Protein PML

NameProtein PML
Synonyms
  • MYL
  • PP8675
  • Promyelocytic leukemia protein
  • RING finger protein 71
  • RNF71
  • TRIM19
  • Tripartite motif-containing protein 19
Gene NamePML
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009837|Protein PML
MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQC
QAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYR
QIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDG
TRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEEL
DAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEA
VDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLR
QEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPE
EAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCS
QTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLP
NSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENL
ADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQ
HFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPG
ASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFAS
LQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPA
FNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS
Number of residues882
Molecular Weight97549.475
Theoretical pINot Available
GO Classification
Functions
  • zinc ion binding
  • DNA binding
  • cobalt ion binding
  • protein heterodimerization activity
  • ubiquitin protein ligase binding
  • transcription coactivator activity
  • SMAD binding
  • protein homodimerization activity
  • SUMO binding
Processes
  • negative regulation of telomere maintenance via telomerase
  • negative regulation of transcription, DNA-templated
  • entrainment of circadian clock by photoperiod
  • intrinsic apoptotic signaling pathway in response to DNA damage
  • extrinsic apoptotic signaling pathway
  • negative regulation of translation in response to oxidative stress
  • positive regulation of defense response to virus by host
  • negative regulation of interleukin-1 beta secretion
  • regulation of transcription, DNA-templated
  • protein stabilization
  • regulation of calcium ion transport into cytosol
  • negative regulation of cell growth
  • negative regulation of mitotic cell cycle
  • apoptotic process
  • negative regulation of angiogenesis
  • regulation of double-strand break repair
  • viral process
  • PML body organization
  • negative regulation of cell proliferation
  • negative regulation of viral release from host cell
  • positive regulation of MHC class I biosynthetic process
  • positive regulation of apoptotic process involved in mammary gland involution
  • positive regulation of histone deacetylation
  • positive regulation of transcription from RNA polymerase II promoter
  • positive regulation of protein localization to chromosome, telomeric region
  • cell cycle arrest
  • regulation of circadian rhythm
  • response to hypoxia
  • branching involved in mammary gland duct morphogenesis
  • protein targeting
  • response to UV
  • fibroblast migration
  • regulation of cell adhesion
  • retinoic acid receptor signaling pathway
  • regulation of signal transduction by p53 class mediator
  • positive regulation of fibroblast proliferation
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
  • transcription, DNA-templated
  • cellular senescence
  • protein complex assembly
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
  • regulation of protein phosphorylation
  • transforming growth factor beta receptor signaling pathway
  • intrinsic apoptotic signaling pathway in response to oxidative stress
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • maintenance of protein location in nucleus
  • positive regulation of extrinsic apoptotic signaling pathway
  • interferon-gamma-mediated signaling pathway
  • cellular response to interleukin-4
  • myeloid cell differentiation
  • response to gamma radiation
  • positive regulation of telomere maintenance
  • response to cytokine
  • common-partner SMAD protein phosphorylation
  • cell fate commitment
  • negative regulation of telomerase activity
  • activation of cysteine-type endopeptidase activity involved in apoptotic process
  • SMAD protein import into nucleus
  • circadian regulation of gene expression
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
  • endoplasmic reticulum calcium ion homeostasis
  • innate immune response
  • defense response to virus
Components
  • cytoplasm
  • PML body
  • nucleus
  • nuclear chromosome, telomeric region
  • heterochromatin
  • nuclear matrix
  • early endosome membrane
  • cytosol
  • extrinsic component of endoplasmic reticulum membrane
  • nuclear membrane
  • nucleolus
  • nucleoplasm
General FunctionFunctions 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.
Specific FunctionCobalt ion binding
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP29590
UniProtKB Entry NamePML_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0051295|Protein PML (PML)
ATGGAGCCTGCACCCGCCCGATCTCCGAGGCCCCAGCAGGACCCCGCCCGGCCCCAGGAG
CCCACCATGCCTCCCCCCGAGACCCCCTCTGAAGGCCGCCAGCCCAGCCCCAGCCCCAGC
CCTACAGAGCGAGCCCCCGCTTCGGAGGAGGAGTTCCAGTTTCTGCGCTGCCAGCAATGC
CAGGCGGAAGCCAAGTGCCCGAAGCTGCTGCCTTGTCTGCACACGCTGTGCTCAGGATGC
CTGGAGGCGTCGGGCATGCAGTGCCCCATCTGCCAGGCGCCCTGGCCCCTAGGTGCAGAC
ACACCCGCCCTGGATAACGTCTTTTTCGAGAGTCTGCAGCGGCGCCTGTCGGTGTACCGG
CAGATTGTGGATGCGCAGGCTGTGTGCACCCGCTGCAAAGAGTCGGCCGACTTCTGGTGC
TTTGAGTGCGAGCAGCTCCTCTGCGCCAAGTGCTTCGAGGCACACCAGTGGTTCCTCAAG
CACGAGGCCCGGCCCCTAGCAGAGCTGCGCAACCAGTCGGTGCGTGAGTTCCTGGACGGC
ACCCGCAAGACCAACAACATCTTCTGCTCCAACCCCAACCACCGCACCCCTACGCTGACC
AGCATCTACTGCCGAGGATGTTCCAAGCCGCTGTGCTGCTCGTGCGCGCTCCTTGACAGC
AGCCACAGTGAGCTCAAGTGCGACATCAGCGCAGAGATCCAGCAGCGACAGGAGGAGCTG
GACGCCATGACGCAGGCGCTGCAGGAGCAGGATAGTGCCTTTGGCGCGGTTCACGCGCAG
ATGCACGCGGCCGTCGGCCAGCTGGGCCGCGCGCGTGCCGAGACCGAGGAGCTGATCCGC
GAGCGCGTGCGCCAGGTGGTAGCTCACGTGCGGGCTCAGGAGCGCGAGCTGCTGGAGGCT
GTGGACGCGCGGTACCAGCGCGACTACGAGGAGATGGCCAGTCGGCTGGGCCGCCTGGAT
GCTGTGCTGCAGCGCATCCGCACGGGCAGCGCGCTGGTGCAGAGGATGAAGTGCTACGCC
TCGGACCAGGAGGTGCTGGACATGCACGGTTTCCTGCGCCAGGCGCTCTGCCGCCTGCGC
CAGGAGGAGCCCCAGAGCCTGCAAGCTGCCGTGCGCACCGATGGCTTCGACGAGTTCAAG
GTGCGCCTGCAGGACCTCAGCTCTTGCATCACCCAGGGGAAAGATGCAGCTGTATCCAAG
AAAGCCAGCCCAGAGGCTGCCAGCACTCCCAGGGACCCTATTGACGTTGACCTGCCCGAG
GAGGCAGAGAGAGTGAAGGCCCAGGTTCAGGCCCTGGGGCTGGCTGAAGCCCAGCCTATG
GCTGTGGTACAGTCAGTGCCCGGGGCACACCCCGTGCCAGTGTACGCCTTCTCCATCAAA
GGCCCTTCCTATGGAGAGGATGTCTCCAATACAACGACAGCCCAGAAGAGGAAGTGCAGC
CAGACCCAGTGCCCCAGGAAGGTCATCAAGATGGAGTCTGAGGAGGGGAAGGAGGCAAGG
TTGGCTCGGAGCTCCCCGGAGCAGCCCAGGCCCAGCACCTCCAAGGCAGTCTCACCACCC
CACCTGGATGGACCGCCTAGCCCCAGGAGCCCCGTCATAGGAAGTGAGGTCTTCCTGCCC
AACAGCAACCACGTGGCCAGTGGCGCCGGGGAGGCAGAGGAACGCGTTGTGGTGATCAGC
AGCTCGGAAGACTCAGATGCCGAAAACTCGTCCTCCCGAGAGCTGGATGACAGCAGCAGT
GAGTCCAGTGACCTCCAGCTGGAAGGCCCCAGCACCCTCAGGGTCCTGGACGAGAACCTT
GCTGACCCCCAAGCAGAAGACAGACCTCTGGTTTTCTTTGACCTCAAGATTGACAATGAA
ACCCAGAAGATTAGCCAGCTGGCTGCGGTGAACCGGGAAAGCAAGTTCCGCGTGGTCATC
CAGCCTGAAGCCTTCTTCAGCATCTACTCCAAGGCCGTGTCCCTGGAGGTGGGGCTGCAG
CACTTCCTCAGCTTTCTGAGCTCCATGCGCCGCCCTATCTTGGCCTGCTACAAGCTGTGG
GGGCCTGGCCTCCCAAACTTCTTCCGGGCCCTGGAGGACATTAACAGGCTGTGGGAATTC
CAGGAGGCCATCTCGGGCTTCCTGGCTGCCCTGCCTCTCATCCGGGAGCGTGTGCCCGGG
GCCAGCAGCTTCAAACTCAAGAACCTGGCCCAGACCTACCTGGCGAGAAACATGAGCGAG
CGCAGCGCCATGGCTGCCGTGCTGGCCATGCGTGACCTGTGCCGCCTCCTCGAGGTCTCC
CCGGGCCCCCAGCTGGCCCAGCATGTCTACCCCTTCAGTAGCCTGCAGTGCTTTGCCTCC
CTGCAGCCCCTGGTGCAGGCAGCTGTGCTGCCCCGGGCTGAGGCCCGCCTCCTGGCCCTA
CACAACGTGAGCTTCATGGAGCTGCTGAGTGCACACCGCCGTGACCGGCAGGGGGGCCTG
AAGAAGTACAGCCGCTATCTAAGCCTGCAGACCACCACGTTGCCCCCTGCCCAGCCTGCT
TTCAACCTGCAGGCTCTGGGCACCTACTTTGAAGGCCTGTTGGAGGGTCCGGCGCTGGCA
CGGGCAGAAGGAGTCTCCACCCCACTTGCTGGCCGTGGCTTGGCAGAGAGGGCCTCCCAG
CAGAGCTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:9113
Chromosome Location15
Locus15q24.1
References
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