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Protein

Transcription factor 7-like 2

Gene

Tcf7l2

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

Functioni

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 CCTTTGATC 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 (By similarity). Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine.By similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi327 – 39569HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • blood vessel development Source: MGI
  • bone mineralization Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition Source: MGI
  • catenin import into nucleus Source: MGI
  • cell cycle arrest Source: MGI
  • cell proliferation Source: MGI
  • cellular glucose homeostasis Source: MGI
  • cellular response to starvation Source: MGI
  • embryonic digestive tract morphogenesis Source: MGI
  • embryonic genitalia morphogenesis Source: MGI
  • embryonic hindgut morphogenesis Source: MGI
  • face morphogenesis Source: MGI
  • fat cell differentiation Source: MGI
  • generation of neurons Source: GO_Central
  • glucose homeostasis Source: MGI
  • glucose metabolic process Source: MGI
  • glycogen metabolic process Source: MGI
  • insulin metabolic process Source: MGI
  • maintenance of DNA repeat elements Source: MGI
  • multicellular organism growth Source: MGI
  • myoblast fate commitment Source: MGI
  • negative regulation of BMP signaling pathway Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of fat cell differentiation Source: MGI
  • negative regulation of fibroblast growth factor receptor signaling pathway Source: MGI
  • negative regulation of organ growth Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of type B pancreatic cell apoptotic process Source: MGI
  • neural tube development Source: MGI
  • odontogenesis of dentin-containing tooth Source: MGI
  • oligodendrocyte development Source: MGI
  • pituitary gland development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of gluconeogenesis Source: MGI
  • positive regulation of heparan sulfate proteoglycan biosynthetic process Source: MGI
  • positive regulation of insulin secretion Source: BHF-UCL
  • positive regulation of lipid biosynthetic process Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of protein export from nucleus Source: MGI
  • positive regulation of protein kinase B signaling Source: MGI
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of triglyceride biosynthetic process Source: MGI
  • post-embryonic development Source: MGI
  • regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of hormone metabolic process Source: MGI
  • regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
  • regulation of myelination Source: MGI
  • regulation of oligodendrocyte differentiation Source: MGI
  • regulation of skeletal muscle tissue development Source: MGI
  • regulation of smooth muscle cell proliferation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • response to glucose Source: BHF-UCL
  • secretory granule localization Source: MGI
  • skin development Source: MGI
  • somatic stem cell maintenance Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_325952. formation of the beta-catenin:TCF transactivating complex.
REACT_331940. Ca2+ pathway.
REACT_333804. repression of WNT target genes.
REACT_351655. deactivation of the beta-catenin transactivating complex.

Names & Taxonomyi

Protein namesi
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:
mTCF-4
Gene namesi
Name:Tcf7l2
Synonyms:Tcf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1202879. Tcf7l2.

Subcellular locationi

  • NucleusPML body

  • Note: Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies (By similarity).By similarity

GO - Cellular componenti

  • beta-catenin-TCF7L2 complex Source: MGI
  • catenin-TCF7L2 complex Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytosol Source: BHF-UCL
  • nuclear chromatin Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: BHF-UCL
  • PML body Source: UniProtKB-SubCell
  • protein-DNA complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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).

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Transcription factor 7-like 2PRO_0000048624Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphothreonine; by NLKBy similarity
Modified residuei189 – 1891Phosphothreonine; by NLKBy similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Phosphorylated at Thr-178 and/or Thr-189 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 (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ924A0.

PTM databases

PhosphoSiteiQ924A0.

Expressioni

Tissue specificityi

Detected in adult brain and liver, and at lower levels in intestine, with a clear increase from the distal colon to the duodenum. Detected at low levels in heart, lung, kidney, pituitary and testis.

Developmental stagei

First detected at E10.5. Highly expressed at E13.5-E16.5 in the central nervous system, in particular in the roof of the mesencephalon, at the ditelencephalic junction and in dorsal thalamus. At E13.5, detected at low levels in gastrointestinal epithelia.

Gene expression databases

BgeeiQ924A0.
CleanExiMM_TCF4.
ExpressionAtlasiQ924A0. baseline and differential.
GenevisibleiQ924A0. MM.

Interactioni

Subunit structurei

Interacts with TGFB1I1. Interacts with SPIN1 (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. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Identified in a complex with CTNNB1 and FERMT2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hic1Q9R1Y54EBI-646713,EBI-5236187
Traf1P394286EBI-646713,EBI-520123

Protein-protein interaction databases

BioGridi204009. 4 interactions.
DIPiDIP-40920N.
IntActiQ924A0. 4 interactions.
MINTiMINT-421706.
STRINGi10090.ENSMUSP00000107284.

Structurei

3D structure databases

ProteinModelPortaliQ924A0.
SMRiQ924A0. Positions 12-49, 326-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5353CTNNB1-bindingAdd
BLAST
Regioni178 – 372195Mediates interaction with MAD2L2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi402 – 4087Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 294140Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the TCF/LEF family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG252916.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ924A0.
KOiK04491.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProiIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR024940. TCF/LEF.
IPR028773. TCF7L2.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF32. PTHR10373:SF32. 1 hit.
PfamiPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q924A0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPQLNGGGGD DLGANDELIS FKDEGEQEEK NSENSSAERD LADVKSSLVN
60 70 80 90 100
ESETNQDSSS DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY
110 120 130 140 150
PGYPFIMIPD LTSPYLPNGS LSPTARTYLQ MKWPLLDVQA GSLQSRQTLK
160 170 180 190 200
DARSPSPAHI VSNKVPVVQH PHHVHPLTPL ITYSNEHFTP GNPPPHLPAD
210 220 230 240 250
VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ QGQPVYPITT
260 270 280 290 300
GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES
310 320 330 340 350
SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT
360 370 380 390 400
LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY
410 420 430 440 450
GKKKKRKRDK QPGETNEHSE CFLNPCLSLP PITDLSAPKK CRARFGLDQQ

NNWCGPCSL
Length:459
Mass (Da):51,217
Last modified:March 25, 2003 - v2
Checksum:i43BC307DC258E83F
GO
Isoform 2 (identifier: Q924A0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: S → SSFLSS
     417-459: EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL → GEKKSAFATYKVKAAASAHPLQMEAY

Show »
Length:447
Mass (Da):49,746
Checksum:iEDD7D6F4E01EBF2D
GO
Isoform 3 (identifier: Q924A0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     237-240: Missing.

Show »
Length:455
Mass (Da):50,779
Checksum:iCAAC8E5E0E20C558
GO
Isoform 4 (identifier: Q924A0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-433: Missing.
     457-459: CSL → ADANTPKKCR...PLSLVTKSLE

Show »
Length:605
Mass (Da):66,406
Checksum:i5E99A68C93632464
GO
Isoform 5 (identifier: Q924A0-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: V → VQSPLPCCTQGHACPHFYTPSDFTVSTQVFRDTKSSHSLQKVGEPWYLE
     270-459: Missing.

Show »
Length:317
Mass (Da):34,803
Checksum:i37F33F08CAF073EF
GO
Isoform 6 (identifier: Q924A0-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-459: Missing.

Show »
Length:269
Mass (Da):29,379
Checksum:i2D77D77415FF4833
GO
Isoform 7 (identifier: Q924A0-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-127: T → TLHFQSGSTHYSAYKTIEHQIAIQ
     237-240: Missing.
     270-459: Missing.

Show »
Length:288
Mass (Da):31,583
Checksum:i62778EB672DF0785
GO
Isoform 8 (identifier: Q924A0-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: S → SSFLSS
     417-459: EHSECFLNPC...QNNWCGPCSL → GERGESGRWR...LGSLFCLCVF

Note: May result from the retention of an intron in the cDNA.
Show »
Length:468
Mass (Da):52,160
Checksum:iA0E7D915D2EC4D0B
GO
Isoform 9 (identifier: Q924A0-9) [UniParc]FASTAAdd to basket

Also known as: dnTcf7l2 exon1b/c

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: MPQLNGGGGD...ARSPSPAHIV → M

Note: Dominant negative form which cannot bind CTNNB1. Expression is VAX2-dependent.
Show »
Length:299
Mass (Da):33,726
Checksum:iE046B2B2BBB11219
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571D → N in AAD16967 (PubMed:9880534).Curated
Sequence conflicti57 – 571D → N in AAK77488 (PubMed:11845287).Curated
Sequence conflicti57 – 571D → N in AAK77489 (PubMed:11845287).Curated
Sequence conflicti57 – 571D → N in AAK77490 (PubMed:11845287).Curated
Sequence conflicti236 – 2361W → R in AAL58534 (Ref. 4) Curated
Sequence conflicti410 – 4101K → Q in AAD16968 (PubMed:9880534).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 161161MPQLN…PAHIV → M in isoform 9. 1 PublicationVSP_043205Add
BLAST
Alternative sequencei127 – 1271T → TLHFQSGSTHYSAYKTIEHQ IAIQ in isoform 7. 1 PublicationVSP_006973
Alternative sequencei161 – 1611V → VQSPLPCCTQGHACPHFYTP SDFTVSTQVFRDTKSSHSLQ KVGEPWYLE in isoform 5. CuratedVSP_006974
Alternative sequencei237 – 2404Missing in isoform 3 and isoform 7. 1 PublicationVSP_006975
Alternative sequencei268 – 2681S → SSFLSS in isoform 2 and isoform 8. 2 PublicationsVSP_006976
Alternative sequencei270 – 459190Missing in isoform 5, isoform 6 and isoform 7. 1 PublicationVSP_006977Add
BLAST
Alternative sequencei417 – 45943EHSEC…GPCSL → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 2. 1 PublicationVSP_006979Add
BLAST
Alternative sequencei417 – 45943EHSEC…GPCSL → GERGESGRWRLEDHSYVRLP SGGGRRNPRPGHCGEPILGS LFCLCVF in isoform 8. 1 PublicationVSP_006980Add
BLAST
Alternative sequencei417 – 43317Missing in isoform 4. CuratedVSP_006978Add
BLAST
Alternative sequencei457 – 4593CSL → ADANTPKKCRALFGLDRQTL WCKPCRRKKKCVRYIQGEGS CLSPPSSDGSLLDSPPPSPH LLGSPPQDAKSQTEQTQPLS LSLKPDPLAHLSMMPPPPAL LLAEAAHGKASALCPNGALD LPPAALQPSMVPSSSLAQPS TSSLHSHNSLAGTQPQPLSL VTKSLE in isoform 4. CuratedVSP_006981

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223070 mRNA. Translation: CAA11071.1.
AF107298 mRNA. Translation: AAD16967.1.
AF107299 mRNA. Translation: AAD16968.1.
AF363722 Genomic DNA. Translation: AAK77485.1.
AF363722 Genomic DNA. Translation: AAK77486.1.
AF363724 mRNA. Translation: AAK77488.1.
AF363725 mRNA. Translation: AAK77489.1.
AF363726 mRNA. Translation: AAK77490.1.
AY072035 mRNA. Translation: AAL58534.1.
AK048536 mRNA. Translation: BAC33366.1.
AC118695 Genomic DNA. No translation available.
AC137148 Genomic DNA. No translation available.
AC157916 Genomic DNA. No translation available.
CCDSiCCDS50470.1. [Q924A0-2]
CCDS50471.1. [Q924A0-1]
CCDS50474.1. [Q924A0-9]
RefSeqiNP_001136390.1. NM_001142918.1.
NP_001136393.1. NM_001142921.1.
NP_001136396.1. NM_001142924.1. [Q924A0-9]
UniGeneiMm.139815.

Genome annotation databases

EnsembliENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9]
GeneIDi21416.
KEGGimmu:21416.
UCSCiuc008hya.2. mouse. [Q924A0-6]
uc008hyb.2. mouse. [Q924A0-5]
uc008hyk.2. mouse. [Q924A0-2]
uc008hyn.2. mouse. [Q924A0-9]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223070 mRNA. Translation: CAA11071.1.
AF107298 mRNA. Translation: AAD16967.1.
AF107299 mRNA. Translation: AAD16968.1.
AF363722 Genomic DNA. Translation: AAK77485.1.
AF363722 Genomic DNA. Translation: AAK77486.1.
AF363724 mRNA. Translation: AAK77488.1.
AF363725 mRNA. Translation: AAK77489.1.
AF363726 mRNA. Translation: AAK77490.1.
AY072035 mRNA. Translation: AAL58534.1.
AK048536 mRNA. Translation: BAC33366.1.
AC118695 Genomic DNA. No translation available.
AC137148 Genomic DNA. No translation available.
AC157916 Genomic DNA. No translation available.
CCDSiCCDS50470.1. [Q924A0-2]
CCDS50471.1. [Q924A0-1]
CCDS50474.1. [Q924A0-9]
RefSeqiNP_001136390.1. NM_001142918.1.
NP_001136393.1. NM_001142921.1.
NP_001136396.1. NM_001142924.1. [Q924A0-9]
UniGeneiMm.139815.

3D structure databases

ProteinModelPortaliQ924A0.
SMRiQ924A0. Positions 12-49, 326-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204009. 4 interactions.
DIPiDIP-40920N.
IntActiQ924A0. 4 interactions.
MINTiMINT-421706.
STRINGi10090.ENSMUSP00000107284.

PTM databases

PhosphoSiteiQ924A0.

Proteomic databases

PRIDEiQ924A0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9]
GeneIDi21416.
KEGGimmu:21416.
UCSCiuc008hya.2. mouse. [Q924A0-6]
uc008hyb.2. mouse. [Q924A0-5]
uc008hyk.2. mouse. [Q924A0-2]
uc008hyn.2. mouse. [Q924A0-9]

Organism-specific databases

CTDi6934.
MGIiMGI:1202879. Tcf7l2.

Phylogenomic databases

eggNOGiNOG252916.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ924A0.
KOiK04491.

Enzyme and pathway databases

ReactomeiREACT_325952. formation of the beta-catenin:TCF transactivating complex.
REACT_331940. Ca2+ pathway.
REACT_333804. repression of WNT target genes.
REACT_351655. deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

ChiTaRSiTcf7l2. mouse.
NextBioi300716.
PROiQ924A0.
SOURCEiSearch...

Gene expression databases

BgeeiQ924A0.
CleanExiMM_TCF4.
ExpressionAtlasiQ924A0. baseline and differential.
GenevisibleiQ924A0. MM.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProiIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR024940. TCF/LEF.
IPR028773. TCF7L2.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF32. PTHR10373:SF32. 1 hit.
PfamiPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Embryo.
  2. "A possible role for the high mobility group box transcription factor Tcf-4 in vertebrate gut epithelial cell differentiation."
    Lee Y.J., Swencki B., Shoichet S., Shivdasani R.A.
    J. Biol. Chem. 274:1566-1572(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
    Strain: ICR.
    Tissue: Fetal intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 6 AND 7), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5).
    Strain: C57BL/6J and CD-1.
    Tissue: Pituitary.
  4. "A novel isoform of the HMG transcription factor Tcf4."
    Bayarsaihan D.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
    Strain: C57BL/6J.
    Tissue: Head.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "Depletion of epithelial stem-cell compartments in the small intestine of mice lacking Tcf-4."
    Korinek V., Barker N., Moerer P., van Donselaar E., Huls G., Peters P.J., Clevers H.
    Nat. Genet. 19:379-383(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription."
    Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.
    J. Biol. Chem. 281:1755-1764(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  9. "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.
  10. "A novel mechanism for the transcriptional regulation of Wnt signaling in development."
    Vacik T., Stubbs J.L., Lemke G.
    Genes Dev. 25:1783-1795(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTF7L2_MOUSE
AccessioniPrimary (citable) accession number: Q924A0
Secondary accession number(s): O70574
, Q8C834, Q91XP2, Q91XP3, Q91XP4, Q924A1, Q9Z0V3, Q9Z0V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: July 22, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

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