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Q924A0

- TF7L2_MOUSE

UniProt

Q924A0 - TF7L2_MOUSE

Protein

Transcription factor 7-like 2

Gene

Tcf7l2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (25 Mar 2003)
      Previous versions | rss
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    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

    1. beta-catenin binding Source: MGI
    2. chromatin binding Source: MGI
    3. protein binding Source: IntAct
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
    5. sequence-specific DNA binding Source: BHF-UCL
    6. sequence-specific DNA binding transcription factor activity Source: RefGenome
    7. transcription regulatory region DNA binding Source: MGI

    GO - Biological processi

    1. bone mineralization Source: MGI
    2. canonical Wnt signaling pathway Source: MGI
    3. catenin import into nucleus Source: MGI
    4. cellular response to starvation Source: MGI
    5. embryonic digestive tract morphogenesis Source: MGI
    6. embryonic genitalia morphogenesis Source: MGI
    7. embryonic hindgut morphogenesis Source: MGI
    8. face morphogenesis Source: MGI
    9. glucose metabolic process Source: MGI
    10. glycogen metabolic process Source: MGI
    11. insulin metabolic process Source: MGI
    12. multicellular organism growth Source: MGI
    13. myoblast fate commitment Source: MGI
    14. negative regulation of BMP signaling pathway Source: MGI
    15. negative regulation of extrinsic apoptotic signaling pathway Source: InterPro
    16. negative regulation of fat cell differentiation Source: MGI
    17. negative regulation of fibroblast growth factor receptor signaling pathway Source: MGI
    18. negative regulation of organ growth Source: MGI
    19. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    20. neural tube development Source: MGI
    21. odontogenesis of dentin-containing tooth Source: MGI
    22. oligodendrocyte development Source: MGI
    23. pituitary gland development Source: MGI
    24. positive regulation of apoptotic process Source: MGI
    25. positive regulation of epithelial cell proliferation Source: MGI
    26. positive regulation of gluconeogenesis Source: MGI
    27. positive regulation of insulin secretion Source: BHF-UCL
    28. positive regulation of lipid biosynthetic process Source: MGI
    29. positive regulation of transcription, DNA-templated Source: BHF-UCL
    30. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    31. positive regulation of triglyceride biosynthetic process Source: MGI
    32. post-embryonic development Source: MGI
    33. regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
    34. regulation of myelination Source: MGI
    35. regulation of oligodendrocyte differentiation Source: MGI
    36. regulation of skeletal muscle tissue development Source: MGI
    37. regulation of transcription, DNA-templated Source: MGI
    38. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    39. response to glucose Source: BHF-UCL
    40. secretory granule localization Source: MGI
    41. skin development Source: MGI
    42. somatic stem cell maintenance Source: MGI
    43. transcription, DNA-templated Source: UniProtKB-KW
    44. Wnt signaling pathway Source: MGI

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.
    REACT_221970. Ca2+ pathway.

    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: 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

    1. catenin-TCF7L2 complex Source: BHF-UCL
    2. cytosol Source: BHF-UCL
    3. nucleus Source: BHF-UCL
    4. PML body Source: UniProtKB-SubCell
    5. transcription factor complex Source: MGI

    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

    ArrayExpressiQ924A0.
    BgeeiQ924A0.
    CleanExiMM_TCF4.
    GenevestigatoriQ924A0.

    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.

    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.
    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. Align

    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

    MPQLNGGGGD DLGANDELIS FKDEGEQEEK NSENSSAERD LADVKSSLVN    50
    ESETNQDSSS DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY 100
    PGYPFIMIPD LTSPYLPNGS LSPTARTYLQ MKWPLLDVQA GSLQSRQTLK 150
    DARSPSPAHI VSNKVPVVQH PHHVHPLTPL ITYSNEHFTP GNPPPHLPAD 200
    VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ QGQPVYPITT 250
    GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES 300
    SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT 350
    LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY 400
    GKKKKRKRDK QPGETNEHSE CFLNPCLSLP PITDLSAPKK CRARFGLDQQ 450
    NNWCGPCSL 459
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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]
    ENSMUST00000111649; ENSMUSP00000107276; ENSMUSG00000024985.
    ENSMUST00000111651; ENSMUSP00000107278; ENSMUSG00000024985.
    ENSMUST00000111652; ENSMUSP00000107279; ENSMUSG00000024985.
    ENSMUST00000111659; ENSMUSP00000107287; ENSMUSG00000024985.
    GeneIDi21416.
    KEGGimmu:21416.
    UCSCiuc008hya.2. mouse. [Q924A0-6]
    uc008hyk.2. mouse. [Q924A0-2]
    uc008hyn.2. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS50470.1. [Q924A0-2 ]
    CCDS50471.1. [Q924A0-1 ]
    CCDS50474.1. [Q924A0-9 ]
    RefSeqi NP_001136390.1. NM_001142918.1.
    NP_001136393.1. NM_001142921.1.
    NP_001136396.1. NM_001142924.1. [Q924A0-9 ]
    UniGenei Mm.139815.

    3D structure databases

    ProteinModelPortali Q924A0.
    SMRi Q924A0. Positions 12-49, 326-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204009. 4 interactions.
    DIPi DIP-40920N.
    IntActi Q924A0. 4 interactions.
    MINTi MINT-421706.

    PTM databases

    PhosphoSitei Q924A0.

    Proteomic databases

    PRIDEi Q924A0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111646 ; ENSMUSP00000107273 ; ENSMUSG00000024985 . [Q924A0-9 ]
    ENSMUST00000111649 ; ENSMUSP00000107276 ; ENSMUSG00000024985 .
    ENSMUST00000111651 ; ENSMUSP00000107278 ; ENSMUSG00000024985 .
    ENSMUST00000111652 ; ENSMUSP00000107279 ; ENSMUSG00000024985 .
    ENSMUST00000111659 ; ENSMUSP00000107287 ; ENSMUSG00000024985 .
    GeneIDi 21416.
    KEGGi mmu:21416.
    UCSCi uc008hya.2. mouse. [Q924A0-6 ]
    uc008hyk.2. mouse. [Q924A0-2 ]
    uc008hyn.2. mouse.

    Organism-specific databases

    CTDi 6934.
    MGIi MGI:1202879. Tcf7l2.

    Phylogenomic databases

    eggNOGi NOG252916.
    GeneTreei ENSGT00390000009964.
    HOGENOMi HOG000116032.
    HOVERGENi HBG000419.
    KOi K04491.

    Enzyme and pathway databases

    Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.
    REACT_221970. Ca2+ pathway.

    Miscellaneous databases

    ChiTaRSi TCF7L2. mouse.
    NextBioi 300716.
    PROi Q924A0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q924A0.
    Bgeei Q924A0.
    CleanExi MM_TCF4.
    Genevestigatori Q924A0.

    Family and domain databases

    Gene3Di 1.10.30.10. 1 hit.
    4.10.900.10. 1 hit.
    InterProi IPR027397. Catenin_binding_dom.
    IPR013558. CTNNB1-bd_N.
    IPR009071. HMG_box_dom.
    IPR024940. TCF/LEF.
    IPR028773. TCF7L2.
    [Graphical view ]
    PANTHERi PTHR10373. PTHR10373. 1 hit.
    PTHR10373:SF32. PTHR10373:SF32. 1 hit.
    Pfami PF08347. CTNNB1_binding. 1 hit.
    PF00505. HMG_box. 1 hit.
    [Graphical view ]
    SMARTi SM00398. HMG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    PROSITEi PS50118. HMG_BOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 122 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