND/OR SER-166 BY
NLK, AND MUTAGENESIS OF THR-155 AND SER-166.
PubMed=12556497; DOI=10.1128/MCB.23.4.1379-1389.2003;
Ishitani T., Ninomiya-Tsuji J., Matsumoto K.;
"Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-
activated protein kinase-related Nemo-like kinase-dependent
phosphorylation in Wnt/beta-catenin signaling.";
Mol. Cell. Biol. 23:1379-1389(2003).
[16]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
VARIANT [LARGE SCALE ANALYSIS] ARG-113.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Participates in the Wnt signaling pathway. Activates
transcription of target genes in the presence of CTNNB1 and EP300.
May play a role in hair cell differentiation and follicle
morphogenesis. TLE1, TLE2, TLE3 and TLE4 repress transactivation
mediated by LEF1 and CTNNB1. Regulates T-cell receptor alpha
enhancer function. Binds DNA in a sequence-specific manner. PIAG
antagonizes both Wnt-dependent and Wnt-independent activation by
LEF1 (By similarity). Isoform 3 lacks the CTNNB1 interaction
domain and may be an antagonist for Wnt signaling. Isoform 5
transcriptionally activates the fibronectin promoter, binds to and
represses transcription from the E-cadherin promoter in a CTNNB1-
independent manner, and is involved in reducing cellular
aggregation and increasing cell migration of pancreatic cancer
cells. Isoform 1 transcriptionally activates MYC and CCND1
expression and enhances proliferation of pancreatic tumor cells.
{ECO:0000250, ECO:0000269|PubMed:11266540,
ECO:0000269|PubMed:19653274, ECO:0000269|PubMed:2010090}.
-!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable
complex. Interacts with EP300, TLE1 and PIASG (By similarity).
Binds ALYREF/THOC4, MDFI and MDFIC. Interacts with NLK.
{ECO:0000250, ECO:0000269|PubMed:12192039,
ECO:0000269|PubMed:12556497, ECO:0000269|PubMed:9119228,
ECO:0000269|PubMed:9488439, ECO:0000269|PubMed:9751710}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=9; IntAct=EBI-926131, EBI-491549;
P49789:FHIT; NbExp=2; IntAct=EBI-926131, EBI-741760;
P08069:IGF1R; NbExp=5; IntAct=EBI-926131, EBI-475981;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00267}. Note=Found in nuclear bodies upon PIASG
binding. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=A;
IsoId=Q9UJU2-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=B, 8A;
IsoId=Q9UJU2-2; Sequence=VSP_002188;
Note=Produced by alternative splicing of isoform 1. May be
produced at very low levels due to a premature stop codon in the
mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=LEF-1-DN;
IsoId=Q9UJU2-3; Sequence=VSP_007022;
Note=Produced by alternative promoter usage. Acts as dominant
negative mutant.;
Name=4;
IsoId=Q9UJU2-4; Sequence=VSP_007022, VSP_002188;
Note=Produced by alternative splicing of isoform 3.;
Name=5;
IsoId=Q9UJU2-5; Sequence=VSP_040068;
Note=Produced by alternative splicing of isoform 1.;
Name=6;
IsoId=Q9UJU2-6; Sequence=VSP_040068, VSP_040069;
Note=Produced by alternative splicing of isoform 1. No
experimental confirmation available.;
Name=7;
IsoId=Q9UJU2-7; Sequence=VSP_044877, VSP_040068;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in thymus. Not detected in normal
colon, but highly expressed in colon cancer biopsies and colon
cancer cell lines. Expressed in several pancreatic tumors and
weakly expressed in normal pancreatic tissue. Isoforms 1 and 5 are
detected in several pancreatic cell lines.
{ECO:0000269|PubMed:19653274}.
-!- DOMAIN: Proline-rich and acidic regions are implicated in the
activation functions of RNA polymerase II transcription factors.
-!- PTM: Phosphorylated at Thr-155 and/or Ser-166 by NLK.
Phosphorylation by NLK at these sites represses LEF1-mediated
transcriptional activation of target genes of the canonical Wnt
signaling pathway. {ECO:0000269|PubMed:12556497}.
-!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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EMBL; AF288571; AAG01022.1; -; mRNA.
EMBL; AF198532; AAF13268.1; -; mRNA.
EMBL; AF294627; AAG26886.1; -; mRNA.
EMBL; AK294395; BAG57649.1; -; mRNA.
EMBL; AK303272; BAH13928.1; -; mRNA.
EMBL; AC092539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC097067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC123576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06223.1; -; Genomic_DNA.
EMBL; CH471057; EAX06225.1; -; Genomic_DNA.
EMBL; BC040559; AAH40559.1; -; mRNA.
EMBL; BC050632; AAH50632.1; -; mRNA.
CCDS; CCDS3679.1; -. [Q9UJU2-1]
CCDS; CCDS47122.1; -. [Q9UJU2-6]
CCDS; CCDS47123.1; -. [Q9UJU2-5]
CCDS; CCDS54791.1; -. [Q9UJU2-7]
PIR; A39625; A39625.
RefSeq; NP_001124185.1; NM_001130713.2. [Q9UJU2-5]
RefSeq; NP_001124186.1; NM_001130714.2. [Q9UJU2-6]
RefSeq; NP_001159591.1; NM_001166119.1. [Q9UJU2-7]
RefSeq; NP_057353.1; NM_016269.4. [Q9UJU2-1]
UniGene; Hs.743478; -.
ProteinModelPortal; Q9UJU2; -.
SMR; Q9UJU2; -.
BioGrid; 119354; 40.
DIP; DIP-29946N; -.
IntAct; Q9UJU2; 21.
MINT; MINT-8329835; -.
STRING; 9606.ENSP00000265165; -.
ChEMBL; CHEMBL3217392; -.
iPTMnet; Q9UJU2; -.
PhosphoSitePlus; Q9UJU2; -.
BioMuta; LEF1; -.
DMDM; 8928194; -.
PaxDb; Q9UJU2; -.
PeptideAtlas; Q9UJU2; -.
PRIDE; Q9UJU2; -.
TopDownProteomics; Q9UJU2-2; -. [Q9UJU2-2]
DNASU; 51176; -.
Ensembl; ENST00000265165; ENSP00000265165; ENSG00000138795. [Q9UJU2-1]
Ensembl; ENST00000379951; ENSP00000369284; ENSG00000138795. [Q9UJU2-6]
Ensembl; ENST00000438313; ENSP00000406176; ENSG00000138795. [Q9UJU2-5]
Ensembl; ENST00000506680; ENSP00000422334; ENSG00000138795. [Q9UJU2-2]
Ensembl; ENST00000510624; ENSP00000422840; ENSG00000138795. [Q9UJU2-7]
GeneID; 51176; -.
KEGG; hsa:51176; -.
UCSC; uc003hyt.3; human. [Q9UJU2-1]
CTD; 51176; -.
DisGeNET; 51176; -.
EuPathDB; HostDB:ENSG00000138795.9; -.
GeneCards; LEF1; -.
HGNC; HGNC:6551; LEF1.
HPA; CAB019405; -.
HPA; HPA002087; -.
MIM; 153245; gene.
neXtProt; NX_Q9UJU2; -.
OpenTargets; ENSG00000138795; -.
PharmGKB; PA30331; -.
eggNOG; KOG3248; Eukaryota.
eggNOG; ENOG41109RU; LUCA.
GeneTree; ENSGT00390000009964; -.
HOGENOM; HOG000116032; -.
HOVERGEN; HBG000419; -.
InParanoid; Q9UJU2; -.
KO; K04492; -.
OMA; QESYHDK; -.
OrthoDB; EOG091G0705; -.
PhylomeDB; Q9UJU2; -.
TreeFam; TF318448; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
Reactome; R-HSA-4641265; Repression of WNT target genes.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
SignaLink; Q9UJU2; -.
SIGNOR; Q9UJU2; -.
ChiTaRS; LEF1; human.
GeneWiki; Lymphoid_enhancer-binding_factor_1; -.
GenomeRNAi; 51176; -.
PRO; PR:Q9UJU2; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138795; -.
CleanEx; HS_LEF1; -.
ExpressionAtlas; Q9UJU2; baseline and differential.
Genevisible; Q9UJU2; HS.
GO; GO:1990907; C:beta-catenin-TCF complex; IPI:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0070016; F:armadillo repeat domain binding; IPI:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
GO; GO:0035326; F:enhancer binding; IDA:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0046632; P:alpha-beta T cell differentiation; IBA:GO_Central.
GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060561; P:apoptotic process involved in morphogenesis; IBA:GO_Central.
GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IBA:GO_Central.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB.
GO; GO:0060710; P:chorio-allantoic fusion; IBA:GO_Central.
GO; GO:0021542; P:dentate gyrus development; IBA:GO_Central.
GO; GO:0030326; P:embryonic limb morphogenesis; IBA:GO_Central.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0048069; P:eye pigmentation; IBA:GO_Central.
GO; GO:0060325; P:face morphogenesis; IBA:GO_Central.
GO; GO:0021873; P:forebrain neuroblast division; IBA:GO_Central.
GO; GO:0021879; P:forebrain neuron differentiation; IBA:GO_Central.
GO; GO:0021861; P:forebrain radial glial cell differentiation; IBA:GO_Central.
GO; GO:0021943; P:formation of radial glial scaffolds; IBA:GO_Central.
GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
GO; GO:0021854; P:hypothalamus development; IBA:GO_Central.
GO; GO:0030879; P:mammary gland development; IBA:GO_Central.
GO; GO:0048747; P:muscle fiber development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0071899; P:negative regulation of estrogen receptor binding; IDA:UniProtKB.
GO; GO:0032696; P:negative regulation of interleukin-13 production; IDA:UniProtKB.
GO; GO:0032713; P:negative regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0032714; P:negative regulation of interleukin-5 production; IDA:UniProtKB.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
GO; GO:0030223; P:neutrophil differentiation; IMP:UniProtKB.
GO; GO:0071895; P:odontoblast differentiation; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
GO; GO:0060021; P:palate development; ISS:BHF-UCL.
GO; GO:0048341; P:paraxial mesoderm formation; IBA:GO_Central.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0090068; P:positive regulation of cell cycle process; IDA:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:UniProtKB.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0022407; P:regulation of cell-cell adhesion; IBA:GO_Central.
GO; GO:0016202; P:regulation of striated muscle tissue development; IBA:GO_Central.
GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IBA:GO_Central.
GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
GO; GO:0045063; P:T-helper 1 cell differentiation; ISS:UniProtKB.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0061153; P:trachea gland development; IBA:GO_Central.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR027397; Catenin_binding_dom.
InterPro; IPR013558; CTNNB1-bd_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR028769; LEF1.
InterPro; IPR024940; TCF/LEF.
PANTHER; PTHR10373; PTHR10373; 1.
PANTHER; PTHR10373:SF11; PTHR10373:SF11; 1.
Pfam; PF08347; CTNNB1_binding; 1.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
Activator; Alternative promoter usage; Alternative splicing;
Complete proteome; Direct protein sequencing; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Wnt signaling pathway.
CHAIN 1 399 Lymphoid enhancer-binding factor 1.
/FTId=PRO_0000048595.
DNA_BIND 299 367 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 62 CTNNB1-binding. {ECO:0000250}.
COMPBIAS 6 13 Poly-Gly.
COMPBIAS 14 52 Asp/Glu-rich (acidic).
COMPBIAS 77 273 Pro-rich.
COMPBIAS 374 379 Poly-Lys.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 155 155 Phosphothreonine; by NLK.
{ECO:0000305|PubMed:12556497}.
MOD_RES 166 166 Phosphoserine; by NLK.
{ECO:0000305|PubMed:12556497}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 115 Missing (in isoform 3 and isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_007022.
VAR_SEQ 1 70 MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEI
SHPEEEGDLADIKSSLVNESEIIPASNGH -> MA (in
isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044877.
VAR_SEQ 214 241 Missing (in isoform 5, isoform 6 and
isoform 7). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19653274}.
/FTId=VSP_040068.
VAR_SEQ 283 399 KPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTL
KESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYP
GWSARDNYGKKKKRKREKLQESASGTGPRMTAAYI -> CS
AFLLPHPFLIPSTPSPNHHHHHLLGSLSMNRERSRSQKDLT
LRSL (in isoform 2 and isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_002188.
VAR_SEQ 390 399 TGPRMTAAYI -> GKRSSFPTCKAKAATPGPLLEMEAC
(in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040069.
VARIANT 113 113 G -> R (in a colorectal cancer sample;
somatic mutation; dbSNP:rs369649181).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035935.
MUTAGEN 155 155 T->A: Reduced phosphorylation by NLK;
when associated with A-166.
{ECO:0000269|PubMed:12556497}.
MUTAGEN 166 166 S->A: Reduced phosphorylation by NLK;
when associated with A-155.
{ECO:0000269|PubMed:12556497}.
CONFLICT 146 146 Q -> R (in Ref. 5; BAH13928).
{ECO:0000305}.
SEQUENCE 399 AA; 44201 MW; D480D440698EEFE3 CRC64;
MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE
SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM
NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS
KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS
RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK
KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE LARKERQLHM
QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI


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