Promyelocytic leukemia protein information

PML
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BOR, 2MVW, 2MWX, 4WJN, 4WJO
Identifiers
Aliases	PML, MYL, PP8675, RNF71, TRIM19, Promyelocytic leukemia protein, promyelocytic leukemia, Probable transcription factor PML nuclear body scaffold
External IDs	OMIM: 102578; MGI: 104662; HomoloGene: 13245; GeneCards: PML; OMA:PML - orthologs
Gene location (Human)
Chr.	Chromosome 15 (human)
End	74,047,827 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	58,157,069 bp
RNA expression pattern
	Top expressed in
	body of uterus; ; upper lobe of left lung; ; canal of the cervix; ; ectocervix; ; right lung; ; subcutaneous adipose tissue; ; right uterine tube; ; apex of heart; ; right lobe of thyroid gland; ; left lobe of thyroid gland;
	Top expressed in
	spleen; ; lymph node; ; parotid gland; ; thymus; ; bone marrow; ; blood; ; submandibular gland; ; jejunum; ; duodenum; ; subcutaneous adipose tissue;
	More reference expression data
	n/a
Gene ontology
Molecular function	SUMO binding; cobalt ion binding; metal ion binding; protein homodimerization activity; zinc ion binding; protein binding; SMAD binding; DNA binding; transcription coactivator activity; protein heterodimerization activity; ubiquitin protein ligase binding; SUMO transferase activity;
Cellular component	cytoplasm; cytosol; endosome; nuclear membrane; membrane; nucleus; nuclear matrix; nucleolus; endoplasmic reticulum; early endosome membrane; intracellular anatomical structure; nucleoplasm; PML body; endoplasmic reticulum membrane; extrinsic component of endoplasmic reticulum membrane; heterochromatin;
Biological process	regulation of protein phosphorylation; positive regulation of histone deacetylation; intrinsic apoptotic signaling pathway in response to oxidative stress; myeloid cell differentiation; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; negative regulation of telomere maintenance via telomerase; rhythmic process; interferon-gamma-mediated signaling pathway; negative regulation of telomerase activity; positive regulation of telomere maintenance; cellular senescence; regulation of cell adhesion; defense response to virus; intrinsic apoptotic signaling pathway in response to DNA damage; positive regulation of extrinsic apoptotic signaling pathway; activation of cysteine-type endopeptidase activity involved in apoptotic process; transforming growth factor beta receptor signaling pathway; proteasome-mediated ubiquitin-dependent protein catabolic process; negative regulation of cell population proliferation; positive regulation of defense response to virus by host; apoptotic process; response to cytokine; cell fate commitment; negative regulation of translation in response to oxidative stress; regulation of transcription, DNA-templated; common-partner SMAD protein phosphorylation; branching involved in mammary gland duct morphogenesis; extrinsic apoptotic signaling pathway; positive regulation of fibroblast proliferation; positive regulation of apoptotic signaling pathway; endoplasmic reticulum calcium ion homeostasis; transcription, DNA-templated; PML body organization; negative regulation of cell growth; intrinsic apoptotic signaling pathway by p53 class mediator; innate immune response; viral process; response to gamma radiation; response to UV; regulation of calcium ion transport into cytosol; positive regulation of protein localization to chromosome, telomeric region; fibroblast migration; protein targeting; immune system process; protein stabilization; positive regulation of apoptotic process involved in mammary gland involution; circadian regulation of gene expression; regulation of MHC class I biosynthetic process; regulation of circadian rhythm; negative regulation of transcription, DNA-templated; maintenance of protein location in nucleus; cellular response to interleukin-4; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; response to hypoxia; regulation of double-strand break repair; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; retinoic acid receptor signaling pathway; negative regulation of angiogenesis; negative regulation of ubiquitin-dependent protein catabolic process; entrainment of circadian clock by photoperiod; negative regulation of mitotic cell cycle; positive regulation of MHC class I biosynthetic process; positive regulation of transcription by RNA polymerase II; regulation of signal transduction by p53 class mediator; cellular response to leukemia inhibitory factor; protein import into nucleus; protein-containing complex assembly; positive regulation of nucleic acid-templated transcription; protein sumoylation;
	Sources:Amigo / QuickGO
Orthologs
	5371
	18854
	ENSG00000140464
	ENSMUSG00000036986
	P29590
	Q60953
NM_033250; NM_002675; NM_033238; NM_033239; NM_033240;
	NM_033244; NM_033246; NM_033247; NM_033249
	NM_008884; NM_178087; NM_001311088
NP_002666; NP_150241; NP_150242; NP_150243; NP_150247;
	NP_150249; NP_150250; NP_150252; NP_150253
	NP_001298017; NP_032910; NP_835188
	Wikidata
View/Edit Human	View/Edit Mouse

Promyelocytic leukemia protein (PML) (also known as MYL, RNF71, PP8675 or TRIM19^[5]) is the protein product of the PML gene. PML protein is a tumor suppressor protein required for the assembly of a number of nuclear structures, called PML-nuclear bodies, which form amongst the chromatin^[5] of the cell nucleus. These nuclear bodies are present in mammalian nuclei, at about 1 to 30 per cell nucleus.^[5] PML-NBs are known to have a number of regulatory cellular functions, including involvement in programmed cell death, genome stability, antiviral effects and controlling cell division.^[5]^[6] PML mutation or loss, and the subsequent dysregulation of these processes, has been implicated in a variety of cancers.^[5]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000140464 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036986 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c ^d ^e Bernardi R, Pandolfi PP (December 2007). "Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies". Nature Reviews. Molecular Cell Biology. 8 (12): 1006–16. doi:10.1038/nrm2277. PMID 17928811. S2CID 8623635.
^ Sahin U, Lallemand-Breitenbach V, de Thé H (November 2014). "PML nuclear bodies: regulation, function and therapeutic perspectives". The Journal of Pathology. 234 (3): 289–91. doi:10.1002/path.4426. PMID 25138686. S2CID 34066050.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000140464 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000036986 – 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.

[Bernardi_2007-5] Bernardi R, Pandolfi PP (December 2007). "Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies". Nature Reviews. Molecular Cell Biology. 8 (12): 1006–16. doi:10.1038/nrm2277. PMID 17928811. S2CID 8623635.

[Sahin_2014-6] Sahin U, Lallemand-Breitenbach V, de Thé H (November 2014). "PML nuclear bodies: regulation, function and therapeutic perspectives". The Journal of Pathology. 234 (3): 289–91. doi:10.1002/path.4426. PMID 25138686. S2CID 34066050.

Promyelocytic leukemia protein information

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