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Aliases for PML Gene

Aliases for PML Gene

  • Promyelocytic Leukemia 2 3
  • MYL 3 4 6
  • Tripartite Motif-Containing Protein 19 3 4
  • Promyelocytic Leukemia Protein 3 4
  • RING Finger Protein 71 3 4
  • PP8675 3 4
  • TRIM19 3 4
  • RNF71 3 4
  • Promyelocytic Leukemia, Inducer Of 3
  • Probable Transcription Factor PML 3
  • Tripartite Motif Protein TRIM19 3
  • Protein PML 3

External Ids for PML Gene

Previous GeneCards Identifiers for PML Gene

  • GC15P070307
  • GC15P067403
  • GC15P071862
  • GC15P072002
  • GC15P072074
  • GC15P074287
  • GC15P051118

Summaries for PML Gene

Entrez Gene Summary for PML 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. [provided by RefSeq, Jul 2008]

GeneCards Summary for PML Gene

PML (Promyelocytic Leukemia) is a Protein Coding gene. Diseases associated with PML include leukemia and neuronal intranuclear inclusion disease. Among its related pathways are Pathways in cancer and Apoptotic Pathways in Synovial Fibroblasts. GO annotations related to this gene include protein homodimerization activity and transcription coactivator activity.

UniProtKB/Swiss-Prot for PML Gene

  • 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. 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

  • 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 (HCMV) 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

Gene Wiki entry for PML Gene

No data available for Tocris Summary , PharmGKB "VIP" Summary , fRNAdb sequence ontologies and piRNA Summary for PML Gene

Genomics for PML Gene

Regulatory Elements for PML Gene

Transcription factor binding sites by QIAGEN in the PML gene promoter:

Epigenetics Products

  • DNA Methylation CpG Assay Predesigned for Pyrosequencing in human,mouse,rat

Genomic Location for PML Gene

Start:
73,994,673 bp from pter
End:
74,047,819 bp from pter
Size:
53,147 bases
Orientation:
Plus strand

Genomic View for PML Gene

UCSC Golden Path with GeneCards custom track
Cytogenetic band:
Genomic Location for PML Gene
GeneLoc Logo Genomic Neighborhood Exon StructureGene Density

RefSeq DNA sequence for PML Gene

Proteins for PML Gene

  • Protein details for PML Gene (UniProtKB/Swiss-Prot)

    Protein Symbol:
    P29590-PML_HUMAN
    Recommended name:
    Protein PML
    Protein Accession:
    P29590
    Secondary Accessions:
    • E9PBR7
    • P29591
    • P29592
    • P29593
    • Q00755
    • Q15959
    • Q59FP9
    • Q8WUA0
    • Q96S41
    • Q9BPW2
    • Q9BWP7
    • Q9BZX6
    • Q9BZX7
    • Q9BZX8
    • Q9BZX9
    • Q9BZY0
    • Q9BZY2
    • Q9BZY3

    Protein attributes for PML Gene

    Size:
    882 amino acids
    Molecular mass:
    97551 Da
    Quaternary structure:
    • Key component of PML bodies. PML bodies are formed by the interaction of PML homodimers (via SUMO-binding motif) with sumoylated PML, leading to the assembly of higher oligomers. Several types of PML bodies have been observed. PML bodies can form hollow spheres that can sequester target proteins inside. Interacts (via SUMO-binding motif) with sumoylated proteins. Interacts (via C-terminus) with p53/TP53. Recruits p53/TP53 and CHEK2 into PML bodies, which promotes p53/TP53 phosphorylation at Ser-20 and prevents its proteasomal degradation. Interacts with MDM2, and sequesters MDM2 in the nucleolus, thereby preventing ubiquitination of p53/TP53. Interaction with PML-RARA oncoprotein and certain viral proteins causes disassembly of PML bodies and abolishes the normal PML function. Interacts with HIPK2, TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts with ITPR3. Interacts (in the cytoplasm) with TGFBR1, TGFBR2 and PKM. Interacts (via the coiled-coil domain and when sumoylated) with SATB1. Interacts with UBE2I; the interaction is enhanced by arsenic binding. Interacts (PML-RARA oncoprotein, via the coiled-coil domain) with UBE2I; the interaction is enhanced by arsenic binding and is required for PML-RARA oncoprotein sumoylation and inhibition of RARA transactivational activity. Interacts with RB1, PPP1A, SMAD2, SMAD3, DAXX, RPL11 and MTOR. Interacts with PPARGC1A and KAT2A. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 interact with RNF4. Isoform PML-1 interacts with NLRP3. Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5 interact with MAGEA2, RBL2, PER2 and E2F4. Isoform PML-2 interacts with CIITA. Isoform PML-2, isoform PML-3 and isoform PML-4 interact with TBX2. Isoform PML-4 interacts with RANBP2, HDAC7, KAT6A, WRN, PIN1, TBX3 and phosphorylated MAPK1/ERK2. Isoform PML-4 interacts with the CTNNB1 and TCF7L2/TCF4 complex. Isoform PML-4 preferentially interacts with MAPK7/BMK1 although other isoforms (isoform PML-1, isoform PML-2, isoform PML-3 and isoform PML-6) also interact with it. Isoform PML-12 interacts with PIAS1, PIAS2 (isoform PIAS2-alpha) and CSNK2A1/CK2. Isoform PML-3 interacts with HFV bel1/tas and bet. Isoform PML-4 interacts with VZV capsid protein VP26/ORF23 capsid protein. Ths sumoylated isoform PML-4 interacts with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-POL (P3D-POL). Isoform PML-1 interacts with herpes simplex virus-1 (HHV-1) ICP0. Isoform PML-2 interacts with human adenovirus 2 E1A and this interaction stimulates E1A-dependent transcriptional activation. Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT).
    SequenceCaution:
    • Sequence=AAA60351.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAA60352.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAA60388.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAA60390.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAB62809.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; Sequence=BAD92648.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};

    Three dimensional structures from OCA and Proteopedia for PML Gene

    Alternative splice isoforms for PML Gene

neXtProt entry for PML Gene

Proteomics data for PML Gene at MOPED

Post-translational modifications for PML Gene

  • Acetylation at Lys-487 is essential for its nuclear localization. Deacetylated at Lys-487 by SIRT1 and this deacetylation promotes PML control of PER2 nuclear localization.
  • Phosphorylation is a major regulatory mechanism that controls PML protein abundance and the number and size of PML nuclear bodies (PML-NBs). Phosphorylated in response to DNA damage, probably by ATR. HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage. CHEK2-mediated phosphorylation at Ser-117 is important for PML-mediated apopotosis following DNA damage. MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation. CK2-mediated phosphorylation at Ser-565 primes PML ubiquitination via an unidentified ubiquitin ligase.
  • Sumoylation regulates PMLs: stability in response to extracellular or intracellular stimuli, transcription directly and indirectly, through sequestration of or dissociation of the transcription factors from PML-NBs, ability to regulate apoptosis and its anti-viral activities. It is also essential for: maintaining proper PML nuclear bodies (PML-NBs) structure and normal function, recruitment of components of PML-NBs, the turnover and retention of PML in PML-NBs and the integrity of PML-NBs. Undergoes Lys-11-linked sumoylation. Sumoylation on all three sites (Lys-65, Lys-160 and Lys-490) is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. Lys-65 and Lys-160 are sumoylated by PISA1 and PIAS2. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-565 which in turn triggers its ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML-RARA promotes its ubiquitin-mediated degradation. The PML-RARA fusion protein requires the coiled-coil domain for sumoylation. Sumoylation at Lys-490 by RANBP2 is essential for the proper assembly of PML-NBs. DNA damage triggers its sumoylation while some but not all viral infections can abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6. Arsenic induces PML and PML-RARA polysumoylation and their subsequent RNF4-dependent ubiquitination and proteasomal degradation, and is used as treatment in acute promyelocytic leukemia (APL). The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6) show an increased sumoylation in response to arsenic trioxide. The cytoplasmic isoform PML-7 is not sumoylated.
  • Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-518 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20. Lys-6-, Lys-11-, Lys-48- and Lys-63-linked polyubiquitination by RNF4 is polysumoylation-dependent.
  • Ubiquitination at Lys380, Lys394, Lys400, Lys401, Lys426, Lys476, and Lys623
  • Modification sites at PhosphoSitePlus

Antibody Products

No data available for DME Specific Peptides for PML Gene

Domains for PML Gene

Gene Families for PML Gene

HGNC:
  • RNF :RING-type (C3HC4) zinc fingers
  • TRIM :Tripartite motif containing / Tripartite motif containing

Suggested Antigen Peptide Sequences for PML Gene

Graphical View of Domain Structure for InterPro Entry

P29590

UniProtKB/Swiss-Prot:

PML_HUMAN :
  • P29590
Domain:
  • The coiled-coil domain mediates a strong homo/multidimerization activity essential for core assembly of PML-NBs. Interacts with PKM via its coiled-coil domain (PubMed:18298799).
  • The B box-type zinc binding domain and the coiled-coil domain mediate its interaction with PIAS1.
  • Binds arsenic via the RING-type zinc finger. The RING-type zinc finger is essential for its interaction with HFV bel1/tas (PubMed:11432836).
  • The unique C-terminal domains of isoform PML-2 and isoform PML-5 play an important role in regulating the localization, assembly dynamics, and functions of PML-NBs.
  • The Sumo interaction motif (SIM) is required for efficient ubiquitination, recruitment of proteasome components within PML-NBs and PML degradation in response to arsenic trioxide.
Similarity:
  • Contains 2 B box-type zinc fingers.
  • Contains 1 RING-type zinc finger.
genes like me logo Genes that share domains with PML: view

Function for PML Gene

Molecular function for PML Gene

GENATLAS Biochemistry: POD (promyelocytic oncogenic domain),nuclear matrix protein,B box family, colocalizing and interacting with CREBBP,TIF2A and with DAXX in special (PML/SP100) nuclear bodies(NB/POD), to form a retinoic acid (RA) dependent growth suppressive RRXA,RARA nuclear complex,involved in development,recombinaison,DNA repair,and in early hematopoiesis and late erythropoiesis,recruiting the nuclear corepressor histone deacetylase complex,essential for multiple apoptotic pathways,putative controller of genes devoted to MHC class I antigen presentation.
UniProtKB/Swiss-Prot Function: 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. 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
UniProtKB/Swiss-Prot 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 (HCMV) 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
UniProtKB/Swiss-Prot Induction: By interferons alpha, beta and gamma. Up-regulated by IRF3 and p53/TP53

Gene Ontology (GO) - Molecular Function for PML Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0003677 DNA binding IEA --
GO:0003713 transcription coactivator activity IDA 11080164
GO:0005515 protein binding IPI 10597310
GO:0008270 zinc ion binding IEA --
GO:0031625 ubiquitin protein ligase binding IPI 12915590
genes like me logo Genes that share ontologies with PML: view
genes like me logo Genes that share phenotypes with PML: view

Animal Models for PML Gene

MGI Knock Outs for PML:

Animal Model Products

CRISPR Products

miRNA for PML Gene

No data available for Enzyme Numbers (IUBMB) , Transcription Factor Targeting and HOMER Transcription for PML Gene

Localization for PML Gene

Subcellular locations from UniProtKB/Swiss-Prot for PML Gene

Nucleus. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Isoform PML-1 can shuttle between the nucleus and cytoplasm. Isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 are nuclear isoforms whereas isoform PML-7 and isoform PML-14 lacking the nuclear localization signal are cytoplasmic isoforms. Detected in the nucleolus after DNA damage. Acetylation at Lys-487 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein.

Subcellular locations from

COMPARTMENTS
Jensen Localization Image for PML Gene COMPARTMENTS Subcellular localization image for PML gene
Compartment Confidence
endoplasmic reticulum 5
endosome 5
nucleus 5
cytosol 4

Gene Ontology (GO) - Cellular Components for PML Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0005622 intracellular --
GO:0005634 nucleus IDA 16778193
GO:0005654 nucleoplasm TAS --
GO:0005730 nucleolus IDA 15195100
GO:0005737 cytoplasm IDA 16778193
genes like me logo Genes that share ontologies with PML: view

Pathways for PML Gene

genes like me logo Genes that share pathways with PML: view

PCR Array Products

Gene Ontology (GO) - Biological Process for PML Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0001666 response to hypoxia IDA 16915281
GO:0001932 regulation of protein phosphorylation ISS --
GO:0002230 positive regulation of defense response to virus by host IMP 16873256
GO:0006351 transcription, DNA-templated IEA --
GO:0006355 regulation of transcription, DNA-templated IMP 23007646
genes like me logo Genes that share ontologies with PML: view

Compounds for PML Gene

(18) Novoseek inferred chemical compound relationships for PML Gene

Compound -log(P) Hits PubMed IDs
retinoic acid 87.5 120
alpha-retinoic acid 81.6 3
arsenite 72 7
pic 1 68.3 3
retinoid 65.1 3

(2) PharmGKB related drug/compound annotations for PML Gene

Drug/compound Annotation
arsenic trioxide
tretinoin
genes like me logo Genes that share compounds with PML: view

Transcripts for PML Gene

Unigene Clusters for PML Gene

Promyelocytic leukemia:
Representative Sequences:

CRISPR Products

Inhibitory RNA Products

  • Predesigned siRNA for gene silencing in human,mouse,rat for PML

Primer Products

Flow Cytometry Products

Alternative Splicing Database (ASD) splice patterns (SP) for PML Gene

ExUns: 1a · 1b · 1c · 1d · 1e ^ 2 ^ 3a · 3b · 3c · 3d · 3e ^ 4 ^ 5 ^ 6a · 6b ^ 7a · 7b ^ 8a · 8b · 8c · 8d · 8e · 8f ^ 9a · 9b · 9c ^
SP1: - - - - - - - - - -
SP2: - - - - - - - -
SP3: - - - - - - - - - - -
SP4: - -
SP5: - - - - - - -
SP6: - - - -
SP7: - - -
SP8: -
SP9: - - - - - - - - -
SP10: - - - - -
SP11: - - - - - - - - - -
SP12: - - -
SP13: - - -
SP14: -
SP15: -
SP16: -

ExUns: 10a · 10b
SP1:
SP2:
SP3:
SP4:
SP5:
SP6:
SP7:
SP8:
SP9:
SP10:
SP11:
SP12:
SP13:
SP14:
SP15:
SP16:

Relevant External Links for PML Gene

GeneLoc Exon Structure for
PML
ECgene alternative splicing isoforms for
PML

Expression for PML Gene

mRNA expression in normal human tissues for PML Gene

mRNA expression in embryonic tissues and stem cells from LifeMap Discovery

Integrated Proteomics: protein expression from ProteomicsDB, PaxDb, MOPED, and MaxQB for PML Gene

SOURCE GeneReport for Unigene cluster for PML Gene Hs.526464

genes like me logo Genes that share expressions with PML: view

In Situ Assay Products

No data available for mRNA differential expression in normal tissues and mRNA Expression by UniProt/SwissProt for PML Gene

Orthologs for PML Gene

This gene was present in the common ancestor of chordates.

Orthologs for PML Gene

Organism Taxonomy Gene Similarity Type Details
chimpanzee
(Pan troglodytes)
Mammalia PML 35
  • 99.62 (n)
  • 99.89 (a)
PML 36
  • 100 (a)
OneToOne
cow
(Bos Taurus)
Mammalia PML 36
  • 76 (a)
OneToOne
dog
(Canis familiaris)
Mammalia PML 35
  • 84.09 (n)
  • 77.84 (a)
PML 36
  • 77 (a)
OneToOne
mouse
(Mus musculus)
Mammalia Pml 35
  • 77.71 (n)
  • 71.33 (a)
Pml 16
Pml 36
  • 68 (a)
OneToOne
oppossum
(Monodelphis domestica)
Mammalia PML 36
  • 35 (a)
OneToOne
platypus
(Ornithorhynchus anatinus)
Mammalia PML 36
  • 53 (a)
OneToOne
rat
(Rattus norvegicus)
Mammalia Pml 35
  • 78.76 (n)
  • 72.29 (a)
chicken
(Gallus gallus)
Aves -- 36
  • 44 (a)
OneToMany
-- 36
  • 36 (a)
OneToMany
LOC100857563 35
  • 54.29 (n)
  • 40.29 (a)
Species with no ortholog for PML:
  • A. gosspyii yeast (Ashbya gossypii)
  • Actinobacteria (Mycobacterium tuberculosis)
  • African clawed frog (Xenopus laevis)
  • African malaria mosquito (Anopheles gambiae)
  • Alicante grape (Vitis vinifera)
  • alpha proteobacteria (Wolbachia pipientis)
  • amoeba (Dictyostelium discoideum)
  • Archea (Pyrococcus horikoshii)
  • baker's yeast (Saccharomyces cerevisiae)
  • barley (Hordeum vulgare)
  • beta proteobacteria (Neisseria meningitidis)
  • bread mold (Neurospora crassa)
  • Chromalveolata (Phytophthora infestans)
  • common water flea (Daphnia pulex)
  • corn (Zea mays)
  • E. coli (Escherichia coli)
  • filamentous fungi (Aspergillus nidulans)
  • Firmicute bacteria (Streptococcus pneumoniae)
  • fission yeast (Schizosaccharomyces pombe)
  • fruit fly (Drosophila melanogaster)
  • green algae (Chlamydomonas reinhardtii)
  • honey bee (Apis mellifera)
  • K. lactis yeast (Kluyveromyces lactis)
  • lizard (Anolis carolinensis)
  • loblloly pine (Pinus taeda)
  • malaria parasite (Plasmodium falciparum)
  • medicago trunc (Medicago Truncatula)
  • moss (Physcomitrella patens)
  • orangutan (Pongo pygmaeus)
  • pig (Sus scrofa)
  • rainbow trout (Oncorhynchus mykiss)
  • rice (Oryza sativa)
  • rice blast fungus (Magnaporthe grisea)
  • schistosome parasite (Schistosoma mansoni)
  • sea anemone (Nematostella vectensis)
  • sea squirt (Ciona intestinalis)
  • sea squirt (Ciona savignyi)
  • sea urchin (Strongylocentrotus purpuratus)
  • sorghum (Sorghum bicolor)
  • soybean (Glycine max)
  • stem rust fungus (Puccinia graminis)
  • sugarcane (Saccharum officinarum)
  • thale cress (Arabidopsis thaliana)
  • tomato (Lycopersicon esculentum)
  • toxoplasmosis (Toxoplasma gondii)
  • Trichoplax (Trichoplax adhaerens)
  • tropical clawed frog (Silurana tropicalis)
  • wheat (Triticum aestivum)
  • worm (Caenorhabditis elegans)
  • zebrafish (Danio rerio)

Evolution for PML Gene

ENSEMBL:
Gene Tree for PML (if available)
TreeFam:
Gene Tree for PML (if available)

Paralogs for PML Gene

genes like me logo Genes that share paralogs with PML: view

No data available for Paralogs for PML Gene

Variants for PML Gene

Sequence variations from dbSNP and Humsavar for PML Gene

SNP ID Clin Chr 15 pos Sequence Context AA Info Type MAF
rs6772 -- 74,046,598(+) TAAAA(C/T)AGGCG utr-variant-3-prime
rs9479 -- 74,036,235(+) CCTGT(A/G)TTCTG intron-variant, utr-variant-3-prime
rs11272 -- 74,043,070(+) TGGAC(A/G/T)AGAAC missense, reference, stop-gained, utr-variant-3-prime
rs16869 -- 74,030,090(+) TGCCT(C/T)AACTC intron-variant
rs743580 -- 74,035,775(+) GGGAA(A/C/G)GCAGA intron-variant, reference, missense, utr-variant-3-prime

Structural Variations from Database of Genomic Variants (DGV) for PML Gene

Variant ID Type Subtype PubMed ID
dgv756e1 CNV Complex 17122850
nsv428308 CNV Gain+Loss 18775914
nsv833052 CNV Gain+Loss 17160897
nsv518316 CNV Gain 19592680
nsv469619 CNV Loss 16826518
nsv457203 CNV Loss 19166990
nsv509575 CNV Insertion 20534489
nsv510666 CNV Loss 20534489
nsv817697 CNV Gain 17921354

Relevant External Links for PML Gene

HapMap Linkage Disequilibrium report
PML
Human Gene Mutation Database (HGMD)
PML

No data available for Polymorphic Variants from UniProtKB/Swiss-Prot for PML Gene

Disorders for PML Gene

MalaCards: The human disease database

MalaCards: The human disease database. (3) Diseases for PML Gene including...

Search for PML Gene in MalaCards »

UniProtKB/Swiss-Prot

PML_HUMAN
  • Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon. {ECO:0000269 PubMed:1652369, ECO:0000269 PubMed:1720570}.

(1) University of Copenhagen DISEASES for PML Gene

(37) Novoseek inferred disease relationships for PML Gene

Disease -log(P) Hits PubMed IDs
promyelocytic leukemia 96.3 121
leukemia promyelocytic acute 95.6 119
leukemogenesis 72.4 7
leukemia 68.7 50
minimal residual disease 60.9 4

Genatlas disease for PML Gene

acute promyelocytic leukemia (APL) with translocation t(15;17)(q22;q12) and with poor prognosis,may be associated with a hemorrhagic diathesis,secundary to an overexpression of annexin II with a secundary itinease of plasmin (see RARA)

Relevant External Links for PML

Genetic Association Database (GAD)
PML
Human Genome Epidemiology (HuGE) Navigator
PML
Tumor Gene Database (TGDB):
PML
genes like me logo Genes that share disorders with PML: view

Publications for PML Gene

  1. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. (PMID: 1652368) Kakizuka A. … Evans R.M. (Cell 1991) 3 4 23
  2. Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. (PMID: 1720570) Goddard A.D. … Solomon E. (Science 1991) 3 4 23
  3. 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. (PMID: 1311253) Kastner P. … Chambon P. (EMBO J. 1992) 3 4 23
  4. Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants. (PMID: 1312695) Tong J.H. … Berger R. (Oncogene 1992) 3 4 23
  5. Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. (PMID: 9570750) Cao T. … Etkin L.D. (J. Cell Sci. 1998) 3 4 23

Products for PML Gene

  • Addgene plasmids for PML

Sources for PML Gene

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