Q9NQB0 (TF7L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor 7-like 2

Alternative name(s):
HMG box transcription factor 4
T-cell-specific transcription factor 4
Short name=T-cell factor 4
Short name=TCF-4
Short name=hTCF-4

Gene names

Name:	TCF7L2
Synonyms:	TCF4

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	619 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. Ref.6 Ref.10 Ref.11 Ref.18
Subunit structure	Interacts with TGFB1I1 By similarity. Interacts with CTNNB1 (via the armadillo repeat); forms stable transcription complex. Interacts with EP300. Interacts with NLK. Interacts with CCDC85B (probably through the HMG box); prevents interaction with CTNNB1. Interacts with TNIK. Interacts with MAD2L2; prevents TCF7L2/TCF4 binding to promZIPK/DAPK3oters, negatively modulating its transcriptional activity. Interacts with ZIPK/DAPK3. Interacts with XIAP/BIRC4 and TLE3. Interacts with DDIT3/CHOP. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Subcellular location	Nucleus › PML body. Note: Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies. Ref.7 Ref.11
Tissue specificity	Detected in epithelium from small intestine, with the highest expression at the top of the crypts and a gradient of expression from crypt to villus. Detected in colon epithelium and colon cancer, and in epithelium from mammary gland and carcinomas derived therefrom. Ref.7
Developmental stage	Highly expressed in crypt regions and barely detectable in villi in epithelium from fetal small intestine at week 16. At week 22 expression in villi had increased strongly.
Domain	The promoter-specific activation domain interacts with the transcriptional coactivator EP300.
Post-translational modification	In vitro, phosphorylated by TNIK. Ref.13 Phosphorylated at Thr-201 and/or Thr-212 by NLK. Phosphorylation by NLK at these sites inhibits DNA-binding by TCF7L2/TCF4, thereby preventing transcriptional activation of target genes of the canonical Wnt/beta-catenin signaling pathway. Ref.13 Polysumoylated. Sumoylation is enhanced by PIAS family members and desumoylation is enhanced by SENP2. Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription activity in the Wnt/beta-catenin signaling pathway without altering interaction with CTNNB1 nor binding to DNA. Ref.11
Involvement in disease	Constitutive activation and subsequent transactivation of target genes may lead to the maintenance of stem-cell characteristics (cycling and longevity) in cells that should normally undergo terminal differentiation and constitute the primary transforming event in colorectal cancer (CRC). Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.23
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 splicing Polymorphism
Disease	Diabetes mellitus
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel development Inferred from mutant phenotype PubMed 15578569. Source: BHF-UCL bone mineralization Inferred from electronic annotation. Source: Compara brain development Inferred from Biological aspect of Ancestor. Source: RefGenome canonical Wnt receptor signaling pathway involved in positive regulation of epithelial to mesenchymal transition Inferred from mutant phenotype PubMed 17072303. Source: BHF-UCL catenin import into nucleus Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from mutant phenotype Ref.10. Source: BHF-UCL cell proliferation Inferred from mutant phenotype Ref.10. Source: BHF-UCL embryonic digestive tract morphogenesis Inferred from electronic annotation. Source: Compara embryonic genitalia morphogenesis Inferred from electronic annotation. Source: Compara embryonic hindgut morphogenesis Inferred from electronic annotation. Source: Compara face morphogenesis Inferred from electronic annotation. Source: Compara fat cell differentiation Inferred from direct assay PubMed 10937998. Source: BHF-UCL generation of neurons Inferred from Biological aspect of Ancestor. Source: RefGenome glucose homeostasis Inferred from direct assay PubMed 15525634. Source: BHF-UCL maintenance of DNA repeat elements Inferred from mutant phenotype PubMed 18755497. Source: BHF-UCL myoblast cell fate commitment Inferred from direct assay PubMed 10937998. Source: BHF-UCL negative regulation of BMP signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 18071026. Source: BHF-UCL negative regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 16532032. Source: UniProtKB negative regulation of fat cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of fibroblast growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of organ growth Inferred from electronic annotation. Source: Compara negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 12799378. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12799378. Source: BHF-UCL neural tube development Inferred from electronic annotation. Source: Compara odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara oligodendrocyte development Inferred from electronic annotation. Source: Compara pancreas development Traceable author statement PubMed 18216022. Source: BHF-UCL pituitary gland development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of heparan sulfate proteoglycan biosynthetic process Inferred from mutant phenotype PubMed 15853773. Source: BHF-UCL positive regulation of insulin secretion Inferred from direct assay PubMed 18071026. Source: BHF-UCL positive regulation of protein binding Inferred from direct assay PubMed 12799378. Source: BHF-UCL positive regulation of protein export from nucleus Inferred from mutant phenotype PubMed 19386626. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 19386626. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19168596Ref.1. Source: BHF-UCL regulation of hormone metabolic process Inferred from direct assay PubMed 15525634. Source: BHF-UCL regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara regulation of myelination Inferred from electronic annotation. Source: Compara regulation of oligodendrocyte differentiation Inferred from electronic annotation. Source: Compara regulation of skeletal muscle tissue development Inferred from electronic annotation. Source: Compara regulation of smooth muscle cell proliferation Inferred from mutant phenotype PubMed 17122440. Source: BHF-UCL response to glucose stimulus Inferred from sequence or structural similarity PubMed 19168596. Source: BHF-UCL secretory granule localization Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara somatic stem cell maintenance Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell beta-catenin-TCF7L2 complex Inferred from direct assay Ref.1PubMed 9065402. Source: BHF-UCL nuclear chromatin Inferred from direct assay Ref.18. Source: BHF-UCL protein-DNA complex Inferred from direct assay PubMed 14661054. Source: BHF-UCL transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.18. Source: BHF-UCL beta-catenin binding Inferred from direct assay Ref.1. Source: BHF-UCL chromatin binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.6. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	27	EBI-924724,EBI-491549
DAXX	Q9UER7	5	EBI-924724,EBI-77321
JUP	P14923	13	EBI-924724,EBI-702484
RUNX3	Q13761	14	EBI-924724,EBI-925990
XRCC6	P12956	9	EBI-924724,EBI-353208

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NQB0-1)

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.

Isoform 2 (identifier: Q9NQB0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     482-494: RKKKCVRYIQGEG → CKYSKEVSGTVRA
     495-619: Missing.

Isoform 3 (identifier: Q9NQB0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     457-478: DLSAPKKCRARFGLDQQNNWCG → DANTPKKCRALFGLDRQTLWCK

Isoform 4 (identifier: Q9NQB0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     440-456: Missing.
     482-494: RKKKCVRYIQGEG → CKYSKEVSGTVRA
     495-619: Missing.

Isoform 5 (identifier: Q9NQB0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     440-456: Missing.

Isoform 6 (identifier: Q9NQB0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     457-619: DLSAPKKCRA...PLSLVTKSLE → GEKKSAFATYKVKAAASAHPLQMEAY

Isoform 7 (identifier: Q9NQB0-7)

The sequence of this isoform differs from the canonical sequence as follows:
     440-456: Missing.
     457-478: DLSAPKKCRARFGLDQQNNWCG → DANTPKKCRALFGLDRQTLWCK

Isoform 8 (identifier: Q9NQB0-8)

The sequence of this isoform differs from the canonical sequence as follows:
     128-150: Missing.

Isoform 9 (identifier: Q9NQB0-9)

The sequence of this isoform differs from the canonical sequence as follows:
     440-465: EHSECFLNPCLSLPPITDLSAPKKCR → GEKKSAFATYKVKAAASAHPLQMEAY
     466-619: Missing.

Isoform 10 (identifier: Q9NQB0-10)

The sequence of this isoform differs from the canonical sequence as follows:
     128-150: Missing.
     260-263: Missing.
     457-482: DLSAPKKCRARFGLDQQNNWCGPCRR → GEKKSAFATYKVKAAASAHPLQMEAY
     483-619: Missing.

Isoform 11 (identifier: Q9NQB0-11)

The sequence of this isoform differs from the canonical sequence as follows:
     128-150: Missing.
     184-184: V → VSPLPCCTQGHDCQHFYPPSDFTVSTQVFRDMKRSHSLQKVGEPWCIE
     440-465: EHSECFLNPCLSLPPITDLSAPKKCR → GEKKSAFATYKVKAAASAHPLQMEAY
     466-619: Missing.

Isoform 12 (identifier: Q9NQB0-12)

The sequence of this isoform differs from the canonical sequence as follows:
     128-150: Missing.
     481-619: RRKKKCVRYI...PLSLVTKSLE → SL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 619

619

Transcription factor 7-like 2

PRO_0000048623

Regions

DNA binding

350 – 418

69

HMG box

Region

1 – 53

53

CTNNB1-binding By similarity

Region

201 – 395

195

Mediates interaction with MAD2L2

Region

459 – 505

47

Promoter-specific activation domain

Motif

425 – 430

6

Nuclear localization signal Potential

Compositional bias

178 – 317

140

Pro-rich

Amino acid modifications

Modified residue

201

1

Phosphothreonine; by NLK Probable

Modified residue

212

1

Phosphothreonine; by NLK Probable

Cross-link

320

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Alternative sequence

128 – 150

23

Missing in isoform 8, isoform 10, isoform 11 and isoform 12.

VSP_006962

Alternative sequence

184

1

V → VSPLPCCTQGHDCQHFYPPS DFTVSTQVFRDMKRSHSLQK VGEPWCIE in isoform 11.

VSP_045821

Alternative sequence

260 – 263

4

Missing in isoform 10.

VSP_006963

Alternative sequence

440 – 465

26

EHSEC…PKKCR → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 9 and isoform 11.

VSP_006965

Alternative sequence

440 – 456

17

Missing in isoform 4, isoform 5 and isoform 7.

VSP_006964

Alternative sequence

457 – 619

163

DLSAP…TKSLE → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 6.

VSP_006967

Alternative sequence

457 – 482

26

DLSAP…GPCRR → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 10.

VSP_006968

Alternative sequence

457 – 478

22

DLSAP…NNWCG → DANTPKKCRALFGLDRQTLW CK in isoform 3 and isoform 7.

VSP_006966

Alternative sequence

466 – 619

154

Missing in isoform 9 and isoform 11.

VSP_006969

Alternative sequence

481 – 619

139

RRKKK…TKSLE → SL in isoform 12.

VSP_045822

Alternative sequence

482 – 494

13

RKKKC…IQGEG → CKYSKEVSGTVRA in isoform 2 and isoform 4.

VSP_006970

Alternative sequence

483 – 619

137

Missing in isoform 10.

VSP_006971

Alternative sequence

495 – 619

125

Missing in isoform 2 and isoform 4.

VSP_006972

Natural variant

346

1

K → N. Ref.2
Corresponds to variant rs2757884 [ dbSNP | Ensembl ].

VAR_047126

Natural variant

465

1

R → C in a colorectal cancer sample; somatic mutation. Ref.24

VAR_035939

Experimental info

Mutagenesis

10 – 11

2

DD → AA: Reduces CTNNB1 binding.

Mutagenesis

16

1

D → A: Abolishes CTNNB1 binding. Ref.8

Mutagenesis

17

1

E → A: Reduces CTNNB1 binding. Ref.8

Mutagenesis

19

1

I → A: Reduces transcription activation. Ref.22

Mutagenesis

21

1

F → A: Reduces transcription activation. Ref.22

Mutagenesis

23 – 24

2

DE → AA: Reduces CTNNB1 binding. Ref.21

Mutagenesis

24

1

E → A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-26; A-28 and A-29. Ref.21

Mutagenesis

26

1

E → A: Abolishes CTNNB1 binding; when associated with A-24; A-28 and A-29. Ref.21

Mutagenesis

28

1

E → A: Abolishes CTNNB1 binding; when associated with A-24; A-26 and A-29. Ref.21

Mutagenesis

29

1

E → A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-24; A-26 and A-28. Ref.21

Mutagenesis

48

1

L → A: Abolishes CTNNB1 binding. Ref.8

Mutagenesis

201

1

T → V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-212. Ref.13

Mutagenesis

212

1

T → V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-201. Ref.13

Mutagenesis

320

1

K → R: Loss of sumoylation. No effect on localization to nuclear bodies. Ref.11

Mutagenesis

322

1

E → A: Loss of sumoylation. Ref.11

Sequence conflict

118 – 121

4

NGSL → KRSV in CAB97212. Ref.2

Sequence conflict

118 – 121

4

NGSL → KRSV in CAB97213. Ref.2

Sequence conflict

290

1

M → V in CAA72166. Ref.1

Sequence conflict

596

1

S → W in CAA72166. Ref.1

Secondary structure

1

.

.

.

.

.

619

Helix Strand Turn

Details...

Helix

22 – 31

10

Helix

38 – 48

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 25, 2003. Version 2. Checksum: 4DD2D3CC814AE16E	FASTA	619	67,919
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETNE HSECFLNPCL SLPPITDLSA PKKCRARFGL DQQNNWCGPC 490 500 510 520 530 540 RRKKKCVRYI QGEGSCLSPP SSDGSLLDSP PPSPNLLGSP PRDAKSQTEQ TQPLSLSLKP 550 560 570 580 590 600 DPLAHLSMMP PPPALLLAEA THKASALCPN GALDLPPAAL QPAAPSSSIA QPSTSSLHSH 610 SSLAGTQPQP LSLVTKSLE
	Isoform 2 [UniParc]. Checksum: AC0B8049DF6F4498	FASTA	494	55,152
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETNE HSECFLNPCL SLPPITDLSA PKKCRARFGL DQQNNWCGPC 490 RCKYSKEVSG TVRA
	Isoform 3 [UniParc]. Checksum: 6F0250E096854CC0	FASTA	619	67,976
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETNE HSECFLNPCL SLPPITDANT PKKCRALFGL DRQTLWCKPC 490 500 510 520 530 540 RRKKKCVRYI QGEGSCLSPP SSDGSLLDSP PPSPNLLGSP PRDAKSQTEQ TQPLSLSLKP 550 560 570 580 590 600 DPLAHLSMMP PPPALLLAEA THKASALCPN GALDLPPAAL QPAAPSSSIA QPSTSSLHSH 610 SSLAGTQPQP LSLVTKSLE
	Isoform 4 [UniParc]. Checksum: 380199CA672A41A8	FASTA	477	53,270
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 DNYGKKKKRK RDKQPGETND LSAPKKCRAR FGLDQQNNWC GPCRCKYSKE VSGTVRA
	Isoform 5 [UniParc]. Checksum: A52CA392A33AB61C	FASTA	602	66,037
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETND LSAPKKCRAR FGLDQQNNWC GPCRRKKKCV RYIQGEGSCL 490 500 510 520 530 540 SPPSSDGSLL DSPPPSPNLL GSPPRDAKSQ TEQTQPLSLS LKPDPLAHLS MMPPPPALLL 550 560 570 580 590 600 AEATHKASAL CPNGALDLPP AALQPAAPSS SIAQPSTSSL HSHSSLAGTQ PQPLSLVTKS LE
	Isoform 6 [UniParc]. Checksum: B68AD303BF9F3E25	FASTA	482	53,676
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETNE HSECFLNPCL SLPPITGEKK SAFATYKVKA AASAHPLQME AY
	Isoform 7 [UniParc]. Checksum: 87FC20BEB4F51BB2	FASTA	602	66,094
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 470 480 DNYGKKKKRK RDKQPGETND ANTPKKCRAL FGLDRQTLWC KPCRRKKKCV RYIQGEGSCL 490 500 510 520 530 540 SPPSSDGSLL DSPPPSPNLL GSPPRDAKSQ TEQTQPLSLS LKPDPLAHLS MMPPPPALLL 550 560 570 580 590 600 AEATHKASAL CPNGALDLPP AALQPAAPSS SIAQPSTSSL HSHSSLAGTQ PQPLSLVTKS LE
	Isoform 8 [UniParc]. Checksum: A022284FEC164B09	FASTA	596	65,291
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTYLQ MKWPLLDVQA GSLQSRQALK DARSPSPAHI VSNKVPVVQH PHHVHPLTPL 190 200 210 220 230 240 ITYSNEHFTP GNPPPHLPAD VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ 250 260 270 280 290 300 QGQPVYPITT GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES 310 320 330 340 350 360 SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT LKESAAINQI 370 380 390 400 410 420 LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY GKKKKRKRDK QPGETNEHSE 430 440 450 460 470 480 CFLNPCLSLP PITDLSAPKK CRARFGLDQQ NNWCGPCRRK KKCVRYIQGE GSCLSPPSSD 490 500 510 520 530 540 GSLLDSPPPS PNLLGSPPRD AKSQTEQTQP LSLSLKPDPL AHLSMMPPPP ALLLAEATHK 550 560 570 580 590 ASALCPNGAL DLPPAALQPA APSSSIAQPS TSSLHSHSSL AGTQPQPLSL VTKSLE
	Isoform 9 [UniParc]. Checksum: 5E1E47B5DCB132BE	FASTA	465	51,794
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP 190 200 210 220 230 240 AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS 250 260 270 280 290 300 PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 310 320 330 340 350 360 HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY 370 380 390 400 410 420 MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR 430 440 450 460 DNYGKKKKRK RDKQPGETNG EKKSAFATYK VKAAASAHPL QMEAY
	Isoform 10 [UniParc]. Checksum: 2775B43A2E392581	FASTA	455	50,611
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTYLQ MKWPLLDVQA GSLQSRQALK DARSPSPAHI VSNKVPVVQH PHHVHPLTPL 190 200 210 220 230 240 ITYSNEHFTP GNPPPHLPAD VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWQGQP 250 260 270 280 290 300 VYPITTGGFR HPYPTALTVN ASMSRFPPHM VPPHHTLHTT GIPHPAIVTP TVKQESSQSD 310 320 330 340 350 360 VGSLHSSKHQ DSKKEEEKKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES AAINQILGRR 370 380 390 400 410 420 WHALSREEQA KYYELARKER QLHMQLYPGW SARDNYGKKK KRKRDKQPGE TNEHSECFLN 430 440 450 PCLSLPPITG EKKSAFATYK VKAAASAHPL QMEAY
	Isoform 11 [UniParc]. Checksum: 9817D6DB995CBCD2	FASTA	489	54,572
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTYLQ MKWPLLDVQA GSLQSRQALK DARSPSPAHI VSPLPCCTQG HDCQHFYPPS 190 200 210 220 230 240 DFTVSTQVFR DMKRSHSLQK VGEPWCIESN KVPVVQHPHH VHPLTPLITY SNEHFTPGNP 250 260 270 280 290 300 PPHLPADVDP KTGIPRPPHP PDISPYYPLS PGTVGQIPHP LGWLVPQQGQ PVYPITTGGF 310 320 330 340 350 360 RHPYPTALTV NASMSRFPPH MVPPHHTLHT TGIPHPAIVT PTVKQESSQS DVGSLHSSKH 370 380 390 400 410 420 QDSKKEEEKK KPHIKKPLNA FMLYMKEMRA KVVAECTLKE SAAINQILGR RWHALSREEQ 430 440 450 460 470 480 AKYYELARKE RQLHMQLYPG WSARDNYGKK KKRKRDKQPG ETNGEKKSAF ATYKVKAAAS AHPLQMEAY
	Isoform 12 [UniParc]. Checksum: 59C37C6D178BD813	FASTA	459	51,159
	10 20 30 40 50 60 MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS 70 80 90 100 110 120 DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 130 140 150 160 170 180 LSPTARTYLQ MKWPLLDVQA GSLQSRQALK DARSPSPAHI VSNKVPVVQH PHHVHPLTPL 190 200 210 220 230 240 ITYSNEHFTP GNPPPHLPAD VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ 250 260 270 280 290 300 QGQPVYPITT GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES 310 320 330 340 350 360 SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT LKESAAINQI 370 380 390 400 410 420 LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY GKKKKRKRDK QPGETNEHSE 430 440 450 CFLNPCLSLP PITDLSAPKK CRARFGLDQQ NNWCGPCSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma." Korinek V., Barker N., Morin P.J., van Wichen D., de Weger R., Kinzler K.W., Vogelstein B., Clevers H. Science 275:1784-1787(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9), INTERACTION WITH CTNNB1. Tissue: Fetus.
[2]	"The human T cell transcription factor-4 gene: structure, extensive characterization of alternative splicings, and mutational analysis in colorectal cancer cell lines." Duval A., Rolland S., Tubacher E., Bui H., Thomas G., Hamelin R. Cancer Res. 60:3872-3879(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 9), VARIANT ASN-346.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 10). Tissue: Uterus.
[5]	"Human TCF-4 splice form B." Saeki H., Tanaka S., Sugimachi K. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 449-494. Tissue: Gastric carcinoma.
[6]	"Identification of c-MYC as a target of the APC pathway." He T.-C., Sparks A.B., Rago C., Hermeking H., Zawel L., da Costa L.T., Morin P.J., Vogelstein B., Kinzler K.W. Science 281:1509-1512(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Restricted high level expression of Tcf-4 protein in intestinal and mammary gland epithelium." Barker N., Huls G., Korinek V., Clevers H. Am. J. Pathol. 154:29-35(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION.
[8]	"Identification of Tcf4 residues involved in high-affinity beta-catenin binding." Omer C.A., Miller P.J., Diehl R.E., Kral A.M. Biochem. Biophys. Res. Commun. 256:584-590(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTNNB1, MUTAGENESIS OF 10-ASP-ASP-11; ASP-16; GLU-17; 23-ASP-GLU-24 AND LEU-48.
[9]	"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: INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
[10]	"The beta-catenin/TCF-4 complex imposes a crypt progenitor phenotype on colorectal cancer cells." van de Wetering M., Sancho E., Verweij C., de Lau W., Oving I., Hurlstone A., van der Horn K., Batlle E., Coudreuse D., Haramis A.-P., Tjon-Pon-Fong M., Moerer P., van den Born M., Soete G., Pals S., Eilers M., Medema R., Clevers H. Cell 111:241-250(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Sumoylation is involved in beta-catenin-dependent activation of Tcf-4." Yamamoto H., Ihara M., Matsuura Y., Kikuchi A. EMBO J. 22:2047-2059(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-320, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-320 AND GLU-322.
[12]	"Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4." Hecht A., Stemmler M.P. J. Biol. Chem. 278:3776-3785(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EP300.
[13]	"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-201 AND/OR THR-212 BY NLK, MUTAGENESIS OF THR-201 AND THR-212.
[14]	"NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)." Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H. J. Biol. Chem. 281:20749-20760(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLK.
[15]	"The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals." Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J. Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDIT3.
[16]	"Coiled-coil domain containing 85B suppresses the beta-catenin activity in a p53-dependent manner." Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K. Oncogene 27:1520-1526(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCDC85B.
[17]	"The kinase TNIK is an essential activator of Wnt target genes." Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H. EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNIK AND CTNNB1.
[18]	"MAD2B, a novel TCF4-binding protein, modulates TCF4-mediated epithelial-mesenchymal transdifferentiation." Hong C.F., Chou Y.T., Lin Y.S., Wu C.W. J. Biol. Chem. 284:19613-19622(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAD2L2.
[19]	"Zipper-interacting protein kinase (ZIPK) modulates canonical Wnt/beta-catenin signaling through interaction with Nemo-like kinase and T-cell factor 4 (NLK/TCF4)." Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R., Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T. J. Biol. Chem. 286:19170-19177(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLK AND ZIPK/DAPK3.
[20]	"XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling." Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E. Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XIAP/BIRC4 AND TLE3.
[21]	"Tcf4 can specifically recognize beta-catenin using alternative conformations." Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W. Nat. Struct. Biol. 8:1048-1052(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-49 IN COMPLEX WITH THE ARMADILLO REPEAT REGION OF CTNNB1, MUTAGENESIS OF GLU-24; GLU-26; GLU-28 AND GLU-29.
[22]	"Structure of a human Tcf4-beta-catenin complex." Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J. Nat. Struct. Biol. 8:1053-1057(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 8-54 IN COMPLEX WITH THE ARMADILLO REPEAT REGION OF CTNNB1, MUTAGENESIS OF ILE-19 AND PHE-21.
[23]	"Variant of transcription factor 7-like 2 (TCF7L2) gene confers risk of type 2 diabetes." Grant S.F.A., Thorleifsson G., Reynisdottir I., Benediktsson R., Manolescu A., Sainz J., Helgason A., Stefansson H., Emilsson V., Helgadottir A., Styrkarsdottir U., Magnusson K.P., Walters G.B., Palsdottir E., Jonsdottir T., Gudmundsdottir T., Gylfason A., Saemundsdottir J. , Wilensky R.L., Reilly M.P., Rader D.J., Bagger Y., Christiansen C., Gudnason V., Sigurdsson G., Thorsteinsdottir U., Gulcher J.R., Kong A., Stefansson K. Nat. Genet. 38:320-323(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN NIDDM.
[24]	"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] CYS-465.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y11306 mRNA. Translation: CAA72166.2.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270776, AJ270778 Genomic DNA. Translation: CAB97212.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270776, AJ270778 Genomic DNA. Translation: CAB97213.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270777, AJ270778 Genomic DNA. Translation: CAB97214.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270777, AJ270778 Genomic DNA. Translation: CAB97215.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270778 Genomic DNA. Translation: CAB97216.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270778 Genomic DNA. Translation: CAB97217.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270776, AJ270777 Genomic DNA. Translation: CAB97218.1.
AJ270770 , AJ270771, AJ270772, AJ270773, AJ270774, AJ270775, AJ270776, AJ270777 Genomic DNA. Translation: CAB97219.1.
AL135792 Genomic DNA. No translation available.
AL158212 Genomic DNA. No translation available.
AL445486 Genomic DNA. No translation available.
AL451084 Genomic DNA. No translation available.
BC032656 mRNA. Translation: AAH32656.1.
AB034691 mRNA. Translation: BAA86225.1.

IPI

IPI00164708.
IPI00221004.
IPI00221005.
IPI00221006.
IPI00221007.
IPI00221008.
IPI00221009.
IPI00221010.
IPI00221011.
IPI00335587.
IPI00479483.
IPI00983769.

PIR

S22807.

RefSeq

NP_001139746.1. NM_001146274.1.
NP_001139755.1. NM_001146283.1.
NP_001139756.1. NM_001146284.1.

UniGene

Hs.593995.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JDH	X-ray	1.90	B	12-49	[»]
1JPW	X-ray	2.50	D/E/F	8-54	[»]
2GL7	X-ray	2.60	B/E	1-53	[»]

DisProt

DP00175.

ProteinModelPortal

Q9NQB0.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36236N.

IntAct

Q9NQB0. 27 interactions.

MINT

MINT-222146.

PTM databases

PhosphoSite

Q9NQB0.

Polymorphism databases

DMDM

29337146.

Proteomic databases

PaxDb

Q9NQB0.

PRIDE

Q9NQB0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000352065; ENSP00000344823; ENSG00000148737.
ENST00000355717; ENSP00000347949; ENSG00000148737.
ENST00000355995; ENSP00000348274; ENSG00000148737.
ENST00000369397; ENSP00000358404; ENSG00000148737.
ENST00000534894; ENSP00000443626; ENSG00000148737.
ENST00000536810; ENSP00000446238; ENSG00000148737.
ENST00000538897; ENSP00000446172; ENSG00000148737.
ENST00000543371; ENSP00000444972; ENSG00000148737.
ENST00000545257; ENSP00000440547; ENSG00000148737.

GeneID

6934.

KEGG

hsa:6934.

UCSC

uc001lad.4. human.
uc001lae.4. human.
uc001lag.4. human.
uc010qrp.2. human.
uc021pyi.1. human.
uc021pyj.1. human.

Organism-specific databases

CTD

6934.

GeneCards

GC10P114700.

HGNC

HGNC:11641. TCF7L2.

HPA

CAB013535.

MIM

125853. phenotype.
602228. gene.

neXtProt

NX_Q9NQB0.

PharmGKB

PA36394.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG252916.

HOVERGEN

HBG000419.

KO

K04491.

OMA

EPWCLES.

OrthoDB

EOG43XV3J.

Enzyme and pathway databases

SignaLink

Q9NQB0.

Gene expression databases

ArrayExpress

Q9NQB0.

Bgee

Q9NQB0.

CleanEx

HS_TCF4.

Genevestigator

Q9NQB0.

GermOnline

ENSG00000148737. Homo sapiens.

Family and domain databases

Gene3D

1.10.30.10. 1 hit.
4.10.900.10. 1 hit.

InterPro

IPR027397. Catenin_binding_dom.
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

ChEMBL

CHEMBL1914264.

ChiTaRS

TCF7L2. human.

EvolutionaryTrace

Q9NQB0.

GenomeRNAi

6934.

NextBio

27133.

SOURCE

Search...

Entry information

Entry name

TF7L2_HUMAN

Accession

Primary (citable) accession number: Q9NQB0
Secondary accession number(s): F8W742 , F8W7T5, O00185, Q9NQB1, Q9NQB2, Q9NQB3, Q9NQB4, Q9NQB5, Q9NQB6, Q9NQB7, Q9ULC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 25, 2003
Last modified:	May 29, 2013
This is version 134 of the entry and version 2 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.