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Q9NQB0

- TF7L2_HUMAN

UniProt

Q9NQB0 - TF7L2_HUMAN

Protein

Transcription factor 7-like 2

Gene

TCF7L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (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 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.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi350 – 41869HMG boxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. armadillo repeat domain binding Source: BHF-UCL
    2. beta-catenin binding Source: BHF-UCL
    3. chromatin binding Source: RefGenome
    4. gamma-catenin binding Source: BHF-UCL
    5. nuclear hormone receptor binding Source: BHF-UCL
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    9. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    10. sequence-specific DNA binding Source: UniProtKB
    11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    12. transcription factor binding Source: BHF-UCL
    13. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. blood vessel development Source: BHF-UCL
    2. bone mineralization Source: Ensembl
    3. brain development Source: RefGenome
    4. canonical Wnt signaling pathway Source: BHF-UCL
    5. canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
    6. catenin import into nucleus Source: Ensembl
    7. cell cycle arrest Source: BHF-UCL
    8. cell proliferation Source: BHF-UCL
    9. embryonic digestive tract morphogenesis Source: Ensembl
    10. embryonic genitalia morphogenesis Source: Ensembl
    11. embryonic hindgut morphogenesis Source: Ensembl
    12. face morphogenesis Source: Ensembl
    13. fat cell differentiation Source: BHF-UCL
    14. generation of neurons Source: RefGenome
    15. glucose homeostasis Source: BHF-UCL
    16. maintenance of DNA repeat elements Source: BHF-UCL
    17. myoblast fate commitment Source: BHF-UCL
    18. negative regulation of BMP signaling pathway Source: Ensembl
    19. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    20. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    21. negative regulation of fat cell differentiation Source: Ensembl
    22. negative regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
    23. negative regulation of organ growth Source: Ensembl
    24. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    25. negative regulation of transcription, DNA-templated Source: UniProtKB
    26. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    27. negative regulation of type B pancreatic cell apoptotic process Source: BHF-UCL
    28. neural tube development Source: Ensembl
    29. odontogenesis of dentin-containing tooth Source: Ensembl
    30. oligodendrocyte development Source: Ensembl
    31. pancreas development Source: BHF-UCL
    32. pituitary gland development Source: Ensembl
    33. positive regulation of apoptotic process Source: Ensembl
    34. positive regulation of epithelial cell proliferation Source: Ensembl
    35. positive regulation of heparan sulfate proteoglycan biosynthetic process Source: BHF-UCL
    36. positive regulation of insulin secretion Source: BHF-UCL
    37. positive regulation of protein binding Source: BHF-UCL
    38. positive regulation of protein export from nucleus Source: BHF-UCL
    39. positive regulation of protein kinase B signaling Source: BHF-UCL
    40. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    41. regulation of hormone metabolic process Source: BHF-UCL
    42. regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    43. regulation of myelination Source: Ensembl
    44. regulation of oligodendrocyte differentiation Source: Ensembl
    45. regulation of skeletal muscle tissue development Source: Ensembl
    46. regulation of smooth muscle cell proliferation Source: BHF-UCL
    47. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    48. response to glucose Source: BHF-UCL
    49. secretory granule localization Source: Ensembl
    50. skin development Source: Ensembl
    51. somatic stem cell maintenance Source: Ensembl
    52. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_172761. Ca2+ pathway.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinkiQ9NQB0.

    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:
    hTCF-4
    Gene namesi
    Name:TCF7L2
    Synonyms:TCF4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:11641. TCF7L2.

    Subcellular locationi

    NucleusPML body 3 Publications
    Note: Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies.

    GO - Cellular componenti

    1. beta-catenin-TCF7L2 complex Source: BHF-UCL
    2. cytoplasm Source: HPA
    3. nuclear chromatin Source: BHF-UCL
    4. nucleoplasm Source: BHF-UCL
    5. nucleus Source: UniProtKB
    6. PML body Source: UniProtKB-SubCell
    7. protein-DNA complex Source: BHF-UCL
    8. transcription factor complex Source: RefGenome

    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).
    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.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 112DD → AA: Reduces CTNNB1 binding.
    Mutagenesisi16 – 161D → A: Abolishes CTNNB1 binding. 1 Publication
    Mutagenesisi17 – 171E → A: Reduces CTNNB1 binding. 1 Publication
    Mutagenesisi19 – 191I → A: Reduces transcription activation. 1 Publication
    Mutagenesisi21 – 211F → A: Reduces transcription activation. 1 Publication
    Mutagenesisi23 – 242DE → AA: Reduces CTNNB1 binding.
    Mutagenesisi24 – 241E → A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-26; A-28 and A-29. 1 Publication
    Mutagenesisi26 – 261E → A: Abolishes CTNNB1 binding; when associated with A-24; A-28 and A-29. 1 Publication
    Mutagenesisi28 – 281E → A: Abolishes CTNNB1 binding; when associated with A-24; A-26 and A-29. 1 Publication
    Mutagenesisi29 – 291E → A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-24; A-26 and A-28. 1 Publication
    Mutagenesisi48 – 481L → A: Abolishes CTNNB1 binding. 1 Publication
    Mutagenesisi201 – 2011T → V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-212. 1 Publication
    Mutagenesisi212 – 2121T → V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-201. 1 Publication
    Mutagenesisi320 – 3201K → R: Loss of sumoylation. No effect on localization to nuclear bodies. 1 Publication
    Mutagenesisi322 – 3221E → A: Loss of sumoylation. 1 Publication

    Keywords - Diseasei

    Diabetes mellitus

    Organism-specific databases

    MIMi125853. phenotype.
    PharmGKBiPA36394.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 619619Transcription factor 7-like 2PRO_0000048623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei201 – 2011Phosphothreonine; by NLK1 Publication
    Modified residuei212 – 2121Phosphothreonine; by NLK1 Publication
    Cross-linki320 – 320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    In vitro, phosphorylated by TNIK.1 Publication
    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.1 Publication
    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.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NQB0.
    PaxDbiQ9NQB0.
    PRIDEiQ9NQB0.

    PTM databases

    PhosphoSiteiQ9NQB0.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Developmental stagei

    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.

    Gene expression databases

    ArrayExpressiQ9NQB0.
    BgeeiQ9NQB0.
    CleanExiHS_TCF4.
    GenevestigatoriQ9NQB0.

    Organism-specific databases

    HPAiCAB013535.
    HPA038800.

    Interactioni

    Subunit structurei

    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. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Identified in a complex with CTNNB1 and FERMT2. Interacts with SPIN1.By similarity19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P3522230EBI-924724,EBI-491549
    DAXXQ9UER75EBI-924724,EBI-77321
    HIC1Q145266EBI-924724,EBI-2507362
    JUPP1492313EBI-924724,EBI-702484
    RUNX3Q1376114EBI-924724,EBI-925990
    TNIKQ9UKE53EBI-924724,EBI-1051794
    XRCC6P129569EBI-924724,EBI-353208

    Protein-protein interaction databases

    BioGridi112795. 22 interactions.
    DIPiDIP-36236N.
    IntActiQ9NQB0. 32 interactions.
    MINTiMINT-222146.

    Structurei

    Secondary structure

    1
    619
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3110
    Helixi38 – 4811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JDHX-ray1.90B12-49[»]
    1JPWX-ray2.50D/E/F6-54[»]
    2GL7X-ray2.60B/E1-53[»]
    DisProtiDP00175.
    ProteinModelPortaliQ9NQB0.
    SMRiQ9NQB0. Positions 12-49, 349-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQB0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5353CTNNB1-bindingBy similarityAdd
    BLAST
    Regioni201 – 395195Mediates interaction with MAD2L2Add
    BLAST
    Regioni459 – 50547Promoter-specific activation domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi425 – 4306Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi178 – 317140Pro-richAdd
    BLAST

    Domaini

    The promoter-specific activation domain interacts with the transcriptional coactivator EP300.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG252916.
    HOVERGENiHBG000419.
    KOiK04491.
    OMAiEPWCLES.
    OrthoDBiEOG7QNVMG.
    PhylomeDBiQ9NQB0.
    TreeFamiTF318448.

    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 (17)i

    Sequence statusi: Complete.

    This entry describes 17 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQB0-1) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4M

    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 SSENSSAERD LADVKSSLVN    50
    ESETNQNSSS DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY 100
    PGYPFIMIPD LTSPYLPNGS LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ 150
    YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP AHIVSNKVPV VQHPHHVHPL 200
    TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS PYYPLSPGTV 250
    GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP 300
    HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI 350
    KKPLNAFMLY MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY 400
    ELARKERQLH MQLYPGWSAR DNYGKKKKRK RDKQPGETNE HSECFLNPCL 450
    SLPPITDLSA PKKCRARFGL DQQNNWCGPC RRKKKCVRYI QGEGSCLSPP 500
    SSDGSLLDSP PPSPNLLGSP PRDAKSQTEQ TQPLSLSLKP DPLAHLSMMP 550
    PPPALLLAEA THKASALCPN GALDLPPAAL QPAAPSSSIA QPSTSSLHSH 600
    SSLAGTQPQP LSLVTKSLE 619
    Length:619
    Mass (Da):67,919
    Last modified:March 25, 2003 - v2
    Checksum:i4DD2D3CC814AE16E
    GO
    Isoform 2 (identifier: Q9NQB0-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:494
    Mass (Da):55,152
    Checksum:iAC0B8049DF6F4498
    GO
    Isoform 3 (identifier: Q9NQB0-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:619
    Mass (Da):67,976
    Checksum:i6F0250E096854CC0
    GO
    Isoform 4 (identifier: Q9NQB0-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:477
    Mass (Da):53,270
    Checksum:i380199CA672A41A8
    GO
    Isoform 5 (identifier: Q9NQB0-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:602
    Mass (Da):66,037
    Checksum:iA52CA392A33AB61C
    GO
    Isoform 6 (identifier: Q9NQB0-6) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4I

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

    Show »
    Length:482
    Mass (Da):53,676
    Checksum:iB68AD303BF9F3E25
    GO
    Isoform 7 (identifier: Q9NQB0-7) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:602
    Mass (Da):66,094
    Checksum:i87FC20BEB4F51BB2
    GO
    Isoform 8 (identifier: Q9NQB0-8) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:596
    Mass (Da):65,291
    Checksum:iA022284FEC164B09
    GO
    Isoform 9 (identifier: Q9NQB0-9) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4G

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

    Show »
    Length:465
    Mass (Da):51,794
    Checksum:i5E1E47B5DCB132BE
    GO
    Isoform 10 (identifier: Q9NQB0-10) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:455
    Mass (Da):50,611
    Checksum:i2775B43A2E392581
    GO
    Isoform 11 (identifier: Q9NQB0-11) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:489
    Mass (Da):54,572
    Checksum:i9817D6DB995CBCD2
    GO
    Isoform 12 (identifier: Q9NQB0-12) [UniParc]FASTAAdd to Basket

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

    Note: Low expression in pancreas and colon.

    Show »
    Length:459
    Mass (Da):51,159
    Checksum:i59C37C6D178BD813
    GO
    Isoform 13 (identifier: Q9NQB0-13) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4J

    The sequence of this isoform differs from the canonical sequence as follows:
         128-150: Missing.
         440-456: Missing.
         457-478: DLSAPKKCRARFGLDQQNNWCG → DANTPKKCRALFGLDRQTLWCK

    Note: Common splicing form, lowest expression in skeletal muscle.

    Show »
    Length:579
    Mass (Da):63,466
    Checksum:iB2DEA916F03B0F63
    GO
    Isoform 14 (identifier: Q9NQB0-14) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4B, short

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

    Note: High transcriptional activity. Major isoform in liver.

    Show »
    Length:442
    Mass (Da):49,166
    Checksum:i57D7E679A87FF4C3
    GO
    Isoform 15 (identifier: Q9NQB0-15) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4A

    The sequence of this isoform differs from the canonical sequence as follows:
         128-150: Missing.
         290-290: M → MSSFLS
         440-465: EHSECFLNPCLSLPPITDLSAPKKCR → GEKKSAFATYKVKAAASAHPLQMEAY
         466-619: Missing.

    Show »
    Length:447
    Mass (Da):49,688
    Checksum:i1363601E57F2AA39
    GO
    Isoform 16 (identifier: Q9NQB0-16) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4K

    The sequence of this isoform differs from the canonical sequence as follows:
         128-150: Missing.
         290-290: M → MSSFLS
         440-456: Missing.

    Show »
    Length:584
    Mass (Da):63,930
    Checksum:i7AA2B6E62420108B
    GO
    Isoform 17 (identifier: Q9NQB0-17) [UniParc]FASTAAdd to Basket

    Also known as: TCF-4X2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MPQLNG → MSSFLS
         7-290: Missing.

    Show »
    Length:335
    Mass (Da):36,884
    Checksum:i6085EDAAE3D893A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1214NGSL → KRSV in CAB97212. (PubMed:10919662)Curated
    Sequence conflicti118 – 1214NGSL → KRSV in CAB97213. (PubMed:10919662)Curated
    Sequence conflicti167 – 1671Q → R in ADK35180. (PubMed:21256126)Curated
    Sequence conflicti226 – 2261P → L in ADK35180. (PubMed:21256126)Curated
    Sequence conflicti290 – 2901M → V in CAA72166. (PubMed:9065401)Curated
    Sequence conflicti331 – 3311L → H in ACI28527. (PubMed:19602480)Curated
    Sequence conflicti596 – 5961S → W in CAA72166. (PubMed:9065401)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti346 – 3461K → N.1 Publication
    Corresponds to variant rs2757884 [ dbSNP | Ensembl ].
    VAR_047126
    Natural varianti465 – 4651R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035939

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MPQLNG → MSSFLS in isoform 17. 1 PublicationVSP_053748
    Alternative sequencei7 – 290284Missing in isoform 17. 1 PublicationVSP_053749Add
    BLAST
    Alternative sequencei128 – 15023Missing in isoform 8, isoform 10, isoform 11, isoform 12, isoform 13, isoform 14, isoform 15 and isoform 16. 5 PublicationsVSP_006962Add
    BLAST
    Alternative sequencei184 – 1841V → VSPLPCCTQGHDCQHFYPPS DFTVSTQVFRDMKRSHSLQK VGEPWCIE in isoform 11. CuratedVSP_045821
    Alternative sequencei260 – 2634Missing in isoform 10. 1 PublicationVSP_006963
    Alternative sequencei290 – 2901M → MSSFLS in isoform 15 and isoform 16. 1 PublicationVSP_053750
    Alternative sequencei440 – 46526EHSEC…PKKCR → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 9, isoform 11, isoform 14 and isoform 15. 5 PublicationsVSP_006965Add
    BLAST
    Alternative sequencei440 – 45617Missing in isoform 4, isoform 5, isoform 7, isoform 13 and isoform 16. 2 PublicationsVSP_006964Add
    BLAST
    Alternative sequencei457 – 619163DLSAP…TKSLE → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 6. 1 PublicationVSP_006967Add
    BLAST
    Alternative sequencei457 – 48226DLSAP…GPCRR → GEKKSAFATYKVKAAASAHP LQMEAY in isoform 10. 1 PublicationVSP_006968Add
    BLAST
    Alternative sequencei457 – 47822DLSAP…NNWCG → DANTPKKCRALFGLDRQTLW CK in isoform 3, isoform 7 and isoform 13. 2 PublicationsVSP_006966Add
    BLAST
    Alternative sequencei466 – 619154Missing in isoform 9, isoform 11, isoform 14 and isoform 15. 5 PublicationsVSP_006969Add
    BLAST
    Alternative sequencei481 – 619139RRKKK…TKSLE → SL in isoform 12. 1 PublicationVSP_045822Add
    BLAST
    Alternative sequencei482 – 49413RKKKC…IQGEG → CKYSKEVSGTVRA in isoform 2 and isoform 4. CuratedVSP_006970Add
    BLAST
    Alternative sequencei483 – 619137Missing in isoform 10. 1 PublicationVSP_006971Add
    BLAST
    Alternative sequencei495 – 619125Missing in isoform 2 and isoform 4. CuratedVSP_006972Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    FJ010167 mRNA. Translation: ACI28525.1.
    FJ010169 mRNA. Translation: ACI28527.1.
    FJ010172 mRNA. Translation: ACI28530.1.
    HM352839 mRNA. Translation: ADK35175.1.
    HM352842 mRNA. Translation: ADK35178.1.
    HM352844 mRNA. Translation: ADK35180.1.
    HM352845 mRNA. Translation: ADK35187.1.
    HM352846 mRNA. Translation: ADK35181.1.
    HM352847 mRNA. Translation: ADK35182.1.
    HM352849 mRNA. Translation: ADK35184.1.
    HM352850 mRNA. Translation: ADK35185.1.
    AB440195 mRNA. Translation: BAH24004.1.
    AK299295 mRNA. Translation: BAG61310.1.
    AL135792 Genomic DNA. No translation available.
    AL158212 Genomic DNA. No translation available.
    AL445486 Genomic DNA. No translation available.
    AL451084 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49513.1.
    CH471066 Genomic DNA. Translation: EAW49515.1.
    CH471066 Genomic DNA. Translation: EAW49516.1.
    BC032656 mRNA. Translation: AAH32656.1.
    AB034691 mRNA. Translation: BAA86225.1.
    CCDSiCCDS53577.1. [Q9NQB0-7]
    CCDS53578.1. [Q9NQB0-11]
    CCDS55729.1. [Q9NQB0-12]
    CCDS7576.1. [Q9NQB0-8]
    PIRiS22807.
    RefSeqiNP_001139746.1. NM_001146274.1. [Q9NQB0-7]
    NP_001139755.1. NM_001146283.1. [Q9NQB0-11]
    NP_001139756.1. NM_001146284.1. [Q9NQB0-10]
    NP_001139758.1. NM_001146286.1. [Q9NQB0-14]
    NP_001185455.1. NM_001198526.1. [Q9NQB0-13]
    NP_001185457.1. NM_001198528.1. [Q9NQB0-12]
    NP_001185460.1. NM_001198531.1. [Q9NQB0-9]
    XP_005270141.1. XM_005270084.1. [Q9NQB0-1]
    XP_005270146.1. XM_005270089.1.
    XP_005270153.1. XM_005270096.1. [Q9NQB0-6]
    XP_005270160.1. XM_005270103.1. [Q9NQB0-15]
    UniGeneiHs.593995.

    Genome annotation databases

    EnsembliENST00000352065; ENSP00000344823; ENSG00000148737. [Q9NQB0-12]
    ENST00000355717; ENSP00000347949; ENSG00000148737. [Q9NQB0-11]
    ENST00000355995; ENSP00000348274; ENSG00000148737. [Q9NQB0-1]
    ENST00000369397; ENSP00000358404; ENSG00000148737. [Q9NQB0-8]
    ENST00000534894; ENSP00000443626; ENSG00000148737. [Q9NQB0-2]
    ENST00000536810; ENSP00000446238; ENSG00000148737. [Q9NQB0-5]
    ENST00000538897; ENSP00000446172; ENSG00000148737. [Q9NQB0-6]
    ENST00000542695; ENSP00000443883; ENSG00000148737. [Q9NQB0-17]
    ENST00000543371; ENSP00000444972; ENSG00000148737. [Q9NQB0-7]
    ENST00000545257; ENSP00000440547; ENSG00000148737. [Q9NQB0-3]
    GeneIDi6934.
    KEGGihsa:6934.
    UCSCiuc001lad.4. human. [Q9NQB0-10]
    uc001lae.4. human. [Q9NQB0-7]
    uc010qro.2. human.
    uc021pyi.1. human. [Q9NQB0-1]
    uc021pyj.1. human. [Q9NQB0-6]
    uc021pyl.1. human.

    Polymorphism databases

    DMDMi29337146.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    FJ010167 mRNA. Translation: ACI28525.1 .
    FJ010169 mRNA. Translation: ACI28527.1 .
    FJ010172 mRNA. Translation: ACI28530.1 .
    HM352839 mRNA. Translation: ADK35175.1 .
    HM352842 mRNA. Translation: ADK35178.1 .
    HM352844 mRNA. Translation: ADK35180.1 .
    HM352845 mRNA. Translation: ADK35187.1 .
    HM352846 mRNA. Translation: ADK35181.1 .
    HM352847 mRNA. Translation: ADK35182.1 .
    HM352849 mRNA. Translation: ADK35184.1 .
    HM352850 mRNA. Translation: ADK35185.1 .
    AB440195 mRNA. Translation: BAH24004.1 .
    AK299295 mRNA. Translation: BAG61310.1 .
    AL135792 Genomic DNA. No translation available.
    AL158212 Genomic DNA. No translation available.
    AL445486 Genomic DNA. No translation available.
    AL451084 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49513.1 .
    CH471066 Genomic DNA. Translation: EAW49515.1 .
    CH471066 Genomic DNA. Translation: EAW49516.1 .
    BC032656 mRNA. Translation: AAH32656.1 .
    AB034691 mRNA. Translation: BAA86225.1 .
    CCDSi CCDS53577.1. [Q9NQB0-7 ]
    CCDS53578.1. [Q9NQB0-11 ]
    CCDS55729.1. [Q9NQB0-12 ]
    CCDS7576.1. [Q9NQB0-8 ]
    PIRi S22807.
    RefSeqi NP_001139746.1. NM_001146274.1. [Q9NQB0-7 ]
    NP_001139755.1. NM_001146283.1. [Q9NQB0-11 ]
    NP_001139756.1. NM_001146284.1. [Q9NQB0-10 ]
    NP_001139758.1. NM_001146286.1. [Q9NQB0-14 ]
    NP_001185455.1. NM_001198526.1. [Q9NQB0-13 ]
    NP_001185457.1. NM_001198528.1. [Q9NQB0-12 ]
    NP_001185460.1. NM_001198531.1. [Q9NQB0-9 ]
    XP_005270141.1. XM_005270084.1. [Q9NQB0-1 ]
    XP_005270146.1. XM_005270089.1.
    XP_005270153.1. XM_005270096.1. [Q9NQB0-6 ]
    XP_005270160.1. XM_005270103.1. [Q9NQB0-15 ]
    UniGenei Hs.593995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JDH X-ray 1.90 B 12-49 [» ]
    1JPW X-ray 2.50 D/E/F 6-54 [» ]
    2GL7 X-ray 2.60 B/E 1-53 [» ]
    DisProti DP00175.
    ProteinModelPortali Q9NQB0.
    SMRi Q9NQB0. Positions 12-49, 349-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112795. 22 interactions.
    DIPi DIP-36236N.
    IntActi Q9NQB0. 32 interactions.
    MINTi MINT-222146.

    Chemistry

    ChEMBLi CHEMBL3038511.

    PTM databases

    PhosphoSitei Q9NQB0.

    Polymorphism databases

    DMDMi 29337146.

    Proteomic databases

    MaxQBi Q9NQB0.
    PaxDbi Q9NQB0.
    PRIDEi Q9NQB0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352065 ; ENSP00000344823 ; ENSG00000148737 . [Q9NQB0-12 ]
    ENST00000355717 ; ENSP00000347949 ; ENSG00000148737 . [Q9NQB0-11 ]
    ENST00000355995 ; ENSP00000348274 ; ENSG00000148737 . [Q9NQB0-1 ]
    ENST00000369397 ; ENSP00000358404 ; ENSG00000148737 . [Q9NQB0-8 ]
    ENST00000534894 ; ENSP00000443626 ; ENSG00000148737 . [Q9NQB0-2 ]
    ENST00000536810 ; ENSP00000446238 ; ENSG00000148737 . [Q9NQB0-5 ]
    ENST00000538897 ; ENSP00000446172 ; ENSG00000148737 . [Q9NQB0-6 ]
    ENST00000542695 ; ENSP00000443883 ; ENSG00000148737 . [Q9NQB0-17 ]
    ENST00000543371 ; ENSP00000444972 ; ENSG00000148737 . [Q9NQB0-7 ]
    ENST00000545257 ; ENSP00000440547 ; ENSG00000148737 . [Q9NQB0-3 ]
    GeneIDi 6934.
    KEGGi hsa:6934.
    UCSCi uc001lad.4. human. [Q9NQB0-10 ]
    uc001lae.4. human. [Q9NQB0-7 ]
    uc010qro.2. human.
    uc021pyi.1. human. [Q9NQB0-1 ]
    uc021pyj.1. human. [Q9NQB0-6 ]
    uc021pyl.1. human.

    Organism-specific databases

    CTDi 6934.
    GeneCardsi GC10P114710.
    HGNCi HGNC:11641. TCF7L2.
    HPAi CAB013535.
    HPA038800.
    MIMi 125853. phenotype.
    602228. gene.
    neXtProti NX_Q9NQB0.
    PharmGKBi PA36394.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252916.
    HOVERGENi HBG000419.
    KOi K04491.
    OMAi EPWCLES.
    OrthoDBi EOG7QNVMG.
    PhylomeDBi Q9NQB0.
    TreeFami TF318448.

    Enzyme and pathway databases

    Reactomei REACT_172761. Ca2+ pathway.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinki Q9NQB0.

    Miscellaneous databases

    ChiTaRSi TCF7L2. human.
    EvolutionaryTracei Q9NQB0.
    GeneWikii TCF7L2.
    GenomeRNAii 6934.
    NextBioi 27133.
    PROi Q9NQB0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQB0.
    Bgeei Q9NQB0.
    CleanExi HS_TCF4.
    Genevestigatori Q9NQB0.

    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. "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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12; 13 AND 14), ALTERNATIVE SPLICING.
      Tissue: Brain.
    4. "Identification of T-cell factor-4 isoforms that contribute to the malignant phenotype of hepatocellular carcinoma cells."
      Tsedensodnom O., Koga H., Rosenberg S.A., Nambotin S.B., Carroll J.J., Wands J.R., Kim M.
      Exp. Cell Res. 317:920-931(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 9; 13; 14; 15 AND 17), ALTERNATIVE SPLICING.
    5. "ALEX1, a putative tumor suppressor, is regulated by CREB-dependent Wnt signaling, and is silenced by promoter methylation in human colorectal cancer."
      Iseki H., Takeda A., Andou T., Takahashi N., Ban S., Kurochkin I.V., Okazaki Y., Koyama I.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
      Tissue: Colon.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 14).
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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.
    10. "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.
    11. Cited for: FUNCTION.
    12. "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.
    13. "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.
    14. "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.
    15. Cited for: FUNCTION.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. Cited for: INVOLVEMENT IN NIDDM.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling."
      Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.
      EMBO Rep. 13:750-758(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH FERMT2 AND CTNNB1, SUBCELLULAR LOCATION.
    27. "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells."
      Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T.
      Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML.
    28. "SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling."
      Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C., Zhou J.N., Jia Y.L., Yue W., Pei X.T.
      Mol. Cancer Res. 10:326-335(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPIN1.
    29. "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.
    30. "Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1."
      Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.
      Genes Dev. 28:622-636(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPIN1.
    31. "Sequence variants in SLC16A11 are a common risk factor for type 2 diabetes in Mexico."
      The SIGMA Type 2 Diabetes Consortium
      Nature 506:97-101(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NIDDM.
    32. "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.
    33. 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.
    34. "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
      Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
      Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-53 IN COMPLEX WITH BCL9 AND CTNNB1, INTERACTION WITH CTNNB1.
    35. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-465.

    Entry informationi

    Entry nameiTF7L2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQB0
    Secondary accession number(s): B4DRJ8
    , B9X074, C6ZRJ8, C6ZRK0, E2GH14, E2GH19, E2GH20, E2GH24, E2GH25, E9PFH9, F8W742, F8W7T5, O00185, Q9NQB1, Q9NQB2, Q9NQB3, Q9NQB4, Q9NQB5, Q9NQB6, Q9NQB7, Q9ULC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3