PBX1
Pre-B-cell leukemia transcription factor 1 is a protein that in humans is encoded by the PBX1 gene.[1]
Interactions
PBX1 has been shown to interact with HOXB1,[2][3] MEIS1[4][5][6] and HOXB7.[7]
References
Further reading
- 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. doi:10.1530/eje.0.1460129. 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. PMC 361792. 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. doi:10.1016/0092-8674(90)90657-Z. 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. doi:10.1016/0092-8674(90)90658-2. 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. PMC 358760. 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. doi:10.1073/pnas.90.13.6061. PMC 46867. 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. PMC 231149. 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. PMC 1170490. 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. PMC 1170491. 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. doi:10.1016/S0092-8674(00)80662-5. 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. PMC 84099. 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. PMC 84356. 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. doi:10.1093/nar/27.18.3752. PMC 148632. 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. doi:10.1073/pnas.96.20.11464. PMC 18056. 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. PMC 84774. 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. doi:10.1016/S0167-4781(01)00189-0. 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. PMC 145490. PMID 11285237.
PDB gallery |
---|
| | 1b72: PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX |
| 1b8i: STRUCTURE OF THE HOMEOTIC UBX/EXD/DNA TERNARY COMPLEX |
| 1du6: SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN |
| 1lfu: NMR solution structure of the extended PBX homeodomain bound to DNA |
| 1puf: Crystal structure of HoxA9 and Pbx1 homeodomains bound to DNA |
|
|
|
External links
|
---|
| | | |
---|
| (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 | |
---|
|
| | | | (4) β-Scaffold factors with minor groove contacts |
---|
| |
| | (0) Other transcription factors |
---|
| |
| | see also transcription factor/coregulator deficiencies
Index of genetics |
---|
| Description |
- Gene expression
- DNA
- replication
- cycle
- recombination
- repair
- binding proteins
- Transcription
- factors
- regulators
- nucleic acids
- RNA
- RNA binding proteins
- ribonucleoproteins
- repeated sequence
- modification
- Translation
- ribosome
- modification
- nexins
- Proteins
- domains
- Structure
- primary
- secondary
- tertiary
- quaternary
|
---|
| Disease |
- Replication and repair
- Transcription factor
- Transcription
- Translation
|
---|
|
|