Q9UJU2 (LEF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lymphoid enhancer-binding factor 1
Short name=LEF-1

Alternative name(s):
T cell-specific transcription factor 1-alpha
Short name=TCF1-alpha

Gene names

Name:

LEF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.3 Ref.13
Subunit structure	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. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
Subcellular location	Nucleus By similarity. Note: Found in nuclear bodies upon PIASG binding By similarity.
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. Ref.3
Domain	Proline-rich and acidic regions are implicated in the activation functions of RNA polymerase II transcription factors.
Post-translational modification	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. Ref.15
Sequence similarities	Belongs to the TCF/LEF family. Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell proliferation Inferred from Biological aspect of Ancestor. Source: RefGenome BMP signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome T cell receptor V(D)J recombination Inferred from electronic annotation. Source: Compara T-helper 1 cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB anatomical structure regression Inferred from electronic annotation. Source: Compara apoptotic process involved in morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 19576624. Source: UniProtKB cell chemotaxis Inferred from direct assay PubMed 19576624. Source: UniProtKB cellular response to interleukin-4 Inferred from direct assay PubMed 18579517. Source: UniProtKB chorio-allantoic fusion Inferred from Biological aspect of Ancestor. Source: RefGenome dentate gyrus development Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic limb morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: BHF-UCL eye pigmentation Inferred from Biological aspect of Ancestor. Source: RefGenome face morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome forebrain neuroblast division Inferred from Biological aspect of Ancestor. Source: RefGenome forebrain neuron differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome forebrain radial glial cell differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome formation of radial glial scaffolds Inferred from Biological aspect of Ancestor. Source: RefGenome histone H3 acetylation Inferred from mutant phenotype PubMed 20363964. Source: UniProtKB histone H4 acetylation Inferred from mutant phenotype PubMed 20363964. Source: UniProtKB hypothalamus development Inferred from Biological aspect of Ancestor. Source: RefGenome induction of apoptosis Inferred from Biological aspect of Ancestor. Source: RefGenome mammary gland development Inferred from Biological aspect of Ancestor. Source: RefGenome muscle fiber development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of DNA binding Inferred from direct assay PubMed 18445004. Source: UniProtKB negative regulation of apoptotic process in bone marrow Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB negative regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 19402906. Source: UniProtKB negative regulation of cell-cell adhesion Inferred from direct assay Ref.3. Source: UniProtKB negative regulation of estrogen receptor binding Inferred from direct assay PubMed 18794125. Source: UniProtKB negative regulation of interleukin-13 production Inferred from direct assay PubMed 18445004. Source: UniProtKB negative regulation of interleukin-4 production Inferred from direct assay PubMed 18445004. Source: UniProtKB negative regulation of interleukin-5 production Inferred from direct assay PubMed 18445004. Source: UniProtKB negative regulation of striated muscle tissue development Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18794125Ref.3. Source: UniProtKB neural crest cell migration Inferred from Biological aspect of Ancestor. Source: RefGenome neutrophil differentiation Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB odontoblast differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from expression pattern PubMed 20128911. Source: UniProtKB palate development Inferred from sequence or structural similarity. Source: BHF-UCL paraxial mesoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome patterning of blood vessels Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation by host of viral transcription Inferred from direct assay PubMed 7657162. Source: UniProtKB positive regulation of cell cycle process Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB positive regulation of cell migration Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of cell proliferation Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of cell proliferation in bone marrow Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB positive regulation of cell-cell adhesion Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of epithelial to mesenchymal transition Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB positive regulation of granulocyte differentiation Inferred from direct assay PubMed 19620402. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.3. Source: UniProtKB regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara regulation of striated muscle tissue development Inferred from Biological aspect of Ancestor. Source: RefGenome sensory perception of taste Inferred from electronic annotation. Source: Compara somitogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome sprouting angiogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome tongue development Inferred from electronic annotation. Source: Compara trachea gland development Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from direct assay PubMed 19402906. Source: UniProtKB protein-DNA complex Inferred from direct assay PubMed 10825188. Source: BHF-UCL transcription factor complex Inferred from direct assay PubMed 11751639PubMed 23001182. Source: BHF-UCL
Molecular_function	DNA binding, bending Inferred from sequence or structural similarity. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome RNA polymerase II regulatory region sequence-specific DNA binding Inferred from direct assay PubMed 23001182. Source: BHF-UCL RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL beta-catenin binding Inferred from direct assay Ref.10. Source: BHF-UCL chromatin binding Inferred from Biological aspect of Ancestor. Source: RefGenome cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB enhancer binding Inferred from direct assay PubMed 7657162. Source: UniProtKB estrogen receptor activity Inferred from direct assay PubMed 18794125. Source: UniProtKB estrogen receptor binding Inferred from direct assay PubMed 18794125. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	4	EBI-926131,EBI-491549

Alternative products

This entry describes 7 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9UJU2-1)

Also known as: A;

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.

Note: Produced by alternative promoter usage.

Isoform 2 (identifier: Q9UJU2-2)

Also known as: B; 8A;

The sequence of this isoform differs from the canonical sequence as follows:
     283-399: KPQHEQRKEQ...TGPRMTAAYI → CSAFLLPHPF...SQKDLTLRSL

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.

Isoform 3 (identifier: Q9UJU2-3)

Also known as: LEF-1-DN;

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.

Note: Produced by alternative promoter usage. Acts as dominant negative mutant.

Isoform 4 (identifier: Q9UJU2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
     283-399: KPQHEQRKEQ...TGPRMTAAYI → CSAFLLPHPF...SQKDLTLRSL

Note: Produced by alternative splicing of isoform 3.

Isoform 5 (identifier: Q9UJU2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     214-241: Missing.

Note: Produced by alternative splicing of isoform 1.

Isoform 6 (identifier: Q9UJU2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     214-241: Missing.
     390-399: TGPRMTAAYI → GKRSSFPTCKAKAATPGPLLEMEAC

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

Isoform 7 (identifier: Q9UJU2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGH → MA
     214-241: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 399	399	Lymphoid enhancer-binding factor 1		PRO_0000048595
Regions
	DNA binding	299 – 367	69	HMG box
	Region	1 – 62	62	CTNNB1-binding By similarity
	Compositional bias	6 – 13	8	Poly-Gly
	Compositional bias	14 – 52	39	Asp/Glu-rich (acidic)
	Compositional bias	77 – 273	197	Pro-rich
	Compositional bias	374 – 379	6	Poly-Lys
Amino acid modifications
	Modified residue	132	1	Phosphoserine Ref.17
	Modified residue	155	1	Phosphothreonine; by NLK Probable
	Modified residue	166	1	Phosphoserine; by NLK Probable
	Cross-link	27		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	269		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 115	115	Missing in isoform 3 and isoform 4.		VSP_007022
	Alternative sequence	1 – 70	70	MPQLS…ASNGH → MA in isoform 7.		VSP_044877
	Alternative sequence	214 – 241	28	Missing in isoform 5, isoform 6 and isoform 7.		VSP_040068
	Alternative sequence	283 – 399	117	KPQHE…TAAYI → CSAFLLPHPFLIPSTPSPNH HHHHLLGSLSMNRERSRSQK DLTLRSL in isoform 2 and isoform 4.		VSP_002188
	Alternative sequence	390 – 399	10	TGPRMTAAYI → GKRSSFPTCKAKAATPGPLL EMEAC in isoform 6.		VSP_040069
	Natural variant	113	1	G → R in a colorectal cancer sample; somatic mutation. Ref.18		VAR_035935
Experimental info
	Mutagenesis	155	1	T → A: Reduced phosphorylation by NLK; when associated with A-166. Ref.15
	Mutagenesis	166	1	S → A: Reduced phosphorylation by NLK; when associated with A-155. Ref.15
	Sequence conflict	146	1	Q → R in BAH13928. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D480D440698EEFE3	FASTA	399	44,201
	10 20 30 40 50 60 MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE 70 80 90 100 110 120 SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM 130 140 150 160 170 180 NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS 190 200 210 220 230 240 KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS 250 260 270 280 290 300 RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK 310 320 330 340 350 360 KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE LARKERQLHM 370 380 390 QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI
	Isoform 2 (B) (8A) [UniParc]. Checksum: 3632325D440CA5DD	FASTA	329	35,672
	10 20 30 40 50 60 MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE 70 80 90 100 110 120 SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM 130 140 150 160 170 180 NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS 190 200 210 220 230 240 KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS 250 260 270 280 290 300 RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVCSAFLLPH PFLIPSTPSP 310 320 NHHHHHLLGS LSMNRERSRS QKDLTLRSL
	Isoform 3 (LEF-1-DN) [UniParc]. Checksum: 22320A1A195401ED	FASTA	284	31,919
	10 20 30 40 50 60 MMPNMNNDPY MSNGSLSPPI PRTSNKVPVV QPSHAVHPLT PLITYSDEHF SPGSHPSHIP 70 80 90 100 110 120 SDVNSKQGMS RHPPAPDIPT FYPLSPGGVG QITPPLGWQG QPVYPITGGF RQPYPSSLSV 130 140 150 160 170 180 DTSMSRFSHH MIPGPPGPHT TGIPHPAIVT PQVKQEHPHT DSDLMHVKPQ HEQRKEQEPK 190 200 210 220 230 240 RPHIKKPLNA FMLYMKEMRA NVVAECTLKE SAAINQILGR RWHALSREEQ AKYYELARKE 250 260 270 280 RQLHMQLYPG WSARDNYGKK KKRKREKLQE SASGTGPRMT AAYI
	Isoform 4 [UniParc]. Checksum: DDBF9358A5E8944C	FASTA	214	23,390
	10 20 30 40 50 60 MMPNMNNDPY MSNGSLSPPI PRTSNKVPVV QPSHAVHPLT PLITYSDEHF SPGSHPSHIP 70 80 90 100 110 120 SDVNSKQGMS RHPPAPDIPT FYPLSPGGVG QITPPLGWQG QPVYPITGGF RQPYPSSLSV 130 140 150 160 170 180 DTSMSRFSHH MIPGPPGPHT TGIPHPAIVT PQVKQEHPHT DSDLMHVCSA FLLPHPFLIP 190 200 210 STPSPNHHHH HLLGSLSMNR ERSRSQKDLT LRSL
	Isoform 5 [UniParc]. Checksum: F929C8679F4EC1A3	FASTA	371	41,162
	10 20 30 40 50 60 MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE 70 80 90 100 110 120 SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM 130 140 150 160 170 180 NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS 190 200 210 220 230 240 KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWFSHHMIP GPPGPHTTGI PHPAIVTPQV 250 260 270 280 290 300 KQEHPHTDSD LMHVKPQHEQ RKEQEPKRPH IKKPLNAFML YMKEMRANVV AECTLKESAA 310 320 330 340 350 360 INQILGRRWH ALSREEQAKY YELARKERQL HMQLYPGWSA RDNYGKKKKR KREKLQESAS 370 GTGPRMTAAY I
	Isoform 6 [UniParc]. Checksum: 918B4201D718A485	FASTA	386	42,676
	10 20 30 40 50 60 MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE 70 80 90 100 110 120 SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM 130 140 150 160 170 180 NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS 190 200 210 220 230 240 KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWFSHHMIP GPPGPHTTGI PHPAIVTPQV 250 260 270 280 290 300 KQEHPHTDSD LMHVKPQHEQ RKEQEPKRPH IKKPLNAFML YMKEMRANVV AECTLKESAA 310 320 330 340 350 360 INQILGRRWH ALSREEQAKY YELARKERQL HMQLYPGWSA RDNYGKKKKR KREKLQESAS 370 380 GGKRSSFPTC KAKAATPGPL LEMEAC
	Isoform 7 [UniParc]. Checksum: 38F7331074A62A79	FASTA	303	34,103
	10 20 30 40 50 60 MAEVARQAQT SQEPYHDKAR EHPDDGKHPD GGLYNKGPSY SSYSGYIMMP NMNNDPYMSN 70 80 90 100 110 120 GSLSPPIPRT SNKVPVVQPS HAVHPLTPLI TYSDEHFSPG SHPSHIPSDV NSKQGMSRHP 130 140 150 160 170 180 PAPDIPTFYP LSPGGVGQIT PPLGWFSHHM IPGPPGPHTT GIPHPAIVTP QVKQEHPHTD 190 200 210 220 230 240 SDLMHVKPQH EQRKEQEPKR PHIKKPLNAF MLYMKEMRAN VVAECTLKES AAINQILGRR 250 260 270 280 290 300 WHALSREEQA KYYELARKER QLHMQLYPGW SARDNYGKKK KRKREKLQES ASGTGPRMTA AYI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A thymus-specific member of the HMG protein family regulates the human T cell receptor C alpha enhancer." Waterman M.L., Fischer W.H., Jones K.A. Genes Dev. 5:656-669(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION.
[2]	"The human LEF-1 gene contains a promoter preferentially active in lymphocytes and encodes multiple isoforms derived from alternative splicing." Hovanes K., Li T.W., Waterman M.L. Nucleic Acids Res. 28:1994-2003(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]	"Lef-1 isoforms regulate different target genes and reduce cellular adhesion." Jesse S., Koenig A., Ellenrieder V., Menke A. Int. J. Cancer 126:1109-1120(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
[4]	"New transcript isoform of the human LEF-1 devoid of HMG domain, derived from alternative splicing of exon 8." Kobielak A., Kobielak K., Trzeciak W.H. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7). Tissue: Amygdala and Thymus.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORMS 1 AND 6). Tissue: Skin and Testis.
[9]	"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function." Bruhn L., Munnerlyn A., Grosschedl R. Genes Dev. 11:640-653(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALYREF/THOC4.
[10]	"Two members of the Tcf family implicated in Wnt/b-catenin signaling during embryogenesis in the mouse." Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., Markman M., Lamers W., Destree O., Clevers H. Mol. Cell. Biol. 18:1248-1256(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTNNB1.
[11]	"Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors." Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y. Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TLE1, INHIBITION OF TRANSCRIPTIONAL ACTIVATION BY TLE1.
[12]	"Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are selectively expressed in colon cancer." Hovanes K., Li T.W.H., Munguia J.E., Truong T., Milovanovic T., Lawrence Marsh J., Holcombe R.F., Waterman M.L. Nat. Genet. 28:53-57(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION (ISOFORM 3), EXPRESSION IN COLON CANCER.
[13]	"All Tcf HMG box transcription factors interact with Groucho-related co-repressors." Brantjes H., Roose J., van De Wetering M., Clevers H. Nucleic Acids Res. 29:1410-1419(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTIONAL INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
[14]	"I-mfa domain proteins interact with Axin and affect its regulation of the Wnt and c-Jun N-terminal kinase signaling pathways." Kusano S., Raab-Traub N. Mol. Cell. Biol. 22:6393-6405(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MDFI AND MDFIC.
[15]	"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." Ishitani T., Ninomiya-Tsuji J., Matsumoto K. Mol. Cell. Biol. 23:1379-1389(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLK, PHOSPHORYLATION AT THR-155 AND/OR SER-166 BY NLK, MUTAGENESIS OF THR-155 AND SER-166.
[16]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF288571 mRNA. Translation: AAG01022.1. AF198532 mRNA. Translation: AAF13268.1. AF294627 mRNA. Translation: AAG26886.1. AK294395 mRNA. Translation: BAG57649.1. AK303272 mRNA. Translation: BAH13928.1. AC092539 Genomic DNA. No translation available. AC097067 Genomic DNA. No translation available. AC118062 Genomic DNA. No translation available. AC123576 Genomic DNA. No translation available. CH471057 Genomic DNA. Translation: EAX06223.1. CH471057 Genomic DNA. Translation: EAX06225.1. BC040559 mRNA. Translation: AAH40559.1. BC050632 mRNA. Translation: AAH50632.1.
IPI	IPI00007156. IPI00220455. IPI00220456. IPI00220457. IPI00651680. IPI00909155. IPI00946679.
PIR	A39625.
RefSeq	NP_001124185.1. NM_001130713.2. NP_001124186.1. NM_001130714.2. NP_001159591.1. NM_001166119.1. NP_057353.1. NM_016269.4.
UniGene	Hs.555947.
3D structure databases
ProteinModelPortal	Q9UJU2.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29946N.
IntAct	Q9UJU2. 5 interactions.
STRING	9606.ENSP00000265165.
PTM databases
PhosphoSite	Q9UJU2.
Polymorphism databases
DMDM	8928194.
Proteomic databases
PaxDb	Q9UJU2.
PRIDE	Q9UJU2.
Protocols and materials databases
DNASU	51176.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265165; ENSP00000265165; ENSG00000138795. ENST00000379951; ENSP00000369284; ENSG00000138795. ENST00000438313; ENSP00000406176; ENSG00000138795. ENST00000506680; ENSP00000422334; ENSG00000138795. ENST00000510624; ENSP00000422840; ENSG00000138795.
GeneID	51176.
KEGG	hsa:51176.
UCSC	uc003hyt.2. human. uc003hyu.2. human. uc003hyv.2. human.
Organism-specific databases
CTD	51176.
GeneCards	GC04M108968.
HGNC	HGNC:6551. LEF1.
HPA	CAB019405. HPA002087.
MIM	153245. gene.
neXtProt	NX_Q9UJU2.
PharmGKB	PA30331.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG299161.
HOGENOM	HOG000116032.
HOVERGEN	HBG000419.
InParanoid	Q9UJU2.
KO	K04492.
OMA	GYSGYIM.
OrthoDB	EOG480HWS.
Enzyme and pathway databases
Pathway_Interaction_DB	wnt_canonical_pathway. Canonical Wnt signaling pathway.
Gene expression databases
ArrayExpress	Q9UJU2.
Bgee	Q9UJU2.
CleanEx	HS_LEF1.
Genevestigator	Q9UJU2.
GermOnline	ENSG00000138795. Homo sapiens.
Family and domain databases
Gene3D	1.10.30.10. 1 hit.
InterPro	IPR013558. CTNNB1-bd_N. IPR009071. HMG_box_dom. IPR024940. TCF/LEF. [Graphical view]
PANTHER	PTHR10373. PTHR10373. 1 hit.
Pfam	PF08347. CTNNB1_binding. 1 hit. PF00505. HMG_box. 1 hit. [Graphical view]
SMART	SM00398. HMG. 1 hit. [Graphical view]
SUPFAM	SSF47095. HMG-box. 1 hit.
PROSITE	PS50118. HMG_BOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LEF1. human.
GenomeRNAi	51176.
NextBio	54133.
SOURCE	Search...

Entry information

Entry name

LEF1_HUMAN

Accession

Primary (citable) accession number: Q9UJU2
Secondary accession number(s): B4DG38 , B7Z8E2, E9PDK3, Q3ZCU4, Q9HAZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.