Promyelocytic leukemia protein

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Protein PML PDB 1bor.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases PML, MYL, PP8675, RNF71, TRIM19, Promyelocytic leukemia protein, promyelocytic leukemia, Probable transcription factor PML
External IDs MGI: 104662 HomoloGene: 13245 GeneCards: 5371
Genetically Related Diseases
Disease Name References
mammary Paget's disease
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 15: 73.99 – 74.05 Mb Chr 9: 58.22 – 58.25 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Promyelocytic leukemia protein (PML) is a tumor suppressor protein that in humans is encoded by the PML gene.


The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies (Nuclear dots) where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.[5]


Promyelocytic leukemia protein has been shown to interact with:

See also[edit]


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  10. ^ Marcello A, Ferrari A, Pellegrini V, Pegoraro G, Lusic M, Beltram F, Giacca M (May 2003). "Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein". EMBO J. 22 (9): 2156–66. doi:10.1093/emboj/cdg205. PMC 156077free to read. PMID 12727882. 
  11. ^ Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, Kamitani T, Yeh ET, Strauss JF, Maul GG (Oct 1999). "PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1". J. Cell Biol. 147 (2): 221–34. doi:10.1083/jcb.147.2.221. PMC 2174231free to read. PMID 10525530. 
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  18. ^ Topcu Z, Mack DL, Hromas RA, Borden KL (Nov 1999). "The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control". Oncogene. 18 (50): 7091–100. doi:10.1038/sj.onc.1203201. PMID 10597310. 
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  20. ^ Dahle Ø, Bakke O, Gabrielsen OS (Jul 2004). "c-Myb associates with PML in nuclear bodies in hematopoietic cells". Exp. Cell Res. 297 (1): 118–26. doi:10.1016/j.yexcr.2004.03.014. PMID 15194430. 
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  23. ^ Zhu H, Wu L, Maki CG (Dec 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53". J. Biol. Chem. 278 (49): 49286–92. doi:10.1074/jbc.M308302200. PMID 14507915. 
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  25. ^ Wu WS, Xu ZX, Ran R, Meng F, Chang KS (May 2002). "Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions". Oncogene. 21 (24): 3925–33. doi:10.1038/sj.onc.1205491. PMID 12032831. 
  26. ^ Hong SH, Yang Z, Privalsky ML (Nov 2001). "Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia". Mol. Cell. Biol. 21 (21): 7172–82. doi:10.1128/MCB.21.21.7172-7182.2001. PMC 99892free to read. PMID 11585900. 
  27. ^ Fogal V, Gostissa M, Sandy P, Zacchi P, Sternsdorf T, Jensen K, Pandolfi PP, Will H, Schneider C, Del Sal G (Nov 2000). "Regulation of p53 activity in nuclear bodies by a specific PML isoform". EMBO J. 19 (22): 6185–95. doi:10.1093/emboj/19.22.6185. PMC 305840free to read. PMID 11080164. 
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  35. ^ Takahashi H, Hatakeyama S, Saitoh H, Nakayama KI (Feb 2005). "Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein". J. Biol. Chem. 280 (7): 5611–21. doi:10.1074/jbc.M408130200. PMID 15569683. 
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Further reading[edit]

External links[edit]