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TCF3

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens

TCF3
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2MH0,2YPA,2YPB,3U5V

Identifiers
AliasesTCF3, E2A, E47, ITF1, TCF-3, VDIR, bHLHb21, AGM8, transcription factor 3, p75
External IDsOMIM:147141;MGI:98510;HomoloGene:2408;GeneCards:TCF3;OMA:TCF3 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for TCF3
Genomic location for TCF3
Band19p13.3Start1,609,290bp[1]
End1,652,605bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for TCF3
Genomic location for TCF3
Band10 C1|10 39.72 cMStart80,245,348bp[2]
End80,269,481bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • ventricular zone

  • right testis

  • left testis

  • pancreatic ductal cell

  • lymph node

  • bone marrow cell

  • gonad

  • appendix

  • stromal cell of endometrium
Top expressed in
  • ventricular zone

  • genital tubercle

  • tail of embryo

  • mandibular prominence

  • maxillary prominence

  • lip

  • epiblast

  • somite

  • abdominal wall

  • yolk sac
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6929

21423

Ensembl

ENSG00000071564

ENSMUSG00000020167

UniProt

P15923

P15806

RefSeq (mRNA)

NM_001136139
NM_003200
NM_001351778
NM_001351779

NM_001164147
NM_001164148
NM_001164149
NM_001164150
NM_001164151

NM_001164152
NM_001164153
NM_011548
NM_001378903
NM_001378904
NM_001378905
NM_001378908
NM_001378910
NM_001378912
NM_001378913
NM_001378914

RefSeq (protein)

NP_001129611
NP_003191
NP_001338707
NP_001338708

NP_001157619
NP_001157620
NP_001157621
NP_001157622
NP_001157623

NP_001157624
NP_001157625
NP_035678
NP_001365832
NP_001365833
NP_001365834
NP_001365837
NP_001365839
NP_001365841
NP_001365842
NP_001365843

Location (UCSC)Chr 19: 1.61 – 1.65 MbChr 10: 80.25 – 80.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor 3 (E2A immunoglobulin enhancer-binding factors E12/E47), also known asTCF3, is aprotein that in humans is encoded by theTCF3gene.[5][6][7] TCF3 has been shown to directly enhance Hes1 (a well-known target ofNotch signaling) expression.[8]

Function

[edit]

This gene encodes a member of the E protein (class I) family ofhelix-loop-helixtranscription factors. The 9aaTAD transactivation domains of E proteins and MLL are very similar and both bind to theKIX domain of general transcriptional mediator CBP.[9][10] E proteins activate transcription by binding to regulatory E-box sequences on target genes as heterodimers or homodimers, and are inhibited by heterodimerization with inhibitor of DNA-binding (class IV) helix-loop-helix proteins. E proteins play a critical role in lymphopoiesis, and the encoded protein is required for theB andT lymphocyte development.[5]

9aaTADs in the E protein familyE2A and MLL binding to the KIX domain of CBP

This gene regulates many developmental patterning processes such as lymphocyte and central nervous system (CNS) development. E proteins are involved in the development of lymphocytes.[11] They initiate transcription by binding to regulatory E-box sequences on target genes.

Clinical significance

[edit]

Deletion of this gene or diminished activity of the encoded protein may play a role inlymphoid malignancies. This gene is also involved in severalchromosomal translocations that are associated with lymphoid malignancies including pre-B-cell acute lymphoblastic leukemia (t(1;19), with PBX1 and t(17;19), with HLF),[12] childhood leukemia (t(19;19), with TFPT) and acute leukemia (t(12;19), with ZNF384).[5]

Interactions

[edit]

TCF3 has been shown tointeract with:

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000071564Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000020167Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^abc"Entrez Gene: TCF3".
  6. ^Henthorn P, McCarrick-Walmsley R, Kadesch T (February 1990)."Sequence of the cDNA encoding ITF-1, a positive-acting transcription factor".Nucleic Acids Research.18 (3): 677.doi:10.1093/nar/18.3.677.PMC 333499.PMID 2308859.
  7. ^Kamps MP, Murre C, Sun XH, Baltimore D (February 1990). "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL".Cell.60 (4):547–555.doi:10.1016/0092-8674(90)90658-2.PMID 1967983.S2CID 39661371.
  8. ^E proteins and Notch signaling cooperate to promote T cell lineage specification and commitment
  9. ^Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities".Genomics.89 (6):756–768.doi:10.1016/j.ygeno.2007.02.003.PMID 17467953.
  10. ^Piskacek M, Vasku A, Hajek R, Knight A (March 2015)."Shared structural features of the 9aaTAD family in complex with CBP".Molecular BioSystems.11 (3):844–851.doi:10.1039/c4mb00672k.PMID 25564305.
  11. ^Quong MW, Romanow WJ, Murre C (2002). "E protein function in lymphocyte development".Annual Review of Immunology.20:301–322.doi:10.1146/annurev.immunol.20.092501.162048.PMID 11861605.
  12. ^Herblot S, Aplan PD, Hoang T (February 2002)."Gradient of E2A activity in B-cell development".Molecular and Cellular Biology.22 (3):886–900.doi:10.1128/MCB.22.3.886-900.2002.PMC 133542.PMID 11784864.
  13. ^abcGoardon N, Lambert JA, Rodriguez P, Nissaire P, Herblot S, Thibault P, et al. (January 2006)."ETO2 coordinates cellular proliferation and differentiation during erythropoiesis".The EMBO Journal.25 (2):357–366.doi:10.1038/sj.emboj.7600934.PMC 1383517.PMID 16407974.
  14. ^abcBradney C, Hjelmeland M, Komatsu Y, Yoshida M, Yao TP, Zhuang Y (January 2003)."Regulation of E2A activities by histone acetyltransferases in B lymphocyte development".The Journal of Biological Chemistry.278 (4):2370–2376.doi:10.1074/jbc.M211464200.PMID 12435739.
  15. ^Maira SM, Wurtz JM, Wasylyk B (November 1996)."Net (ERP/SAP2) one of the Ras-inducible TCFs, has a novel inhibitory domain with resemblance to the helix-loop-helix motif".The EMBO Journal.15 (21):5849–5865.doi:10.1002/j.1460-2075.1996.tb00972.x.PMC 452333.PMID 8918463.
  16. ^Deed RW, Jasiok M, Norton JD (April 1998)."Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells".The Journal of Biological Chemistry.273 (14):8278–8286.doi:10.1074/jbc.273.14.8278.PMID 9525934.
  17. ^abcLanglands K, Yin X, Anand G, Prochownik EV (August 1997)."Differential interactions of Id proteins with basic-helix-loop-helix transcription factors".The Journal of Biological Chemistry.272 (32):19785–19793.doi:10.1074/jbc.272.32.19785.PMID 9242638.
  18. ^Johnson JD, Zhang W, Rudnick A, Rutter WJ, German MS (July 1997)."Transcriptional synergy between LIM-homeodomain proteins and basic helix-loop-helix proteins: the LIM2 domain determines specificity".Molecular and Cellular Biology.17 (7):3488–3496.doi:10.1128/mcb.17.7.3488.PMC 232202.PMID 9199284.
  19. ^Miyamoto A, Cui X, Naumovski L, Cleary ML (May 1996)."Helix-loop-helix proteins LYL1 and E2a form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells".Molecular and Cellular Biology.16 (5):2394–2401.doi:10.1128/mcb.16.5.2394.PMC 231228.PMID 8628307.
  20. ^Neufeld B, Grosse-Wilde A, Hoffmeyer A, Jordan BW, Chen P, Dinev D, et al. (July 2000)."Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity".The Journal of Biological Chemistry.275 (27):20239–20242.doi:10.1074/jbc.C901040199.PMID 10781029.
  21. ^Maleki SJ, Royer CA, Hurlburt BK (June 1997). "MyoD-E12 heterodimers and MyoD-MyoD homodimers are equally stable".Biochemistry.36 (22):6762–6767.doi:10.1021/bi970262m.PMID 9184158.
  22. ^Chakraborty T, Martin JF, Olson EN (September 1992)."Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system".The Journal of Biological Chemistry.267 (25):17498–17501.doi:10.1016/S0021-9258(19)37069-3.PMID 1325437.
  23. ^Hsu HL, Wadman I, Baer R (April 1994)."Formation of in vivo complexes between the TAL1 and E2A polypeptides of leukemic T cells".Proceedings of the National Academy of Sciences of the United States of America.91 (8):3181–3185.Bibcode:1994PNAS...91.3181H.doi:10.1073/pnas.91.8.3181.PMC 43539.PMID 8159721.
  24. ^El Ghouzzi V, Legeai-Mallet L, Aresta S, Benoist C, Munnich A, de Gunzburg J, et al. (March 2000)."Saethre-Chotzen mutations cause TWIST protein degradation or impaired nuclear location".Human Molecular Genetics.9 (5):813–819.doi:10.1093/hmg/9.5.813.PMID 10749989.
  25. ^Huggins GS, Chin MT, Sibinga NE, Lee SL, Haber E, Lee ME (October 1999)."Characterization of the mUBC9-binding sites required for E2A protein degradation".The Journal of Biological Chemistry.274 (40):28690–28696.doi:10.1074/jbc.274.40.28690.PMID 10497239.

Further reading

[edit]
(1) Basic domains
(1.1) Basicleucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3)bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2)Zinc finger DNA-binding domains
(2.1)Nuclear receptor(Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3.1)Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3)Fork head /winged helix
(3.4)Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4)β-Scaffold factors with minor groove contacts
(4.1)Rel homology region
(4.2)STAT
(4.3) p53-like
(4.4)MADS box
(4.6)TATA-binding proteins
(4.7)High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3)Pocket domain
(0.5)AP-2/EREBP-related factors
(0.6) Miscellaneous

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

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