PML report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of PML at tissue level.

III. Associated gene sets

GO_1901798Biological processpositive regulation of signal transduction by p53 class mediator
GO_0097191Biological processextrinsic apoptotic signaling pathway
GO_0070059Biological processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
GO_0016925Biological processprotein sumoylation
GO_0008285Biological processnegative regulation of cell population proliferation
GO_0048146Biological processpositive regulation of fibroblast proliferation
GO_2001238Biological processpositive regulation of extrinsic apoptotic signaling pathway
GO_2000059Biological processnegative regulation of ubiquitin-dependent protein catabolic process
GO_2000779Biological processregulation of double-strand break repair
GO_0090402Biological processoncogene-induced cell senescence
GO_0060444Biological processbranching involved in mammary gland duct morphogenesis
GO_0045087Biological processinnate immune response
GO_0010332Biological processresponse to gamma radiation
GO_0034097Biological processresponse to cytokine
GO_0010761Biological processfibroblast migration
GO_1990830Biological processcellular response to leukemia inhibitory factor
GO_0042771Biological processintrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
GO_0009411Biological processresponse to UV
GO_0010522Biological processregulation of calcium ion transport into cytosol
GO_0071353Biological processcellular response to interleukin-4
GO_0030578Biological processPML body organization
GO_0032691Biological processnegative regulation of interleukin-1 beta production
GO_0032922Biological processcircadian regulation of gene expression
GO_0042752Biological processregulation of circadian rhythm
GO_0065003Biological processprotein-containing complex assembly
GO_0016525Biological processnegative regulation of angiogenesis
GO_2000758Biological processpositive regulation of peptidyl-lysine acetylation
GO_0051457Biological processmaintenance of protein location in nucleus
GO_0060395Biological processSMAD protein signal transduction
GO_0045165Biological processcell fate commitment
GO_0030099Biological processmyeloid cell differentiation
GO_0032206Biological processpositive regulation of telomere maintenance
GO_0001666Biological processresponse to hypoxia
GO_0008630Biological processintrinsic apoptotic signaling pathway in response to DNA damage
GO_0006606Biological processprotein import into nucleus
GO_0006355Biological processregulation of DNA-templated transcription
GO_0006977Biological processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
GO_0043153Biological processentrainment of circadian clock by photoperiod
GO_0090398Biological processcellular senescence
GO_0044790Biological processsuppression of viral release by host
GO_0008631Biological processintrinsic apoptotic signaling pathway in response to oxidative stress
GO_0048384Biological processretinoic acid receptor signaling pathway
GO_0030155Biological processregulation of cell adhesion
GO_0007179Biological processtransforming growth factor beta receptor signaling pathway
GO_0045892Biological processnegative regulation of DNA-templated transcription
GO_0031503Biological processprotein-containing complex localization
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0032469Biological processendoplasmic reticulum calcium ion homeostasis
GO_0030308Biological processnegative regulation of cell growth
GO_0005730Cellular componentnucleolus
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0031901Cellular componentearly endosome membrane
GO_0005654Cellular componentnucleoplasm
GO_0016363Cellular componentnuclear matrix
GO_0005829Cellular componentcytosol
GO_0016605Cellular componentPML body
GO_0005737Cellular componentcytoplasm
GO_0000781Cellular componentchromosome, telomeric region
GO_0005634Cellular componentnucleus
GO_0003677Molecular functionDNA binding
GO_0019789Molecular functionSUMO transferase activity
GO_0042803Molecular functionprotein homodimerization activity
GO_0060090Molecular functionmolecular adaptor activity
GO_0046332Molecular functionSMAD binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0032183Molecular functionSUMO binding
GO_0061659Molecular functionubiquitin-like protein ligase activity
GO_0008270Molecular functionzinc ion binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene namePML
Protein nameProtein PML (E3 SUMO-protein ligase PML) (EC 2.3.2.-) (Promyelocytic leukemia protein) (RING finger protein 71) (RING-type E3 SUMO transferase PML) (Tripartite motif-containing protein 19) (TRIM19)
PML nuclear body scaffold
PML protein
Promyelocytic leukemia gene protein
SynonymsTRIM19
MYL
PP8675
RNF71
DescriptionFUNCTION: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Inhibits EIF4E-mediated mRNA nuclear export by reducing EIF4E affinity for the 5' 7-methylguanosine (m7G) cap of target mRNAs . Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration. .; FUNCTION: Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response . Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity . .

AccessionsENST00000562086.1
ENST00000354026.10 [P29590-13]
ENST00000569477.5 [P29590-9]
ENST00000564428.5 [P29590-12]
ENST00000566068.1
H3BVD2
H3BUJ5
ENST00000435786.6 [P29590-2]
ENST00000565239.5
ENST00000268059.10 [P29590-8]
ENST00000565898.5 [P29590-11]
Q9UE85
H3BT29
H3BRN3
ENST00000567543.5 [P29590-14]
ENST00000395135.7 [P29590-5]
ENST00000436891.7 [P29590-4]
ENST00000268058.8 [P29590-1]
ENST00000563500.5
P29590
ENST00000359928.8 [P29590-14]
A4VCI9
ENST00000567606.5
ENST00000395132.6 [P29590-10]
H3BT57
ENST00000569965.5 [P29590-4]