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Entry version 237 (16 Oct 2019)
Sequence version 3 (25 Nov 2008)
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Protein

Protein PML

Gene

PML

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi57Zinc 11
Metal bindingi60Zinc 11
Metal bindingi72Zinc 21
Metal bindingi74Zinc 21
Metal bindingi77Zinc 11
Metal bindingi80Zinc 11
Metal bindingi88Zinc 21
Metal bindingi91Zinc 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri57 – 92RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri124 – 166B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST43
Zinc fingeri183 – 236B box-type 2PROSITE-ProRule annotationAdd BLAST54

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processAntiviral defense, Apoptosis, Biological rhythms, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-877300 Interferon gamma signaling
R-HSA-8934593 Regulation of RUNX1 Expression and Activity
R-HSA-8948747 Regulation of PTEN localization
R-HSA-9616222 Transcriptional regulation of granulopoiesis [P29590-4]

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P29590

SIGNOR Signaling Network Open Resource

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SIGNORi
P29590

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein PML
Alternative name(s):
Promyelocytic leukemia protein
RING finger protein 71
Tripartite motif-containing protein 19
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PML
Synonyms:MYL, PP8675, RNF71, TRIM19
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:9113 PML

Online Mendelian Inheritance in Man (OMIM)

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MIMi
102578 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P29590

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi57C → S: Strongly reduced sumoylation; when associated with S-60. 1 Publication1
Mutagenesisi60C → S: Strongly reduced sumoylation; when associated with S-57. 1 Publication1
Mutagenesisi65K → 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. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-160 and R-490. 2 Publications1
Mutagenesisi65K → 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 Publication1
Mutagenesisi68K → R: No effect on sumoylation levels. 1
Mutagenesisi88C → S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89. 1 Publication1
Mutagenesisi89P → R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88. 1 Publication1
Mutagenesisi133K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication1
Mutagenesisi150K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication1
Mutagenesisi160K → R: Compromised the formation of high molecular weight species of SUMO1P1/SUMO5 conjugation on PML. 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. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-490. 2 Publications1
Mutagenesisi160K → 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 Publication1
Mutagenesisi380K → R: Does not affect SUMO1P1/SUMO5 conjugation. 1 Publication1
Mutagenesisi400K → R: Does not affect SUMO1P1/SUMO5 conjugation. 1 Publication1
Mutagenesisi487K → A: Loss of nuclear localization; when associated with A-490. 2 Publications1
Mutagenesisi487K → R: Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515. 2 Publications1
Mutagenesisi490K → A: Loss of nuclear localization; when associated with A-487. 2 Publications1
Mutagenesisi490K → R: Abolished conjugation of one SUMO1P1/SUMO5. 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. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-160. 3 Publications1
Mutagenesisi490K → 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 Publications1
Mutagenesisi497K → R: Does not affect SUMO1P1/SUMO5 conjugation. 1 Publication1
Mutagenesisi515K → R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487. 1 Publication1
Mutagenesisi518S → A: Abolishes ubiquitination by the BCR(KLHL20) E3 ubiquitin ligase complex. 1 Publication1
Mutagenesisi556 – 559VVVI → AAAS: Abolishes SUMO1 binding. 4

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei394 – 395Breakpoint for translocation to form PML-RARA oncogene in type A APL2
Sitei552 – 553Breakpoint for translocation to form PML-RARA oncogene in type B APL2

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
5371

MalaCards human disease database

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MalaCardsi
PML

Open Targets

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OpenTargetsi
ENSG00000140464

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
520 Acute promyelocytic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33439

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P29590

Chemistry databases

Drug and drug target database

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DrugBanki
DB01169 Arsenic trioxide

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PML

Domain mapping of disease mutations (DMDM)

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DMDMi
215274219

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000560011 – 882Protein PMLAdd BLAST882

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei8Phosphoserine; by HIPK2Combined sources1 Publication1
Modified residuei36Phosphoserine; by HIPK2 and MAPK1Combined sources1
Modified residuei38Phosphoserine; by HIPK2 and MAPK1Combined sources1 Publication1
Modified residuei48PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate1 Publication
Cross-linki65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei117Phosphoserine; by CHEK21 Publication1
Cross-linki160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate1 Publication
Cross-linki160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5); alternate1 Publication
Cross-linki160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in /SUMO5); alternate1 Publication
Cross-linki380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki394Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5); alternate1 Publication
Cross-linki400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei403Phosphoserine; by MAPK1 and MAPK7Combined sources1 Publication1
Cross-linki460Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki478Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei487N6-acetyllysine; alternate2 Publications1
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate1 Publication
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5); alternate1 Publication
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei493PhosphoserineBy similarity1
Cross-linki497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-linki497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5); alternate1 Publication
Cross-linki497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei504PhosphoserineBy similarity1
Modified residuei505Phosphoserine; by MAPK1Combined sources1 Publication1
Modified residuei512PhosphoserineCombined sources1
Modified residuei515N6-acetyllysine1 Publication1
Modified residuei518Phosphoserine; by CDK1 and CDK2Combined sources2 Publications1
Modified residuei527Phosphoserine; by MAPK1Combined sources1 Publication1
Modified residuei530Phosphoserine; by MAPK1Combined sources1
Modified residuei565Phosphoserine; by CK21 Publication1
Modified residuei867PhosphothreonineCombined sources1
Isoform PML-6 (identifier: P29590-4)
Modified residuei518PhosphoserineCombined sources1
Modified residuei527PhosphoserineCombined sources1
Modified residuei530PhosphoserineCombined sources1
Isoform PML-5 (identifier: P29590-2)
Modified residuei565PhosphoserineCombined sourcesCurated1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated; mediated by RNF4, RNF111, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation (PubMed:18408734, PubMed:21840486, PubMed:22033920). 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 (PubMed:21840486, PubMed:22033920). 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent (PubMed:18408734). Ubiquitination by RNF111 is polysumoylation-dependent (By similarity).By similarity3 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. SUMO1P1/SUMO5 conjugated PML at Lys-160, Lys-380, Lys-400, Lys-490 and Lys-497, but Lys-380, Lys-400 and Lys-497 are not key acceptor lysines. SUMO1P1/SUMO5 forms polymeric chain on Lys-160 of PML by successive conjugation at 'Lys-18'; facilitating recruitment of PML-NB components, which enlarges PML. SUMO1P1/SUMO5 conjugation of PML increases SUMO2/3 conjugation, which leads to the recruitment of RNF4 and ubiquitin-dependent disintegration of PML-NBs. SUMO1P1/SUMO5 monoconjugated Lys-490 (PubMed:27211601). DNA damage triggers its sumoylation while some but not all viral infections can abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 (PubMed:27211601, PubMed:12419228, PubMed:21148299). 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.7 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 apoptosis 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.7 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

Encyclopedia of Proteome Dynamics

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EPDi
P29590

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P29590

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P29590

MaxQB - The MaxQuant DataBase

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MaxQBi
P29590

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P29590

PeptideAtlas

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PeptideAtlasi
P29590

PRoteomics IDEntifications database

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PRIDEi
P29590

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
19281
54589 [P29590-1]
54590 [P29590-10]
54591 [P29590-11]
54592 [P29590-12]
54593 [P29590-13]
54594 [P29590-14]
54595 [P29590-2]
54596 [P29590-3]
54597 [P29590-4]
54598 [P29590-5]
54599 [P29590-8]
54600 [P29590-9]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P29590

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P29590

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P29590

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000140464 Expressed in 199 organ(s), highest expression level in left lobe of thyroid gland

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P29590 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P29590 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB010194
CAB016304
HPA008312

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 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.

Interacts (via SUMO-interacting motif) with sumoylated MORC3 (PubMed:20501696). 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.

Interacts with TRIM16.

38 Publications

(Microbial infection) Interacts with Lassa virus Z protein and rabies virus phosphoprotein.

1 Publication

(Microbial infection) Isoform PML-1 interacts with herpes simplex virus-1/HHV-1 ICP0.

1 Publication

(Microbial infection) Isoform PML-2 interacts with human adenovirus 2 E1A and this interaction stimulates E1A-dependent transcriptional activation.

1 Publication

(Microbial infection) Isoform PML-4 interacts with VZV capsid protein VP26/ORF23 capsid protein.

1 Publication

(Microbial infection) The sumoylated isoform PML-4 interacts with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-POL (P3D-POL).

1 Publication

(Microbial infection) Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT).

1 Publication

(Microbial infection) Isoform PML-4 and isoform PML-5 interact with human adenovirus 5 E1B-55K protein; these interactions promote efficient subnuclear targeting of E1B-55K to PML nuclear bodies.

3 Publications

(Microbial infection) Isoform PML-3 interacts with human foamy virus bel1/tas and bet.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111384, 262 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P29590

Database of interacting proteins

More...
DIPi
DIP-33053N

Protein interaction database and analysis system

More...
IntActi
P29590, 120 interactors

Molecular INTeraction database

More...
MINTi
P29590

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000268058

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1882
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P29590

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P29590

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni448 – 555Interaction with PER21 PublicationAdd BLAST108
Regioni556 – 562Sumo interaction motif (SIM)7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili228 – 253Sequence analysisAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi476 – 490Nuclear localization signalAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi3 – 46Pro-richAdd BLAST44

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri57 – 92RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri124 – 166B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST43
Zinc fingeri183 – 236B box-type 2PROSITE-ProRule annotationAdd BLAST54

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2177 Eukaryota
ENOG4111G04 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00510000048454

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29590

KEGG Orthology (KO)

More...
KOi
K10054

Identification of Orthologs from Complete Genome Data

More...
OMAi
CCICALL

Database of Orthologous Groups

More...
OrthoDBi
421875at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P29590

TreeFam database of animal gene trees

More...
TreeFami
TF336434

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR021978 DUF3583
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12126 DUF3583, 1 hit
PF00643 zf-B_box, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (12+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 12 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 12 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform PML-1 (identifier: P29590-1) [UniParc]FASTAAdd to basket
Also known as: PML-I, TRIM19alpha

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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.

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):90,242
Checksum:i5DA06243F18A8492
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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BT57H3BT57_HUMAN
Protein PML
PML
568Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BVD2H3BVD2_HUMAN
Protein PML
PML
217Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BRN3H3BRN3_HUMAN
Protein PML
PML
110Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BUJ5H3BUJ5_HUMAN
Protein PML
PML
261Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BT29H3BT29_HUMAN
Protein PML
PML
240Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA60351 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAA60352 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAA60388 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAA60390 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAB62809 differs from that shown. Chimeric cDNA.Curated
The sequence BAD92648 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti224E → D in AAP88913 (Ref. 7) Curated1
Sequence conflicti224E → D in AAH00080 (PubMed:15489334).Curated1
Sequence conflicti224E → D in AAH20994 (PubMed:15489334).Curated1
Sequence conflicti419P → A in AAA60351 (PubMed:1720570).Curated1
Sequence conflicti419P → A in AAA60388 (PubMed:1720570).Curated1
Sequence conflicti419P → A in AAA60390 (PubMed:1720570).Curated1
Sequence conflicti419P → A in AAA60352 (PubMed:1652368).Curated1
Sequence conflicti419P → A in AAG50182 (PubMed:11331580).Curated1
Sequence conflicti419P → A in AAG50184 (PubMed:11331580).Curated1
Sequence conflicti419P → A in AAG50185 (PubMed:11331580).Curated1
Isoform PML-7 (identifier: P29590-10)
Sequence conflicti419L → V in AAG50187 (PubMed:11331580).Curated1
Isoform PML-5 (identifier: P29590-2)
Sequence conflicti578P → A in AAG50181 (PubMed:11331580).Combined sourcesCurated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_052090645F → L2 PublicationsCorresponds to variant dbSNP:rs5742915Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_040590419 – 466Missing in isoform PML-11, isoform PML-12 and isoform PML-13. 4 PublicationsAdd BLAST48
Alternative sequenceiVSP_040591419 – 435PEEAE…ALGLA → LPPPAHALTGPAQSSTH in isoform PML-7. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_040592419 – 423PEEAE → RNALW in isoform PML-14. 1 Publication5
Alternative sequenceiVSP_040593424 – 882Missing in isoform PML-14. 1 PublicationAdd BLAST459
Alternative sequenceiVSP_040594436 – 882Missing in isoform PML-7. 1 PublicationAdd BLAST447
Alternative sequenceiVSP_005742553 – 560EERVVVIS → GRERNALW in isoform PML-6. 3 Publications8
Alternative sequenceiVSP_005743561 – 882Missing in isoform PML-6. 3 PublicationsAdd BLAST322
Alternative sequenceiVSP_040595571 – 882SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPAHSSPVQSLLRAQGAS SLPCGTYHPPAWPPHQPAEQ AATPDAEPHSEPPDHQERPA VHRGIRYLLYRAQRAIRLRH ALRLHPQLHRAPIRTWSPHV VQASTPAITGPLNHPANAQE HPAQLQRGISPPHRIRGAVR SRSRSLRGSSHLSQWLNNFF ALPFSSMASQLDMSSVVGAG ESRAQTLGAGVPPGDSVRGS MEASQVQVPLEASPITFPPP CAPERPPISPVPGARQAGL in isoform PML-2 and isoform PML-13. 3 PublicationsAdd BLAST312
Alternative sequenceiVSP_005741571 – 882SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGESRAQ TLGAGVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-8. 2 PublicationsAdd BLAST312
Alternative sequenceiVSP_040596571 – 641SSREL…RVVIQ → VSSSPQSEVLYWKVHGAHGD RRATVLASPLLASPLLASPL LASPVSAESTRSLQPALWHI PPPSLASPPAR in isoform PML-3. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_005739571 – 611SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-5. 2 PublicationsAdd BLAST41
Alternative sequenceiVSP_005740612 – 882Missing in isoform PML-5. 2 PublicationsAdd BLAST271
Alternative sequenceiVSP_005744621 – 633TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-4 and isoform PML-12. 2 PublicationsAdd BLAST13
Alternative sequenceiVSP_005745634 – 882Missing in isoform PML-4 and isoform PML-12. 2 PublicationsAdd BLAST249
Alternative sequenceiVSP_040597642 – 882Missing in isoform PML-3. 1 PublicationAdd BLAST241

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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.

The Consensus CDS (CCDS) project

More...
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]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40044
I38054
S19244
S42516
S44381

NCBI Reference Sequences

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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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
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]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5371

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5371

UCSC genome browser

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UCSCi
uc002awk.4 human [P29590-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
2MVWNMR-A/B120-168[»]
2MWXNMR-A49-104[»]
4WJNX-ray1.50B547-573[»]
4WJOX-ray1.46B547-573[»]
5YUFX-ray1.60A/B/C/D49-99[»]
6IMQX-ray2.06A/B/C/D120-168[»]
SMRiP29590
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111384, 262 interactors
CORUMiP29590
DIPiDIP-33053N
IntActiP29590, 120 interactors
MINTiP29590
STRINGi9606.ENSP00000268058

Chemistry databases

DrugBankiDB01169 Arsenic trioxide

PTM databases

iPTMnetiP29590
PhosphoSitePlusiP29590

Polymorphism and mutation databases

BioMutaiPML
DMDMi215274219

Proteomic databases

EPDiP29590
jPOSTiP29590
MassIVEiP29590
MaxQBiP29590
PaxDbiP29590
PeptideAtlasiP29590
PRIDEiP29590
ProteomicsDBi19281
54589 [P29590-1]
54590 [P29590-10]
54591 [P29590-11]
54592 [P29590-12]
54593 [P29590-13]
54594 [P29590-14]
54595 [P29590-2]
54596 [P29590-3]
54597 [P29590-4]
54598 [P29590-5]
54599 [P29590-8]
54600 [P29590-9]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5371

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.4 human [P29590-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5371
DisGeNETi5371

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PML
HGNCiHGNC:9113 PML
HPAiCAB010194
CAB016304
HPA008312
MalaCardsiPML
MIMi102578 gene
neXtProtiNX_P29590
OpenTargetsiENSG00000140464
Orphaneti520 Acute promyelocytic leukemia
PharmGKBiPA33439

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2177 Eukaryota
ENOG4111G04 LUCA
GeneTreeiENSGT00510000048454
InParanoidiP29590
KOiK10054
OMAiCCICALL
OrthoDBi421875at2759
PhylomeDBiP29590
TreeFamiTF336434

Enzyme and pathway databases

ReactomeiR-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-877300 Interferon gamma signaling
R-HSA-8934593 Regulation of RUNX1 Expression and Activity
R-HSA-8948747 Regulation of PTEN localization
R-HSA-9616222 Transcriptional regulation of granulopoiesis [P29590-4]
SignaLinkiP29590
SIGNORiP29590

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PML human
EvolutionaryTraceiP29590

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Promyelocytic_leukemia_protein

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5371
PharosiP29590
PMAP-CutDBiP29590

Protein Ontology

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PROi
PR:P29590

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000140464 Expressed in 199 organ(s), highest expression level in left lobe of thyroid gland
ExpressionAtlasiP29590 baseline and differential
GenevisibleiP29590 HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR021978 DUF3583
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF12126 DUF3583, 1 hit
PF00643 zf-B_box, 1 hit
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPML_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>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
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: October 16, 2019
This is version 237 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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