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Core-binding factor, runt domain, alpha subunit 2; translocated to, 3
Protein CBFA2T3 PDB 2h7b.png
PDB rendering based on 2h7b.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CBFA2T3 ; ETO2; MTG16; MTGR2; ZMYND4
External IDs OMIM603870 MGI1338013 HomoloGene74543 GeneCards: CBFA2T3 Gene
RNA expression pattern
PBB GE CBFA2T3 208056 s at tn.png
More reference expression data
Species Human Mouse
Entrez 863 12398
Ensembl ENSG00000129993 ENSMUSG00000006362
UniProt O75081 O54972
RefSeq (mRNA) NM_005187 NM_001109873
RefSeq (protein) NP_005178 NP_001103343
Location (UCSC) Chr 16:
88.94 – 89.04 Mb
Chr 8:
122.63 – 122.7 Mb
PubMed search [1] [2]

Protein CBFA2T3 is a protein that in humans is encoded by the CBFA2T3 gene.[1][2]

The t(16;21)(q24;q22) translocation is a rare but recurrent chromosomal abnormality associated with therapy-related myeloid malignancies. The translocation produces a chimeric gene made up of the 5'-region of the AML1 gene fused to the 3'-region of this gene. In addition, this gene is a putative breast tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene, and a brefeldin A-sensitive association of RII-alpha protein with one of the isoforms has been demonstrated in the Golgi apparatus.[2]


CBFA2T3 has been shown to interact with HDAC1,[3][4] HDAC3,[3][4] TCF3,[5] LDB1,[5] TAL1,[5] RUNX1T1[6][3] and PRKAR2A.[7]


  1. ^ Calabi F, Cilli V (Dec 1998). "CBFA2T1, a gene rearranged in human leukemia, is a member of a multigene family". Genomics 52 (3): 332–41. doi:10.1006/geno.1998.5429. PMID 9790752. 
  2. ^ a b "Entrez Gene: CBFA2T3 core-binding factor, runt domain, alpha subunit 2; translocated to, 3". 
  3. ^ a b c Hoogeveen, André T; Rossetti Stefano; Stoyanova Violeta; Schonkeren Joris; Fenaroli Angelia; Schiaffonati Luisa; van Unen Leontine; Sacchi Nicoletta (Sep 2002). "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies". Oncogene (England) 21 (43): 6703–12. doi:10.1038/sj.onc.1205882. ISSN 0950-9232. PMID 12242670. 
  4. ^ a b Amann, J M; Nip J; Strom D K; Lutterbach B; Harada H; Lenny N; Downing J R; Meyers S; Hiebert S W (Oct 2001). "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain". Mol. Cell. Biol. (United States) 21 (19): 6470–83. doi:10.1128/MCB.21.19.6470-6483.2001. ISSN 0270-7306. PMC 99794. PMID 11533236. 
  5. ^ a b c Goardon, Nicolas; Lambert Julie A; Rodriguez Patrick; Nissaire Philippe; Herblot Sabine; Thibault Pierre; Dumenil Dominique; Strouboulis John; Romeo Paul-Henri; Hoang Trang (Jan 2006). "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". EMBO J. (England) 25 (2): 357–66. doi:10.1038/sj.emboj.7600934. ISSN 0261-4189. PMC 1383517. PMID 16407974. 
  6. ^ Lindberg, Sofia Rondin; Olsson André; Persson Ann-Maj; Olsson Inge (Dec 2003). "Interactions between the leukaemia-associated ETO homologues of nuclear repressor proteins". Eur. J. Haematol. (Denmark) 71 (6): 439–47. doi:10.1046/j.0902-4441.2003.00166.x. ISSN 0902-4441. PMID 14703694. 
  7. ^ Schillace, Robynn V; Andrews Sarah F; Liberty Greg A; Davey Michael P; Carr Daniel W (Feb 2002). "Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes". J. Immunol. (United States) 168 (4): 1590–9. doi:10.4049/jimmunol.168.4.1590. ISSN 0022-1767. PMID 11823486. 

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.