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IID00900
 UniprotP29590
ProteinProtein PML
GenePML
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
882
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 49-99 Homo tetramer :
 Evidence X-RAY 5yuf D Reference
       Region 5yuf D 49-50 disorder
       Region 5yuf D 51-96 order
       Region 5yuf D 97-99 disorder
 Evidence X-RAY 5yuf C Reference
       Region 5yuf C 49-51 disorder
       Region 5yuf C 52-97 order
       Region 5yuf C 98-99 disorder
 Evidence X-RAY 5yuf B Reference
       Region 5yuf B 49-50 disorder
       Region 5yuf B 51-97 order
       Region 5yuf B 98-99 disorder
 Evidence X-RAY 5yuf A Reference
       Region 5yuf A 49-50 disorder
       Region 5yuf A 51-97 order
       Region 5yuf A 98-99 disorder
Seq 49-104 Monomer :
 Evidence NMR 2mwx A Reference
       Region 2mwx A 49-104 order
       Region 2mwx A 49-51 high_rmsd
 Evidence NMR 1bor A Reference
       Region 1bor A 49-104 order
Seq 120-168 Homo tetramer :
 Evidence X-RAY 6imq D Reference
       Region 6imq D 120-167 order
       Region 6imq D 168-168 disorder
 Evidence X-RAY 6imq C Reference
       Region 6imq C 120-167 order
       Region 6imq C 168-168 disorder
 Evidence X-RAY 6imq B Reference
       Region 6imq B 120-168 order
 Evidence X-RAY 6imq A Reference
       Region 6imq A 120-167 order
       Region 6imq A 168-168 disorder
Seq 120-168 Homo dimer :
 Evidence NMR 2mvw B Reference
       Region 2mvw B 120-168 order
       Region 2mvw B 120-122 high_rmsd
 Evidence NMR 2mvw A Reference
       Region 2mvw A 120-168 order
       Region 2mvw A 120-123 high_rmsd
Seq 183-236 Homo dimer :
 Evidence X-RAY 8j2p E Reference
       Region 8j2p E 183-185 disorder
       Region 8j2p E 186-227 order
       Region 8j2p E 228-236 disorder
 Evidence X-RAY 8j2p A Reference
       Region 8j2p A 183-185 disorder
       Region 8j2p A 186-227 order
       Region 8j2p A 228-236 disorder
Seq 183-236 Monomer :
 Evidence X-RAY 8j25 A Reference
       Region 8j25 A 183-185 disorder
       Region 8j25 A 186-227 order
       Region 8j25 A 228-236 disorder
Seq 546-574 Hetero dimer : IID00378Complex
 Evidence X-RAY 4wjn B Reference
       Region 4wjn B 547-551 disorder
       Region 4wjn B 552-562 order
       Region 4wjn B 563-568 disorder
       Region 4wjn B 569-573 order
 Evidence X-RAY 4wjo B Reference
       Region 4wjo B 547-551 disorder
       Region 4wjo B 552-560 order
       Region 4wjo B 561-568 disorder
       Region 4wjo B 569-573 order
 Evidence X-RAY 8djh B Reference
       Region 8djh B 546-551 disorder
       Region 8djh B 552-562 order
       Region 8djh B 563-565 disorder
       Region 8djh B 566-573 order
 Evidence X-RAY 8dji B Reference
       Region 8dji B 547-551 disorder
       Region 8dji B 552-560 order
       Region 8dji B 561-568 disorder
       Region 8dji B 569-574 order
 Evidence X-RAY 6uyp B Reference
       Region 6uyp B 547-551 disorder
       Region 6uyp B 552-560 order
       Region 6uyp B 561-568 disorder
       Region 6uyp B 569-574 order
 Evidence X-RAY 6uyq B Reference
       Region 6uyq B 547-551 disorder
       Region 6uyq B 552-560 order
       Region 6uyq B 561-568 disorder
       Region 6uyq B 569-574 order
 Evidence X-RAY 6uyr B Reference
       Region 6uyr B 547-550 disorder
       Region 6uyr B 551-560 order
       Region 6uyr B 561-568 disorder
       Region 6uyr B 569-574 order
 Evidence X-RAY 6uyt B Reference
       Region 6uyt B 547-551 disorder
       Region 6uyt B 552-562 order
       Region 6uyt B 563-568 disorder
       Region 6uyt B 569-574 order
 Evidence X-RAY 6uyv B Reference
       Region 6uyv B 547-550 disorder
       Region 6uyv B 551-560 order
       Region 6uyv B 561-568 disorder
       Region 6uyv B 569-574 order
Seq 547-574 Hetero tetramer : IID00378Complex
 Evidence X-RAY 6uyo B Reference
       Region 6uyo B 547-551 disorder
       Region 6uyo B 552-563 order
       Region 6uyo B 564-574 disorder
 Evidence X-RAY 6uyo D Reference
       Region 6uyo D 547-551 disorder
       Region 6uyo D 552-560 order
       Region 6uyo D 561-574 disorder
 Evidence X-RAY 6uys B Reference
       Region 6uys B 547-551 disorder
       Region 6uys B 552-563 order
       Region 6uys B 564-574 disorder
 Evidence X-RAY 6uys D Reference
       Region 6uys D 547-551 disorder
       Region 6uys D 552-562 order
       Region 6uys D 563-574 disorder
 Evidence X-RAY 6uyu B Reference
       Region 6uyu B 547-550 disorder
       Region 6uyu B 551-562 order
       Region 6uyu B 563-574 disorder
 Evidence X-RAY 6uyu D Reference
       Region 6uyu D 547-551 disorder
       Region 6uyu D 552-562 order
       Region 6uyu D 563-574 disorder
SeqProS predicted 551-574 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00378Complex
       Region 4wjo B 552-560 order
       Region 4wjo B 569-573 order
       Region 4wjn B 552-562 order
       Region 4wjn B 569-573 order
       Region 6uyt B 552-562 order
       Region 6uyt B 569-574 order
       Region 6uyq B 552-560 order
       Region 6uyq B 569-574 order
       Region 6uyp B 552-560 order
       Region 6uyp B 569-574 order
       Region 6uyr B 551-560 order
       Region 6uyr B 569-574 order
       Region 6uyv B 551-560 order
       Region 8dji B 552-560 order
       Region 8dji B 569-574 order
       Region 8djh B 552-562 order
       Region 8djh B 566-573 order
SeqProS predicted 551-574 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero tetramer : IID00378Complex
       Region 6uys B 552-563 order
       Region 6uys D 552-562 order
       Region 6uyu B 551-562 order
       Region 6uyu D 552-562 order
       Region 6uyo B 552-563 order
       Region 6uyo D 552-560 order
Seqphosphorylation
    530-530 Phosphoserine
    527-527 Phosphoserine
    518-518 Phosphoserine
    565-565 Phosphoserine
    867-867 Phosphothreonine
    530-530 Phosphoserine; by MAPK1
    565-565 Phosphoserine; by CK2
    527-527 Phosphoserine; by MAPK1
    518-518 Phosphoserine; by CDK1 and CDK2
    512-512 Phosphoserine
    505-505 Phosphoserine; by MAPK1
    504-504 Phosphoserine
    493-493 Phosphoserine
    403-403 Phosphoserine; by MAPK1 and MAPK7
    117-117 Phosphoserine; by CHEK2
    36-36 Phosphoserine; by HIPK2 and MAPK1
    48-48 Phosphoserine
    38-38 Phosphoserine; by HIPK2 and MAPK1
    8-8 Phosphoserine; by HIPK2
Seqacetylation
    515-515 N6-acetyllysine
    487-487 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-50,177-181,395-604,831-882
Order 51-176,186-394,605-830
ProS 177-181,454-458,487-490,521-525,553-559,842-854,871-876
AlphaFold
Disorder 1-50,83-85,97-101,183-185,365-372,392-607,642-650,760-764,828-840,855-882
Order 51-82,86-96,102-182,186-364,373-391,608-641,651-759,765-827,841-854
Pfam Hmmer
PF00097 57-91 4.8e-05
PF00643 124-166 5e-11
PF00643 184-232 3.2e-05
SEG 15-29 ,280-295 ,560-588
Function
Function in SwissProt
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 (HHV-5) 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. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response (PubMed:20972456, PubMed:28250117). Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity (PubMed:20972456, PubMed:28250117).