PBX1

From Wikipedia, the free encyclopedia


Pre-B-cell leukemia homeobox 1
PDB rendering based on 1b72.
Available structures: 1b72, 1b8i, 1du6, 1lfu, 1puf
Identifiers
Symbol(s) PBX1; DKFZp686B09108; MGC126627
External IDs OMIM: 176310 MGI97495 HomoloGene20574
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5087 18514
Ensembl ENSG00000185630 n/a
Uniprot P40424 n/a
Refseq NM_002585 (mRNA)
NP_002576 (protein)
NM_008783 (mRNA)
NP_032809 (protein)
Location Chr 1: 162.8 - 163.09 Mb n/a
Pubmed search [1] [2]

Pre-B-cell leukemia homeobox 1, also known as PBX1, is a human gene.[1]


[edit] References

[edit] Further reading

  • Sanyal M, Tung JW (2007). "B-cell development fails in the absence of the Pbx1 proto-oncogene.". Blood. 109 (10): 4191–9. doi:10.1182/blood-2006-10-054213. PMID 17244677. 
  • Hui H, Perfetti R (2002). "Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood.". Eur. J. Endocrinol. 146 (2): 129–41. PMID 11834421. 
  • Hunger SP, Galili N, Carroll AJ, et al. (1991). "The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias.". Blood 77 (4): 687–93. PMID 1671560. 
  • Monica K, Galili N, Nourse J, et al. (1991). "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1.". Mol. Cell. Biol. 11 (12): 6149–57. PMID 1682799. 
  • Nourse J, Mellentin JD, Galili N, et al. (1990). "Chromosomal translocation t(1;19) results in synthesis of a homeobox fusion mRNA that codes for a potential chimeric transcription factor.". Cell 60 (4): 535–45. PMID 1967982. 
  • Kamps MP, Murre C, Sun XH, Baltimore D (1990). "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL.". Cell 60 (4): 547–55. PMID 1967983. 
  • Lu Q, Wright DD, Kamps MP (1994). "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation.". Mol. Cell. Biol. 14 (6): 3938–48. PMID 7910944. 
  • Van Dijk MA, Voorhoeve PM, Murre C (1993). "Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia.". Proc. Natl. Acad. Sci. U.S.A. 90 (13): 6061–5. PMID 8327485. 
  • Lu Q, Kamps MP (1996). "Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1-Hox-DNA complex.". Mol. Cell. Biol. 16 (4): 1632–40. PMID 8657138. 
  • Berthelsen J, Zappavigna V, Mavilio F, Blasi F (1998). "Prep1, a novel functional partner of Pbx proteins.". EMBO J. 17 (5): 1423–33. doi:10.1093/emboj/17.5.1423. PMID 9482739. 
  • Berthelsen J, Zappavigna V, Ferretti E, et al. (1998). "The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity.". EMBO J. 17 (5): 1434–45. doi:10.1093/emboj/17.5.1434. PMID 9482740. 
  • Piper DE, Batchelor AH, Chang CP, et al. (1999). "Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation.". Cell 96 (4): 587–97. PMID 10052460. 
  • Shen WF, Rozenfeld S, Kwong A, et al. (1999). "HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.". Mol. Cell. Biol. 19 (4): 3051–61. PMID 10082572. 
  • Jacobs Y, Schnabel CA, Cleary ML (1999). "Trimeric association of Hox and TALE homeodomain proteins mediates Hoxb2 hindbrain enhancer activity.". Mol. Cell. Biol. 19 (7): 5134–42. PMID 10373562. 
  • Knoepfler PS, Bergstrom DA, Uetsuki T, et al. (1999). "A conserved motif N-terminal to the DNA-binding domains of myogenic bHLH transcription factors mediates cooperative DNA binding with pbx-Meis1/Prep1.". Nucleic Acids Res. 27 (18): 3752–61. PMID 10471746. 
  • McWhirter JR, Neuteboom ST, Wancewicz EV, et al. (1999). "Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT gene in pre-B acute lymphoblastoid leukemia.". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11464–9. PMID 10500199. 
  • Shanmugam K, Green NC, Rambaldi I, et al. (1999). "PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins.". Mol. Cell. Biol. 19 (11): 7577–88. PMID 10523646. 
  • Mikkola I, Bruun JA, Holm T, Johansen T (2001). "Superactivation of Pax6-mediated transactivation from paired domain-binding sites by dna-independent recruitment of different homeodomain proteins.". J. Biol. Chem. 276 (6): 4109–18. doi:10.1074/jbc.M008882200. PMID 11069920. 
  • Thameem F, Wolford JK, Bogardus C, Prochazka M (2001). "Analysis of PBX1 as a candidate gene for type 2 diabetes mellitus in Pima Indians.". Biochim. Biophys. Acta 1518 (1-2): 215–20. PMID 11267683. 
  • Liu Y, MacDonald RJ, Swift GH (2001). "DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer and cooperation with a pancreas-specific basic helix-loop-helix complex.". J. Biol. Chem. 276 (21): 17985–93. doi:10.1074/jbc.M100678200. PMID 11279116. 
  • Mal A, Sturniolo M, Schiltz RL, et al. (2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program.". EMBO J. 20 (7): 1739–53. doi:10.1093/emboj/20.7.1739. PMID 11285237. 
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