PML iso2 a zinc-finger protein that can regulate transcription and can localize to nuclear bodies. Cytoplasmic forms regulate glycolysis by inhibiting the tetrameric form of PKM2. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Interacts with SIRT1, TOPBP1, TRIM27 and TRIM69. Sumoylated forms interact with SATB1 and localize to the PML nuclear bodies. Sumoylation on three sites is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. The B1 box and the RING finger are also required for localization to nuclear bodies. May play an important role in recruitment of ELF4 into PML nuclear bodies. A chromosomal aberration involving PML can cause acute promyelocytic leukemia (APL). Seven alternatively-spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Nucleolus; Oncoprotein; Transcription factor; Tumor suppressor; Ubiquitin conjugating system
Chromosomal Location of Human Ortholog: 15q24.1
Cellular Component:  cytoplasm; cytosol; early endosome membrane; heterochromatin; nuclear chromosome, telomeric region; nuclear matrix; nucleolus; nucleoplasm; nucleus; PML body
Molecular Function:  DNA binding; protein binding; protein homodimerization activity; SMAD binding; SUMO binding; ubiquitin protein ligase binding; zinc ion binding
Biological Process:  activation of cysteine-type endopeptidase activity involved in apoptotic process; cell cycle arrest; cell fate commitment; circadian regulation of gene expression; common-partner SMAD protein phosphorylation; defense response to virus; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; endoplasmic reticulum calcium ion homeostasis; entrainment of circadian clock by photoperiod; induction of apoptosis by oxidative stress; innate immune response; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; maintenance of protein location in nucleus; myeloid cell differentiation; negative regulation of angiogenesis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of interleukin-1 beta secretion; negative regulation of transcription, DNA-dependent; PML body organization and biogenesis; positive regulation of fibroblast proliferation; positive regulation of MHC class I biosynthetic process; positive regulation of telomere maintenance; positive regulation of transcription from RNA polymerase II promoter; proteasomal ubiquitin-dependent protein catabolic process; protein complex assembly; regulation of cell adhesion; regulation of circadian rhythm; regulation of protein amino acid phosphorylation; regulation of transcription, DNA-templated; response to cytokine; response to gamma radiation; response to hypoxia; response to UV; retinoic acid receptor signaling pathway; SMAD protein import into nucleus; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; viral process
Reference #:  P29590-2 (UniProtKB)
Alt. Names/Synonyms: MYL; PML; PP8675; Probable transcription factor PML; promyelocytic leukemia; promyelocytic leukemia protein; promyelocytic leukemia, inducer of; Protein PML; RING finger protein 71; RNF71; TRIM19; tripartite motif protein TRIM19; Tripartite motif-containing protein 19
Gene Symbols: PML
Molecular weight: 67,471 Da
Basal Isoelectric point: 5.96  Predict pI for various phosphorylation states
Select Structure to View Below

PML iso2

Protein Structure Not Found.


Cross-references to other databases:  cBioPortal  |  Wikipedia  |  Pfam  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein