Promyelocytic leukemia protein

From Wikipedia, the free encyclopedia

Promyelocytic leukemia

PDB rendering based on 1bor.

Available structures: 1bor

Identifiers

Symbol(s)

PML; MYL; PP8675; RNF71; TRIM19

External IDs

OMIM: 102578 MGI: 104662 HomoloGene: 13245

Gene ontology
Molecular Function:	• nucleic acid binding • transcription factor activity • transcription coactivator activity • protein binding • zinc ion binding • transcription repressor activity • metal ion binding • protein heterodimerization activity
Cellular Component:	• intracellular • insoluble fraction • nucleus • nucleoplasm • nuclear matrix • PML body
Biological Process:	• DNA repair • transcription • regulation of transcription, DNA-dependent • protein complex assembly • apoptosis • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • cell cycle arrest • cell aging • negative regulation of cell growth • PML body organization and biogenesis • positive regulation of histone deacetylation • DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis

Orthologs

Human

Mouse

n/a

n/a

Refseq

XM_001132060 (mRNA)
XP_001132060 (protein)

NM_008884 (mRNA)
NP_032910 (protein)

Location

n/a

Chr 9: 58.02 - 58.05 Mb

Pubmed search

[1]

[2]

Promyelocytic leukemia, also known as PML, is a human 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 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.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

RING finger domain

[edit] References

^ Entrez Gene: PML promyelocytic leukemia.

[edit] Further reading

Zhong S, Salomoni P, Pandolfi PP (2000). "The transcriptional role of PML and the nuclear body.". Nat. Cell Biol. 2 (5): E85–90. doi:10.1038/35010583. PMID 10806494.
Jensen K, Shiels C, Freemont PS (2001). "PML protein isoforms and the RBCC/TRIM motif.". Oncogene 20 (49): 7223–33. doi:10.1038/sj.onc.1204765. PMID 11704850.
Pearson M, Pelicci PG (2001). "PML interaction with p53 and its role in apoptosis and replicative senescence.". Oncogene 20 (49): 7250–6. doi:10.1038/sj.onc.1204856. PMID 11704853.
Salomoni P, Pandolfi PP (2002). "The role of PML in tumor suppression.". Cell 108 (2): 165–70. PMID 11832207.
Combes R, Balls M, Bansil L, et al. (2002). "An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991).". Alternatives to laboratory animals : ATLA 30 (4): 365–406. PMID 12234245.
Bernardi R, Pandolfi PP (2004). "Role of PML and the PML-nuclear body in the control of programmed cell death.". Oncogene 22 (56): 9048–57. doi:10.1038/sj.onc.1207106. PMID 14663483.