BACH2

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BTB and CNC homology 1, basic leucine zipper transcription factor 2
3ohu.png
Crystal structure of the human Bach2 BTB/POZ domain dimer. PDB entry 3ohu[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols BACH2 ; BTBD25
External IDs OMIM605394 HomoloGene7240 GeneCards: BACH2 Gene
RNA expression pattern
PBB GE BACH2 221234 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 60468 12014
Ensembl ENSG00000112182 ENSMUSG00000040270
UniProt Q9BYV9 P97303
RefSeq (mRNA) NM_001170794 NM_001109661
RefSeq (protein) NP_001164265 NP_001103131
Location (UCSC) Chr 6:
90.64 – 91.01 Mb
Chr 4:
32.24 – 32.59 Mb
PubMed search [1] [2]

Transcription regulator protein BACH2 is a protein that in humans is encoded by the BACH2 gene.[2][3][4] It contains a BTB/POZ domain at its N-terminus which forms a disulphide-linked dimer [5] and a bZip_Maf domain at the C-terminus.


References[edit]

  1. ^ Rosbrook, G. O.; Stead, M. A.; Carr, S. B.; Wright, S. C. (2011). "The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond". Acta Crystallographica Section D Biological Crystallography 68 (Pt 1): 26–34. doi:10.1107/S0907444911048335. PMID 22194330.  edit
  2. ^ Sasaki S, Ito E, Toki T, Maekawa T, Kanezaki R, Umenai T, Muto A, Nagai H, Kinoshita T, Yamamoto M, Inazawa J, Taketo MM, Nakahata T, Igarashi K, Yokoyama M (Sep 2000). "Cloning and expression of human B cell-specific transcription factor BACH2 mapped to chromosome 6q15". Oncogene 19 (33): 3739–49. doi:10.1038/sj.onc.1203716. PMID 10949928. 
  3. ^ Kamio T, Toki T, Kanezaki R, Sasaki S, Tandai S, Terui K, Ikebe D, Igarashi K, Ito E (Oct 2003). "B-cell-specific transcription factor BACH2 modifies the cytotoxic effects of anticancer drugs". Blood 102 (9): 3317–22. doi:10.1182/blood-2002-12-3656. PMID 12829606. 
  4. ^ "Entrez Gene: BACH2 BTB and CNC homology 1, basic leucine zipper transcription factor 2". 
  5. ^ Rosbrook, G. O.; Stead, M. A.; Carr, S. B.; Wright, S. C. (2011). "The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond". Acta Crystallographica Section D Biological Crystallography 68 (Pt 1): 26–34. doi:10.1107/S0907444911048335. PMID 22194330.  edit

Further reading[edit]

External links[edit]


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