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Q924A0 (TF7L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Tcf7l2
Synonyms:Tcf4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Ref.7 Ref.10

Subunit structure

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. Ref.8 Ref.9

Subcellular location

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

Tissue specificity

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 stage

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.

Post-translational modification

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.

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.

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).

Sequence similarities

Belongs to the TCF/LEF family.

Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from direct assay Ref.1. Source: MGI

bone mineralization

Inferred from genetic interaction PubMed 19213727. Source: MGI

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 10937998. Source: MGI

catenin import into nucleus

Inferred from direct assay PubMed 9792805. Source: MGI

cellular response to starvation

Inferred from mutant phenotype PubMed 23260145. Source: MGI

embryonic digestive tract morphogenesis

Inferred from genetic interaction PubMed 15057272. Source: MGI

embryonic genitalia morphogenesis

Inferred from genetic interaction PubMed 15057272. Source: MGI

embryonic hindgut morphogenesis

Inferred from genetic interaction PubMed 15057272. Source: MGI

face morphogenesis

Inferred from genetic interaction PubMed 17699607. Source: MGI

glucose metabolic process

Inferred from mutant phenotype PubMed 23260145. Source: MGI

glycogen metabolic process

Inferred from mutant phenotype PubMed 23260145. Source: MGI

insulin metabolic process

Inferred from mutant phenotype PubMed 23260145. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 23260145. Source: MGI

myoblast fate commitment

Inferred from mutant phenotype PubMed 10937998. Source: MGI

negative regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 17919533. Source: MGI

negative regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 10937998. Source: MGI

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 17919533. Source: MGI

negative regulation of organ growth

Inferred from mutant phenotype PubMed 17919533. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23260145. Source: MGI

neural tube development

Inferred from genetic interaction PubMed 15057272. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from genetic interaction PubMed 17699607. Source: MGI

oligodendrocyte development

Inferred from mutant phenotype PubMed 19741146. Source: MGI

pituitary gland development

Inferred from mutant phenotype PubMed 17919533. Source: MGI

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17919533. Source: MGI

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 19251639. Source: MGI

positive regulation of gluconeogenesis

Inferred from mutant phenotype PubMed 23260145. Source: MGI

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 19168596. Source: BHF-UCL

positive regulation of lipid biosynthetic process

Inferred from mutant phenotype PubMed 23260145. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21335239. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19168596. Source: BHF-UCL

positive regulation of triglyceride biosynthetic process

Inferred from mutant phenotype PubMed 23260145. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 23260145. Source: MGI

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 19168596. Source: MGI

regulation of myelination

Inferred from mutant phenotype PubMed 19503085. Source: MGI

regulation of oligodendrocyte differentiation

Inferred from mutant phenotype PubMed 19503085. Source: MGI

regulation of skeletal muscle tissue development

Inferred from mutant phenotype PubMed 21177349. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19168596. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12861022. Source: MGI

response to glucose

Inferred from mutant phenotype PubMed 19168596. Source: BHF-UCL

secretory granule localization

Inferred from mutant phenotype PubMed 19168596. Source: MGI

skin development

Inferred from genetic interaction PubMed 19718027. Source: MGI

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 10027409PubMed 19251639Ref.7. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

catenin-TCF7L2 complex

Inferred from direct assay Ref.1. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 15578569. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 15578569. Source: BHF-UCL

transcription factor complex

Inferred from direct assay PubMed 12861022. Source: MGI

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 23260145. Source: MGI

beta-catenin binding

Inferred from direct assay PubMed 19503085PubMed 9784592. Source: MGI

chromatin binding

Inferred from direct assay PubMed 17727834. Source: MGI

protein binding

Inferred from physical interaction PubMed 15102471PubMed 16724116. Source: IntAct

sequence-specific DNA binding

Inferred from direct assay Ref.1. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription regulatory region DNA binding

Inferred from direct assay PubMed 20044351. Source: MGI

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q924A0-1)

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: Q924A0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: S → SSFLSS
     417-459: EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL → GEKKSAFATYKVKAAASAHPLQMEAY
Isoform 3 (identifier: Q924A0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     237-240: Missing.
Isoform 4 (identifier: Q924A0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     417-433: Missing.
     457-459: CSL → ADANTPKKCR...PLSLVTKSLE
Isoform 5 (identifier: Q924A0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: V → VQSPLPCCTQGHACPHFYTPSDFTVSTQVFRDTKSSHSLQKVGEPWYLE
     270-459: Missing.
Isoform 6 (identifier: Q924A0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     270-459: Missing.
Isoform 7 (identifier: Q924A0-7)

The sequence of this isoform differs from the canonical sequence as follows:
     127-127: T → TLHFQSGSTHYSAYKTIEHQIAIQ
     237-240: Missing.
     270-459: Missing.
Isoform 8 (identifier: Q924A0-8)

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.
Isoform 9 (identifier: Q924A0-9)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Transcription factor 7-like 2
PRO_0000048624

Regions

DNA binding327 – 39569HMG box
Region1 – 5353CTNNB1-binding
Region178 – 372195Mediates interaction with MAD2L2 By similarity
Motif402 – 4087Nuclear localization signal Potential
Compositional bias155 – 294140Pro-rich

Amino acid modifications

Modified residue1781Phosphothreonine; by NLK By similarity
Modified residue1891Phosphothreonine; by NLK By similarity
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 161161MPQLN…PAHIV → M in isoform 9.
VSP_043205
Alternative sequence1271T → TLHFQSGSTHYSAYKTIEHQ IAIQ in isoform 7.
VSP_006973
Alternative sequence1611V → VQSPLPCCTQGHACPHFYTP SDFTVSTQVFRDTKSSHSLQ KVGEPWYLE in isoform 5.
VSP_006974
Alternative sequence237 – 2404Missing in isoform 3 and isoform 7.
VSP_006975
Alternative sequence2681S → SSFLSS in isoform 2 and isoform 8.
VSP_006976
Alternative sequence270 – 459190Missing in isoform 5, isoform 6 and isoform 7.
VSP_006977
Alternative sequence417 – 45943EHSEC…GPCSL → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 2.
VSP_006979
Alternative sequence417 – 45943EHSEC…GPCSL → GERGESGRWRLEDHSYVRLP SGGGRRNPRPGHCGEPILGS LFCLCVF in isoform 8.
VSP_006980
Alternative sequence417 – 43317Missing in isoform 4.
VSP_006978
Alternative sequence457 – 4593CSL → ADANTPKKCRALFGLDRQTL WCKPCRRKKKCVRYIQGEGS CLSPPSSDGSLLDSPPPSPH LLGSPPQDAKSQTEQTQPLS LSLKPDPLAHLSMMPPPPAL LLAEAAHGKASALCPNGALD LPPAALQPSMVPSSSLAQPS TSSLHSHNSLAGTQPQPLSL VTKSLE in isoform 4.
VSP_006981

Experimental info

Sequence conflict571D → N in AAD16967. Ref.2
Sequence conflict571D → N in AAK77488. Ref.3
Sequence conflict571D → N in AAK77489. Ref.3
Sequence conflict571D → N in AAK77490. Ref.3
Sequence conflict2361W → R in AAL58534. Ref.4
Sequence conflict4101K → Q in AAD16968. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: 43BC307DC258E83F

FASTA45951,217
        10         20         30         40         50         60 
MPQLNGGGGD DLGANDELIS FKDEGEQEEK NSENSSAERD LADVKSSLVN ESETNQDSSS 

        70         80         90        100        110        120 
DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS 

       130        140        150        160        170        180 
LSPTARTYLQ MKWPLLDVQA GSLQSRQTLK 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 

« Hide

Isoform 2 [UniParc].

Checksum: EDD7D6F4E01EBF2D
Show »

FASTA44749,746
Isoform 3 [UniParc].

Checksum: CAAC8E5E0E20C558
Show »

FASTA45550,779
Isoform 4 [UniParc].

Checksum: 5E99A68C93632464
Show »

FASTA60566,406
Isoform 5 [UniParc].

Checksum: 37F33F08CAF073EF
Show »

FASTA31734,803
Isoform 6 [UniParc].

Checksum: 2D77D77415FF4833
Show »

FASTA26929,379
Isoform 7 [UniParc].

Checksum: 62778EB672DF0785
Show »

FASTA28831,583
Isoform 8 [UniParc].

Checksum: A0E7D915D2EC4D0B
Show »

FASTA46852,160
Isoform 9 (dnTcf7l2 exon1b/c) [UniParc].

Checksum: E046B2B2BBB11219
Show »

FASTA29933,726

References

« Hide 'large scale' references
[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]"Identification of members of the Wnt signaling pathway in the embryonic pituitary gland."
Douglas K.R., Brinkmeier M.L., Kennell J.A., Eswara P., Harrison T.A., Patrianakos A.I., Sprecher B.S., Potok M.A., Lyons R.H. Jr., MacDougald O.A., Camper S.A.
Mamm. Genome 12:843-851(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS50470.1. [Q924A0-2]
CCDS50471.1. [Q924A0-1]
CCDS50474.1. [Q924A0-9]
RefSeqNP_001136390.1. NM_001142918.1.
NP_001136393.1. NM_001142921.1.
NP_001136396.1. NM_001142924.1. [Q924A0-9]
UniGeneMm.139815.

3D structure databases

ProteinModelPortalQ924A0.
SMRQ924A0. Positions 12-49, 326-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204009. 4 interactions.
DIPDIP-40920N.
IntActQ924A0. 4 interactions.
MINTMINT-421706.

PTM databases

PhosphoSiteQ924A0.

Proteomic databases

PRIDEQ924A0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9]
ENSMUST00000111649; ENSMUSP00000107276; ENSMUSG00000024985.
ENSMUST00000111651; ENSMUSP00000107278; ENSMUSG00000024985.
ENSMUST00000111652; ENSMUSP00000107279; ENSMUSG00000024985.
ENSMUST00000111659; ENSMUSP00000107287; ENSMUSG00000024985.
GeneID21416.
KEGGmmu:21416.
UCSCuc008hya.2. mouse. [Q924A0-6]
uc008hyk.2. mouse. [Q924A0-2]
uc008hyn.2. mouse.

Organism-specific databases

CTD6934.
MGIMGI:1202879. Tcf7l2.

Phylogenomic databases

eggNOGNOG252916.
GeneTreeENSGT00390000009964.
HOGENOMHOG000116032.
HOVERGENHBG000419.
KOK04491.

Gene expression databases

ArrayExpressQ924A0.
BgeeQ924A0.
CleanExMM_TCF4.
GenevestigatorQ924A0.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR024940. TCF/LEF.
IPR028773. TCF7L2.
[Graphical view]
PANTHERPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF32. PTHR10373:SF32. 1 hit.
PfamPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTCF7L2. mouse.
NextBio300716.
PROQ924A0.
SOURCESearch...

Entry information

Entry nameTF7L2_MOUSE
AccessionPrimary (citable) accession number: Q924A0
Secondary accession number(s): O70574 expand/collapse secondary AC list , Q8C834, Q91XP2, Q91XP3, Q91XP4, Q924A1, Q9Z0V3, Q9Z0V4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot