Details for: PML

Gene ID: 5371

Symbol: PML

Ensembl ID: ENSG00000140464

Description: PML nuclear body scaffold

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 141.3094
    Cell Significance Index: -21.9800
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 81.1375
    Cell Significance Index: -20.5800
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 63.6489
    Cell Significance Index: -26.2200
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 54.5833
    Cell Significance Index: -25.7700
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 54.2021
    Cell Significance Index: -22.0200
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 48.7961
    Cell Significance Index: -25.1000
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 38.4935
    Cell Significance Index: -25.8300
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 23.2104
    Cell Significance Index: -22.1600
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 19.7736
    Cell Significance Index: -24.3800
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 8.4588
    Cell Significance Index: -22.6600
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 6.5156
    Cell Significance Index: -14.2600
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 6.3152
    Cell Significance Index: -24.9200
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 5.7139
    Cell Significance Index: -17.5500
  • Cell Name: decidual cell (CL2000002)
    Fold Change: 1.7172
    Cell Significance Index: 27.5500
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 1.6789
    Cell Significance Index: 87.4500
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 1.3451
    Cell Significance Index: 218.7700
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 1.1516
    Cell Significance Index: 1039.8100
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 0.9436
    Cell Significance Index: 16.6800
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 0.8522
    Cell Significance Index: 44.2700
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.8203
    Cell Significance Index: 89.2200
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 0.8090
    Cell Significance Index: 22.6100
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.7599
    Cell Significance Index: 45.6200
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 0.6224
    Cell Significance Index: 16.9400
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.6206
    Cell Significance Index: 111.8700
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 0.6123
    Cell Significance Index: 75.2900
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.4592
    Cell Significance Index: 250.7600
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 0.3890
    Cell Significance Index: 7.1900
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 0.3711
    Cell Significance Index: 17.4400
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 0.3694
    Cell Significance Index: 23.8400
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: 0.3518
    Cell Significance Index: 5.0600
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 0.3420
    Cell Significance Index: 7.4100
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 0.3210
    Cell Significance Index: 41.4700
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 0.3119
    Cell Significance Index: 42.8300
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 0.2646
    Cell Significance Index: 7.7700
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.2636
    Cell Significance Index: 12.2900
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.2355
    Cell Significance Index: 104.1000
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: 0.2284
    Cell Significance Index: 5.7100
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.2275
    Cell Significance Index: 45.6400
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.2166
    Cell Significance Index: 21.4300
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 0.2110
    Cell Significance Index: 14.6000
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.1843
    Cell Significance Index: 5.3100
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.1811
    Cell Significance Index: 35.9300
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 0.1654
    Cell Significance Index: 19.5100
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.1447
    Cell Significance Index: 100.0800
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.1217
    Cell Significance Index: 15.6000
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.0976
    Cell Significance Index: 3.4300
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 0.0890
    Cell Significance Index: 0.5800
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.0686
    Cell Significance Index: 24.6200
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: 0.0627
    Cell Significance Index: 1.0500
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.0614
    Cell Significance Index: 4.7100
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 0.0302
    Cell Significance Index: 1.3700
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.0280
    Cell Significance Index: 5.3300
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 0.0273
    Cell Significance Index: 1.9300
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.0081
    Cell Significance Index: 15.3200
  • Cell Name: endothelial cell of placenta (CL0009092)
    Fold Change: -0.0033
    Cell Significance Index: -0.0200
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0062
    Cell Significance Index: -11.4800
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: -0.0068
    Cell Significance Index: -5.1700
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0069
    Cell Significance Index: -10.6900
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0140
    Cell Significance Index: -1.4300
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0142
    Cell Significance Index: -9.0200
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0177
    Cell Significance Index: -24.0000
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -0.0235
    Cell Significance Index: -0.5000
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0275
    Cell Significance Index: -20.1500
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0299
    Cell Significance Index: -4.3400
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0308
    Cell Significance Index: -14.0000
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0328
    Cell Significance Index: -24.2800
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: -0.0429
    Cell Significance Index: -1.2300
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0444
    Cell Significance Index: -25.0600
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0454
    Cell Significance Index: -28.3600
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -0.0516
    Cell Significance Index: -1.3800
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: -0.0585
    Cell Significance Index: -4.3600
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.0663
    Cell Significance Index: -19.0900
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: -0.0799
    Cell Significance Index: -2.0400
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.0863
    Cell Significance Index: -14.7400
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.0896
    Cell Significance Index: -10.4500
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.1335
    Cell Significance Index: -28.1100
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -0.1356
    Cell Significance Index: -1.8500
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -0.1369
    Cell Significance Index: -6.9200
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: -0.1419
    Cell Significance Index: -2.7700
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -0.1474
    Cell Significance Index: -4.7200
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.1523
    Cell Significance Index: -17.4500
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.1944
    Cell Significance Index: -10.9100
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.2239
    Cell Significance Index: -23.3100
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.2247
    Cell Significance Index: -13.8100
  • Cell Name: peg cell (CL4033014)
    Fold Change: -0.2316
    Cell Significance Index: -5.3500
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -0.2322
    Cell Significance Index: -6.2000
  • Cell Name: oral mucosa squamous cell (CL1001576)
    Fold Change: -0.2391
    Cell Significance Index: -2.0600
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: -0.2411
    Cell Significance Index: -2.2200
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.2550
    Cell Significance Index: -16.0700
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.2578
    Cell Significance Index: -15.8100
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: -0.2934
    Cell Significance Index: -7.7200
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.2960
    Cell Significance Index: -23.4400
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.3023
    Cell Significance Index: -15.8700
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.3144
    Cell Significance Index: -21.1400
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: -0.3254
    Cell Significance Index: -8.7200
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: -0.3569
    Cell Significance Index: -7.4700
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: -0.3857
    Cell Significance Index: -4.9400
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -0.3940
    Cell Significance Index: -13.6900
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: -0.4077
    Cell Significance Index: -8.7200
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.4402
    Cell Significance Index: -19.4700

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics** 1. **Nuclear Body Scaffold**: PML is a critical component of the nuclear body, a dynamic structure that regulates chromatin organization and gene expression. 2. **Apoptosis Regulator**: PML modulates the intrinsic and extrinsic apoptotic pathways, influencing programmed cell death in response to DNA damage, oxidative stress, and other forms of cellular stress. 3. **DNA Damage Response**: PML interacts with DNA damage response proteins, such as ATM and ATR, to regulate DNA repair and maintain genome stability. 4. **Gene Expression Regulation**: PML modulates gene expression through its interactions with transcription factors, such as p53 and Runx1, and its involvement in chromatin remodeling complexes. 5. **Cellular Signaling**: PML is involved in various signaling pathways, including cytokine signaling, interferon signaling, and the transforming growth factor beta receptor signaling pathway. **Pathways and Functions** PML is involved in numerous signaling pathways and cellular processes, including: 1. **Apoptosis**: PML regulates the intrinsic and extrinsic apoptotic pathways, influencing programmed cell death in response to DNA damage, oxidative stress, and other forms of cellular stress. 2. **DNA Damage Response**: PML interacts with DNA damage response proteins, such as ATM and ATR, to regulate DNA repair and maintain genome stability. 3. **Gene Expression Regulation**: PML modulates gene expression through its interactions with transcription factors, such as p53 and Runx1, and its involvement in chromatin remodeling complexes. 4. **Cellular Signaling**: PML is involved in various signaling pathways, including cytokine signaling, interferon signaling, and the transforming growth factor beta receptor signaling pathway. 5. **Circadian Rhythm**: PML is involved in the regulation of the circadian rhythm, influencing the expression of genes involved in clock-related processes. **Clinical Significance** Dysregulation of the PML gene has been implicated in various human diseases, including: 1. **Cancer**: PML is frequently mutated or deleted in various types of cancer, including leukemia, lymphoma, and solid tumors. 2. **Neurodegenerative Diseases**: PML has been implicated in the pathogenesis of neurodegenerative diseases, such as Alzheimer's disease and amyotrophic lateral sclerosis. 3. **Infectious Diseases**: PML is involved in the regulation of immune responses to viral infections, such as HIV and HCMV. 4. **Autoimmune Diseases**: PML has been implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis and lupus. In conclusion, the PML gene plays a crucial role in maintaining cellular homeostasis and regulating various cellular processes, including apoptosis, DNA damage response, and gene expression. Dysregulation of the PML gene has been implicated in various human diseases, highlighting the importance of understanding its function and regulation in the context of human health and disease.

Genular Protein ID: 857406512

Symbol: PML_HUMAN

Name: Protein PML

UniProtKB Accession Codes:

P29590 E9PBR7 P29591 P29592 P29593 Q00755 Q15959 Q59FP9 Q8WUA0 Q96S41 Q9BPW2 Q9BWP7 Q9BZX6 Q9BZX7 Q9BZX8 Q9BZX9 Q9BZY0 Q9BZY2 Q9BZY3

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 9 CDD 3 CORUM 1 CTD 1 ChEBI 16 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 1 EMBL 25 Ensembl 13 EvolutionaryTrace 1 ExpressionAtlas 1 GO 85 Gene3D 2 GeneCards 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 7 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 19 PDBsum 19 PIR 5 PRO 1 PROSITE 3 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 13 Pumba 1 RNAct 1 Reactome 8 RefSeq 9 SIGNOR 1 SMART 2 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 UniPathway 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 1652369

Title: The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR.

PubMed ID: 1652369

DOI: 10.1016/0092-8674(91)90113-d

PubMed ID: 1720570

Title: Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia.

PubMed ID: 1720570

DOI: 10.1126/science.1720570

PubMed ID: 1311253

Title: Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins.

PubMed ID: 1311253

DOI: 10.1002/j.1460-2075.1992.tb05095.x

PubMed ID: 1652368

Title: Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML.

PubMed ID: 1652368

DOI: 10.1016/0092-8674(91)90112-c

PubMed ID: 11331580

Title: The tripartite motif family identifies cell compartments.

PubMed ID: 11331580

DOI: 10.1093/emboj/20.9.2140

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1312695

Title: Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants.

PubMed ID: 1312695

PubMed ID: 12691149

Title: Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic leukemia: structure of the fusion point in a case lacking classic t(15;17) translocation.

PubMed ID: 12691149

DOI: 10.1080/1042819021000040305

PubMed ID: 9756909

Title: Identification of three major sentrinization sites in PML.

PubMed ID: 9756909

DOI: 10.1074/jbc.273.41.26675

PubMed ID: 9570750

Title: Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML.

PubMed ID: 9570750

DOI: 10.1242/jcs.111.10.1319

PubMed ID: 9420283

Title: An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm.

PubMed ID: 9420283

DOI: 10.1128/jvi.72.1.758-766.1998

PubMed ID: 10233977

Title: Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption.

PubMed ID: 10233977

DOI: 10.1128/jvi.73.6.5137-5143.1999

PubMed ID: 10610177

Title: A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins.

PubMed ID: 10610177

DOI: 10.1038/15463

PubMed ID: 10779416

Title: Role of SUMO-1-modified PML in nuclear body formation.

PubMed ID: 10779416

PubMed ID: 10684855

Title: Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis.

PubMed ID: 10684855

DOI: 10.1084/jem.191.4.631

PubMed ID: 10669754

Title: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML.

PubMed ID: 10669754

DOI: 10.1128/mcb.20.5.1784-1796.2000

PubMed ID: 11025664

Title: The function of PML in p53-dependent apoptosis.

PubMed ID: 11025664

DOI: 10.1038/35036365

PubMed ID: 11432836

Title: PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator.

PubMed ID: 11432836

DOI: 10.1093/emboj/20.13.3495

PubMed ID: 11500381

Title: PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA.

PubMed ID: 11500381

DOI: 10.1093/emboj/20.16.4547

PubMed ID: 11575918

Title: The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor eIF4E.

PubMed ID: 11575918

DOI: 10.1006/jmbi.2001.5003

PubMed ID: 11704850

Title: PML protein isoforms and the RBCC/TRIM motif.

PubMed ID: 11704850

DOI: 10.1038/sj.onc.1204765

PubMed ID: 12006491

Title: Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.

PubMed ID: 12006491

DOI: 10.1093/emboj/21.10.2383

PubMed ID: 12419228

Title: SUMO-1 protease-1 regulates gene transcription through PML.

PubMed ID: 12419228

DOI: 10.1016/s1097-2765(02)00699-8

PubMed ID: 12402044

Title: PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2.

PubMed ID: 12402044

DOI: 10.1038/ncb869

PubMed ID: 12439746

Title: Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies.

PubMed ID: 12439746

DOI: 10.1038/sj.onc.1205931

PubMed ID: 12810724

Title: The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation.

PubMed ID: 12810724

DOI: 10.1074/jbc.m301264200

PubMed ID: 12773567

Title: PML colocalizes with and stabilizes the DNA damage response protein TopBP1.

PubMed ID: 12773567

DOI: 10.1128/mcb.23.12.4247-4256.2003

PubMed ID: 14645235

Title: The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome.

PubMed ID: 14645235

DOI: 10.1074/jbc.m306407200

PubMed ID: 15163746

Title: Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells.

PubMed ID: 15163746

DOI: 10.1128/jvi.78.12.6527-6542.2004

PubMed ID: 14976184

Title: Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein.

PubMed ID: 14976184

DOI: 10.1074/jbc.m312439200

PubMed ID: 15136035

Title: The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle.

PubMed ID: 15136035

DOI: 10.1016/j.jmb.2004.03.071

PubMed ID: 15195100

Title: PML regulates p53 stability by sequestering Mdm2 to the nucleolus.

PubMed ID: 15195100

DOI: 10.1038/ncb1147

PubMed ID: 15467728

Title: PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein.

PubMed ID: 15467728

DOI: 10.1038/nsmb837

PubMed ID: 15356634

Title: Cytoplasmic PML function in TGF-beta signalling.

PubMed ID: 15356634

DOI: 10.1038/nature02783

PubMed ID: 15809060

Title: Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation.

PubMed ID: 15809060

DOI: 10.1016/j.bbrc.2005.03.052

PubMed ID: 16778193

Title: Characterization of endogenous human promyelocytic leukemia isoforms.

PubMed ID: 16778193

DOI: 10.1158/0008-5472.can-05-3792

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17030982

Title: Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR.

PubMed ID: 17030982

DOI: 10.1083/jcb.200604009

PubMed ID: 16912307

Title: Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense.

PubMed ID: 16912307

DOI: 10.1128/jvi.00031-06

PubMed ID: 17081985

Title: The mechanisms of PML-nuclear body formation.

PubMed ID: 17081985

DOI: 10.1016/j.molcel.2006.09.013

PubMed ID: 18298799

Title: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein.

PubMed ID: 18298799

DOI: 10.1111/j.1365-2443.2008.01165.x

PubMed ID: 18621739

Title: Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis.

PubMed ID: 18621739

DOI: 10.1074/jbc.m802217200

PubMed ID: 17942542

Title: Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection.

PubMed ID: 17942542

DOI: 10.1128/jvi.01685-07

PubMed ID: 18716620

Title: The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network.

PubMed ID: 18716620

DOI: 10.1038/nature07290

PubMed ID: 18408734

Title: RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.

PubMed ID: 18408734

DOI: 10.1038/ncb1716

PubMed ID: 17173041

Title: Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus.

PubMed ID: 17173041

DOI: 10.1038/ncb1516

PubMed ID: 18391071

Title: The eIF4E RNA regulon promotes the Akt signaling pathway.

PubMed ID: 18391071

DOI: 10.1083/jcb.200707018

PubMed ID: 18509536

Title: A role for cytoplasmic PML in cellular resistance to viral infection.

PubMed ID: 18509536

DOI: 10.1371/journal.pone.0002277

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19703418

Title: Differential suppressive effect of promyelocytic leukemia protein on the replication of different subtypes/strains of influenza A virus.

PubMed ID: 19703418

DOI: 10.1016/j.bbrc.2009.08.091

PubMed ID: 19567472

Title: PML-IV functions as a negative regulator of telomerase by interacting with TERT.

PubMed ID: 19567472

DOI: 10.1242/jcs.048066

PubMed ID: 19015637

Title: PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage.

PubMed ID: 19015637

DOI: 10.1038/onc.2008.420

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20501696

Title: Two-step colocalization of MORC3 with PML nuclear bodies.

PubMed ID: 20501696

DOI: 10.1242/jcs.063586

PubMed ID: 20702643

Title: Resistance to rabies virus infection conferred by the PMLIV isoform.

PubMed ID: 20702643

DOI: 10.1128/jvi.01286-10

PubMed ID: 20719947

Title: Epstein-Barr virus nuclear antigen 1 Hijacks the host kinase CK2 to disrupt PML nuclear bodies.

PubMed ID: 20719947

DOI: 10.1128/jvi.01183-10

PubMed ID: 20639899

Title: SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML.

PubMed ID: 20639899

DOI: 10.1038/onc.2010.284

PubMed ID: 20943951

Title: Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies.

PubMed ID: 20943951

DOI: 10.1091/mbc.e10-05-0449

PubMed ID: 20625391

Title: Functional polymorphism of the CK2alpha intronless gene plays oncogenic roles in lung cancer.

PubMed ID: 20625391

DOI: 10.1371/journal.pone.0011418

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 20378816

Title: Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML.

PubMed ID: 20378816

DOI: 10.1126/science.1183424

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21639834

Title: Promyelocytic leukemia protein interacts with werner syndrome helicase and regulates double-strand break repair in gamma-irradiation-induced DNA damage responses.

PubMed ID: 21639834

DOI: 10.1134/s000629791105004x

PubMed ID: 21840486

Title: A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression.

PubMed ID: 21840486

DOI: 10.1016/j.ccr.2011.07.008

PubMed ID: 21475307

Title: The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites.

PubMed ID: 21475307

DOI: 10.1038/cdd.2011.31

PubMed ID: 21501958

Title: The nuclear bodies inside out: PML conquers the cytoplasm.

PubMed ID: 21501958

DOI: 10.1016/j.ceb.2011.03.011

PubMed ID: 22033920

Title: Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover.

PubMed ID: 22033920

DOI: 10.1074/jbc.m111.289512

PubMed ID: 21172801

Title: PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication.

PubMed ID: 21172801

DOI: 10.1242/jcs.075390

PubMed ID: 21198351

Title: Role of promyelocytic leukemia protein in host antiviral defense.

PubMed ID: 21198351

DOI: 10.1089/jir.2010.0111

PubMed ID: 21994459

Title: Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies.

PubMed ID: 21994459

DOI: 10.1128/jvi.05808-11

PubMed ID: 21148299

Title: The SUMO protease SENP6 is a direct regulator of PML nuclear bodies.

PubMed ID: 21148299

DOI: 10.1091/mbc.e10-06-0504

PubMed ID: 21161613

Title: The role of PML in the nervous system.

PubMed ID: 21161613

DOI: 10.1007/s12035-010-8156-y

PubMed ID: 20972456

Title: SUMO E3 ligase activity of TRIM proteins.

PubMed ID: 20972456

DOI: 10.1038/onc.2010.462

PubMed ID: 21304940

Title: Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against Varicella-Zoster virus.

PubMed ID: 21304940

DOI: 10.1371/journal.ppat.1001266

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22406621

Title: The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA.

PubMed ID: 22406621

DOI: 10.1158/0008-5472.can-11-3159

PubMed ID: 22117195

Title: MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs.

PubMed ID: 22117195

DOI: 10.1038/cdd.2011.173

PubMed ID: 22237204

Title: Role of the promyelocytic leukaemia protein in cell death regulation.

PubMed ID: 22237204

DOI: 10.1038/cddis.2011.122

PubMed ID: 22002537

Title: Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence.

PubMed ID: 22002537

DOI: 10.1038/emboj.2011.370

PubMed ID: 22274616

Title: PML regulates PER2 nuclear localization and circadian function.

PubMed ID: 22274616

DOI: 10.1038/emboj.2012.1

PubMed ID: 23316480

Title: Post-translational modifications of PML: consequences and implications.

PubMed ID: 23316480

DOI: 10.3389/fonc.2012.00210

PubMed ID: 22155184

Title: Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells.

PubMed ID: 22155184

DOI: 10.1053/j.gastro.2011.11.041

PubMed ID: 22685230

Title: Moloney murine leukemia virus integrase and reverse transcriptase interact with PML proteins.

PubMed ID: 22685230

DOI: 10.1093/jb/mvs063

PubMed ID: 22589541

Title: Promyelocytic leukemia protein (PML) regulates endothelial cell network formation and migration in response to tumor necrosis factor alpha (TNFalpha) and interferon alpha (IFNalpha).

PubMed ID: 22589541

DOI: 10.1074/jbc.m112.340505

PubMed ID: 22773875

Title: Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation.

PubMed ID: 22773875

DOI: 10.1074/jbc.m112.374769

PubMed ID: 22935031

Title: The role of PML ubiquitination in human malignancies.

PubMed ID: 22935031

DOI: 10.1186/1423-0127-19-81

PubMed ID: 23007646

Title: PML promotes MHC class II gene expression by stabilizing the class II transactivator.

PubMed ID: 23007646

DOI: 10.1083/jcb.201112015

PubMed ID: 22886304

Title: A metabolic prosurvival role for PML in breast cancer.

PubMed ID: 22886304

DOI: 10.1172/jci62129

PubMed ID: 22875967

Title: Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation.

PubMed ID: 22875967

DOI: 10.1128/jvi.01145-12

PubMed ID: 22629402

Title: TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.

PubMed ID: 22629402

DOI: 10.1371/journal.pone.0037470

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 22869143

Title: BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction.

PubMed ID: 22869143

DOI: 10.1038/onc.2012.332

PubMed ID: 22945642

Title: The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein.

PubMed ID: 22945642

DOI: 10.1038/onc.2012.406

PubMed ID: 23028697

Title: Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms.

PubMed ID: 23028697

DOI: 10.1371/journal.pone.0044949

PubMed ID: 23219818

Title: PML tumor suppressor protein is required for HCV production.

PubMed ID: 23219818

DOI: 10.1016/j.bbrc.2012.11.108

PubMed ID: 23430110

Title: Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human.

PubMed ID: 23430110

DOI: 10.1182/blood-2012-05-432104

PubMed ID: 23135708

Title: The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription.

PubMed ID: 23135708

DOI: 10.1128/jvi.02023-12

PubMed ID: 23431171

Title: MOZ increases p53 acetylation and premature senescence through its complex formation with PML.

PubMed ID: 23431171

DOI: 10.1073/pnas.1300490110

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

Sequence Information:

  • Length: 882
  • Mass: 97551
  • Checksum: D50968A977E34287
  • Sequence:
    • MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 
QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 
QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 
TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 
DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 
VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 
QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 
EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 
QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 
NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 
ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ 
HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG 
ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS 
LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA 
FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.