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PML Gene

protein-coding   GIFtS: 69
GCID: GC15P074287

Promyelocytic Leukemia

  See related diseases
at  

(According to 1HGNC, 2Entrez Gene,
3UniProtKB/Swiss-Prot, 4UniProtKB/TrEMBL, 5OMIM, 6GeneLoc, 7Ensembl, 8DME, 9miRBase, 10fRNAdb, 12H-InvDB, 13NCBI, 14NONCODE, and/or 15RNAdb)
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Aliases
Promyelocytic Leukemia1 2     TRIM192 3
MYL2 3 5     RING Finger Protein 712 3
Promyelocytic Leukemia Protein2 3     Probable Transcription Factor PML2
Tripartite Motif-Containing Protein 192 3     Promyelocytic Leukemia, Inducer Of2
PP86752 3     Protein PML2
RNF712 3     Tripartite Motif Protein TRIM192

External Ids:    HGNC: 91131   Entrez Gene: 53712   Ensembl: ENSG000001404647   OMIM: 1025785   UniProtKB: P295903   

Export aliases for PML gene to outside databases

Previous GC identifers: GC15P070307 GC15P067403 GC15P071862 GC15P072002 GC15P072074 GC15P051118


(According to Entrez Gene, GeneCards, Tocris Bioscience, Wikipedia's Gene Wiki, PharmGKB,
UniProtKB/Swiss-Prot, and/or UniProtKB/TrEMBL)
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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, acute promyelocytic, pml/rara type, and acute promyelocytic leukemia. GO annotations related to this gene include transcription coactivator activity and protein homodimerization activity.

UniProtKB/Swiss-Prot: PML_HUMAN, P29590
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
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

Gene Wiki entry for PML (Promyelocytic leukemia protein) Gene


(According to GeneLoc and/or HGNC, and/or
Entrez Gene (NCBI build 37),
and/or miRBase,
Genomic Views according to UCSC (hg19) and Ensembl (release 75), Regulatory elements and Epigenetics data according to QIAGEN, and/or SwitchGear Genomics)
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RefSeq DNA sequence:
NC_000015.10  NC_018926.2  NT_010194.18  
Regulatory elements:
   Regulatory transcription factor binding sites in the PML gene promoter:
         AML1a   STAT3   
         Other transcription factors

SwitchGear Promoter luciferase reporter plasmids (see all 2): PML promoter sequence
   Search Chromatin IP Primers for PML

Epigenetics:
DNA Methylation CpG Assay Predesigned for Pyrosequencing in human, mouse, rat PML


Genomic Location:
Genomic View: UCSC Golden Path with GeneCards custom track

Entrez Gene cytogenetic band: 15q22   Ensembl cytogenetic band:  15q24.1   HGNC cytogenetic band: 15q24.1

PML Gene in genomic location: bands according to Ensembl, locations according to (and/or Entrez Gene and/or Ensembl if different)
PML gene location

GeneLoc information about chromosome 15         GeneLoc Exon Structure

GeneLoc location for GC15P074287:  view genomic region     (about GC identifiers)

Start:
74,287,014 bp from pter      End:
74,340,160 bp from pter
Size:
53,147 bases      Orientation:
plus strand

(According to 1UniProtKB, HORDE, 2neXtProt, Ensembl, and/or Reactome, Modification sites according to PhosphoSitePlus, Specific Peptides from DME, RefSeq according to NCBI, PDB rendering according to OCA and/or Proteopedia, Recombinant Proteins from EMD Millipore, R&D Systems, GenScript, Enzo Life Sciences, OriGene, Novus Biologicals, Sino Biological, ProSpec, and/or Cloud-Clone Corp.,
Biochemical Assays by EMD Millipore, R&D Systems, OriGene, GenScript, Cell Signaling Technology, Enzo Life Sciences, and/or Cloud-Clone Corp., Antibodies by EMD Millipore, R&D Systems, Cell Signaling Technology, OriGene, Novus Biologicals, Thermo Fisher Scientific, LSBio, Abcam, Cloud-Clone Corp, and/or others.)
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UniProtKB/Swiss-Prot: PML_HUMAN, P29590 (See protein sequence)
Recommended Name: Protein PML  
Size: 882 amino acids; 97551 Da
Subunit: 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)
Sequence caution: Sequence=AAA60351.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
Sequence=AAA60352.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=AAA60388.1;
Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=AAA60390.1; Type=Erroneous
initiation; Note=Translation N-terminally extended; Sequence=BAB62809.1; Type=Miscellaneous discrepancy;
Note=Chimeric cDNA; Sequence=BAD92648.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
1 PDB 3D structure from and Proteopedia for PML:
1BOR (3D)    
Secondary accessions: E9PBR7 P29591 P29592 P29593 Q00755 Q15959 Q59FP9 Q8WUA0 Q96S41 Q9BPW2
Q9BWP7 Q9BZX6 Q9BZX7 Q9BZX8 Q9BZX9 Q9BZY0 Q9BZY2 Q9BZY3
Alternative splicing: 12 isoforms:  P29590-1   P29590-8   P29590-9   P29590-5   P29590-2   P29590-4   P29590-10   P29590-3   
P29590-11   P29590-12   P29590-13   P29590-14   (No experimental confirmation available)

Explore the universe of human proteins at neXtProt for PML: NX_P29590

Explore proteomics data for PML at MOPED

Post-translational modifications: 

  • Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, KLHL20-based E3 ligase complex, SIAH1 or SIAH2 and leading to
    subsequent proteasomal degradation. Ubiquitination by KLHL20-based 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-dependent1
  • Sumoylation regulates PML's: 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 sumoylated1
  • 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
    ligase1
  • 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 localization1
  • Ubiquitination2 at Lys380, Lys394, Lys400, Lys401, Lys426, Lys476, Lys623
  • Modification sites at PhosphoSitePlus

  • See PML Protein Expression from SPIRE MOPED, PaxDB, and MaxQB

    REFSEQ proteins (9 alternative transcripts): 
    NP_002666.1  NP_150241.2  NP_150242.1  NP_150243.2  NP_150247.2  NP_150249.1  NP_150250.2  NP_150252.1  
    NP_150253.2  

    ENSEMBL proteins: 
     ENSP00000378567   ENSP00000378564   ENSP00000268059   ENSP00000315434   ENSP00000268058  
     ENSP00000455838   ENSP00000455612   ENSP00000456486   ENSP00000456277   ENSP00000394642  
     ENSP00000395576   ENSP00000457023   ENSP00000353004   ENSP00000457032   ENSP00000456989  
     ENSP00000457669   ENSP00000458061   ENSP00000456329  
    Reactome Protein details: P29590

    PML Human Recombinant Protein Products:

    Browse Purified and Recombinant Proteins at EMD Millipore
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    Browse recombinant and purified proteins available from Enzo Life Sciences
    OriGene Purified Proteins for PML
    OriGene Protein Over-expression Lysate for PML
    OriGene MassSpec for PML
    OriGene Custom Protein Services for PML
    GenScript Custom Purified and Recombinant Proteins Services for PML
    Novus Biologicals PML Protein
    Novus Biologicals PML Lysate
    Browse Sino Biological Recombinant Proteins
    Browse Sino Biological Cell Lysates
    Browse ProSpec Recombinant Proteins
    Cloud-Clone Corp. Proteins for PML

    PML Antibody Products:

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    OriGene Custom Antibody Services for PML
    Novus Biologicals PML Antibodies
    Abcam antibodies for PML (P29590, P10276)
    Cloud-Clone Corp. Antibodies for PML
    ThermoFisher Antibodies for PML
    LSBio Antibodies in human, mouse, rat for PML

    PML Assay Products:

    Browse Kits and Assays available from EMD Millipore
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    Browse R&D Systems for biochemical assays
    GenScript Custom Assay Services for PML
    Browse Enzo Life Sciences for kits & assays
    Cloud-Clone Corp. ELISAs for PML
    Cloud-Clone Corp. CLIAs for PML


    (According to HGNC, IUPHAR, InterPro, ProtoNet, UniProtKB, and/or BLOCKS, Sets of similar genes according to GeneDecks)
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    HGNC Gene Families:
    TRIM: Tripartite motif containing / Tripartite motif containing
    RNF: RING-type (C3HC4) zinc fingers

    5 InterPro protein domains:
     IPR021978 DUF3583
     IPR001841 Znf_RING
     IPR013083 Znf_RING/FYVE/PHD
     IPR017907 Znf_RING_CS
     IPR000315 Znf_B-box

    Graphical View of Domain Structure for InterPro Entry P29590

    ProtoNet protein and cluster: P29590

    2 Blocks protein domains:
    IPB000315 B-box zinc finger signature
    IPB001841 Zn-finger


    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)
    Domain: The B box-type zinc binding domain and the coiled-coil domain mediate its interaction with PIAS1
    (PubMed:22406621)
    Domain: Binds arsenic via the RING-type zinc finger. The RING-type zinc finger is essential for its interaction
    with HFV bel1/tas (PubMed:11432836)
    Domain: 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 (PubMed:22773875)
    Domain: 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 (PubMed:23028697)
    Similarity: Contains 2 B box-type zinc fingers
    Similarity: Contains 1 RING-type zinc finger


    PML for domains           About GeneDecksing


    (According to 1UniProtKB, Genatlas, LifeMap Discovery™, IUBMB, and/or 2DME, Human phenotypes from GenomeRNAi, Animal models from MGI Mar 06 2013, inGenious Targeting Laboratory, genOway,
    transcription factor targeting from QIAGEN and/or HOMER, miRNA Gene Targets from miRTarBase, shRNA from OriGene, siRNAs from OriGene, QIAGEN, microRNA from QIAGEN, SwitchGear Genomics, Gene Editing from DNA2.0, Clones from OriGene, GenScript, Sino Biological, DNA2.0, and Vector BioLabs, Cell Lines from GenScript, ESI BIO, In Situ Hybridization Assays from Advanced Cell Diagnostics, Ontologies according to Gene Ontology Consortium 01 Apr 2014 via Entrez Gene.)
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    Molecular Function:

         UniProtKB/Swiss-Prot Summary: PML_HUMAN, P29590
    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
    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
    Induction: By interferons alpha, beta and gamma. Up-regulated by IRF3 and p53/TP53

         Genatlas biochemistry entry for PML:
    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.

         Gene Ontology (GO): Selected molecular function terms (see all 10):    About this table

    GO IDQualified GO termEvidencePubMed IDs
    GO:0003677DNA binding IEA--
    GO:0003713transcription coactivator activity IDA11080164
    GO:0005515protein binding IPI10597310
    GO:0008270zinc ion binding IEA--
    GO:0031625ubiquitin protein ligase binding IPI12915590
         
    PML for ontologies           About GeneDecksing


    Phenotypes:
         2 GenomeRNAi human phenotypes for PML:
     Decreased viability of wild-ty  Increased S DNA content 

         7 MGI mutant phenotypes (inferred from 3 alleles(MGI details for Pml):
     cellular  hematopoietic system  immune system  mortality/aging  no phenotypic analysis 
     normal  tumorigenesis 

    PML for phenotypes           About GeneDecksing

    Animal Models:
         MGI mouse knock-out Pmltm1Ppp for PML

       inGenious Targeting Laboratory: Let us create your new Knockout/Knockin mouse model for PML
       inGenious Targeting Laboratory: Contact us about creating complex and humanized mouse models for PML

       genOway customized KO model: permanent, tissue-specific or time-controlled inactivation for PML
       genOway customized Knockin model: humanization, point mutation, expression monitoring, etc. for PML

    miRNA
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    miRTarBase miRNAs that target PML:
    hsa-mir-378a-3p (MIRT043919), hsa-mir-423-3p (MIRT042535), hsa-mir-335-5p (MIRT018318)

    Block miRNA regulation of human, mouse, rat PML using miScript Target Protectors
    Selected qRT-PCR Assays for microRNAs that regulate PML (see all 14):
    hsa-miR-1266 hsa-miR-323b-3p hsa-miR-133b hsa-miR-221* hsa-miR-124 hsa-miR-214 hsa-miR-149 hsa-miR-133a
    SwitchGear 3'UTR luciferase reporter plasmidPML 3' UTR sequence
    Inhib. RNA
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    Gene Editing
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    GenScript: all cDNA clones in your preferred vector (see all 9): PML (NM_033244)
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    In Situ Assay
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    Advanced Cell Diagnostics RNAscope RNA in situ hybridization assays for PML


    (According to UniProtKB, COMPARTMENTS Subcellular localization database, Ontologies according to Gene Ontology Consortium 01 Apr 2014 via Entrez Gene.)
    About This Section

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    Subcellular locations from UniProtKB/Swiss-Prot
    PML_HUMAN, P29590: Nucleus. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus. Endoplasmic
    reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). 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: 

    CompartmentConfidence
    endoplasmic reticulum5
    endosome5
    nucleus5
    cytosol4

    Gene Ontology (GO): Selected cellular component terms (see all 11):    About this table

    GO IDQualified GO termEvidencePubMed IDs
    GO:0005622intracellular ----
    GO:0005634nucleus IDA--
    GO:0005654nucleoplasm TAS--
    GO:0005730NOT nucleolus IDA--
    GO:0005737cytoplasm IDA16778193

    PML for ontologies           About GeneDecksing


    (SuperPaths according to PathCards, Pathways according to R&D Systems, Cell Signaling Technology, KEGG, PharmGKB, BioSystems, Sino Biological, Reactome, Tocris Bioscience, GeneGo (Thomson Reuters), QIAGEN, and/or UniProtKB, Sets of similar genes according to GeneDecks, Interaction Networks according to QIAGEN, and/or STRING, Interactions according to 1UniProtKB, 2MINT, 3I2D, and/or 4STRING, with links to IntAct and Ensembl, Ontologies according to Gene Ontology Consortium 01 Apr 2014 via Entrez Gene).
    About This Section

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    SuperPaths for PML About   (see all 19)  
    See pathways by source

    SuperPathContained pathways About
    1Interferon Signaling
    Interferon Signaling0.59
    Interferon gamma signaling0.41
    Cytokine Signaling in Immune system0.59
    2Proteolysis Putative SUMO 1 pathway
    DNA damage Role of SUMO in p53 regulation0.33
    Proteolysis Putative SUMO 1 pathway0.33
    3Influenza A
    Influenza A0.34
    Herpes simplex infection0.33
    4Apoptotic Pathways in Synovial Fibroblasts
    Cellular Apoptosis Pathway0.85
    5Immune response IFN alpha beta signaling pathway
    Immune response IFN alpha beta signaling pathway0.69

    Pathways by source                                                                                                                                                                 See SuperPaths
    Show all pathways

    3 Downloadable PowerPoint Slides of GeneGlobe Pathway Central Maps for PML
        p53 Signaling
    Cellular Apoptosis Pathway
    SUMO Pathway

    3 GeneGo (Thomson Reuters) Pathways for PML
        Proteolysis Putative SUMO-1 pathway
    DNA damage Role of SUMO in p53 regulation
    Immune response IFN alpha/beta signaling pathway

    Selected BioSystems Pathways for PML (see all 7)
        DNA damage response
    Integrated Breast Cancer Pathway
    TNF-alpha/NF-kB Signaling Pathway
    Integrated Pancreatic Cancer Pathway
    mTOR signaling pathway

    1 Reactome Pathway for PML
        Interferon gamma signaling


    Selected Kegg Pathways  (Kegg details for PML) (see all 7):
        Ubiquitin mediated proteolysis
    Endocytosis
    Influenza A
    Herpes simplex infection
    Pathways in cancer


    PML for pathways           About GeneDecksing

        Pathway & Disease-focused RT2 Profiler PCR Arrays including PML: 
              Oncogenes & Tumor Suppressor Genes in human mouse rat
              Leukemia in human mouse rat
              Type I Interferon Response in human mouse rat
              Apoptosis 384HT in human mouse rat
              Ubiquitin Ligases in human mouse rat

    Interactions:

        GeneGlobe Interaction Network for PML

    STRING Interaction Network Preview (showing 5 interactants - click image to see 25)

    Selected Interacting proteins for PML (P295901, 2, 3 ENSP000002680584) via UniProtKB, MINT, STRING, and/or I2D (see all 218)
    InteractantInteraction Details
    GeneCardExternal ID(s)
    MDM2Q009871, 2, 3, ENSP000004172814EBI-295890,EBI-389668 MINT-4793330 MINT-4793420 MINT-4793448 I2D: score=5 STRING: ENSP00000417281
    TP53P046371, 2, 3, ENSP000002693054EBI-295890,EBI-366083 MINT-4793478 MINT-4793489 I2D: score=5 STRING: ENSP00000269305
    ENSG00000231617Q9UER71, 3, ENSP000004046234EBI-295890,EBI-77321 I2D: score=6 STRING: ENSP00000404623
    ENSG00000206206Q9UER71, 3EBI-295890,EBI-77321 I2D: score=6 
    ENSG00000206279Q9UER71, 3EBI-295890,EBI-77321 I2D: score=6 
    About this table

    Gene Ontology (GO): Selected biological process terms (see all 58):    About this table

    GO IDQualified GO termEvidencePubMed IDs
    GO:0001666response to hypoxia IDA16915281
    GO:0001932regulation of protein phosphorylation ISS--
    GO:0002230positive regulation of defense response to virus by host IMP16873256
    GO:0006351transcription, DNA-templated IEA--
    GO:0006355regulation of transcription, DNA-templated IMP--

    PML for ontologies           About GeneDecksing



    (Chemical Compounds according to UniProtKB, Enzo Life Sciences, EMD Millipore, Tocris Bioscience, ApexBio, HMDB, BitterDB, and/or Novoseek, Ligands according to IUPHAR, and Drugs according to DrugBank, Enzo Life Sciences, and/or PharmGKB)
    About This Section

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    Browse Small Molecules at EMD Millipore
       Browse drugs & compounds from Enzo Life Sciences
      Browse compounds at ApexBio 

    Browse Tocris compounds for PML

    Selected Novoseek inferred chemical compound relationships for PML gene (see all 18)    About this table
    Compound   -log (P-Val)   Hits   PubMed IDs for Articles with Shared Sentences (# sentences)
    retinoic acid 87.5 151 16740359 (5), 8400236 (4), 15529177 (3), 7784078 (3) (see all 99)
    alpha-retinoic acid 81.6 3 8396481 (1), 8207983 (1), 7815831 (1)
    arsenite 72 10 16891316 (3), 12667397 (2), 19380586 (1), 18413806 (1)
    pic 1 68.3 3 9658103 (2), 10187798 (1)
    retinoid 65.1 3 8916959 (1), 8649787 (1), 8704214 (1)
    glutamine 21.4 4 12430715 (2), 16409557 (1), 15977647 (1)
    zinc 17.2 9 12794076 (2), 12759344 (1), 17988991 (1), 10938104 (1) (see all 8)
    etoposide 14.5 4 9209367 (1)
    lysine 13 2 20205709 (1)
    bromodeoxyuridine 11.5 1 12773567 (1)

    2 PharmGKB related drug/compound annotations for PML gene    About this table
    Drug/compound PharmGKB Annotation
    arsenic trioxide
    tretinoin



    PML for compounds           About GeneDecksing



    (Secondary structures according to fRNAdb,
    GenBank/EMBL/DDBJ Accessions according to
    Unigene (Build 236 Homo sapiens; Apr 25 2013) or GenBank,
    RefSeq according to Entrez Gene,
    DOTS (version 10), and/or AceView, transcript ids from Ensembl with links to UCSC,
    exon structure from GeneLoc, alternative splicing isoforms according to ASD and/or ECgene,
    siRNAs from OriGene, QIAGEN, shRNA from OriGene, microRNA from QIAGEN, SwitchGear Genomics,
    Tagged/untagged cDNA clones from OriGene, GenScript, DNA2.0, Vector BioLabs, Primers from OriGene, and/or QIAGEN )
    About This Section

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    REFSEQ mRNAs for PML gene (9 alternative transcripts): 
    NM_002675.3  NM_033238.2  NM_033239.2  NM_033240.2  NM_033244.3  NM_033246.2  NM_033247.2  NM_033249.2  
    NM_033250.2  

    Unigene Cluster for PML:

    Promyelocytic leukemia
    Hs.526464  [show with all ESTs]
    Unigene Representative Sequence: NM_033238
    Selected Ensembl transcripts including schematic representations, and UCSC links where relevant (see all 22):
    ENST00000395135(uc002awq.3 uc002awr.3 uc002aws.3 uc002awt.3)
    ENST00000395132(uc002awp.3) ENST00000268059(uc002awk.3 uc002awn.3)
    ENST00000354026(uc002awo.3) ENST00000268058 ENST00000565898(uc002awu.3 uc002awv.3 uc010ule.2)
    ENST00000569477 ENST00000569965 ENST00000567543 ENST00000436891(uc002awx.3)
    ENST00000435786(uc002awm.3 uc002awl.3) ENST00000564428 ENST00000359928
    ENST00000563500(uc002awj.1 uc002awy.3) ENST00000564725(uc002aww.1)
    ENST00000569161 ENST00000565239 ENST00000567606
    miRNA
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    Block miRNA regulation of human, mouse, rat PML using miScript Target Protectors
    Selected qRT-PCR Assays for microRNAs that regulate PML (see all 14):
    hsa-miR-1266 hsa-miR-323b-3p hsa-miR-133b hsa-miR-221* hsa-miR-124 hsa-miR-214 hsa-miR-149 hsa-miR-133a
    SwitchGear 3'UTR luciferase reporter plasmidPML 3' UTR sequence
    Inhib. RNA
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    Predesigned siRNA for gene silencing in human, mouse, rat PML
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    OriGene clones in human, mouse for PML (see all 52)
    OriGene ORF clones in mouse, rat for PML
    OriGene custom cloning services - gene synthesis, subcloning, mutagenesis, variant library, vector shuttling
    GenScript: all cDNA clones in your preferred vector (see all 9): PML (NM_033244)
    DNA2.0 Custom Codon Optimized Gene Synthesis Service for PML
    Vector BioLabs ready-to-use adenovirus/AAV for human, mouse, rat PML
    Primer
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    OriGene qPCR primer pairs and template standards for PML
    OriGene qSTAR qPCR primer pairs in human, mouse for PML
    Pre-validated RT2 qPCR Primer Assay in human, mouse, rat PML
      QuantiTect SYBR Green Assays in human, mouse, rat PML
      QuantiFast Probe-based Assays in human, mouse, rat PML

    Additional mRNA sequence: 

    AB067754.1 AB208950.1 AB209051.1 AB209411.1 AF230401.1 AF230402.1 AF230403.1 AF230404.1 
    AF230405.1 AF230406.1 AF230407.1 AF230408.1 AF230409.1 AF230410.1 AF230411.1 AF370432.1 
    AF388193.1 AF388194.1 AK026871.1 AK300256.1 AK300951.1 BC000080.2 BC020994.2 BC034251.1 
    BC139795.1 BT009911.1 BX647287.1 M73778.1 M79462.1 M79463.1 M79464.1 M80185.1 
    S50913.1 X63131.1 

    24 DOTS entries:

    DT.97791923  DT.447813  DT.100792863  DT.100792859  DT.91792314  DT.91783610  DT.97787374  DT.210086 
    DT.317724  DT.102827730  DT.91836290  DT.100792858  DT.92352534  DT.100792875  DT.91722067  DT.100792857 
    DT.101959716  DT.97772804  DT.100718623  DT.100792873  DT.100792874  DT.92011830  DT.92362935  DT.99993975 

    298 AceView cDNA sequences (see top 24):

    BU753248 BQ642940 CA487430 BI793248 BX647287 CF272229 BE336744 BI757312 
    BQ642937 CR602508 NM_033249 AI160099 BQ919042 NM_033240 BM917894 BM469516 
    BI962511 BI963945 BQ438276 NM_002675 AI469853 AA312138 BI962969 AI146508 
    AI635829 AW451754 BU196211 NM_033246 BU617120 BM021512 BQ933226 BQ054226 
    BQ441173 AW452151 BC034251 AI659853 BQ059293 BU902386 BQ670496 NM_033239 
    AA788922 BF939193 BQ430284 BM127636 BQ052031 AA293080 BU543691 AI744517 
    AI650742 BU633408 AF230406 AI472295 AA234052 CO248567 BI792960 CA503154 
    AF230407 BU727460 AF230402 AI811376 AA417794 AA678328 BU857157 AI761394 
    AK026871 BI789072 AI439653 BQ231406 NM_033244 BV183755 T49642 AW444772 
    BG170901 CD675609 AF230404 AL120723 BE893872 BG760665 BQ669518 AW024593 
    M79462 BM127331 BX355229 BG231723 BC020994 BG491451 BI819943 AI796970 
    AA291742 CO247224 NM_033242 AA291865 CA488694 BX091891 CA422861 AF230409 
    CA411578 CF125733 AW950135 BV183756 AA280067 AF230408 BQ447002 CD634897 
    NM_033238 AW327445 AI687279 AA548929 AF230411 BM546503 BQ673191 AF230410 
    M79464 BI061736 M79463 NM_033245 AL562894 AW327444 BU151171 BT009911 
    AA428666 BG676913 BG765781 AW192731 AF230403 BM686982 BE395856 BC000080 
    T28747 BF528762 AI150607 CA441716 T98108 BU957325 BU538477 AA232665 
    AW135192 AA515669 AA504458 BM723511 BI966792 AA553942 AF230405 AK096663 
    BI963693 BM989250 AA700809 CD557466 CA436615 BQ893905 BG248766 AI591030 
    AI929767 AA283199 BM917135 BQ225369 BE785259 BQ941327 NM_033247 BM457439 
    X63131 BU856057 BM838167 NM_033250 BU157264 BM263182 BG675701 AF370432 
    BG424845 AA197247 BQ062454 AA279838 AA522918 AI290612 AA293079 AA730613 
    AA524560 AI571116 BG422880 BQ668564 R35883 BE885773 AI610633 BM464977 
    BX373996 BQ939653 BF347963 BI771557 AA910162 BG330549 BF433545 AI126359 
    BE614693 BG469471 AA417793 AW401490 BG105695 BU731038 BX362260 AA205848 
    R35882 BE220987 AW451827 BF916740 BQ896605 BG981771 CF132456 AF230401 
    AL515152 AI637859 BX329779 AW339228 AI241493 BM006810 AA864671 AW235168 
    AA604561 BG502461 AW192714 AI268896 AW135632 BF447020 R55296 AI940146 
    AW339645 AA039542 AI760964 BE707918 AW975630 BM554598 AW503839 AA243463 
    BI037016 AA492559 BG960274 AW138912 AA580406 AL562011 AA622609 BF338360 
    AI492334 AA482618 BU754194 BQ005581 AW606071 BX386977 BE562821 AI138252 
    AL521594 AI826869 AW088203 AL527438 AA995147 BI063654 BF669692 N67643 
    AI273873 BF510860 AA251040 AA910163 BF886673 W38850 W01092 AA806898 
    BF926284 BF869162 AI682851 AA004215 BI860029 R44151 AW951035 AA808555 
    AA504532 BG008808 AA662846 BM007120 AA250795 AW732416 BE041688 R20447 
    BE925456 AI497893 CA487302 AA548924 AI031697 CF264979 BQ228534 BG290281 
    AA039541 AW844051 AW951027 AI215966 R55395 AA206362 AF388194 AA206657 
    BE245558 CB989888 

    GeneLoc Exon Structure

    Selected Alternative Splicing Database (ASD) splice patterns (SP) for PML (see all 16)    About this scheme

    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:                                                                                                  -     -     -     -     -     -     -                     

    ExUns: 10a · 10b
    SP1:            
    SP2:            
    SP3:            
    SP4:            
    SP5:            


    ECgene alternative splicing isoforms for PML

    (RNA expression data according to H-InvDB, NONCODE, miRBase, and RNAdb, Expression images according to data from BioGPS, Illumina Human BodyMap, and CGAP SAGE, Sets of similar genes according to GeneDecks, in vivo and in vitro expression data from LifeMap Discovery™, Protein expression images according to data from SPIRE 1MOPED, 2PaxDb, and 3MaxQB, plus additional links to SOURCE, and/or BioGPS, and/or UniProtKB,
    PCR Arrays from QIAGEN, Primers from OriGene, and/or QIAGEN, In Situ Hybridization Assays from Advanced Cell Diagnostics)
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    PML expression in normal human tissues (normalized intensities)
    See probesets specificity/sensitivity at GeneAnnot
    About this imageBioGPS <intensity>2/3
    CGAP TAG: --
    PML Expression
    About this image


    PML expression in embryonic tissues and stem cells    About this table
    Data from LifeMap, the Embryonic Development and Stem Cells Database
     selected tissues (see all 6) fully expand
     
     Ovary (Reproductive System)    fully expand to see all 2 entries
             Ovarian Mesenchymal Stroma Cells Ovary Interstitium
             Oviduct
     
     Trophoblast (Extraembryonic Tissues)
             Trophoblast Cells Trophoblast
     
     Testis (Reproductive System)
             Leydig Cells Testis Interstitium
     
     Bone (Muscoskeletal System)
             Bone Marrow
     
     Brain (Nervous System)
             Cerebral Cortex
    PML Protein expression data from MOPED1, PaxDb2 and MaxQB3    About this image

    PML Protein Expression

    SOURCE GeneReport for Unigene cluster: Hs.526464
        Pathway & Disease-focused RT2 Profiler PCR Arrays including PML: 
              Oncogenes & Tumor Suppressor Genes in human mouse rat
              Leukemia in human mouse rat
              Type I Interferon Response in human mouse rat
              Apoptosis 384HT in human mouse rat
              Ubiquitin Ligases in human mouse rat

    Primer
    Products:
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    OriGene qSTAR qPCR primer pairs in human, mouse for PML
    Pre-validated RT2 qPCR Primer Assay in human, mouse, rat PML
    QuantiTect SYBR Green Assays in human, mouse, rat PML
    QuantiFast Probe-based Assays in human, mouse, rat PML
    In Situ
    Assay Products:
     

     
    Advanced Cell Diagnostics RNAscope RNA in situ hybridization assays for PML

    (Orthologs according to 1,2HomoloGene (2older version, for species not in 1newer version), 3euGenes, 4SGD , 5MGI Mar 06 2013, with possible further links to Flybase and/or WormBase, and/or 6Ensembl pan taxonomic compara , Gene Trees according to Ensembl and TreeFam)
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    This gene was present in the common ancestor of chordates.

    Orthologs for PML gene from Selected species (see all 8)    About this table
    Organism Taxonomic
    classification
    Gene Description Human
    Similarity
    Orthology
    Type
    Details
    mouse
    (Mus musculus)
    Mammalia Pml1 , 5 promyelocytic leukemia1, 5 77.71(n)1
    71.33(a)1
      9 (31.63 cM)5
    188541  NM_178087.41  NP_835188.21 
     582180765 
    chicken
    (Gallus gallus)
    Aves LOC1008575631 protein PML-like 54.29(n)
    40.29(a)
      100857563  XM_004943698.1  XP_004943755.1 


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

    (Paralogs according to 1HomoloGene,
    2Ensembl, and 3SIMAP, Pseudogenes according to 4Pseudogene.org Build 68)
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    Paralogs for PML gene
    2 SIMAP similar genes for PML using alignment to 8 protein entries:     PML_HUMAN (see all proteins):
    promyelocytic leukemia protein    PML-RAR

    PML for paralogs           About GeneDecksing



    (SNPs/Variants according to the 1NCBI SNP Database, 2Ensembl, 3PupaSUITE, 4UniProtKB, and DNA2.0, Linkage Disequilibrium by HapMap, Structural Variations(CNVs/InDels/Inversions) from the Database of Genomic Variants, Mutations from the Human Gene Mutation Database (HGMD), the Human Cytochrome P450 Allele Nomenclature Database, and the Locus Specific Mutation Databases (LSDB), Blood group antigen gene mutations by BGMUT, Resequencing Primers, Cancer Mutation PCR Arrays and Assays, and Copy Number PCR Arrays from QIAGEN)
    About This Section

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    Selected SNPs for PML (see all 1092)    About this table    
    Genomic DataTranscription Related DataAllele Frequencies
    SNP IDValidClinical
    significance
    Chr 15 posSequence#AA
    Chg
    TypeMore#Allele
    freq
    PopTotal
    sample
    More
    ----------
    rs1903575291,2
    --51117006(+) ATCTTC/TTCCAG 9 -- us2k10--------
    rs792336081,2
    C,F--51117012(+) TCCAGG/AATCAA 9 -- us2k11Minor allele frequency- A:0.03NA 120
    rs1810660111,2
    --51117091(+) CTTTGC/GGTTTC 9 -- us2k10--------
    rs1379040231,2
    --51117113(+) GTCTGC/TAAATT 9 -- us2k10--------
    rs780071071,2
    C,F--51117201(+) GGCCTG/AGCCAG 9 -- us2k11Minor allele frequency- A:0.06WA 118
    rs1424398641,2
    C--51117204(+) CTGGCC/GAGGTC 9 -- us2k10--------
    rs734397051,2
    C,F--51117322(+) CAGAGC/TTACAT 9 -- us2k13Minor allele frequency- T:0.14WA CSA 122
    rs1853131801,2
    --51117365(+) AGGCCA/CTCAGT 9 -- us2k10--------
    rs1459762681,2
    --51117661(+) TTTGGC/TTTTCA 9 -- us2k10--------
    rs2012290761,2
    --51117870(+) GTACA-/CA    
       GGAGC
    CAGCA
    9 -- us2k10--------

    HapMap Linkage Disequilibrium report for PML (74287014 - 74340160 bp)

    Structural Variations
         Database of Genomic Variants (DGV) 9 variations for PML:    About this table    
    Variant IDTypeSubtypePubMed ID
    nsv509575CNV Insertion20534489
    nsv457203CNV Loss19166990
    nsv469619CNV Loss16826518
    nsv510666CNV Loss20534489
    nsv518316CNV Gain19592680
    nsv817697CNV Gain17921354
    nsv833052CNV Gain+Loss17160897
    nsv428308CNV Gain+Loss18775914
    dgv756e1CNV Complex17122850

    Human Gene Mutation Database (HGMD): PML
    Site Specific Mutation Identification with PCR Assays
    SeqTarget long-range PCR primers for resequencing PML
    DNA2.0 Custom Variant and Variant Library Synthesis for PML

    (in which this Gene is Involved, According to MalaCards, OMIM, UniProtKB, the University of Copenhagen DISEASES database, Novoseek, Genatlas, GeneTests, GAD, HuGE Navigator, and/or TGDB.)
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    OMIM gene information: 102578    OMIM disorders: --

    UniProtKB/Swiss-Prot: PML_HUMAN, P29590
  • 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

  • Selected diseases for PML (see all 79):    
    About MalaCards
    leukemia, acute promyelocytic, pml/rara type    acute promyelocytic leukemia    leukemia    neuronal intranuclear inclusion disease
    parotitis    langerhans-cell histiocytosis    bloom syndrome    histiocytosis
    megakaryocytic leukemia    nijmegen breakage syndrome    chronic graft versus host disease    lymphoid leukemia
    herpes simplex    paget's disease of bone    essential thrombocythemia    rabies
    werner syndrome    pilocytic astrocytoma    frontotemporal dementia    acute lymphocytic leukemia

    1 disease from the University of Copenhagen DISEASES database for PML:
    Leukemia

    PML for disorders           About GeneDecksing

    Selected Novoseek inferred disease relationships for PML gene (see all 37)    About this table

    Disease   -log (P-Val)   Hits   PubMed IDs for Articles with Shared Sentences (# sentences)
    promyelocytic leukemia 96.3 303 11511788 (3), 16154611 (2), 19380586 (2), 8550548 (2) (see all 99)
    leukemia promyelocytic acute 95.6 154 1310060 (2), 1353379 (2), 9452416 (2), 11068554 (2) (see all 99)
    leukemogenesis 72.4 8 8580793 (1), 18809579 (1), 8609713 (1), 8400236 (1) (see all 7)
    leukemia 68.7 64 19088278 (2), 9591778 (2), 9734655 (2), 18716620 (2) (see all 45)
    minimal residual disease 60.9 4 1310060 (1), 1375840 (1), 8180596 (1), 9260053 (1)
    bloom syndrome 58.3 2 10637504 (1)
    drpla 43.3 1 12901837 (1)
    biliary cirrhosis primary 31.8 6 9362351 (2), 8986606 (1), 9193756 (1), 8749719 (1)
    tumors 30.2 88 14970276 (8), 18566754 (6), 18856066 (3), 19652541 (2) (see all 32)
    herpes simplex 29.4 11 19279115 (2), 10574707 (1), 10233977 (1), 9151854 (1) (see all 9)

    Genatlas disease: PML
    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)

    Genetic Association Database (GAD): PML
    Human Genome Epidemiology (HuGE) Navigator: PML (24 documents)
    Tumor Gene Database (TGDB): PML

    Export disorders for PML gene to outside databases

    (in PubMed. Associations of this gene to articles via 1Entrez Gene, 2UniProtKB/Swiss-Prot, 3HGNC, 4GAD, 5PharmGKB, 6HMDB, 7DrugBank, 8UniProtKB/TrEMBL, 9 Novoseek, and/or 10fRNAdb)
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    PubMed articles for PML gene, integrated from 10 sources (see all 716):
    (articles sorted by number of sources associating them with PML)
        Utopia: connect your pdf to the dynamic
    world of online information

    1. PML colocalizes with and stabilizes the DNA damage response protein TopBP1. (PubMed id 12773567)1, 2, 9 Xu Z.-X.... Chang K.-S. (Mol. Cell. Biol. 2003)
    2. Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. (PubMed id 10684855)1, 2, 9 Zhong S....Pandolfi P.P. (J. Exp. Med. 2000)
    3. PML protein isoforms and the RBCC/TRIM motif. (PubMed id 11704850)1, 2, 9 Jensen K.... Freemont P.S. (Oncogene 2001)
    4. The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. (PubMed id 12810724)1, 2, 9 Louria-Hayon I....Haupt Y. (J. Biol. Chem. 2003)
    5. 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)1, 2, 9 Kastner P.... Chambon P. (EMBO J. 1992)
    6. Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. (PubMed id 9570750)1, 2, 9 Cao T.... Etkin L.D. (J. Cell Sci. 1998)
    7. PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein. (PubMed id 15467728)1, 2, 9 Daniels M.J.... Venkitaraman A.R. (Nat. Struct. Mol. Biol. 2004)
    8. The function of PML in p53-dependent apoptosis. (PubMed id 11025664)1, 2, 9 Guo A.... Pandolfi P.P. (Nat. Cell Biol. 2000)
    9. Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. (PubMed id 17942542)1, 2, 9 Tavalai N.... Stamminger T. (J. Virol. 2008)
    10. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. (PubMed id 18716620)1, 2, 9 Song M.S.... Pandolfi P.P. (Nature 2008)

    (in PubMed, OMIM, and NCBI Bookshelf)
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     ANDOR
    Aliases
    Disorders
    Free Text  

      Query String
    PubMed
    OMIM
    NCBI Bookshelf
      (Note: In FireFox, select the above section and copy using Ctrl-C)

    (According to Entrez Gene, HGNC, AceView, euGenes, Ensembl, miRBase, ECgene, Kegg, and/or H-InvDB)
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    Entrez Gene: 5371 HGNC: 9113 AceView: PML Ensembl:ENSG00000140464 euGenes: HUgn5371
    ECgene: PML Kegg: 5371 H-InvDB: PML

    (According to HUGE)
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      --

    (According to PharmGKB, ATLAS, HORDE, IMGT, LEIDEN, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL, and/or others, e.g. Wikipedia and GeneReviews, via UniProtKB/Swiss-Prot)
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    NameDescription
    PharmGKB entry for PML Pharmacogenomics, SNPs, Pathways
    ATLAS Chromosomes in Cancer entry for PML Genetics and Cytogenetics in Oncology and Haematology

    (Patent information from GeneIP,
    Licensable technologies from WIS Yeda, Salk, Tufts,
    IP news from LifeMap Sciences, Inc.)
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    Patent Information for PML gene:
    Search GeneIP for patents involving PML

    GeneCards and IP:
    Japan Patent Office Licenses GeneCards     European Patent Office Licenses GeneCards     Improving the IP Search



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