Pre-B-cell leukemia transcription factor 1 is a protein that in humans is encoded by the PBX1 gene.[5] The homologous protein in Drosophila is known as extradenticle, and causes changes in embryonic development.

PBX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPBX1, PBX homeobox 1, CAKUHED
External IDsOMIM: 176310; MGI: 97495; HomoloGene: 20574; GeneCards: PBX1; OMA:PBX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001204961
NM_001204963
NM_002585
NM_001353130
NM_001353131

NM_001291508
NM_001291509
NM_008783
NM_183355

RefSeq (protein)

NP_001191890
NP_001191892
NP_002576
NP_001340059
NP_001340060

NP_001278437
NP_001278438
NP_032809
NP_899198

Location (UCSC)Chr 1: 164.56 – 164.9 MbChr 1: 167.95 – 168.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Mice studies suggest PBX1 is involved in bone generation and skeletal patterning.[6]

Interactions

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PBX1 has been shown to interact with:

Fruit fly homolog

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The Drosophila melangoster gene called extradenticle encodes a homeodomain protein that is 71% similar to the Pbx1 protein, and is considered homologous to PBX1.[14] extradenticle is a homeodomain transcription factor[15] expressed during embryogenesis and is related to morphological changes and development.[14]

Reduced levels of extradenticle cause segmental transformations, without affecting the functionality or location of homeotic genes. Complete removal of extradenticle both maternally and zygotically leads to alterations from failure of non-extradenticle protein expression.[16]

A monoclonal antibody study of the expression of extradenticle protein in embryonic development found that it is uniformly distributed, as well as excluded from cell nuclei, until gastrulation. During the germ band retraction stage of development, extradenticle protein begins to accumulate in the nuclei of cells in a specific pattern. Proximal areas of wing and leg imaginal discs have extradenticle present in the nucleus, while distal areas only have it in the cytoplasm.[17]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185630Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052534Ensembl, 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. ^ "Entrez Gene: PBX1 Pre-B-cell leukemia homeobox 1".
  6. ^ "PBX1 PBX homeobox 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2023-06-11.
  7. ^ Berthelsen J, Zappavigna V, Ferretti E, Mavilio F, Blasi F (March 1998). "The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity". The EMBO Journal. 17 (5): 1434–1445. doi:10.1093/emboj/17.5.1434. PMC 1170491. PMID 9482740.
  8. ^ Piper DE, Batchelor AH, Chang CP, Cleary ML, Wolberger C (February 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): 587–597. doi:10.1016/S0092-8674(00)80662-5. PMID 10052460. S2CID 16122785.
  9. ^ Chang CP, Shen WF, Rozenfeld S, Lawrence HJ, Largman C, Cleary ML (March 1995). "Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins". Genes & Development. 9 (6): 663–674. doi:10.1101/gad.9.6.663. PMID 7729685.
  10. ^ Shen WF, Rozenfeld S, Kwong A, Köm ves LG, Lawrence HJ, Largman C (April 1999). "HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells". Molecular and Cellular Biology. 19 (4): 3051–3061. doi:10.1128/MCB.19.4.3051. PMC 84099. PMID 10082572.
  11. ^ Shanmugam K, Green NC, Rambaldi I, Saragovi HU, Featherstone MS (November 1999). "PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins". Molecular and Cellular Biology. 19 (11): 7577–7588. doi:10.1128/MCB.19.11.7577. PMC 84774. PMID 10523646.
  12. ^ Jacobs Y, Schnabel CA, Cleary ML (July 1999). "Trimeric association of Hox and TALE homeodomain proteins mediates Hoxb2 hindbrain enhancer activity". Molecular and Cellular Biology. 19 (7): 5134–5142. doi:10.1128/MCB.19.7.5134. PMC 84356. PMID 10373562.
  13. ^ Zubair M, Ishihara S, Oka S, Okumura K, Morohashi K (June 2006). "Two-step regulation of Ad4BP/SF-1 gene transcription during fetal adrenal development: initiation by a Hox-Pbx1-Prep1 complex and maintenance via autoregulation by Ad4BP/SF-1". Molecular and Cellular Biology. 26 (11): 4111–4121. doi:10.1128/MCB.00222-06. PMC 1489093. PMID 16705164.
  14. ^ a b Rauskolb C, Peifer M, Wieschaus E (September 1993). "extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1". Cell. 74 (6): 1101–1112. doi:10.1016/0092-8674(93)90731-5. PMID 8104703. S2CID 44721382.
  15. ^ Aspland SE, White RA (February 1997). "Nucleocytoplasmic localisation of extradenticle protein is spatially regulated throughout development in Drosophila". Development. 124 (3): 741–747. doi:10.1242/dev.124.3.741. PMID 9043089.
  16. ^ Peifer M, Wieschaus E (July 1990). "Mutations in the Drosophila gene extradenticle affect the way specific homeo domain proteins regulate segmental identity". Genes & Development. 4 (7): 1209–1223. doi:10.1101/gad.4.7.1209. PMID 1976570.
  17. ^ "Nucleocytoplasmic localisation of extradenticle protein is spatially regulated throughout development in Drosophila". journals.biologists.com. Retrieved 2023-06-06.

Further reading

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