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Protein

Protein PML

Gene

PML

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Zinc 1
Metal bindingi60 – 601Zinc 1
Metal bindingi72 – 721Zinc 2
Metal bindingi74 – 741Zinc 2
Metal bindingi77 – 771Zinc 1
Metal bindingi80 – 801Zinc 1
Metal bindingi88 – 881Zinc 2
Metal bindingi91 – 911Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9236RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 16643B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23654B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • cobalt ion binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • SUMO binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Antiviral defense, Apoptosis, Biological rhythms, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-877300. Interferon gamma signaling.
SignaLinkiP29590.
SIGNORiP29590.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PML
Alternative name(s):
Promyelocytic leukemia protein
RING finger protein 71
Tripartite motif-containing protein 19
Gene namesi
Name:PML
Synonyms:MYL, PP8675, RNF71, TRIM19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9113. PML.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • early endosome membrane Source: UniProtKB-SubCell
  • extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear matrix Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane, Nucleus

Pathology & Biotechi

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571C → S: Strongly reduced sumoylation; when associated with S-60. 1 Publication
Mutagenesisi60 – 601C → S: Strongly reduced sumoylation; when associated with S-57. 1 Publication
Mutagenesisi65 – 651K → 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 Publication
Mutagenesisi68 – 681K → R: No effect on sumoylation levels.
Mutagenesisi88 – 881C → S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89. 1 Publication
Mutagenesisi89 – 891P → R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88. 1 Publication
Mutagenesisi133 – 1331K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication
Mutagenesisi150 – 1501K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. 1 Publication
Mutagenesisi160 – 1601K → 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 Publication
Mutagenesisi487 – 4871K → A: Loss of nuclear localization; when associated with A-490. 2 Publications
Mutagenesisi487 – 4871K → R: Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515. 2 Publications
Mutagenesisi490 – 4901K → A: Loss of nuclear localization; when associated with A-487. 2 Publications
Mutagenesisi490 – 4901K → 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 Publications
Mutagenesisi515 – 5151K → R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487. 1 Publication
Mutagenesisi518 – 5181S → A: Abolishes ubiquitination by the BCR(KLHL20) E3 ubiquitin ligase complex. 1 Publication
Mutagenesisi556 – 5594VVVI → AAAS: Abolishes SUMO1 binding.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei394 – 3952Breakpoint for translocation to form PML-RARA oncogene in type A APL
Sitei552 – 5532Breakpoint for translocation to form PML-RARA oncogene in type B APL

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

MalaCardsiPML.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA33439.

Polymorphism and mutation databases

BioMutaiPML.
DMDMi215274219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 882882Protein PMLPRO_0000056001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by HIPK2Combined sources1 Publication
Modified residuei28 – 281Phosphothreonine; by MAPK11 Publication
Modified residuei36 – 361Phosphoserine; by HIPK2 and MAPK1Combined sources1 Publication
Modified residuei38 – 381Phosphoserine; by HIPK2 and MAPK1Combined sources1 Publication
Modified residuei40 – 401Phosphoserine; by MAPK11 Publication
Modified residuei42 – 421Phosphothreonine1 Publication
Modified residuei48 – 481PhosphoserineCombined sources
Cross-linki65 – 65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki65 – 65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei117 – 1171Phosphoserine; by CHEK21 Publication
Cross-linki160 – 160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki160 – 160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki394 – 394Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki400 – 400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei403 – 4031Phosphoserine; by MAPK1 and MAPK7Combined sources1 Publication
Modified residuei409 – 4091Phosphothreonine; by MAPK71 Publication
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki478 – 478Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei487 – 4871N6-acetyllysine2 Publications
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei493 – 4931PhosphoserineBy similarity
Cross-linki497 – 497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei504 – 5041PhosphoserineBy similarity
Modified residuei505 – 5051Phosphoserine; by MAPK1Combined sources1 Publication
Modified residuei512 – 5121PhosphoserineCombined sources
Modified residuei515 – 5151N6-acetyllysine1 Publication
Modified residuei518 – 5181Phosphoserine; by CDK1 and CDK2Combined sources2 Publications
Modified residuei527 – 5271Phosphoserine; by MAPK1Combined sources1 Publication
Modified residuei530 – 5301Phosphoserine; by MAPK1Combined sources
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei565 – 5651Phosphoserine; by CK21 Publication
Modified residuei867 – 8671PhosphothreonineCombined sources
Isoform PML-6 (identifier: P29590-4)
Modified residuei518 – 5181PhosphoserineCombined sources
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei530 – 5301PhosphoserineCombined sources
Isoform PML-5 (identifier: P29590-2)
Modified residuei565 – 5651PhosphoserineCombined sourcesCurated

Post-translational modificationi

Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. 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. 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.3 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. DNA damage triggers its sumoylation while some but not all viral infections can abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6. 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.4 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 apopotosis 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

EPDiP29590.
MaxQBiP29590.
PaxDbiP29590.
PeptideAtlasiP29590.
PRIDEiP29590.

PTM databases

iPTMnetiP29590.
PhosphoSiteiP29590.

Miscellaneous databases

PMAP-CutDBP29590.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000140464.
CleanExiHS_PML.
ExpressionAtlasiP29590. baseline and differential.
GenevisibleiP29590. HS.

Organism-specific databases

HPAiCAB010194.
CAB016304.
HPA008312.

Interactioni

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 Lassa virus Z protein and rabies virus phosphoprotein. 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. Isoform PML-3 interacts with HFV bel1/tas and bet. Isoform PML-4 interacts with VZV capsid protein VP26/ORF23 capsid protein. Ths sumoylated isoform PML-4 interacts with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-POL (P3D-POL). Isoform PML-1 interacts with herpes simplex virus-1 (HHV-1) ICP0. Isoform PML-2 interacts with human adenovirus 2 E1A and this interaction stimulates E1A-dependent transcriptional activation (PubMed:23135708). Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT). 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 (PubMed:20639899, PubMed:25772236).46 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03243-12EBI-303996,EBI-1927377From a different organism.
P044894EBI-8099068,EBI-6398911From a different organism.
P279586EBI-295890,EBI-6377335From a different organism.
CSNK2A1P684002EBI-295890,EBI-347804
DAXXQ9UER76EBI-295890,EBI-77321
FASP254454EBI-295890,EBI-494743
gag-pro-polQ8UN004EBI-295890,EBI-6692904From a different organism.
KLHL20Q9Y2M59EBI-295890,EBI-714379
MAPK7Q131646EBI-295890,EBI-1213983
MDM2Q009876EBI-304008,EBI-389668
PSMA3P257882EBI-295890,EBI-348380
SUMO1P631653EBI-295890,EBI-80140
TBX2Q132072EBI-295890,EBI-2853051
TERTO147467EBI-304008,EBI-1772203
TGIF1Q155833EBI-295890,EBI-714215
TP53P046374EBI-295890,EBI-366083
ZBTB16Q055167EBI-295890,EBI-711925

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • SUMO binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111384. 236 interactions.
DIPiDIP-33053N.
IntActiP29590. 98 interactions.
MINTiMINT-158826.
STRINGi9606.ENSP00000268058.

Structurei

Secondary structure

1
882
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603Combined sources
Beta strandi82 – 876Combined sources
Helixi90 – 923Combined sources
Beta strandi93 – 964Combined sources
Turni130 – 1323Combined sources
Beta strandi133 – 1408Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 1483Combined sources
Helixi149 – 15810Combined sources
Beta strandi163 – 1664Combined sources
Beta strandi556 – 5583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
2MVWNMR-A/B120-168[»]
2MWXNMR-A49-104[»]
4WJNX-ray1.50B547-573[»]
4WJOX-ray1.46B547-573[»]
ProteinModelPortaliP29590.
SMRiP29590. Positions 49-104, 120-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29590.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni448 – 555108Interaction with PER2Add
BLAST
Regioni556 – 5627Sumo interaction motif (SIM)

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili228 – 25326Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi476 – 49015Nuclear localization signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 4644Pro-richAdd
BLAST

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

Sequence similaritiesi

Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9236RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 16643B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23654B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00510000048454.
HOVERGENiHBG000552.
InParanoidiP29590.
KOiK10054.
OMAiANAQEHP.
OrthoDBiEOG091G02GY.
PhylomeDBiP29590.
TreeFamiTF336434.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform PML-1 (identifier: P29590-1) [UniParc]FASTAAdd to basket
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.

« 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
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):90,254
Checksum:i5DA9DD2E4EEE8492
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

Sequence cautioni

The sequence AAA60351 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA60352 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA60388 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA60390 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB62809 differs from that shown.Chimeric cDNA.Curated
The sequence BAD92648 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241E → D in AAP88913 (Ref. 7) Curated
Sequence conflicti224 – 2241E → D in AAH00080 (PubMed:15489334).Curated
Sequence conflicti224 – 2241E → D in AAH20994 (PubMed:15489334).Curated
Sequence conflicti419 – 4191P → A in AAA60351 (PubMed:1720570).Curated
Sequence conflicti419 – 4191P → A in AAA60388 (PubMed:1720570).Curated
Sequence conflicti419 – 4191P → A in AAA60390 (PubMed:1720570).Curated
Sequence conflicti419 – 4191P → A in AAA60352 (PubMed:1652368).Curated
Sequence conflicti419 – 4191P → A in AAG50182 (PubMed:11331580).Curated
Sequence conflicti419 – 4191P → A in AAG50184 (PubMed:11331580).Curated
Sequence conflicti419 – 4191P → A in AAG50185 (PubMed:11331580).Curated
Isoform PML-7 (identifier: P29590-10)
Sequence conflicti419 – 4191L → V in AAG50187 (PubMed:11331580).Curated
Isoform PML-5 (identifier: P29590-2)
Sequence conflicti578 – 5781P → A in AAG50181 (PubMed:11331580).Combined sourcesCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti645 – 6451F → L.2 Publications
Corresponds to variant rs5742915 [ dbSNP | Ensembl ].
VAR_052090

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei419 – 46648Missing in isoform PML-11, isoform PML-12 and isoform PML-13. 4 PublicationsVSP_040590Add
BLAST
Alternative sequencei419 – 43517PEEAE…ALGLA → LPPPAHALTGPAQSSTH in isoform PML-7. 1 PublicationVSP_040591Add
BLAST
Alternative sequencei419 – 4235PEEAE → RNALW in isoform PML-14. 1 PublicationVSP_040592
Alternative sequencei424 – 882459Missing in isoform PML-14. 1 PublicationVSP_040593Add
BLAST
Alternative sequencei436 – 882447Missing in isoform PML-7. 1 PublicationVSP_040594Add
BLAST
Alternative sequencei553 – 5608EERVVVIS → GRERNALW in isoform PML-6. 3 PublicationsVSP_005742
Alternative sequencei561 – 882322Missing in isoform PML-6. 3 PublicationsVSP_005743Add
BLAST
Alternative sequencei571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPAHSSPVQSLLRAQGAS SLPCGTYHPPAWPPHQPAEQ AATPDAEPHSEPPDHQERPA VHRGIRYLLYRAQRAIRLRH ALRLHPQLHRAPIRTWSPHV VQASTPAITGPLNHPANAQE HPAQLQRGISPPHRIRGAVR SRSRSLRGSSHLSQWLNNFF ALPFSSMASQLDMSSVVGAG ESRAQTLGAGVPPGDSVRGS MEASQVQVPLEASPITFPPP CAPERPPISPVPGARQAGL in isoform PML-2 and isoform PML-13. 3 PublicationsVSP_040595Add
BLAST
Alternative sequencei571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-8. 2 PublicationsVSP_005741Add
BLAST
Alternative sequencei571 – 64171SSREL…RVVIQ → VSSSPQSEVLYWKVHGAHGD RRATVLASPLLASPLLASPL LASPVSAESTRSLQPALWHI PPPSLASPPAR in isoform PML-3. 1 PublicationVSP_040596Add
BLAST
Alternative sequencei571 – 61141SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-5. 2 PublicationsVSP_005739Add
BLAST
Alternative sequencei612 – 882271Missing in isoform PML-5. 2 PublicationsVSP_005740Add
BLAST
Alternative sequencei621 – 63313TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-4 and isoform PML-12. 2 PublicationsVSP_005744Add
BLAST
Alternative sequencei634 – 882249Missing in isoform PML-4 and isoform PML-12. 2 PublicationsVSP_005745Add
BLAST
Alternative sequencei642 – 882241Missing in isoform PML-3. 1 PublicationVSP_040597Add
BLAST

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]
UniGeneiHs.526464.
Hs.654583.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

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]
UniGeneiHs.526464.
Hs.654583.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
2MVWNMR-A/B120-168[»]
2MWXNMR-A49-104[»]
4WJNX-ray1.50B547-573[»]
4WJOX-ray1.46B547-573[»]
ProteinModelPortaliP29590.
SMRiP29590. Positions 49-104, 120-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111384. 236 interactions.
DIPiDIP-33053N.
IntActiP29590. 98 interactions.
MINTiMINT-158826.
STRINGi9606.ENSP00000268058.

PTM databases

iPTMnetiP29590.
PhosphoSiteiP29590.

Polymorphism and mutation databases

BioMutaiPML.
DMDMi215274219.

Proteomic databases

EPDiP29590.
MaxQBiP29590.
PaxDbiP29590.
PeptideAtlasiP29590.
PRIDEiP29590.

Protocols and materials databases

DNASUi5371.
Structural Biology KnowledgebaseSearch...

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

CTDi5371.
GeneCardsiPML.
HGNCiHGNC:9113. PML.
HPAiCAB010194.
CAB016304.
HPA008312.
MalaCardsiPML.
MIMi102578. gene.
neXtProtiNX_P29590.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA33439.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00510000048454.
HOVERGENiHBG000552.
InParanoidiP29590.
KOiK10054.
OMAiANAQEHP.
OrthoDBiEOG091G02GY.
PhylomeDBiP29590.
TreeFamiTF336434.

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-877300. Interferon gamma signaling.
SignaLinkiP29590.
SIGNORiP29590.

Miscellaneous databases

ChiTaRSiPML. human.
EvolutionaryTraceiP29590.
GeneWikiiPromyelocytic_leukemia_protein.
GenomeRNAii5371.
PMAP-CutDBP29590.
PROiP29590.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140464.
CleanExiHS_PML.
ExpressionAtlasiP29590. baseline and differential.
GenevisibleiP29590. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPML_HUMAN
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
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: September 7, 2016
This is version 206 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.