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Category   Symbol Source: HGNC EntrezGene Ensembl GeneCards RNA genes CroW21
GIFtS

PML Gene

protein-coding   GIFtS: 68
GCID: GC15P074287

Promyelocytic Leukemia

Microbiology & Infectious Diseases Congress
  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)
About This Section

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, Tocris Bioscience, Wikipedia's Gene Wiki, PharmGKB,
UniProtKB/Swiss-Prot, and/or UniProtKB/TrEMBL)
About This Section

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 acute promyelocytic leukemia, and leukemia, and among its related super-pathways are Interferon Signaling and Proteolysis Putative SUMO-1 pathway. 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 73), Regulatory elements and Epigenetics data according to QIAGEN, SABiosciences, and/or SwitchGear Genomics)
About This Section
RefSeq DNA sequence:
NC_000015.9  NT_010194.17  NC_018926.2  
Regulatory elements:
   SABiosciences 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 SABiosciences Chromatin IP Primers for PML

Epigenetics:
QIAGEN PyroMark CpG Assay predesigned Pyrosequencing DNA Methylation assays 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 UniProtKB, HORDE, neXtProt, Ensembl, and/or Reactome, Modification sites according to PhosphoSitePlus, Specific Peptides from DME, Protein expression images according to data from SPIRE 1MOPED, 2PaxDb, and 3MAXQB 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., Ontologies according to Gene Ontology Consortium 01 Oct 2013 and Entrez Gene, Antibodies by EMD Millipore, R&D Systems, GenScript, Cell Signaling Technology, OriGene, Novus Biologicals, Thermo Fisher Scientific, LSBio, Abcam, and/or Cloud-Clone Corp.)
About This Section

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
(By similarity). 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 (By similarity). Interacts
with CSNK2A1 and CSNK2A3. 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 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)
Subcellular location: 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
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:

  • UniProtKB: 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-dependent
  • UniProtKB: 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 sumoylated
  • UniProtKB: 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
  • UniProtKB: 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
  • View modification sites using PhosphoSitePlus
  • View neXtProt modification sites for NX_P29590

  • PML Protein expression data from MOPED1, PaxDb2 and MAXQB3 :    About this image 

    PML Protein Expression
    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
    Human Recombinant Protein Products for PML: 
    Browse Purified and Recombinant Proteins at EMD Millipore
    Browse R&D Systems for human recombinant proteins
    Browse recombinant and purified proteins available from Enzo Life Sciences
    OriGene Purified Protein 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 

    Gene Ontology (GO): 5/11 cellular component terms (GO ID links to tree view) (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



    PML Antibody Products: 
    EMD Millipore Mono- and Polyclonal Antibodies for the study of PML
    Browse R&D Systems for Antibodies
    OriGene Antibodies for PML
    OriGene Custom Antibody Services for PML
    GenScript Custom Superior Antibodies Services for PML
    Novus Biologicals PML Antibodies
    Abcam antibodies for PML
    Cloud-Clone Corp. Antibodies for PML 
    ThermoFisher Antibodies for PML
    LSBio Antibodies in human, mouse, rat for PML 

    Assay Products for PML: 
    Browse Kits and Assays available from EMD Millipore
    OriGene Custom Assay Services for PML
    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)
    About This Section
    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,
    bound targets from SABiosciences, miRNA Gene Targets from miRTarBase, shRNA from OriGene, RNAi from EMD Millipore, siRNAs from OriGene, QIAGEN, microRNA from QIAGEN, Gene Editing from DNA2.0, Sirion Biotech, Clones from EMD Millipore, OriGene, SwitchGear Genomics, GenScript, Sino Biological, DNA2.0, Vector BioLabs, and Sirion Biotech, Cell Lines from GenScript, LifeMap BioReagents, In Situ Hybridization Assays from Advanced Cell Diagnostics, Ontologies according to Gene Ontology Consortium 01 Oct 2013 via Entrez Gene.)
    About This Section

    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): 5/10 molecular function terms (GO ID links to tree view) (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 - Custom generated mouse model solutions for PML 
       inGenious Targeting Laboratory - Custom generated inducible mouse model solutions for PML

       genOway customized KO model: permanent, tissue-specific or time-controlled inactivation for PML 
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    Inhib. RNA
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    (Pathways according to EMD Millipore, 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 SABiosciences, 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 Oct 2013 via Entrez Gene).
    About This Section

    SuperPaths for PML About   (see top 5)                                                                                              See pathways by source

    SuperPathContained pathways About
    1Interferon Signaling
    Interferon Signaling0.61
    Interferon gamma signaling0.41
    Cytokine Signaling in Immune system0.61
    2DNA damage Role of SUMO in p53 regulation
    Proteolysis Putative SUMO-1 pathway0.33
    DNA damage Role of SUMO in p53 regulation0.33
    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 pathway0.71
    6Immune System
    Immune System0.56
    7p53 signaling pathway
    DNA damage response0.41
    8Endometrial cancer
    Acute myeloid leukemia0.40
    9p53 Pathway
    p53 Signaling0.38
    10Antigen processing: Ubiquitination & Proteasome degradation
    Ubiquitin mediated proteolysis0.36
    114-1BB Pathway
    SUMO Pathway0.30
    12mTOR signaling pathway
    mTOR signaling pathway
    13Transcriptional misregulation in cancer
    Transcriptional misregulation in cancer
    14TNF-alpha/NF-kB Signaling Pathway
    TNF-alpha/NF-kB Signaling Pathway
    15TGF-beta receptor signaling
    TGF-beta receptor signaling
    16Pathways in cancer
    Pathways in cancer
    17Integrated Breast Cancer Pathway
    Integrated Breast Cancer Pathway
    18Endocytosis
    Endocytosis
    19Direct p53 effectors
    Direct p53 effectors
    20Integrated Pancreatic Cancer Pathway
    Integrated Pancreatic Cancer Pathway

    Pathways by source                                                                                                                                                                 See SuperPaths
    Show all pathways

    3 EMD Millipore Pathways for PML
        Immune response IFN alpha/beta signaling pathway
    Proteolysis Putative SUMO-1 pathway
    DNA damage Role of SUMO in p53 regulation

    3 Downloadable PowerPoint Slides of QIAGEN 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

    5/7 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

    4        Reactome Pathways for PML
        Interferon gamma signaling
    Cytokine Signaling in Immune system
    Interferon Signaling
    Immune System


    5/7         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

    Interactions:

        SABiosciences Gene Network CentralTM Interacting Genes and Proteins Network for PML

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

    5/217 Interacting proteins for PML (P295901, 2, 3 ENSP000002680584) via UniProtKB, MINT, STRING, and/or I2D (see all 217)
    InteractantInteraction Details
    GeneCardExternal ID(s)
    MDM2Q009871, 2, 3, ENSP000004172814EBI-304008,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): 5/50 biological process terms (GO ID links to tree view) (see all 50):    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-dependent IEA--
    GO:0006355regulation of transcription, DNA-dependent IMP--

    PML for ontologies           About GeneDecksing



    (Chemical Compounds according to UniProtKB, Enzo Life Sciences, EMD Millipore, Tocris Bioscience HMDB, BitterDB, and/or Novoseek, Ligands according to IUPHAR, and Drugs according to DrugBank, Enzo Life Sciences, and/or PharmGKB, with drugs/clinical trials/news search links to CenterWatch)
    About This Section

    PML for compounds           About GeneDecksing

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

    Browse Tocris compounds for PML

    10/18 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

    Search CenterWatch for drugs/clinical trials and news about PML

    (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,
    Conferences by KenesGroup, exon structure from GeneLoc, alternative splicing isoforms according to ASD and/or ECgene,
    RNAi Products from EMD Millipore,
    siRNAs from OriGene, QIAGEN, shRNA from OriGene, microRNA from QIAGEN,
    Tagged/untagged cDNA clones from OriGene, SwitchGear Genomics, GenScript, DNA2.0, Vector BioLabs, Sirion Biotech, Primers from OriGene, SABiosciences, and/or QIAGEN )
    About This Section

    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
    18/22 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
    Congresses - knowledge worth sharing:  
    European Congress of Clinical Microbiology and Infectious Diseases (ECCMID) 10 - 13 May 2014

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    SwitchGear 3'UTR luciferase reporter plasmidPML 3' UTR sequence
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      QIAGEN 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 

    24/298 AceView cDNA sequences (see all 298):

    AW452151 BQ430284 BX647287 BM127636 BQ919042 BM021512 AI635829 BU196211 
    BM917894 BQ933226 BI793248 NM_033240 BU902386 BC034251 BE336744 BQ059293 
    AI160099 BI962511 BF939193 BU617120 AI469853 CF272229 AI744517 AI146508 

    GeneLoc Exon Structure

    5/16 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™, plus additional links to Genevestigator, and/or SOURCE, and/or BioGPS, and/or UniProtKB,
    PCR Arrays from SABiosciences, Primers from OriGene, SABiosciences, and/or QIAGEN, In Situ Hybridization Assays from Advanced Cell Diagnostics)
    About This Section

    PML expression in normal human tissues (normalized intensities)      PML embryonic expression: see
    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 
     5/31 selected tissues (see all 31) fully expand
     
     Epithelium
             vagina ; squamous epithelial cells   
     
     Testis (Reproductive System)    fully expand to see all 4 entries
             Leydig Cells Testis Interstitium
             seminal vesicle ; glandular cells   
     
     Colon (Gastrointestinal Tract)    fully expand to see all 3 entries
             colon ; peripheral nerve/ganglion   
     
     Tonsil (Hematopoietic System)    fully expand to see all 3 entries
             tonsil ; squamous epithelial cells   
     
     Breast
             breast ; myoepithelial cells   

    See PML Protein Expression from SPIRE MOPED and PaxDB
    Genevestigator expression for PML

    SOURCE GeneReport for Unigene cluster: Hs.526464
        SABiosciences Expression via Pathway-Focused 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

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    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)
    About This Section

    This gene was present in the common ancestor of chordates.

    Orthologs for PML gene from 2/8 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 77.26(n)1
    71.04(a)1
      9 (31.63 cM)5
    188541  NM_178087.41  NP_835188.21 
     582180765 
    chicken
    (Gallus gallus)
    Aves LOC1008575631 protein PML-like 60.16(n)
    43.68(a)
      100857563  XM_003641812.1  XP_003641860.1 


    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)
    About This Section
    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) and the Locus Specific Mutation Databases (LSDB), Blood group antigen gene mutations by BGMUT, Resequencing Primers from QIAGEN, Cancer Mutation PCR Arrays and Assays and Copy Number PCR Arrays from SABiosciences)
    About This Section

    10/1092 SNPs in PML are shown (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
    SABiosciences Cancer Mutation 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, Conferences by KenesGroup, Novoseek, Genatlas, GeneTests, GAD, HuGE Navigator, and/or TGDB.)
    About This Section
    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

  • 20/72 diseases for PML (see all 72):    About MalaCards
    acute promyelocytic leukemia    leukemia    neuronal intranuclear inclusion disease    parotitis
    langerhans-cell histiocytosis    bloom syndrome    histiocytosis    megakaryocytic leukemia
    chronic graft versus host disease    nijmegen breakage syndrome    herpes simplex    paget's disease of bone
    essential thrombocythemia    rabies    werner syndrome    soft tissue sarcoma
    pilocytic astrocytoma    acute lymphocytic leukemia    myelofibrosis    frontotemporal dementia

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

    PML for disorders           About GeneDecksing


    Congresses - knowledge worth sharing:  
    The International Symposium on Pneumococci and Pneumococcal Diseases (ISPPD) 9 - 13 March 2014
    Alzheimer's & Parkinson's Diseases Congress (ADPD) 18 - 22 March 2015

    10/37 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 9 sources (see all 707):
    (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. (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. (2000)
    3. PML protein isoforms and the RBCC/TRIM motif. (PubMed id 11704850)1, 2, 9 Jensen K....Freemont P.S. (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. (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. (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. (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. (2004)
    8. The function of PML in p53-dependent apoptosis. (PubMed id 11025664)1, 2, 9 Guo A....Pandolfi P.P. (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. (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. (2008)

    (in PubMed, OMIM, and NCBI Bookshelf)
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    (According to Entrez Gene, HGNC, AceView, euGenes, Ensembl, miRBase, ECgene, Kegg, and/or H-InvDB)
    About This Section
    Entrez Gene: 5371 HGNC: 9113 AceView: PML Ensembl:ENSG00000140464 euGenes: HUgn5371
    ECgene: PML Kegg: 5371 H-InvDB: PML

    (According to HUGE)
    About This Section
      --

    (According to PharmGKB, ATLAS, HORDE, IMGT, LEIDEN, UniProtKB/Swiss-Prot, and/or UniProtKB/TrEMBL,
    Wikipedia and/or GeneReviews via UniProtKB/Swiss-Prot)
    About This Section
    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.)
    About This Section
    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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