PKNOX1

PKNOX1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X2N
Identifiers
Aliases	PKNOX1 , PREP1, pkonx1c, PBX/knotted 1 homeobox 1
External IDs	OMIM: 602100; MGI: 1201409; HomoloGene: 3363; GeneCards: PKNOX1; OMA:PKNOX1 - orthologs
Gene location (Human) Chr. Chromosome 21 (human) [1] Band 21q22.3 Start 42,974,510 bp [1] End 43,033,931 bp [1]
Gene location (Mouse) Chr. Chromosome 17 (mouse) [2] Band 17 B1|17 16.78 cM Start 31,783,708 bp [2] End 31,826,667 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad right lobe of thyroid gland testicle left testis right testis left lobe of thyroid gland ganglionic eminence ventricular zone sural nerve stromal cell of endometrium Top expressed in Rostral migratory stream granulocyte vas deferens thymus internal carotid artery efferent ductule spermatocyte human fetus blood external carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity DNA-binding transcription activator activity, RNA polymerase II-specific transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding sequence-specific DNA binding DNA binding protein heterodimerization activity DNA-binding transcription factor activity, RNA polymerase II-specific protein binding Cellular component cytoplasm nucleus transcription regulator complex cytosol Biological process erythrocyte differentiation regulation of transcription by RNA polymerase II camera-type eye development T cell differentiation regulation of transcription, DNA-templated angiogenesis positive regulation of transcription by RNA polymerase II transcription by RNA polymerase II hemopoiesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5316 18771 Ensembl ENSG00000160199 ENSMUSG00000006705 UniProt P55347 Q96I87 O70477 RefSeq (mRNA) NM_001286258 NM_004571 NM_001320694 NM_197976 NM_016670 RefSeq (protein) NP_001273187 NP_001307623 NP_004562 NP_001273187.1 NP_004562.2 NP_001307623.1 NP_057879 Location (UCSC) Chr 21: 42.97 – 43.03 Mb Chr 17: 31.78 – 31.83 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

PBX/Knotted 1 Homeobox 1 (PKNOX1) is a protein that in humans is encoded by the PKNOX1 gene. ^{[5] [6]}

An important paralog of this gene is PKNOX2 .

Function

PKNOX1 belongs to the three amino acid loop extension (TALE) class of homeodomain transcription factors that form transcriptionally active complexes involved in development and organogenesis. PKNOX1 is essential for embryogenesis, but it can also act as a tumor suppressor in adulthood. ^[7]

See also: Homeobox

References

1. GRCh38: Ensembl release 89: ENSG00000160199 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006705 – Ensembl, 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. Berthelsen J, Viggiano L, Schulz H, Ferretti E, Consalez GG, Rocchi M, Blasi F (January 1998). "PKNOX1, a gene encoding PREP1, a new regulator of Pbx activity, maps on human chromosome 21q22.3 and murine chromosome 17B/C". Genomics. 47 (2): 323–4. doi:10.1006/geno.1997.5086. PMID   9479508.
6. "Entrez Gene: PKNOX1 PBX/knotted 1 homeobox 1". Archived from the original on 2010-12-05. Retrieved 2017-09-07.
7. Purushothaman D, Blasi F (2018). "The genetics and the molecular functions of the PREP1 homeodomain transcription factor". The International Journal of Developmental Biology. 62 (11–12): 819–825. doi: 10.1387/ijdb.180238fb . PMID   30604851.

Further reading

• Allen TD, Zhu YX, Hawley TS, Hawley RG (October 2000). "TALE homeoproteins as HOX11-interacting partners in T-cell leukemia". Leukemia & Lymphoma. 39 (3–4): 241–56. doi:10.3109/10428190009065824. PMID   11342305. S2CID   27407074.
• 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): 663–74. doi: 10.1101/gad.9.6.663 . PMID   7729685.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, et al. (September 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–28. doi: 10.1101/gr.6.9.807 . PMID   8889549.
• Phelan ML, Featherstone MS (March 1997). "Distinct HOX N-terminal arm residues are responsible for specificity of DNA recognition by HOX monomers and HOX.PBX heterodimers". The Journal of Biological Chemistry. 272 (13): 8635–43. doi: 10.1074/jbc.272.13.8635 . PMID   9079695.
• Chen H, Rossier C, Nakamura Y, Lynn A, Chakravarti A, Antonarakis SE (April 1997). "Cloning of a novel homeobox-containing gene, PKNOX1, and mapping to human chromosome 21q22.3". Genomics. 41 (2): 193–200. doi:10.1006/geno.1997.4632. PMID   9143494.
• LeBrun DP, Matthews BP, Feldman BJ, Cleary ML (October 1997). "The chimeric oncoproteins E2A-PBX1 and E2A-HLF are concentrated within spherical nuclear domains". Oncogene. 15 (17): 2059–67. doi: 10.1038/sj.onc.1201367 . PMID   9366523.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Berthelsen J, Zappavigna V, Mavilio F, Blasi F (March 1998). "Prep1, a novel functional partner of Pbx proteins". The EMBO Journal. 17 (5): 1423–33. doi:10.1093/emboj/17.5.1423. PMC   1170490 . PMID   9482739.
• 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): 1434–45. doi:10.1093/emboj/17.5.1434. PMC   1170491 . PMID   9482740.
• Green NC, Rambaldi I, Teakles J, Featherstone MS (May 1998). "A conserved C-terminal domain in PBX increases DNA binding by the PBX homeodomain and is not a primary site of contact for the YPWM motif of HOXA1". The Journal of Biological Chemistry. 273 (21): 13273–9. doi: 10.1074/jbc.273.21.13273 . PMID   9582372.
• Berthelsen J, Kilstrup-Nielsen C, Blasi F, Mavilio F, Zappavigna V (April 1999). "The subcellular localization of PBX1 and EXD proteins depends on nuclear import and export signals and is modulated by association with PREP1 and HTH". Genes & Development. 13 (8): 946–53. doi:10.1101/gad.13.8.946. PMC   316640 . PMID   10215622.
• 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): 5134–42. doi:10.1128/mcb.19.7.5134. PMC   84356 . PMID   10373562.
• Knoepfler PS, Bergstrom DA, Uetsuki T, Dac-Korytko I, Sun YH, Wright WE, et al. (September 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 Research. 27 (18): 3752–61. doi:10.1093/nar/27.18.3752. PMC   148632 . PMID   10471746.
• Kömüves LG, Shen WF, Kwong A, Stelnicki E, Rozenfeld S, Oda Y, et al. (August 2000). "Changes in HOXB6 homeodomain protein structure and localization during human epidermal development and differentiation". Developmental Dynamics. 218 (4): 636–47. doi: 10.1002/1097-0177(2000)9999:9999<::AID-DVDY1014>3.0.CO;2-I . PMID   10906782.
• Okada Y, Matsuura E, Nagai R, Sato T, Watanabe A, Morita I, Doi T (May 2003). "PREP1, MEIS1 homolog protein, regulates PF4 gene expression". Biochemical and Biophysical Research Communications. 305 (1): 155–9. doi:10.1016/S0006-291X(03)00718-6. PMID   12732210.

External links

• PKNOX1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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