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P29590

- PML_HUMAN

UniProt

P29590 - PML_HUMAN

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Protein

Protein PML

Gene

PML

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Zinc 1
Metal bindingi60 – 601Zinc 1
Metal bindingi72 – 721Zinc 2
Metal bindingi74 – 741Zinc 2
Metal bindingi77 – 771Zinc 1
Metal bindingi80 – 801Zinc 1
Metal bindingi88 – 881Zinc 2
Metal bindingi91 – 911Zinc 2
Sitei394 – 3952Breakpoint for translocation to form PML-RARA oncogene in type A APL
Sitei552 – 5532Breakpoint for translocation to form PML-RARA oncogene in type B APL

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9236RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 16643B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23654B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cobalt ion binding Source: UniProtKB
  2. DNA binding Source: UniProtKB-KW
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: BHF-UCL
  5. SUMO binding Source: UniProtKB
  6. transcription coactivator activity Source: UniProtKB
  7. ubiquitin protein ligase binding Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. apoptotic process Source: UniProtKB
  3. branching involved in mammary gland duct morphogenesis Source: Ensembl
  4. cell cycle arrest Source: UniProtKB
  5. cell fate commitment Source: Ensembl
  6. cellular response to interleukin-4 Source: Ensembl
  7. cellular senescence Source: UniProtKB
  8. circadian regulation of gene expression Source: UniProtKB
  9. common-partner SMAD protein phosphorylation Source: Ensembl
  10. cytokine-mediated signaling pathway Source: Reactome
  11. defense response to virus Source: UniProtKB-KW
  12. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  13. endoplasmic reticulum calcium ion homeostasis Source: UniProtKB
  14. entrainment of circadian clock by photoperiod Source: UniProtKB
  15. extrinsic apoptotic signaling pathway Source: Ensembl
  16. innate immune response Source: UniProt
  17. interferon-gamma-mediated signaling pathway Source: Reactome
  18. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  19. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  20. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  21. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  22. maintenance of protein location in nucleus Source: MGI
  23. myeloid cell differentiation Source: Ensembl
  24. negative regulation of angiogenesis Source: UniProtKB
  25. negative regulation of cell growth Source: UniProtKB
  26. negative regulation of cell proliferation Source: BHF-UCL
  27. negative regulation of mitotic cell cycle Source: UniProtKB
  28. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  29. negative regulation of telomerase activity Source: UniProtKB
  30. negative regulation of telomere maintenance via telomerase Source: UniProtKB
  31. negative regulation of transcription, DNA-templated Source: UniProtKB
  32. negative regulation of translation in response to oxidative stress Source: UniProtKB
  33. negative regulation of viral release from host cell Source: UniProt
  34. PML body organization Source: UniProtKB
  35. positive regulation of apoptotic process involved in mammary gland involution Source: UniProtKB
  36. positive regulation of defense response to virus by host Source: UniProtKB
  37. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  38. positive regulation of histone deacetylation Source: UniProtKB
  39. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  40. protein complex assembly Source: UniProtKB
  41. protein stabilization Source: UniProtKB
  42. protein targeting Source: UniProtKB
  43. regulation of calcium ion transport into cytosol Source: UniProtKB
  44. regulation of circadian rhythm Source: UniProtKB
  45. regulation of double-strand break repair Source: UniProtKB
  46. regulation of MHC class I biosynthetic process Source: Ensembl
  47. regulation of protein phosphorylation Source: UniProtKB
  48. regulation of transcription, DNA-templated Source: UniProtKB
  49. response to cytokine Source: BHF-UCL
  50. response to gamma radiation Source: Ensembl
  51. response to hypoxia Source: UniProtKB
  52. response to UV Source: Ensembl
  53. retinoic acid receptor signaling pathway Source: Ensembl
  54. SMAD protein import into nucleus Source: Ensembl
  55. transcription, DNA-templated Source: UniProtKB-KW
  56. transforming growth factor beta receptor signaling pathway Source: Ensembl
  57. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Antiviral defense, Apoptosis, Biological rhythms, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.
SignaLinkiP29590.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PML
Alternative name(s):
Promyelocytic leukemia protein
RING finger protein 71
Tripartite motif-containing protein 19
Gene namesi
Name:PML
Synonyms:MYL, PP8675, RNF71, TRIM19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:9113. PML.

Subcellular locationi

Nucleus. Nucleusnucleoplasm. Cytoplasm. NucleusPML body. Nucleusnucleolus. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; 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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endosome Source: UniProtKB-KW
  4. extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  5. nuclear matrix Source: UniProtKB
  6. nuclear membrane Source: UniProtKB
  7. nucleolus Source: UniProtKB
  8. nucleoplasm Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571C → S: Strongly reduced sumoylation; when associated with S-60. 1 Publication
Mutagenesisi60 – 601C → S: Strongly reduced sumoylation; when associated with S-57. 1 Publication
Mutagenesisi65 – 651K → R: Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. No sumoylation nor nuclear body formation; when associated with R-160 and R-490. 1 Publication
Mutagenesisi68 – 681K → R: No effect on sumoylation levels.
Mutagenesisi88 – 881C → S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89. 1 Publication
Mutagenesisi89 – 891P → R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88. 1 Publication
Mutagenesisi133 – 1331K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication
Mutagenesisi150 – 1501K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication
Mutagenesisi160 – 1601K → R: Loss of 2 sumoylations; when associated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. 1 Publication
Mutagenesisi487 – 4871K → A: Loss of nuclear localization; when associated with A-490. 2 Publications
Mutagenesisi487 – 4871K → R: Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515. 2 Publications
Mutagenesisi490 – 4901K → A: Loss of nuclear localization; when associated with A-487. 2 Publications
Mutagenesisi490 – 4901K → R: Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160. 2 Publications
Mutagenesisi515 – 5151K → R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487. 1 Publication
Mutagenesisi518 – 5181S → A: Abolishes ubiquitination by the BCR(KLHL20) E3 ubiquitin ligase complex. 1 Publication
Mutagenesisi556 – 5594VVVI → AAAS: Abolishes SUMO1 binding.

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA33439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 882882Protein PMLPRO_0000056001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by HIPK21 Publication
Modified residuei28 – 281Phosphothreonine; by MAPK11 Publication
Modified residuei36 – 361Phosphoserine; by HIPK2 and MAPK11 Publication
Modified residuei38 – 381Phosphoserine; by HIPK2 and MAPK11 Publication
Modified residuei40 – 401Phosphoserine; by MAPK11 Publication
Modified residuei42 – 421Phosphothreonine1 Publication
Cross-linki65 – 65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei117 – 1171Phosphoserine; by CHEK21 Publication
Cross-linki160 – 160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki400 – 400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei403 – 4031Phosphoserine; by MAPK1 and MAPK73 Publications
Modified residuei409 – 4091Phosphothreonine; by MAPK71 Publication
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei487 – 4871N6-acetyllysine2 Publications
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki497 – 497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei504 – 5041PhosphoserineBy similarity
Modified residuei505 – 5051Phosphoserine; by MAPK11 Publication
Modified residuei515 – 5151N6-acetyllysine1 Publication
Modified residuei518 – 5181Phosphoserine; by CDK1 and CDK26 Publications
Modified residuei527 – 5271Phosphoserine; by MAPK15 Publications
Modified residuei530 – 5301Phosphoserine; by MAPK14 Publications
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei565 – 5651Phosphoserine; by CK21 Publication

Post-translational modificationi

Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-518 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20. 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.7 Publications
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.4 Publications
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.12 Publications
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.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP29590.
PaxDbiP29590.
PRIDEiP29590.

PTM databases

PhosphoSiteiP29590.

Miscellaneous databases

PMAP-CutDBP29590.

Expressioni

Inductioni

By interferons alpha, beta and gamma. Up-regulated by IRF3 and p53/TP53.

Gene expression databases

BgeeiP29590.
CleanExiHS_PML.
ExpressionAtlasiP29590. baseline and differential.
GenevestigatoriP29590.

Organism-specific databases

HPAiCAB010194.
CAB016304.
HPA008312.

Interactioni

Subunit structurei

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).43 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03243-12EBI-304008,EBI-1927377From a different organism.
P044894EBI-8099068,EBI-6398911From a different organism.
P279586EBI-295890,EBI-6377335From a different organism.
CSNK2A1P684002EBI-295890,EBI-347804
DAXXQ9UER76EBI-295890,EBI-77321
FASP254454EBI-295890,EBI-494743
KLHL20Q9Y2M59EBI-295890,EBI-714379
MAPK7Q131646EBI-295890,EBI-1213983
MDM2Q009876EBI-304008,EBI-389668
PSMA3P257882EBI-295890,EBI-348380
SUMO1P631653EBI-295890,EBI-80140
TBX2Q132072EBI-295890,EBI-2853051
TERTO147467EBI-304008,EBI-1772203
TGIF1Q155833EBI-295890,EBI-714215
TP53P046374EBI-295890,EBI-366083
ZBTB16Q055167EBI-295890,EBI-711925

Protein-protein interaction databases

BioGridi111384. 179 interactions.
IntActiP29590. 67 interactions.
MINTiMINT-158826.
STRINGi9606.ENSP00000268058.

Structurei

Secondary structure

1
882
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603
Beta strandi82 – 876
Beta strandi93 – 964

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
ProteinModelPortaliP29590.
SMRiP29590. Positions 49-104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29590.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni448 – 555108Interaction with PER2Add
BLAST
Regioni476 – 49015Nuclear localization signalAdd
BLAST
Regioni556 – 5627Sumo interaction motif (SIM)

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili228 – 25326Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 4644Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9236RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 16643B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23654B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG326718.
GeneTreeiENSGT00510000048454.
HOVERGENiHBG000552.
InParanoidiP29590.
KOiK10054.
OMAiSDAENSC.
OrthoDBiEOG7M98FM.
PhylomeDBiP29590.
TreeFamiTF336434.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. Align

Isoform PML-1 (identifier: P29590) [UniParc]FASTAAdd to Basket

Also known as: PML-I, TRIM19alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE
60 70 80 90 100
EFQFLRCQQC QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD
110 120 130 140 150
TPALDNVFFE SLQRRLSVYR QIVDAQAVCT RCKESADFWC FECEQLLCAK
160 170 180 190 200
CFEAHQWFLK HEARPLAELR NQSVREFLDG TRKTNNIFCS NPNHRTPTLT
210 220 230 240 250
SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL DAMTQALQEQ
260 270 280 290 300
DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA
310 320 330 340 350
VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG
360 370 380 390 400
FLRQALCRLR QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK
410 420 430 440 450
KASPEAASTP RDPIDVDLPE EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH
460 470 480 490 500
PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS QTQCPRKVIK MESEEGKEAR
510 520 530 540 550
LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP NSNHVASGAG
560 570 580 590 600
EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL
610 620 630 640 650
ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS
660 670 680 690 700
KAVSLEVGLQ HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF
710 720 730 740 750
QEAISGFLAA LPLIRERVPG ASSFKLKNLA QTYLARNMSE RSAMAAVLAM
760 770 780 790 800
RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS LQPLVQAAVL PRAEARLLAL
810 820 830 840 850
HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA FNLQALGTYF
860 870 880
EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS
Length:882
Mass (Da):97,551
Last modified:November 25, 2008 - v3
Checksum:iD50968A977E34287
GO
Isoform PML-2 (identifier: P29590-8) [UniParc]FASTAAdd to Basket

Also known as: PML-II, TRIM19kappa

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Show »
Length:829
Mass (Da):90,721
Checksum:i25824778A4AB6AB1
GO
Isoform PML-3 (identifier: P29590-9) [UniParc]FASTAAdd to Basket

Also known as: PML-III

The sequence of this isoform differs from the canonical sequence as follows:
     571-641: SSRELDDSSS...RESKFRVVIQ → VSSSPQSEVL...PPSLASPPAR
     642-882: Missing.

Show »
Length:641
Mass (Da):70,368
Checksum:i8262393E2B00CBC7
GO
Isoform PML-4 (identifier: P29590-5) [UniParc]FASTAAdd to Basket

Also known as: PML-IV, PML-X, TRIM19zeta

The sequence of this isoform differs from the canonical sequence as follows:
     621-633: TQKISQLAAVNRE → SGFSWGYPHPFLI
     634-882: Missing.

Show »
Length:633
Mass (Da):70,024
Checksum:i85FBAEC9F162C8E0
GO
Isoform PML-5 (identifier: P29590-2) [UniParc]FASTAAdd to Basket

Also known as: PML-2, PML-V, TRIM19beta

The sequence of this isoform differs from the canonical sequence as follows:
     571-611: SSRELDDSSS...DPQAEDRPLV → VSGPEVQPRT...LRLGNFPVRH
     612-882: Missing.

Note: Contains a phosphoserine at position 565.Curated

Show »
Length:611
Mass (Da):67,471
Checksum:i52E7FB5D57D59233
GO
Isoform PML-6 (identifier: P29590-4) [UniParc]FASTAAdd to Basket

Also known as: PML-3B, PML-VI, TRIM19epsilon

The sequence of this isoform differs from the canonical sequence as follows:
     553-560: EERVVVIS → GRERNALW
     561-882: Missing.

Note: Contains a phosphoserine at position 518. Contains a phosphoserine at position 527. Contains a phosphoserine at position 530.

Show »
Length:560
Mass (Da):62,007
Checksum:i9DC795A6542BA778
GO
Isoform PML-7 (identifier: P29590-10) [UniParc]FASTAAdd to Basket

Also known as: PML-VII, TRIM19theta

The sequence of this isoform differs from the canonical sequence as follows:
     419-435: PEEAERVKAQVQALGLA → LPPPAHALTGPAQSSTH
     436-882: Missing.

Show »
Length:435
Mass (Da):48,598
Checksum:i2565113DBF5F9229
GO
Isoform PML-8 (identifier: P29590-3) [UniParc]FASTAAdd to Basket

Also known as: PML-2G, PML-IIG, TRIM19gamma

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Note: Non-canonical splice sites. Might alternatively represent a polymorphic variation.

Show »
Length:824
Mass (Da):90,254
Checksum:i5DA9DD2E4EEE8492
GO
Isoform PML-11 (identifier: P29590-11) [UniParc]FASTAAdd to Basket

Also known as: PML-1A, PML-IA

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.

Note: No experimental confirmation available.

Show »
Length:834
Mass (Da):92,564
Checksum:i16772D51354CFDAC
GO
Isoform PML-12 (identifier: P29590-12) [UniParc]FASTAAdd to Basket

Also known as: PML-4A, PML-IVA, TRIM19lambda

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.
     621-633: TQKISQLAAVNRE → SGFSWGYPHPFLI
     634-882: Missing.

Show »
Length:585
Mass (Da):65,037
Checksum:iFF1E5A8D845780B2
GO
Isoform PML-13 (identifier: P29590-13) [UniParc]FASTAAdd to Basket

Also known as: PML-2A, PML-IIA

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Show »
Length:781
Mass (Da):85,734
Checksum:iC6C163ECD9FA6FB2
GO
Isoform PML-14 (identifier: P29590-14) [UniParc]FASTAAdd to Basket

Also known as: PML-6B, PML-VIB, TRIM19eta, TRIM19iota

The sequence of this isoform differs from the canonical sequence as follows:
     419-423: PEEAE → RNALW
     424-882: Missing.

Show »
Length:423
Mass (Da):47,575
Checksum:iEE5031BE9C3B33C8
GO

Sequence cautioni

The sequence BAB62809.1 differs from that shown. Reason: Chimeric cDNA.
The sequence AAA60351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAA60352.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAA60388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAA60390.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAD92648.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241E → D in AAP88913. 1 PublicationCurated
Sequence conflicti224 – 2241E → D in AAH00080. (PubMed:15489334)Curated
Sequence conflicti224 – 2241E → D in AAH20994. (PubMed:15489334)Curated
Sequence conflicti419 – 4191P → A in AAA60351. (PubMed:1720570)Curated
Sequence conflicti419 – 4191P → A in AAA60388. (PubMed:1720570)Curated
Sequence conflicti419 – 4191P → A in AAA60390. (PubMed:1720570)Curated
Sequence conflicti419 – 4191P → A in AAA60352. (PubMed:1652368)Curated
Sequence conflicti419 – 4191P → A in AAG50182. (PubMed:11331580)Curated
Sequence conflicti419 – 4191P → A in AAG50184. (PubMed:11331580)Curated
Sequence conflicti419 – 4191P → A in AAG50185. (PubMed:11331580)Curated
Isoform PML-7 (identifier: P29590-10)
Sequence conflicti419 – 4191L → V in AAG50187. (PubMed:11331580)Curated
Isoform PML-5 (identifier: P29590-2)
Sequence conflicti578 – 5781P → A in AAG50181. (PubMed:11331580)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti645 – 6451F → L.2 Publications
Corresponds to variant rs5742915 [ dbSNP | Ensembl ].
VAR_052090

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei419 – 46648Missing in isoform PML-11, isoform PML-12 and isoform PML-13. 4 PublicationsVSP_040590Add
BLAST
Alternative sequencei419 – 43517PEEAE…ALGLA → LPPPAHALTGPAQSSTH in isoform PML-7. 1 PublicationVSP_040591Add
BLAST
Alternative sequencei419 – 4235PEEAE → RNALW in isoform PML-14. 1 PublicationVSP_040592
Alternative sequencei424 – 882459Missing in isoform PML-14. 1 PublicationVSP_040593Add
BLAST
Alternative sequencei436 – 882447Missing in isoform PML-7. 1 PublicationVSP_040594Add
BLAST
Alternative sequencei553 – 5608EERVVVIS → GRERNALW in isoform PML-6. 3 PublicationsVSP_005742
Alternative sequencei561 – 882322Missing in isoform PML-6. 3 PublicationsVSP_005743Add
BLAST
Alternative sequencei571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPAHSSPVQSLLRAQGAS SLPCGTYHPPAWPPHQPAEQ AATPDAEPHSEPPDHQERPA VHRGIRYLLYRAQRAIRLRH ALRLHPQLHRAPIRTWSPHV VQASTPAITGPLNHPANAQE HPAQLQRGISPPHRIRGAVR SRSRSLRGSSHLSQWLNNFF ALPFSSMASQLDMSSVVGAG ESRAQTLGAGVPPGDSVRGS MEASQVQVPLEASPITFPPP CAPERPPISPVPGARQAGL in isoform PML-2 and isoform PML-13. 3 PublicationsVSP_040595Add
BLAST
Alternative sequencei571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-8. 2 PublicationsVSP_005741Add
BLAST
Alternative sequencei571 – 64171SSREL…RVVIQ → VSSSPQSEVLYWKVHGAHGD RRATVLASPLLASPLLASPL LASPVSAESTRSLQPALWHI PPPSLASPPAR in isoform PML-3. 1 PublicationVSP_040596Add
BLAST
Alternative sequencei571 – 61141SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-5. 2 PublicationsVSP_005739Add
BLAST
Alternative sequencei612 – 882271Missing in isoform PML-5. 2 PublicationsVSP_005740Add
BLAST
Alternative sequencei621 – 63313TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-4 and isoform PML-12. 2 PublicationsVSP_005744Add
BLAST
Alternative sequencei634 – 882249Missing in isoform PML-4 and isoform PML-12. 2 PublicationsVSP_005745Add
BLAST
Alternative sequencei642 – 882241Missing in isoform PML-3. 1 PublicationVSP_040597Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S50913 mRNA. Translation: AAB19601.2.
M79462 mRNA. Translation: AAA60388.1. Different initiation.
M79463 mRNA. Translation: AAA60351.1. Different initiation.
M79464 mRNA. Translation: AAA60390.1. Different initiation.
X63131 mRNA. Translation: CAA44841.1.
M73778 mRNA. Translation: AAA60125.1.
M80185 mRNA. Translation: AAA60352.1. Different initiation.
AF230401 mRNA. Translation: AAG50180.1.
AF230402 mRNA. Translation: AAG50181.1.
AF230403 mRNA. Translation: AAG50182.1.
AF230405 mRNA. Translation: AAG50184.1.
AF230406 mRNA. Translation: AAG50185.1.
AF230407 mRNA. Translation: AAG50186.1.
AF230408 mRNA. Translation: AAG50187.1.
AF230409 mRNA. Translation: AAG50188.1.
AF230410 mRNA. Translation: AAG50189.1.
AF230411 mRNA. Translation: AAG50190.1.
BT009911 mRNA. Translation: AAP88913.1.
AB209411 mRNA. Translation: BAD92648.1. Different initiation.
AC013486 Genomic DNA. No translation available.
AC108137 Genomic DNA. No translation available.
BC000080 mRNA. Translation: AAH00080.2.
BC020994 mRNA. Translation: AAH20994.1.
X64800 Genomic DNA. Translation: CAA46026.1.
AB067754 mRNA. Translation: BAB62809.1. Sequence problems.
CCDSiCCDS10255.1. [P29590-1]
CCDS10256.1. [P29590-10]
CCDS10257.1. [P29590-8]
CCDS10258.1. [P29590-13]
CCDS45297.1. [P29590-5]
CCDS45298.1. [P29590-2]
CCDS45299.1. [P29590-4]
CCDS45300.1. [P29590-14]
CCDS58386.1. [P29590-12]
PIRiA40044.
I38054.
S19244.
S42516.
S44381.
RefSeqiNP_002666.1. NM_002675.3. [P29590-5]
NP_150241.2. NM_033238.2. [P29590-1]
NP_150242.1. NM_033239.2. [P29590-8]
NP_150243.2. NM_033240.2. [P29590-2]
NP_150247.2. NM_033244.3. [P29590-4]
NP_150249.1. NM_033246.2. [P29590-14]
NP_150250.2. NM_033247.2. [P29590-10]
NP_150252.1. NM_033249.2. [P29590-12]
NP_150253.2. NM_033250.2. [P29590-13]
UniGeneiHs.526464.

Genome annotation databases

EnsembliENST00000268058; ENSP00000268058; ENSG00000140464. [P29590-1]
ENST00000268059; ENSP00000268059; ENSG00000140464. [P29590-8]
ENST00000354026; ENSP00000315434; ENSG00000140464. [P29590-13]
ENST00000359928; ENSP00000353004; ENSG00000140464. [P29590-14]
ENST00000395132; ENSP00000378564; ENSG00000140464. [P29590-10]
ENST00000395135; ENSP00000378567; ENSG00000140464. [P29590-5]
ENST00000435786; ENSP00000395576; ENSG00000140464. [P29590-2]
ENST00000436891; ENSP00000394642; ENSG00000140464. [P29590-4]
ENST00000564428; ENSP00000457023; ENSG00000140464. [P29590-12]
ENST00000565898; ENSP00000455838; ENSG00000140464. [P29590-11]
ENST00000567543; ENSP00000456277; ENSG00000140464. [P29590-14]
ENST00000569477; ENSP00000455612; ENSG00000140464. [P29590-9]
ENST00000569965; ENSP00000456486; ENSG00000140464. [P29590-4]
GeneIDi5371.
KEGGihsa:5371.
UCSCiuc002awk.3. human. [P29590-8]
uc002awl.3. human. [P29590-14]
uc002awm.3. human. [P29590-2]
uc002awn.3. human. [P29590-4]
uc002awo.3. human. [P29590-13]
uc002awr.3. human. [P29590-5]
uc002aws.3. human. [P29590-12]
uc002awu.3. human. [P29590-11]
uc002awv.3. human. [P29590-1]

Polymorphism databases

DMDMi215274219.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S50913 mRNA. Translation: AAB19601.2 .
M79462 mRNA. Translation: AAA60388.1 . Different initiation.
M79463 mRNA. Translation: AAA60351.1 . Different initiation.
M79464 mRNA. Translation: AAA60390.1 . Different initiation.
X63131 mRNA. Translation: CAA44841.1 .
M73778 mRNA. Translation: AAA60125.1 .
M80185 mRNA. Translation: AAA60352.1 . Different initiation.
AF230401 mRNA. Translation: AAG50180.1 .
AF230402 mRNA. Translation: AAG50181.1 .
AF230403 mRNA. Translation: AAG50182.1 .
AF230405 mRNA. Translation: AAG50184.1 .
AF230406 mRNA. Translation: AAG50185.1 .
AF230407 mRNA. Translation: AAG50186.1 .
AF230408 mRNA. Translation: AAG50187.1 .
AF230409 mRNA. Translation: AAG50188.1 .
AF230410 mRNA. Translation: AAG50189.1 .
AF230411 mRNA. Translation: AAG50190.1 .
BT009911 mRNA. Translation: AAP88913.1 .
AB209411 mRNA. Translation: BAD92648.1 . Different initiation.
AC013486 Genomic DNA. No translation available.
AC108137 Genomic DNA. No translation available.
BC000080 mRNA. Translation: AAH00080.2 .
BC020994 mRNA. Translation: AAH20994.1 .
X64800 Genomic DNA. Translation: CAA46026.1 .
AB067754 mRNA. Translation: BAB62809.1 . Sequence problems.
CCDSi CCDS10255.1. [P29590-1 ]
CCDS10256.1. [P29590-10 ]
CCDS10257.1. [P29590-8 ]
CCDS10258.1. [P29590-13 ]
CCDS45297.1. [P29590-5 ]
CCDS45298.1. [P29590-2 ]
CCDS45299.1. [P29590-4 ]
CCDS45300.1. [P29590-14 ]
CCDS58386.1. [P29590-12 ]
PIRi A40044.
I38054.
S19244.
S42516.
S44381.
RefSeqi NP_002666.1. NM_002675.3. [P29590-5 ]
NP_150241.2. NM_033238.2. [P29590-1 ]
NP_150242.1. NM_033239.2. [P29590-8 ]
NP_150243.2. NM_033240.2. [P29590-2 ]
NP_150247.2. NM_033244.3. [P29590-4 ]
NP_150249.1. NM_033246.2. [P29590-14 ]
NP_150250.2. NM_033247.2. [P29590-10 ]
NP_150252.1. NM_033249.2. [P29590-12 ]
NP_150253.2. NM_033250.2. [P29590-13 ]
UniGenei Hs.526464.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BOR NMR - A 49-104 [» ]
ProteinModelPortali P29590.
SMRi P29590. Positions 49-104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111384. 179 interactions.
IntActi P29590. 67 interactions.
MINTi MINT-158826.
STRINGi 9606.ENSP00000268058.

PTM databases

PhosphoSitei P29590.

Polymorphism databases

DMDMi 215274219.

Proteomic databases

MaxQBi P29590.
PaxDbi P29590.
PRIDEi P29590.

Protocols and materials databases

DNASUi 5371.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268058 ; ENSP00000268058 ; ENSG00000140464 . [P29590-1 ]
ENST00000268059 ; ENSP00000268059 ; ENSG00000140464 . [P29590-8 ]
ENST00000354026 ; ENSP00000315434 ; ENSG00000140464 . [P29590-13 ]
ENST00000359928 ; ENSP00000353004 ; ENSG00000140464 . [P29590-14 ]
ENST00000395132 ; ENSP00000378564 ; ENSG00000140464 . [P29590-10 ]
ENST00000395135 ; ENSP00000378567 ; ENSG00000140464 . [P29590-5 ]
ENST00000435786 ; ENSP00000395576 ; ENSG00000140464 . [P29590-2 ]
ENST00000436891 ; ENSP00000394642 ; ENSG00000140464 . [P29590-4 ]
ENST00000564428 ; ENSP00000457023 ; ENSG00000140464 . [P29590-12 ]
ENST00000565898 ; ENSP00000455838 ; ENSG00000140464 . [P29590-11 ]
ENST00000567543 ; ENSP00000456277 ; ENSG00000140464 . [P29590-14 ]
ENST00000569477 ; ENSP00000455612 ; ENSG00000140464 . [P29590-9 ]
ENST00000569965 ; ENSP00000456486 ; ENSG00000140464 . [P29590-4 ]
GeneIDi 5371.
KEGGi hsa:5371.
UCSCi uc002awk.3. human. [P29590-8 ]
uc002awl.3. human. [P29590-14 ]
uc002awm.3. human. [P29590-2 ]
uc002awn.3. human. [P29590-4 ]
uc002awo.3. human. [P29590-13 ]
uc002awr.3. human. [P29590-5 ]
uc002aws.3. human. [P29590-12 ]
uc002awu.3. human. [P29590-11 ]
uc002awv.3. human. [P29590-1 ]

Organism-specific databases

CTDi 5371.
GeneCardsi GC15P074287.
HGNCi HGNC:9113. PML.
HPAi CAB010194.
CAB016304.
HPA008312.
MIMi 102578. gene.
neXtProti NX_P29590.
Orphaneti 520. Acute promyelocytic leukemia.
PharmGKBi PA33439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG326718.
GeneTreei ENSGT00510000048454.
HOVERGENi HBG000552.
InParanoidi P29590.
KOi K10054.
OMAi SDAENSC.
OrthoDBi EOG7M98FM.
PhylomeDBi P29590.
TreeFami TF336434.

Enzyme and pathway databases

Reactomei REACT_25078. Interferon gamma signaling.
SignaLinki P29590.

Miscellaneous databases

ChiTaRSi PML. human.
EvolutionaryTracei P29590.
GeneWikii Promyelocytic_leukemia_protein.
GenomeRNAii 5371.
NextBioi 20820.
PMAP-CutDB P29590.
PROi P29590.
SOURCEi Search...

Gene expression databases

Bgeei P29590.
CleanExi HS_PML.
ExpressionAtlasi P29590. baseline and differential.
Genevestigatori P29590.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view ]
SMARTi SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR."
    de The H., Lavau C., Marchio A., Chomienne C., Degos L., Dejean A.
    Cell 66:675-684(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3), DISEASE.
  2. "Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia."
    Goddard A.D., Borrow J., Freemont P.S., Solomon E.
    Science 254:1371-1374(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-5 AND PML-8), CHROMOSOMAL TRANSLOCATION WITH RARA, DISEASE, VARIANT LEU-645.
  3. "Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins."
    Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., Chambon P.
    EMBO J. 11:629-642(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-4).
  4. "Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML."
    Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr., Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M.
    Cell 66:663-674(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2; PML-4; PML-5; PML-6; PML-7; PML-8; PML-12 AND PML-14), VARIANT LEU-645.
  6. Goddard A.D., Solomon E.
    Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13).
  8. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-11).
    Tissue: Brain.
  9. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13).
    Tissue: Kidney.
  11. "Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants."
    Tong J.H., Dong S., Geng J.P., Huang W., Wang Z.Y., Sun G.L., Chen S.J., Chen Z., Larsen C.-J., Berger R.
    Oncogene 7:311-316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466, CHROMOSOMAL TRANSLOCATION WITH RARA.
  12. "Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic leukemia: structure of the fusion point in a case lacking classic t(15;17) translocation."
    Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K., Omine M.
    Leuk. Lymphoma 44:111-115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, CHROMOSOMAL TRANSLOCATION WITH RARA.
  13. Cited for: SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65; LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, FUNCTION.
  14. "Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML."
    Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.
    J. Cell Sci. 111:1319-1329(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM27.
  15. "An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm."
    Borden K.L., Campbell-Dwyer E.J., Salvato M.S.
    J. Virol. 72:758-766(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LASSA VIRUS Z PROTEIN.
  16. "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins."
    Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H., Kalantry S., Freedman L.P., Pandolfi P.P.
    Nat. Genet. 23:287-295(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RARA; RXRA AND TRIM24.
  17. "Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis."
    Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P.
    J. Exp. Med. 191:631-640(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX.
  18. "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
    Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
    Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
  19. Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
  20. "PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator."
    Regad T., Saib A., Lallemand-Breitenbach V., Pandolfi P.P., de The H., Chelbi-Alix M.K.
    EMBO J. 20:3495-3505(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HFV RESTRICTION, INTERACTION WITH HFV BEL1 AND BET, SUBCELLULAR LOCATION.
  21. "PML protein isoforms and the RBCC/TRIM motif."
    Jensen K., Shiels C., Freemont P.S.
    Oncogene 20:7223-7233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE OF ISOFORMS PML-1 THROUGH PML-7.
  22. "Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence."
    Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T.
    EMBO J. 21:2383-2396(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRT1.
  23. Cited for: SUMOYLATION, DESUMOYLATION BY SENP2.
  24. "PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2."
    Yang S., Kuo C., Bisi J.E., Kim M.K.
    Nat. Cell Biol. 4:865-870(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR, PHOSPHORYLATION AT SER-117 BY CHEK2, INTERACTION WITH CHEK2.
  25. "Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies."
    Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P., De The H., Chelbi-Alix M.K.
    Oncogene 21:7957-7970(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABIES VIRUS PHOSPHOPROTEINS, SUBCELLULAR LOCATION, FUNCTION.
  26. "The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation."
    Louria-Hayon I., Grossman T., Sionov R.V., Alsheich O., Pandolfi P.P., Haupt Y.
    J. Biol. Chem. 278:33134-33141(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2 AND TP53.
  27. "PML colocalizes with and stabilizes the DNA damage response protein TopBP1."
    Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S.
    Mol. Cell. Biol. 23:4247-4256(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOPBP1.
  28. "The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome."
    Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S.
    J. Biol. Chem. 279:5374-5379(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH1, DEGRADATION.
  29. "Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein."
    Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., Matsuzaki K., Nakao M., Li J.-D., Kai H.
    J. Biol. Chem. 279:19091-19098(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ELF4, SUBCELLULAR LOCATION.
  30. "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle."
    Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V., Valle G., Faulkner G.
    J. Mol. Biol. 339:313-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD2.
  31. "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
    Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
    Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2 AND RPL11, PHOSPHORYLATION BY ATR IN RESPONSE TO DNA DAMAGE, SUBCELLULAR LOCATION.
  32. "PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein."
    Daniels M.J., Marson A., Venkitaraman A.R.
    Nat. Struct. Mol. Biol. 11:1114-1121(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHFR.
  33. "Cytoplasmic PML function in TGF-beta signalling."
    Lin H.K., Bergmann S., Pandolfi P.P.
    Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFBR1; TGFBR2; SMAD2; SMAD3 AND ZFYVE9/SARA.
  34. "Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation."
    Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.
    Biochem. Biophys. Res. Commun. 330:746-754(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF PML-RARALPHA ONCOPROTEIN WITH UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF CYS-88 AND PRO-89.
  35. "Characterization of endogenous human promyelocytic leukemia isoforms."
    Condemine W., Takahashi Y., Zhu J., Puvion-Dutilleul F., Guegan S., Janin A., de The H.
    Cancer Res. 66:6192-6198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  36. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527 AND SER-530, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565 (ISOFORM PML-5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-527 AND SER-530 (ISOFORM PML-6), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. "Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR."
    Dellaire G., Ching R.W., Ahmed K., Jalali F., Tse K.C., Bristow R.G., Bazett-Jones D.P.
    J. Cell Biol. 175:55-66(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. "Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense."
    Pampin M., Simonin Y., Blondel B., Percherancier Y., Chelbi-Alix M.K.
    J. Virol. 80:8582-8592(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POLIOVIRUS RESTRICTION.
  39. Cited for: SUBUNIT, SUMOYLATION, SUMO-BINDING MOTIF, MUTAGENESIS OF CYS-57 AND CYS-60, SUBCELLULAR LOCATION.
  40. "Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein."
    Shimada N., Shinagawa T., Ishii S.
    Genes Cells 13:245-254(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKM, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-487 AND LYS-490.
  41. "Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis."
    Hayakawa F., Abe A., Kitabayashi I., Pandolfi P.P., Naoe T.
    J. Biol. Chem. 283:24420-24425(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-487 AND LYS-515, MUTAGENESIS OF LYS-487 AND LYS-515.
  42. "Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection."
    Tavalai N., Papior P., Rechter S., Stamminger T.
    J. Virol. 82:126-137(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HCMV RESTRICTION.
  43. "The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network."
    Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F., Teruya-Feldstein J., Pandolfi P.P.
    Nature 455:813-817(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  44. "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
    Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
    Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYUBIQUITINATION AT LYS-380; LYS-400; LYS-401 AND LYS-476 BY RNF4, PROTEASOMAL DEGRADATION, SUMOYLATION.
  45. "Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus."
    Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A., Galande S.
    Nat. Cell Biol. 9:45-56(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SATB1.
  46. "A role for cytoplasmic PML in cellular resistance to viral infection."
    McNally B.A., Trgovcich J., Maul G.G., Liu Y., Zheng P.
    PLoS ONE 3:E2277-E2277(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HHV-1 RESTRICTION, SUBCELLULAR LOCATION.
  47. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  48. "Differential suppressive effect of promyelocytic leukemia protein on the replication of different subtypes/strains of influenza A virus."
    Li W., Wang G., Zhang H., Zhang D., Zeng J., Chen X., Xu Y., Li K.
    Biochem. Biophys. Res. Commun. 389:84-89(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLUENZA A VIRUS RESTRICTION.
  49. "PML-IV functions as a negative regulator of telomerase by interacting with TERT."
    Oh W., Ghim J., Lee E.W., Yang M.R., Kim E.T., Ahn J.H., Song J.
    J. Cell Sci. 122:2613-2622(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TERT.
  50. "PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage."
    Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K., Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L.
    Oncogene 28:698-708(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-8 AND SER-38 BY HIPK2, INTERACTION WITH HIPK2.
  51. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  52. "Resistance to rabies virus infection conferred by the PMLIV isoform."
    Blondel D., Kheddache S., Lahaye X., Dianoux L., Chelbi-Alix M.K.
    J. Virol. 84:10719-10726(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RABIES VIRUS RESTRICTION.
  53. "Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies."
    Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T.
    Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, UBIQUITINATION.
  54. "Functional polymorphism of the CK2alpha intronless gene plays oncogenic roles in lung cancer."
    Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M., You L.
    PLoS ONE 5:E11418-E11418(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK2A1 AND CSNK2A3.
  55. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-527, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  56. Cited for: INTERACTION WITH UBC9, SUBUNIT, UBIQUITINATION, SUMOYLATION, ARSENIC BINDING, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.
  57. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  58. "Promyelocytic leukemia protein interacts with werner syndrome helicase and regulates double-strand break repair in gamma-irradiation-induced DNA damage responses."
    Liu J., Song Y., Qian J., Liu B., Dong Y., Tian B., Sun Z.
    Biochemistry (Mosc.) 76:550-554(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH WRN.
  59. "A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression."
    Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C., Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H., Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.
    Cancer Cell 20:214-228(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, PHOSPHORYLATION AT SER-518, MUTAGENESIS OF SER-518.
  60. "The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites."
    Pinton P., Giorgi C., Pandolfi P.P.
    Cell Death Differ. 18:1450-1456(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  61. "The nuclear bodies inside out: PML conquers the cytoplasm."
    Carracedo A., Ito K., Pandolfi P.P.
    Curr. Opin. Cell Biol. 23:360-366(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  62. "Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
    Lim J.H., Liu Y., Reineke E., Kao H.Y.
    J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-403; SER-505; SER-518 AND SER-527, INTERACTION WITH PIN1 AND MAPK1.
  63. "PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication."
    Cuchet D., Sykes A., Nicolas A., Orr A., Murray J., Sirma H., Heeren J., Bartelt A., Everett R.D.
    J. Cell Sci. 124:280-291(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  64. "Role of promyelocytic leukemia protein in host antiviral defense."
    Geoffroy M.C., Chelbi-Alix M.K.
    J. Interferon Cytokine Res. 31:145-158(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN ANTIVIRAL DEFENSE.
  65. "Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies."
    Maroui M.A., Pampin M., Chelbi-Alix M.K.
    J. Virol. 85:13164-13173(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EMCV RESTRICTION, INTERACTION WITH EMCV P3D-POL.
  66. "The SUMO protease SENP6 is a direct regulator of PML nuclear bodies."
    Hattersley N., Shen L., Jaffray E.G., Hay R.T.
    Mol. Biol. Cell 22:78-90(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, DESUMOYLATION BY SENP6.
  67. Cited for: REVIEW ON FUNCTION.
  68. "Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against Varicella-Zoster virus."
    Reichelt M., Wang L., Sommer M., Perrino J., Nour A.M., Sen N., Baiker A., Zerboni L., Arvin A.M.
    PLoS Pathog. 7:E1001266-E1001266(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN VARICELLA ZOSTER RESTRICTION, SUBCELLULAR LOCATION, INTERACTION WITH VZV VP26.
  69. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-527 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  70. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
    Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
    Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-65 AND LYS-160, PHOSPHORYLATION AT SER-565, SUBCELLULAR LOCATION, INTERACTION WITH PIAS1; PIAS2 AND CSNK2A1.
  71. "MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs."
    Peche L.Y., Scolz M., Ladelfa M.F., Monte M., Schneider C.
    Cell Death Differ. 19:926-936(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MAGEA2.
  72. "Role of the promyelocytic leukaemia protein in cell death regulation."
    Salomoni P., Dvorkina M., Michod D.
    Cell Death Dis. 3:E247-E247(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  73. "Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence."
    Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M., Dejean A., Bischof O.
    EMBO J. 31:95-109(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBX2; TBX3; E2F4 AND RBL2.
  74. Cited for: FUNCTION IN CIRCADIAN CLOCK, SUBCELLULAR LOCATION, INTERACTION WITH PER2, ACETYLATION AT LYS-487, DEACETYLATION BY SIRT1.
  75. "Post-translational modifications of PML: consequences and implications."
    Cheng X., Kao H.Y.
    Front. Oncol. 2:210-210(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON PTM.
  76. "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells."
    Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T.
    Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-490, INTERACTION WITH HDAC7; RANBP2 AND CTNNB1-TCF7L2 COMPLEX.
  77. "Moloney murine leukemia virus integrase and reverse transcriptase interact with PML proteins."
    Okino Y., Inayoshi Y., Kojima Y., Kidani S., Kaneoka H., Honkawa A., Higuchi H., Nishijima K., Miyake K., Iijima S.
    J. Biochem. 152:161-169(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOMLV IN AND RT, SUBCELLULAR LOCATION.
  78. "Promyelocytic leukemia protein (PML) regulates endothelial cell network formation and migration in response to tumor necrosis factor alpha (TNFalpha) and interferon alpha (IFNalpha)."
    Cheng X., Liu Y., Chu H., Kao H.Y.
    J. Biol. Chem. 287:23356-23367(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  79. "Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation."
    Geng Y., Monajembashi S., Shao A., Cui D., He W., Chen Z., Hemmerich P., Tang J.
    J. Biol. Chem. 287:30729-30742(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN C-TERMINAL.
  80. "The role of PML ubiquitination in human malignancies."
    Chen R.H., Lee Y.R., Yuan W.C.
    J. Biomed. Sci. 19:81-81(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON UBIQUITINATION.
  81. "PML promotes MHC class II gene expression by stabilizing the class II transactivator."
    Ulbricht T., Alzrigat M., Horch A., Reuter N., von Mikecz A., Steimle V., Schmitt E., Kraemer O.H., Stamminger T., Hemmerich P.
    J. Cell Biol. 199:49-63(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CIITA.
  82. Cited for: FUNCTION, TISSUE SPECIFICITY.
  83. "Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation."
    Cuchet-Lourenco D., Vanni E., Glass M., Orr A., Everett R.D.
    J. Virol. 86:11209-11222(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 ICP0.
  84. "BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction."
    Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D.
    Oncogene 32:3156-3164(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MDM2 AND MAPK7.
  85. "The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein."
    Guan D., Factor D., Liu Y., Wang Z., Kao H.Y.
    Oncogene 32:3819-3828(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY UHRF1.
  86. "Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms."
    Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K.
    PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, INTERACTION WITH RNF4, DOMAIN SIM.
  87. Cited for: FUNCTION.
  88. "Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human."
    Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., Kuo W.C., Chuang Y.T., Jiang S.T., Shih H.M., Lai M.Z.
    Blood 121:3185-3194(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRP3.
  89. "The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription."
    Berscheminski J., Groitl P., Dobner T., Wimmer P., Schreiner S.
    J. Virol. 87:965-977(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS 2 E1A.
  90. "MOZ increases p53 acetylation and premature senescence through its complex formation with PML."
    Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., Prives C.
    Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KAT6A.
  91. "The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML."
    Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S., Howe K., Solomon E., Freemont P.S.
    EMBO J. 14:1532-1541(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 49-104.

Entry informationi

Entry nameiPML_HUMAN
AccessioniPrimary (citable) accession number: P29590
Secondary accession number(s): E9PBR7
, P29591, P29592, P29593, Q00755, Q15959, Q59FP9, Q8WUA0, Q96S41, Q9BPW2, Q9BWP7, Q9BZX6, Q9BZX7, Q9BZX8, Q9BZX9, Q9BZY0, Q9BZY2, Q9BZY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 185 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3