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Q924A0

- TF7L2_MOUSE

UniProt

Q924A0 - TF7L2_MOUSE

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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

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
  4. sequence-specific DNA binding Source: BHF-UCL
  5. sequence-specific DNA binding transcription factor activity Source: RefGenome
  6. 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
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_221970. Ca2+ pathway.
REACT_233471. repression of WNT target genes.
REACT_254498. TCF7L2 mutants don't bind CTBP.
REACT_259776. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

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. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Constitutive activation and subsequent transactivation of target genes may lead to the maintenance of stem-cell characteristics (cycling and longevity) in cells that should normally undergo terminal differentiation and constitute the primary transforming event in colorectal cancer (CRC).

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

Phosphorylated at Thr-178 and/or Thr-189 by NLK. Phosphorylation by NLK at these sites inhibits DNA-binding by TCF7L2/TCF4, thereby preventing transcriptional activation of target genes of the canonical Wnt/beta-catenin signaling pathway (By similarity).By similarity
Polysumoylated. Sumoylation is enhanced by PIAS family members and desumoylation is enhanced by SENP2. Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription activity in the Wnt/beta-catenin signaling pathway without altering interaction with CTNNB1 nor binding to DNA (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ924A0.

PTM databases

PhosphoSiteiQ924A0.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiQ924A0.
CleanExiMM_TCF4.
ExpressionAtlasiQ924A0. baseline and differential.
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.
InParanoidiQ924A0.
KOiK04491.

Family and domain databases

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

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Note: May result from the retention of an intron in the cDNA.

Show »
Length:468
Mass (Da):52,160
Checksum:iA0E7D915D2EC4D0B
GO
Isoform 9 (identifier: Q924A0-9) [UniParc]FASTAAdd to Basket

Also known as: dnTcf7l2 exon1b/c

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

Note: Dominant negative form which cannot bind CTNNB1. Expression is VAX2-dependent.

Show »
Length:299
Mass (Da):33,726
Checksum:iE046B2B2BBB11219
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571D → N in AAD16967. (PubMed:9880534)Curated
Sequence conflicti57 – 571D → N in AAK77488. (PubMed:11845287)Curated
Sequence conflicti57 – 571D → N in AAK77489. (PubMed:11845287)Curated
Sequence conflicti57 – 571D → N in AAK77490. (PubMed:11845287)Curated
Sequence conflicti236 – 2361W → R in AAL58534. 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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223070 mRNA. Translation: CAA11071.1.
AF107298 mRNA. Translation: AAD16967.1.
AF107299 mRNA. Translation: AAD16968.1.
AF363722 Genomic DNA. Translation: AAK77485.1.
AF363722 Genomic DNA. Translation: AAK77486.1.
AF363724 mRNA. Translation: AAK77488.1.
AF363725 mRNA. Translation: AAK77489.1.
AF363726 mRNA. Translation: AAK77490.1.
AY072035 mRNA. Translation: AAL58534.1.
AK048536 mRNA. Translation: BAC33366.1.
AC118695 Genomic DNA. No translation available.
AC137148 Genomic DNA. No translation available.
AC157916 Genomic DNA. No translation available.
CCDSiCCDS50470.1. [Q924A0-2]
CCDS50471.1. [Q924A0-1]
CCDS50474.1. [Q924A0-9]
RefSeqiNP_001136390.1. NM_001142918.1.
NP_001136393.1. NM_001142921.1.
NP_001136396.1. NM_001142924.1. [Q924A0-9]
UniGeneiMm.139815.

Genome annotation databases

EnsembliENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9]
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223070 mRNA. Translation: CAA11071.1 .
AF107298 mRNA. Translation: AAD16967.1 .
AF107299 mRNA. Translation: AAD16968.1 .
AF363722 Genomic DNA. Translation: AAK77485.1 .
AF363722 Genomic DNA. Translation: AAK77486.1 .
AF363724 mRNA. Translation: AAK77488.1 .
AF363725 mRNA. Translation: AAK77489.1 .
AF363726 mRNA. Translation: AAK77490.1 .
AY072035 mRNA. Translation: AAL58534.1 .
AK048536 mRNA. Translation: BAC33366.1 .
AC118695 Genomic DNA. No translation available.
AC137148 Genomic DNA. No translation available.
AC157916 Genomic DNA. No translation available.
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.
InParanoidi Q924A0.
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.
REACT_233471. repression of WNT target genes.
REACT_254498. TCF7L2 mutants don't bind CTBP.
REACT_259776. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

Miscellaneous databases

ChiTaRSi Tcf7l2. mouse.
NextBioi 300716.
PROi Q924A0.
SOURCEi Search...

Gene expression databases

Bgeei Q924A0.
CleanExi MM_TCF4.
ExpressionAtlasi Q924A0. baseline and differential.
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

« Hide 'large scale' publications
  1. "Two members of the Tcf family implicated in Wnt/b-catenin signaling during embryogenesis in the mouse."
    Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., Markman M., Lamers W., Destree O., Clevers H.
    Mol. Cell. Biol. 18:1248-1256(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Embryo.
  2. "A possible role for the high mobility group box transcription factor Tcf-4 in vertebrate gut epithelial cell differentiation."
    Lee Y.J., Swencki B., Shoichet S., Shivdasani R.A.
    J. Biol. Chem. 274:1566-1572(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
    Strain: ICR.
    Tissue: Fetal intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 6 AND 7), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5).
    Strain: C57BL/6J and CD-1.
    Tissue: Pituitary.
  4. "A novel isoform of the HMG transcription factor Tcf4."
    Bayarsaihan D.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
    Strain: C57BL/6J.
    Tissue: Head.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "Depletion of epithelial stem-cell compartments in the small intestine of mice lacking Tcf-4."
    Korinek V., Barker N., Moerer P., van Donselaar E., Huls G., Peters P.J., Clevers H.
    Nat. Genet. 19:379-383(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription."
    Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.
    J. Biol. Chem. 281:1755-1764(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  9. "The kinase TNIK is an essential activator of Wnt target genes."
    Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
    EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNIK AND CTNNB1.
  10. "A novel mechanism for the transcriptional regulation of Wnt signaling in development."
    Vacik T., Stubbs J.L., Lemke G.
    Genes Dev. 25:1783-1795(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTF7L2_MOUSE
AccessioniPrimary (citable) accession number: Q924A0
Secondary accession number(s): O70574
, Q8C834, Q91XP2, Q91XP3, Q91XP4, Q924A1, Q9Z0V3, Q9Z0V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: November 26, 2014
This is version 124 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