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P29590 (PML_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PML
Alternative name(s):
Promyelocytic leukemia protein
RING finger protein 71
Tripartite motif-containing protein 19
Gene names
Name:PML
Synonyms:MYL, RNF71, TRIM19
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum By similarity. Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM2. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitinylation. Ref.13 Ref.16 Ref.17 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.29 Ref.30 Ref.32 Ref.36 Ref.40 Ref.42 Ref.45 Ref.46 Ref.51 Ref.53

Subunit structure

Key component of PML bodies. PML bodies are formed by the interaction of PML homodimers (via SUMO-binding motif) with sumoylated PML, leading to the assembly of higher oligomers. Several types of PML bodies have been observed. PML bodies can form hollow spheres that can sequester target proteins inside. Interacts (via SUMO-binding motif) with sumoylated proteins. Interacts (via C-terminus) with p53/TP53. Recruits p53/TP53 and CHEK2 into PML bodies, which promotes p53/TP53 phosphorylation at 'Ser-20' and prevents its proteasomal degradation. Interacts with MDM2, and sequesters MDM2 in the nucleolus, thereby preventing ubiquitination of p53/TP53. Interaction with PML-RARA oncoprotein and certain viral proteins causes disassembly of PML bodies and abolishes the normal PML function. Interacts with HIPK2, TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts with ITPR3 By similarity. Interacts (in the cytoplasm) with TGFBR1, TGFBR2 and PKM2. 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. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.37 Ref.40 Ref.45 Ref.46 Ref.47 Ref.50

Subcellular location

Nucleus › nucleoplasm. Cytoplasm. Nucleus › PML body. Nucleus › nucleolus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Sumoylated forms localize to the PML nuclear bodies. The B1 box and the RING finger are also required for this nuclear localization. Isoforms lacking a nuclear localization signal are cytoplasmic. Detected in the nucleolus after DNA damage. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein. Ref.13 Ref.18 Ref.19 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.37 Ref.40 Ref.42

Domain

Interacts with PKM2 via its coiled-coil domain. Ref.40 Ref.50

Binds arsenic via the RING-type zinc finger. Ref.40 Ref.50

Post-translational modification

Ubiquitinated; mediated by RNF4, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent. Ref.28 Ref.43 Ref.49 Ref.50

Undergoes 'Lys-11'-linked sumoylation. Sumoylation on all three sites is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. The PML-RARA fusion protein requires the coiled-coil domain for sumoylation. Desumoylated by SENP2 and SENP6. Arsenic induces PML and PML-RARA oncogenic fusion proteins polysumoylation and their subsequent RNF4-dependent ubiquitination and proteasomal degradation, and is used as treatment in acute promyelocytic leukemia (APL). Ref.13 Ref.23 Ref.33 Ref.37 Ref.43 Ref.49 Ref.50 Ref.52

Phosphorylated in response to DNA damage, probably by ATR. Stabilized by HIPK2-mediated phosphorylation at Ser-8 and Ser-38 in response to DNA damage. Ref.24 Ref.30 Ref.35 Ref.38 Ref.39 Ref.44 Ref.47 Ref.48

Acetylation may promote sumoylation and enhance induction of apoptosis.

Involvement in disease

Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon. Ref.1 Ref.2

Sequence similarities

Contains 2 B box-type zinc fingers.

Contains 1 RING-type zinc finger.

Sequence caution

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 BAB62809.1 differs from that shown. Reason: Chimeric cDNA.

The sequence BAD92648.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAntiviral defense
Apoptosis
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
Tumor suppressor
   DomainCoiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

DNA damage response, signal transduction resulting in induction of apoptosis

Inferred from direct assay Ref.24. Source: UniProtKB

PML body organization

Inferred from mutant phenotype Ref.37. Source: UniProtKB

cell cycle arrest

Inferred from direct assay Ref.27. Source: UniProtKB

endoplasmic reticulum calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

induction of apoptosis

Inferred from direct assay. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

maintenance of protein location in nucleus

Inferred from direct assay. Source: MGI

negative regulation of angiogenesis

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

negative regulation of mitotic cell cycle

Inferred from direct assay. Source: UniProtKB

negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.30. Source: UniProtKB

negative regulation of telomerase activity

Inferred from mutant phenotype Ref.46. Source: UniProtKB

negative regulation of telomere maintenance via telomerase

Inferred from mutant phenotype Ref.46. Source: UniProtKB

negative regulation of transcription, DNA-dependent

Inferred from direct assay. Source: UniProtKB

negative regulation of translation in response to oxidative stress

Inferred from direct assay. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of histone deacetylation

Inferred from direct assay. Source: UniProtKB

protein complex assembly

Inferred from direct assay. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.27. Source: UniProtKB

protein targeting

Inferred from direct assay. Source: UniProtKB

regulation of calcium ion transport into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from direct assay. Source: UniProtKB

response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentPML body

Inferred from direct assay Ref.5Ref.30Ref.37. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.34Ref.40. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic to endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

insoluble fraction

Inferred from direct assay. Source: UniProtKB

nuclear matrix

Inferred from direct assay. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.34. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.30Ref.34. Source: UniProtKB

nucleus

Inferred from direct assay Ref.34. Source: UniProtKB

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

SUMO binding

Inferred from physical interaction Ref.37. Source: UniProtKB

cobalt ion binding

Inferred from direct assay Ref.54. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18. Source: IntAct

protein heterodimerization activity

Inferred from direct assay. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 14 isoforms produced by alternative splicing. [Align] [Select]
Isoform PML-1 (identifier: P29590-1)

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.
Isoform PML-2 (identifier: P29590-8)

Also known as: PML-II; TRIM19kappa;

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL
Isoform PML-3 (identifier: P29590-9)

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.
Isoform PML-4 (identifier: P29590-5)

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.
Isoform PML-5 (identifier: P29590-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflict5781P → A in AAG50181. Ref.5
Isoform PML-6 (identifier: P29590-4)

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.
Isoform PML-7 (identifier: P29590-10)

Also known as: PML-VII; TRIM19theta;

The sequence of this isoform differs from the canonical sequence as follows:
     419-435: PEEAERVKAQVQALGLA → VPPPAHALTGPAQSSTH
     436-882: Missing.
Isoform PML-8 (identifier: P29590-3)

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
Isoform PML-9 (identifier: P29590-6)

The sequence of this isoform differs from the canonical sequence as follows:
     404-466: Missing.
Isoform PML-10 (identifier: P29590-7)

The sequence of this isoform differs from the canonical sequence as follows:
     648-664: Missing.
Isoform PML-11 (identifier: P29590-11)

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.
Isoform PML-12 (identifier: P29590-12)

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.
Isoform PML-13 (identifier: P29590-13)

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
Isoform PML-14 (identifier: P29590-14)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 882882Protein PML
PRO_0000056001

Regions

Zinc finger57 – 9236RING-type
Zinc finger124 – 16643B box-type 1; atypical
Zinc finger183 – 23654B box-type 2
Region476 – 49015Nuclear localization signal
Coiled coil228 – 25326 Potential
Motif556 – 5594Interaction with SUMO1 and sumoylated proteins
Compositional bias3 – 4644Pro-rich

Sites

Metal binding571Zinc 1
Metal binding601Zinc 1
Metal binding721Zinc 2
Metal binding741Zinc 2
Metal binding771Zinc 1
Metal binding801Zinc 1
Metal binding881Zinc 2
Metal binding911Zinc 2
Site394 – 3952Breakpoint for translocation to form PML-RARA oncogene in type A APL
Site552 – 5532Breakpoint for translocation to form PML-RARA oncogene in type B APL

Amino acid modifications

Modified residue81Phosphoserine; by HIPK2 Ref.35 Ref.47
Modified residue381Phosphoserine; by HIPK2 Ref.47
Modified residue1171Phosphoserine; by CHEK2 Ref.24
Modified residue4031Phosphoserine Ref.35 Ref.39 Ref.44
Modified residue4091Phosphothreonine Ref.44
Modified residue4871N6-acetyllysine Probable
Modified residue5041Phosphoserine Ref.39
Modified residue5051Phosphoserine Ref.38
Modified residue5121Phosphoserine Ref.38
Modified residue5151N6-acetyllysine Probable
Modified residue5181Phosphoserine Ref.35 Ref.44
Modified residue5271Phosphoserine Ref.35 Ref.44
Modified residue5301Phosphoserine Ref.35 Ref.44 Ref.48
Modified residue5351Phosphoserine Ref.35
Modified residue5601Phosphoserine Ref.35
Modified residue5611Phosphoserine Ref.35
Modified residue5621Phosphoserine Ref.35
Modified residue5651Phosphoserine Ref.35
Modified residue8671Phosphothreonine Ref.48
Cross-link65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43
Cross-link400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43
Cross-link401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43
Cross-link476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43
Cross-link490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence404 – 46663Missing in isoform PML-9.
VSP_005737
Alternative sequence419 – 46648Missing in isoform PML-11, isoform PML-12 and isoform PML-13.
VSP_040590
Alternative sequence419 – 43517PEEAE…ALGLA → VPPPAHALTGPAQSSTH in isoform PML-7.
VSP_040591
Alternative sequence419 – 4235PEEAE → RNALW in isoform PML-14.
VSP_040592
Alternative sequence424 – 882459Missing in isoform PML-14.
VSP_040593
Alternative sequence436 – 882447Missing in isoform PML-7.
VSP_040594
Alternative sequence553 – 5608EERVVVIS → GRERNALW in isoform PML-6.
VSP_005742
Alternative sequence561 – 882322Missing in isoform PML-6.
VSP_005743
Alternative sequence571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPAHSSPVQSLLRAQGAS SLPCGTYHPPAWPPHQPAEQ AATPDAEPHSEPPDHQERPA VHRGIRYLLYRAQRAIRLRH ALRLHPQLHRAPIRTWSPHV VQASTPAITGPLNHPANAQE HPAQLQRGISPPHRIRGAVR SRSRSLRGSSHLSQWLNNFF ALPFSSMASQLDMSSVVGAG ESRAQTLGAGVPPGDSVRGS MEASQVQVPLEASPITFPPP CAPERPPISPVPGARQAGL in isoform PML-2 and isoform PML-13.
VSP_040595
Alternative sequence571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-8.
VSP_005741
Alternative sequence571 – 64171SSREL…RVVIQ → VSSSPQSEVLYWKVHGAHGD RRATVLASPLLASPLLASPL LASPVSAESTRSLQPALWHI PPPSLASPPAR in isoform PML-3.
VSP_040596
Alternative sequence571 – 61141SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-5.
VSP_005739
Alternative sequence612 – 882271Missing in isoform PML-5.
VSP_005740
Alternative sequence621 – 63313TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-4 and isoform PML-12.
VSP_005744
Alternative sequence634 – 882249Missing in isoform PML-4 and isoform PML-12.
VSP_005745
Alternative sequence642 – 882241Missing in isoform PML-3.
VSP_040597
Alternative sequence648 – 66417Missing in isoform PML-10.
VSP_005738
Natural variant6451F → L. Ref.2 Ref.5
Corresponds to variant rs5742915 [ dbSNP | Ensembl ].
VAR_052090

Experimental info

Mutagenesis571C → S: Strongly reduced sumoylation; when associated with S-60. Ref.37
Mutagenesis601C → S: Strongly reduced sumoylation; when associated with S-57. Ref.37
Mutagenesis651K → 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. Ref.13
Mutagenesis681K → R: No effect on sumoylation levels.
Mutagenesis881C → S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89. Ref.33
Mutagenesis891P → R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88. Ref.33
Mutagenesis1331K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.13
Mutagenesis1501K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.13
Mutagenesis1601K → 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. Ref.13
Mutagenesis4871K → A: Loss of nuclear localization; when associated with A-490. Ref.40 Ref.41
Mutagenesis4871K → R: Reduced acetylation. Further decrease in acetylation; when associated with R-515. Ref.40 Ref.41
Mutagenesis4901K → A: Loss of nuclear localization; when associated with A-487. Ref.13 Ref.40
Mutagenesis4901K → 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. Ref.13 Ref.40
Mutagenesis5151K → R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487. Ref.41
Mutagenesis556 – 5594VVVI → AAAS: Abolishes SUMO1 binding.
Sequence conflict2241E → D in AAP88913. Ref.7
Sequence conflict2241E → D in AAH00080. Ref.10
Sequence conflict2241E → D in AAH20994. Ref.10
Sequence conflict4191P → A in AAA60351. Ref.2
Sequence conflict4191P → A in AAA60388. Ref.2
Sequence conflict4191P → A in AAA60390. Ref.2
Sequence conflict4191P → A in AAA60352. Ref.4
Sequence conflict4191P → A in AAG50182. Ref.5
Sequence conflict4191P → A in AAG50184. Ref.5
Sequence conflict4191P → A in AAG50185. Ref.5

Secondary structure

1 ....... 882
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PML-1 (PML-I) (TRIM19alpha) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: D50968A977E34287

FASTA88297,551
        10         20         30         40         50         60 
MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 

        70         80         90        100        110        120 
QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 

       130        140        150        160        170        180 
QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 

       190        200        210        220        230        240 
TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 

       250        260        270        280        290        300 
DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 

       310        320        330        340        350        360 
VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 

       370        380        390        400        410        420 
QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 

       430        440        450        460        470        480 
EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 

       490        500        510        520        530        540 
QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 

       550        560        570        580        590        600 
NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 

       610        620        630        640        650        660 
ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ 

       670        680        690        700        710        720 
HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG 

       730        740        750        760        770        780 
ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS 

       790        800        810        820        830        840 
LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA 

       850        860        870        880 
FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS

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Isoform PML-2 (PML-II) (TRIM19kappa) [UniParc].

Checksum: 25824778A4AB6AB1
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FASTA82990,721
Isoform PML-3 (PML-III) [UniParc].

Checksum: 8262393E2B00CBC7
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FASTA64170,368
Isoform PML-4 (PML-IV) (PML-X) (TRIM19zeta) [UniParc].

Checksum: 85FBAEC9F162C8E0
Show »

FASTA63370,024
Isoform PML-5 (PML-2) (PML-V) (TRIM19beta) [UniParc].

Checksum: 52E7FB5D57D59233
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FASTA61167,471
Isoform PML-6 (PML-3B) (PML-VI) (TRIM19epsilon) [UniParc].

Checksum: 9DC795A6542BA778
Show »

FASTA56062,007
Isoform PML-7 (PML-VII) (TRIM19theta) [UniParc].

Checksum: 35BF713DBF5F9229
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FASTA43548,584
Isoform PML-8 (PML-2G) (PML-IIG) (TRIM19gamma) [UniParc].

Checksum: 5DA9DD2E4EEE8492
Show »

FASTA82490,254
Isoform PML-9 [UniParc].

Checksum: 08A61429A471F3EA
Show »

FASTA81990,986
Isoform PML-10 [UniParc].

Checksum: FF6BC26D338E89CB
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FASTA86595,677
Isoform PML-11 (PML-1A) (PML-IA) [UniParc].

Checksum: 16772D51354CFDAC
Show »

FASTA83492,564
Isoform PML-12 (PML-4A) (PML-IVA) (TRIM19lambda) [UniParc].

Checksum: FF1E5A8D845780B2
Show »

FASTA58565,037
Isoform PML-13 (PML-2A) (PML-IIA) [UniParc].

Checksum: C6C163ECD9FA6FB2
Show »

FASTA78185,734
Isoform PML-14 (PML-6B) (PML-VIB) (TRIM19eta) (TRIM19iota) [UniParc].

Checksum: EE5031BE9C3B33C8
Show »

FASTA42347,575

References

« Hide 'large scale' references
[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: 1652369] [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: 1720570] [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: 1311253] [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: 1652368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
[5]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed: 11331580] [Abstract]
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. expand/collapse author list , 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: 16572171] [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: 15489334] [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: 1312695] [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: 12691149] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, CHROMOSOMAL TRANSLOCATION WITH RARA.
[13]"Identification of three major sentrinization sites in PML."
Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T., Yeh E.T.H.
J. Biol. Chem. 273:26675-26682(1998) [PubMed: 9756909] [Abstract]
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: 9570750] [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: 9420283] [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: 10610177] [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: 10684855] [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: 10669754] [Abstract]
Cited for: INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
[19]"The function of PML in p53-dependent apoptosis."
Guo A., Salomoni P., Luo J., Shih A., Zhong S., Gu W., Pandolfi P.P.
Nat. Cell Biol. 2:730-736(2000) [PubMed: 11025664] [Abstract]
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: 11432836] [Abstract]
Cited for: FUNCTION.
[21]"PML protein isoforms and the RBCC/TRIM motif."
Jensen K., Shiels C., Freemont P.S.
Oncogene 20:7223-7233(2001) [PubMed: 11704850] [Abstract]
Cited for: NOMENCLATURE OF ISOFORMS 1 THROUGH 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: 12006491] [Abstract]
Cited for: INTERACTION WITH SIRT1.
[23]"SUMO-1 protease-1 regulates gene transcription through PML."
Best J.L., Ganiatsas S., Agarwal S., Changou A., Salomoni P., Shirihai O., Meluh P.B., Pandolfi P.P., Zon L.I.
Mol. Cell 10:843-855(2002) [PubMed: 12419228] [Abstract]
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: 12402044] [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: 12439746] [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: 12810724] [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: 12773567] [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: 14645235] [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: 14976184] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ELF4, SUBCELLULAR LOCATION.
[30]"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: 15195100] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2 AND RPL11, PHOSPHORYLATION BY ATR IN RESPONSE TO DNA DAMAGE, SUBCELLULAR LOCATION.
[31]"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: 15467728] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHFR.
[32]"Cytoplasmic PML function in TGF-beta signalling."
Lin H.K., Bergmann S., Pandolfi P.P.
Nature 431:205-211(2004) [PubMed: 15356634] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFBR1; TGFBR2; SMAD2; SMAD3 AND ZFYVE9/SARA.
[33]"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: 15809060] [Abstract]
Cited for: INTERACTION OF PML-RARALPHA ONCOPROTEIN WITH UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF CYS-88 AND PRO-89.
[34]"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: 16778193] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[35]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-403; SER-518; SER-527; SER-530; SER-535; SER-560; SER-561; SER-562 AND SER-565, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[36]"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: 17030982] [Abstract]
Cited for: FUNCTION.
[37]"The mechanisms of PML-nuclear body formation."
Shen T.H., Lin H.K., Scaglioni P.P., Yung T.M., Pandolfi P.P.
Mol. Cell 24:331-339(2006) [PubMed: 17081985] [Abstract]
Cited for: SUBUNIT, SUMOYLATION, SUMO-BINDING MOTIF, MUTAGENESIS OF CYS-57 AND CYS-60, SUBCELLULAR LOCATION.
[38]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-512, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[39]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-504, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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: 18298799] [Abstract]
Cited for: INTERACTION WITH PKM2, 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: 18621739] [Abstract]
Cited for: ACETYLATION AT LYS-487 AND LYS-515, MUTAGENESIS OF LYS-487 AND LYS-515.
[42]"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: 18716620] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[43]"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: 18408734] [Abstract]
Cited for: POLYUBIQUITINATION AT LYS-380; LYS-400; LYS-401 AND LYS-476 BY RNF4, PROTEASOMAL DEGRADATION, SUMOYLATION.
[44]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; THR-409; SER-518; SER-527 AND SER-530, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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: 17173041] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SATB1.
[46]"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: 19567472] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TERT.
[47]"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: 19015637] [Abstract]
Cited for: PHOSPHORYLATION AT SER-8 AND SER-38 BY HIPK2, INTERACTION WITH HIPK2.
[48]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND THR-867, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[49]"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: 20943951] [Abstract]
Cited for: SUMOYLATION, UBIQUITINATION.
[50]"Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML."
Zhang X.W., Yan X.J., Zhou Z.R., Yang F.F., Wu Z.Y., Sun H.B., Liang W.X., Song A.X., Lallemand-Breitenbach V., Jeanne M., Zhang Q.Y., Yang H.Y., Huang Q.H., Zhou G.B., Tong J.H., Zhang Y., Wu J.H., Hu H.Y. expand/collapse author list , de The H., Chen S.J., Chen Z.
Science 328:240-243(2010) [PubMed: 20378816] [Abstract]
Cited for: INTERACTION WITH UBC9, SUBUNIT, UBIQUITINATION, SUMOYLATION, ARSENIC BINDING, DOMAIN, MASS SPECTROMETRY.
[51]"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: 21172801] [Abstract]
Cited for: FUNCTION.
[52]"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: 21148299] [Abstract]
Cited for: SUMOYLATION, DESUMOYLATION BY SENP6.
[53]"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: 21304940] [Abstract]
Cited for: FUNCTION.
[54]"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: 7729428] [Abstract]
Cited for: STRUCTURE BY NMR OF 49-104.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00022348.
IPI00220453.
IPI00291097.
IPI00303999.
IPI00304000.
IPI00332110.
IPI00395707.
IPI00744329.
IPI00922350.
IPI00922504.
IPI00940182.
IPI00973909.
IPI00974368.
IPI00974373.
PIRA40044.
I38054.
S19244.
S42516.
S44381.
RefSeqNP_002666.1. NM_002675.3.
NP_150241.2. NM_033238.2.
NP_150242.1. NM_033239.2.
NP_150243.2. NM_033240.2.
NP_150247.2. NM_033244.3.
NP_150249.1. NM_033246.2.
NP_150250.2. NM_033247.2.
NP_150252.1. NM_033249.2.
NP_150253.2. NM_033250.2.
UniGeneHs.526464.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
ProteinModelPortalP29590.
SMRP29590. Positions 49-104.
ModBaseSearch...

Protein-protein interaction databases

IntActP29590. 52 interactions.
MINTMINT-158826.
STRINGP29590.

PTM databases

PhosphoSiteP29590.

Polymorphism databases

DMDM215274219.

Proteomic databases

PRIDEP29590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268058; ENSP00000268058; ENSG00000140464.
GeneID5371.
KEGGhsa:5371.
UCSCuc002awm.1. human.
uc002awn.1. human.
uc002awr.1. human.
uc002awv.1. human.

Organism-specific databases

CTD5371.
GeneCardsGC15P074287.
HGNCHGNC:9113. PML.
HPACAB010194.
CAB016304.
HPA008312.
MIM102578. gene.
neXtProtNX_P29590.
Orphanet520. Acute promyelocytic leukemia.
PharmGKBPA33439.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17841.
HOGENOMHBG127220.
HOVERGENHBG000552.
InParanoidP29590.
OMAGLQCPIC.
OrthoDBEOG4H19V2.
PhylomeDBP29590.

Enzyme and pathway databases

Pathway_Interaction_DBtgfbrpathway. TGF-beta receptor signaling.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP29590.
BgeeP29590.
CleanExHS_PML.
GenevestigatorP29590.
GermOnlineENSG00000140464. Homo sapiens.

Family and domain databases

InterProIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KOK10054.
PfamPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20820.
PMAP-CutDBP29590.
SOURCESearch...

Entry information

Entry namePML_HUMAN
AccessionPrimary (citable) accession number: P29590
Secondary accession number(s): P29591 expand/collapse secondary AC list , P29592, P29593, Q00755, Q15959, Q59FP9, Q8WUA0, Q96S41, Q9BPW2, Q9BWP7, Q9BZX6, Q9BZX7, Q9BZX8, Q9BZX9, Q9BZY0, Q9BZY2, Q9BZY3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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