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PML (promyelocytic leukemia)

Written2014-05Andrea Rabellino, Pier Paolo Scaglioni
Division of Hematology, Oncology, Simmons Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX, USA
This article is an update of :
2000-10Franck Viguié
Laboratoire de Cytogenetique - Service d'Hematologie Biologique, Hopital Hotel-Dieu - 75181 Paris Cedex 04, France

(Note : for Links provided by Atlas : click)


HGNC Alias symbMYL
HGNC Previous namepromyelocytic leukemia
LocusID (NCBI) 5371
Atlas_Id 41
Location 15q24.1  [Link to chromosome band 15q24]
Location_base_pair Starts at 73994716 and ends at 74036394 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping PML.png]
  Top: Courtesy Mariano Rocchi, Resources for Molecular Cytogenetics. Bottom: Metaphase FISH analysis of PML (green); red dots indicate centromere of chromosome 15 (Subramaniyam et al., 2006).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CAMSAP3 (19p13.2)::PML (15q24.1)MYH9 (22q12.3)::PML (15q24.1)PAX5 (9p13.2)::PML (15q24.1)
PML (15q24.1)::MAPK1IP1L (14q22.3)PML (15q24.1)::PAX5 (9p13.2)PML (15q24.1)::PML (15q24.1)
PML (15q24.1)::POLN (4p16.3)PML (15q24.1)::RAB40B (17q25.3)PML (15q24.1)::RARA (17q21.2)
RAB40B (17q25.3)::PML (15q24.1)RARA (17q21.2)::PML (15q24.1)


  Structural organization of PML human gene (Nisole et al., 2013).
Description PML is composed of 9 exons. Exons 7 and 8 can be divided into exons 7a, 7b, 8a and 8b.
Transcription Transcription of PML generates 22 transcripts (splice variants) with at least 11 different isoforms (PMLI, PMLIa, PMLII, PMLIIa, PMLIII, PMLIV, PMLIVa, PMLV, PMLVI, PMLVIIa, PMLVIIb). Names of PML isoforms are based on the original nomenclature defined by Jensen et al., 2001.
Pseudogene No pseudogenes have been reported so far.


  Schematic representation of PML isoforms (Nisole et al., 2013).
Description Alternative splicing of PML gives rise to several isoforms with different molecular weight: PMLI is the longest isoform and is composed of 882 amino acids, while the shortest is PMLVIIb (435 amino acids). PML belongs to the family of the tripartite motif (TRIM). The RBCC/TRIM motif is present in all PML isoforms and is encoded by the exons 1-3. The RBCC domain is composed of a RING finger domain (R), two B-boxes domains (B1 and B2) and an α-helical coiled-coil domain (CC). The RING finger motif is a conserved cysteine-rich zinc-binding domain found in several classes of proteins. The RING domain of PML is involved in the formation of the PML nuclear bodies (PML-NBs, see below) and in several others PML functions. Adjacent to the RING domain lay two cysteine-rich domains named B-boxes: these two domains have been proposed to work as second zinc-binding domain and they are involved in PML-NBs formation and in several others PML functions. The coiled-coil domain mediate PML homo- and hetero-dimerization. The CC domain is also essential for PML-NBs formation and PML functions. A nuclear localization signal (NLS) is present in the isoforms but not in PMLVIIb. The SUMO interacting motif (SIM) of PML is required for the recognition and binding of SUMOylated proteins (Jensen et al., 2001; Nisole et al., 2013). The SIM domain also contains the PML degron, involved in the CK2-dependent PML degradation (Scaglioni et al., 2006). PML undergoes several post-translational modifications. Several kinases phosphorylate PML on serine and threonine residues regulating its functions (Bernardi et al., 2004; Hayakawa and Privalsky, 2004; Scaglioni et al., 2006; Yang et al., 2006). SUMOylation is the most intensely studied post-translational modification of PML. Both SUMO1 and SUMO2/SUMO3 bind covalently to PML. SUMOylation facilitates PML-NBs formation promoting tumor suppressive response PML-dependent, but also promotes leukemogenesis by the SUMOylation of PML-RARA. Finally, SUMOylation also promotes ubiquitin-mediate degradation of PML and PML-RARA (Fu et al., 2005; Shen et al., 2006; Lallemand-Breitenbach et al., 2008; Kamitani et al., 1998a; Kamitani et al., 1998b; Rabellino et al., 2012). Ubiquitination regulates PML functions and activity and deregulation of PML appears to be the common mechanism accounting for PML loss in tumors (reviewed in Rabellino and Scaglioni, 2013). Finally, PML can be also acetylated (Hayakawa et al., 2008).
PML is the major constituent of the PML-NBs. PML-NBs are highly dynamic nuclear structures tightly bound to the nuclear matrix. Several functions of PML are related to the PML-NBs functions (reviewed in Bernardi et al., 2007). More than 150 different proteins have been shown to localize into PML-NBs (Van Damme et al., 2010).
  Schematic representation of PML isoform IV protein domains. R = RING-finger domains, aa 55-91; B1, B2 = B-boxes 1 aa 124-166 and 2 aa 184-228; CC = α-helical coiled-coil domain, aa 233-360; N = nuclear localization signal, aa 428-442; SIM = SUMO interacting motif, 508-518; D = degron. The three major SUMOylation sites (K60, K160 and K442) are indicated, as well as the major phosphorylation sites (T28, S36, S40, S480, T482, S517).
Expression PML is ubiquitously expressed.
Localisation Nuclear (PMLI-VI) and cytoplasmic (PMLVIIb).
Function PML has been implicated in several cellular functions.
Cellular senescence: PML is a key regulator of cellular senescence. PML is involved in oncogenic-induced senescence (OIS) K-RAS dependent in a p53 dependent way (de Stanchina et al., 2004; Ferbeyre et al., 2000; Pearson et al., 2000; Scaglioni et al., 2012). PML is also involved in Rb-dependent senescence (Mallette et al., 2004).
Apoptosis: PML promotes apoptosis primarily by its ability to interact with p53 (Wang et al., 1998). Moreover, a pro-apoptotic function has been also attributed to the cytoplasmic isoform of PML (Giorgi et al., 2010).
Neoangiogenesis: PML represses HIF1 transcription, blocking de novo angiogenesis (Bernardi et al., 2006).
Cell migration: PML is involved in the regulation of cell migration by the negatively regulating of β-1 integrins (Reineke et al., 2010).
DNA damage response: several proteins involved in DNA repair have been report to reside into PML-NBs. Therefore, PML is also involved in DNA-repair, even though the mechanisms are still not completely clear (reviewed in Dellaire and Bazett-Jones, 2004).
Anti-viral response: several viral proteins interact with PML and the PML-NBs; moreover, several reports implicate PML and PML-NBs in anti-viral response (reviewed in Geoffroy and Chelbi-Alix, 2011).
Hematopoietic stem cell maintenance: PML has been reported being involved in hematopoietic stem cell maintenance by the regulation of the fatty acid oxidation (Ito et al., 2008; Ito et al., 2012).
Several functions of PML are related to its ability to form PML-NBs. PML-NBs have been involved in tumor suppression, senescence and apoptosis, DNA-damage response, cell migration, neoangiogenesis and anti-viral response (reviewed in Bernardi et al., 2007).
Homology PML is conserved in Amniota (source: HomoloGene).


Note PML-RARA is the product of the chromosomal translocation t(15;17) and it causes acute promyelocytic leukemia (APL) (de Thé et al., 1990; Goddard et al., 1991; Kakizuka et al., 1991; Pandolfi et al., 1991).
  Schematic representation of the mutations type of human PML found in human tumor samples (source COSMIC).
Germinal No germinal mutations of PML have been reported.
Somatic At least 65 different somatic mutations have been described. All the informations in this regard can be found at the COSMIC website.

Implicated in

Entity Acute promyelocytic leukemia (APL)
Note (de Thé et al., 1990; Goddard et al., 1991; Kakizuka et al., 1991; Pandolfi et al., 1991)
Disease The balanced chromosomal translocation causes APL by driving the synthesis of the PML-RARA oncoprotein. This translocation drives the production of three different PML-RARA variants, depending on the length of the PML module: a short variant PML(S)-RARA, an intermediate variant PML(V)-RARA and a long variant PML(L)-RARA. Generally, 70% of the APL patients carry the PML(L)-RARA variant, followed by the PML(S)-RARA variant (20%) and the PML(V)-RARA (10%) (Melnick and Licht, 1999). PML staining in APL cells show a characteristic pattern commonly named "microspeckles" due to the fact that PML-RARA disrupts the PML-NBs. PML-RARA acts as a transcriptional repressor of RARA target genes. At the same time PML-RARA physically interacts with PML, impairing its tumor-suppressive functions. Combined, these features lead to the aberrant self-renewal of hematopoietic stem cells and block of differentiation of myeloid precursor cells at the promyelocytic stage (de Thé et al., 2012). APL is a distinct subtype of acute myeloid leukemia (AML), is a rare condition though extremely aggressive and malignant. Clinically, APL symptoms tend to be similar to AML. APL is characterized by a severe coagulopathy, including disseminated intravascular coagulation (DIC).
Prognosis APL is normally treated with the combination of retinoic acid (ATRA) and arsenic trioxide (ATO). This therapy leads to the remission of the disease in more than 90% of the cases. Notably, APL was the first malignant disease cured with targeted therapy (Lo-Coco et al., 2013).
Entity B-cell acute lymphoblastic leukemia (B-ALL)
Note (Nebral et al., 2007; Qiu et al., 2011; Kurahashi et al., 2011)
Disease The transcription factor PAX5 is required for development and maintenance of B-cell. Several chromosomal translocations involving PAX5 have been described, including the in which the 5' region of PAX5 is fused to PML. So far, two cases of B-ALL PAX5-PML-dependent have been reported. The fused PAX5-PML oncoprotein has a dominant-negative effect on both PML and PAX5, inhibiting PAX5 activation of B-cell specific genes and disrupting PML-NBs formation.
Prognosis Kurahashi and colleagues suggest that B-ALL PAX5-PML dependent could be treated with ATO (Kurahashi et al., 2011).
Entity Various cancers
Note Several reports indicate a reduced PML expression in several cancer types (Gurrieri et al., 2004; Rabellino et al., 2012; Rabellino and Scaglioni, 2013).
Disease PML protein expression was reduced or abolished in prostate adenocarcinomas (63% [95% confidence interval {CI} = 48% to 78%] and 28% [95% CI = 13% to 43%], respectively), colon adenocarcinomas (31% [95% CI = 22% to 40%] and 17% [95% CI = 10% to 24%]), breast carcinomas (21% [95% CI = 8% to 34%] and 31% [95% CI = 16% to 46%]), lung carcinomas (36% [95% CI = 15% to 57%] and 21% [95% = 3% to 39%]), lymphomas (14% [95% CI = 10% to 18%] and 69% [95% CI = 63% to 75%]), CNS tumors (24% [95% CI = 13% to 35%] and 49% [95% CI = 36% to 62%]), and germ cell tumors (36% [95% CI = 24% to 48%] and 48% [95% CI = 36% to 60%]) but not in thyroid or adrenal carcinomas (Gurrieri et al., 2004). In all the cases, PML mRNA levels are comparable to the healthy tissues and the PML gene is rarely mutated, but the protein levels of PML are reduced. This correlates with several reports that underline the role of PML degradation in tumor progression and maintenance (reviewed in Rabellino and Scaglioni, 2013).
Prognosis In most of the cases, loss of PML is associated with tumor progression, like was reported for prostate cancer, breast cancer and CNS tumors (Gurrieri et al., 2004).


Note Breakpoint at q24, responsible of translocation t(15;17)(q24;q21).


Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies.
Bernardi R, Pandolfi PP.
Nat Rev Mol Cell Biol. 2007 Dec;8(12):1006-16. (REVIEW)
PMID 17928811
PML nuclear bodies: dynamic sensors of DNA damage and cellular stress.
Dellaire G, Bazett-Jones DP.
Bioessays. 2004 Sep;26(9):963-77. (REVIEW)
PMID 15351967
PML is induced by oncogenic ras and promotes premature senescence.
Ferbeyre G, de Stanchina E, Querido E, Baptiste N, Prives C, Lowe SW.
Genes Dev. 2000 Aug 15;14(16):2015-27.
PMID 10950866
Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3.
Fu C, Ahmed K, Ding H, Ding X, Lan J, Yang Z, Miao Y, Zhu Y, Shi Y, Zhu J, Huang H, Yao X.
Oncogene. 2005 Aug 18;24(35):5401-13.
PMID 15940266
Role of promyelocytic leukemia protein in host antiviral defense.
Geoffroy MC, Chelbi-Alix MK.
J Interferon Cytokine Res. 2011 Jan;31(1):145-58. doi: 10.1089/jir.2010.0111. Epub 2011 Jan 3. (REVIEW)
PMID 21198351
PML regulates apoptosis at endoplasmic reticulum by modulating calcium release.
Giorgi C, Ito K, Lin HK, Santangelo C, Wieckowski MR, Lebiedzinska M, Bononi A, Bonora M, Duszynski J, Bernardi R, Rizzuto R, Tacchetti C, Pinton P, Pandolfi PP.
Science. 2010 Nov 26;330(6008):1247-51. doi: 10.1126/science.1189157. Epub 2010 Oct 28.
PMID 21030605
Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia.
Goddard AD, Borrow J, Freemont PS, Solomon E.
Science. 1991 Nov 29;254(5036):1371-4.
PMID 1720570
Loss of the tumor suppressor PML in human cancers of multiple histologic origins.
Gurrieri C, Capodieci P, Bernardi R, Scaglioni PP, Nafa K, Rush LJ, Verbel DA, Cordon-Cardo C, Pandolfi PP.
J Natl Cancer Inst. 2004 Feb 18;96(4):269-79.
PMID 14970276
Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis.
Hayakawa F, Abe A, Kitabayashi I, Pandolfi PP, Naoe T.
J Biol Chem. 2008 Sep 5;283(36):24420-5. doi: 10.1074/jbc.M802217200. Epub 2008 Jul 11.
PMID 18621739
PML targeting eradicates quiescent leukaemia-initiating cells.
Ito K, Bernardi R, Morotti A, Matsuoka S, Saglio G, Ikeda Y, Rosenblatt J, Avigan DE, Teruya-Feldstein J, Pandolfi PP.
Nature. 2008 Jun 19;453(7198):1072-8. doi: 10.1038/nature07016. Epub 2008 May 11.
PMID 18469801
A PML-PPAR-delta pathway for fatty acid oxidation regulates hematopoietic stem cell maintenance.
Ito K, Carracedo A, Weiss D, Arai F, Ala U, Avigan DE, Schafer ZT, Evans RM, Suda T, Lee CH, Pandolfi PP.
Nat Med. 2012 Sep;18(9):1350-8.
PMID 22902876
PML protein isoforms and the RBCC/TRIM motif.
Jensen K, Shiels C, Freemont PS.
Oncogene. 2001 Oct 29;20(49):7223-33. (REVIEW)
PMID 11704850
Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML.
Kakizuka A, Miller WH Jr, Umesono K, Warrell RP Jr, Frankel SR, Murty VV, Dmitrovsky E, Evans RM.
Cell. 1991 Aug 23;66(4):663-74.
PMID 1652368
Covalent modification of PML by the sentrin family of ubiquitin-like proteins.
Kamitani T, Nguyen HP, Kito K, Fukuda-Kamitani T, Yeh ET.
J Biol Chem. 1998b Feb 6;273(6):3117-20.
PMID 9452416
PAX5-PML acts as a dual dominant-negative form of both PAX5 and PML.
Kurahashi S, Hayakawa F, Miyata Y, Yasuda T, Minami Y, Tsuzuki S, Abe A, Naoe T.
Oncogene. 2011 Apr 14;30(15):1822-30. doi: 10.1038/onc.2010.554. Epub 2011 Jan 10.
PMID 21217775
Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway.
Lallemand-Breitenbach V, Jeanne M, Benhenda S, Nasr R, Lei M, Peres L, Zhou J, Zhu J, Raught B, de The H.
Nat Cell Biol. 2008 May;10(5):547-55. doi: 10.1038/ncb1717. Epub 2008 Apr 13.
PMID 18408733
Retinoic acid and arsenic trioxide for acute promyelocytic leukemia.
Lo-Coco F, Avvisati G, Vignetti M, Thiede C, Orlando SM, Iacobelli S, Ferrara F, Fazi P, Cicconi L, Di Bona E, Specchia G, Sica S, Divona M, Levis A, Fiedler W, Cerqui E, Breccia M, Fioritoni G, Salih HR, Cazzola M, Melillo L, Carella AM, Brandts CH, Morra E, von Lilienfeld-Toal M, Hertenstein B, Wattad M, Lubbert M, Hanel M, Schmitz N, Link H, Kropp MG, Rambaldi A, La Nasa G, Luppi M, Ciceri F, Finizio O, Venditti A, Fabbiano F, Dohner K, Sauer M, Ganser A, Amadori S, Mandelli F, Dohner H, Ehninger G, Schlenk RF, Platzbecker U; Gruppo Italiano Malattie Ematologiche dell'Adulto; German-Austrian Acute Myeloid Leukemia Study Group; Study Alliance Leukemia.
N Engl J Med. 2013 Jul 11;369(2):111-21. doi: 10.1056/NEJMoa1300874.
PMID 23841729
Human fibroblasts require the Rb family of tumor suppressors, but not p53, for PML-induced senescence.
Mallette FA, Goumard S, Gaumont-Leclerc MF, Moiseeva O, Ferbeyre G.
Oncogene. 2004 Jan 8;23(1):91-9.
PMID 14712214
Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia.
Melnick A, Licht JD.
Blood. 1999 May 15;93(10):3167-215. (REVIEW)
PMID 10233871
Identification of PML as novel PAX5 fusion partner in childhood acute lymphoblastic leukaemia.
Nebral K, Konig M, Harder L, Siebert R, Haas OA, Strehl S.
Br J Haematol. 2007 Oct;139(2):269-74.
PMID 17897302
Differential Roles of PML Isoforms.
Nisole S, Maroui MA, Mascle XH, Aubry M, Chelbi-Alix MK.
Front Oncol. 2013 May 22;3:125. doi: 10.3389/fonc.2013.00125. eCollection 2013.
PMID 23734343
Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties.
Pandolfi PP, Grignani F, Alcalay M, Mencarelli A, Biondi A, LoCoco F, Grignani F, Pelicci PG.
Oncogene. 1991 Jul;6(7):1285-92.
PMID 1650447
PML regulates p53 acetylation and premature senescence induced by oncogenic Ras.
Pearson M, Carbone R, Sebastiani C, Cioce M, Fagioli M, Saito S, Higashimoto Y, Appella E, Minucci S, Pandolfi PP, Pelicci PG.
Nature. 2000 Jul 13;406(6792):207-10.
PMID 10910364
The reduced and altered activities of PAX5 are linked to the protein-protein interaction motif (coiled-coil domain) of the PAX5-PML fusion protein in t(9;15)-associated acute lymphocytic leukemia.
Qiu JJ, Chu H, Lu X, Jiang X, Dong S.
Oncogene. 2011 Feb 24;30(8):967-77. doi: 10.1038/onc.2010.473. Epub 2010 Oct 25.
PMID 20972455
PML Degradation: Multiple Ways to Eliminate PML.
Rabellino A, Scaglioni PP.
Front Oncol. 2013 Mar 22;3:60. doi: 10.3389/fonc.2013.00060. eCollection 2013.
PMID 23526763
Promyelocytic leukemia protein controls cell migration in response to hydrogen peroxide and insulin-like growth factor-1.
Reineke EL, Liu Y, Kao HY.
J Biol Chem. 2010 Mar 26;285(13):9485-92. doi: 10.1074/jbc.M109.063362. Epub 2010 Jan 25.
PMID 20100838
Translation-dependent mechanisms lead to PML upregulation and mediate oncogenic K-RAS-induced cellular senescence.
Scaglioni PP, Rabellino A, Yung TM, Bernardi R, Choi S, Konstantinidou G, Nardella C, Cheng K, Pandolfi PP.
EMBO Mol Med. 2012 Jul;4(7):594-602. doi: 10.1002/emmm.201200233. Epub 2012 Mar 21.
PMID 22359342
The mechanisms of PML-nuclear body formation.
Shen TH, Lin HK, Scaglioni PP, Yung TM, Pandolfi PP.
Mol Cell. 2006 Nov 3;24(3):331-9.
PMID 17081985
Do RARA/PML fusion gene deletions confer resistance to ATRA-based therapy in patients with acute promyelocytic leukemia?
Subramaniyam S, Nandula SV, Nichols G, Weiner M, Satwani P, Alobeid B, Bhagat G, Murty VV.
Leukemia. 2006 Dec;20(12):2193-5. Epub 2006 Sep 28.
PMID 17008891
A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.
Van Damme E, Laukens K, Dang TH, Van Ostade X.
Int J Biol Sci. 2010 Jan 12;6(1):51-67. (REVIEW)
PMID 20087442
PML is essential for multiple apoptotic pathways.
Wang ZG, Ruggero D, Ronchetti S, Zhong S, Gaboli M, Rivi R, Pandolfi PP.
Nat Genet. 1998 Nov;20(3):266-72.
PMID 9806545
Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation.
Yang S, Jeong JH, Brown AL, Lee CH, Pandolfi PP, Chung JH, Kim MK.
J Biol Chem. 2006 Sep 8;281(36):26645-54. Epub 2006 Jul 11.
PMID 16835227
PML is a direct p53 target that modulates p53 effector functions.
de Stanchina E, Querido E, Narita M, Davuluri RV, Pandolfi PP, Ferbeyre G, Lowe SW.
Mol Cell. 2004 Feb 27;13(4):523-35.
PMID 14992722
The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus.
de The H, Chomienne C, Lanotte M, Degos L, Dejean A.
Nature. 1990 Oct 11;347(6293):558-61.
PMID 2170850
The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies.
de The H, Le Bras M, Lallemand-Breitenbach V.
J Cell Biol. 2012 Jul 9;198(1):11-21. doi: 10.1083/jcb.201112044. (REVIEW)
PMID 22778276


This paper should be referenced as such :
A Rabellino, PP Scaglioni
PML (promyelocytic leukemia)
Atlas Genet Cytogenet Oncol Haematol. 2015;19(1):44-49.
Free journal version : [ pdf ]   [ DOI ]
History of this paper:
Viguié, F. PML (promyelocytic leukemia). Atlas Genet Cytogenet Oncol Haematol. 2000;4(4):193-194.

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 15 ]
  Classification of acute myeloid leukemias
M3::M3v acute myeloid leukemia (AML M3::M3v)
::Acute promyelocytic leukemia (APL)
::Acute promyelocytic leukemia (APL) PML::RARA

t(1;9)(p13;p12) PAX5::HIPK1
t(1;17)(q42;q21) IRF2BP2::RARA
t(3;17)(q26;q12-21) TBL1XR1::RARA
t(4;17)(q12;q21) FIP1L1::RARA
t(9;15)(p13;q24) PAX5::PML
t(X;17)(p11;q21) BCOR::RARA
t(11;17)(q23;q21) ZBTB16::RARA
t(11;17)(q13;q21) NUMA1::RARA
t(12;13)(p13;q14) LIN00598::ETV6
t(15;17)(q24;q21) PML::RARA
t(15;17)(q22;q21) in treatment related leukemia
t(5;17)(q35;q21) NPM1::RARA
Therapy-Related Hematopoietic Neoplasia

External links

HGNC (Hugo)PML   9113
LRG (Locus Reference Genomic)LRG_1069
Entrez_Gene (NCBI)PML    PML nuclear body scaffold
AliasesMYL; PP8675; RNF71; TRIM19
GeneCards (Weizmann)PML
Ensembl hg19 (Hinxton)ENSG00000140464 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000140464 [Gene_View]  ENSG00000140464 [Sequence]  chr15:73994716-74036394 [Contig_View]  PML [Vega]
ICGC DataPortalENSG00000140464
TCGA cBioPortalPML
Genatlas (Paris)PML
SOURCE (Princeton)PML
Genetics Home Reference (NIH)PML
Genomic and cartography
GoldenPath hg38 (UCSC)PML  -     chr15:73994716-74036394 +  15q24.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PML  -     15q24.1   [Description]    (hg19-Feb_2009)
GoldenPathPML - 15q24.1 [CytoView hg19]  PML - 15q24.1 [CytoView hg38]
Genome Data Viewer NCBIPML [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB208950 AB209051 AB209411 AF230401 AF230402
RefSeq transcript (Entrez)NM_002675 NM_033238 NM_033239 NM_033240 NM_033244 NM_033246 NM_033247 NM_033249 NM_033250
Consensus coding sequences : CCDS (NCBI)PML
Gene ExpressionPML [ NCBI-GEO ]   PML [ EBI - ARRAY_EXPRESS ]   PML [ SEEK ]   PML [ MEM ]
Gene Expression Viewer (FireBrowse)PML [ Firebrowse - Broad ]
GenevisibleExpression of PML in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5371
GTEX Portal (Tissue expression)PML
Human Protein AtlasENSG00000140464-PML [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)PML
Human Protein Atlas [tissue]ENSG00000140464-PML [tissue]
Protein Interaction databases
Ontologies - Pathways
PubMed499 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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