P29590 (PML_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein PML

Alternative name(s):
Promyelocytic leukemia protein
RING finger protein 71
Tripartite motif-containing protein 19

Gene names

Name:	PML
Synonyms:	MYL, PP8675, RNF71, TRIM19

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	882 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.13 Ref.16 Ref.17 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.29 Ref.30 Ref.32 Ref.36 Ref.37 Ref.39 Ref.41 Ref.42 Ref.44 Ref.45 Ref.47 Ref.48 Ref.51 Ref.57 Ref.61 Ref.63 Ref.66 Ref.71 Ref.72 Ref.74 Ref.76 Ref.79 Ref.80 Ref.85 Ref.87 Ref.88 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. Ref.13 Ref.16 Ref.17 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.29 Ref.30 Ref.32 Ref.36 Ref.37 Ref.39 Ref.41 Ref.42 Ref.44 Ref.45 Ref.47 Ref.48 Ref.51 Ref.57 Ref.61 Ref.63 Ref.66 Ref.71 Ref.72 Ref.74 Ref.76 Ref.79 Ref.80 Ref.85 Ref.87 Ref.88
Subunit structure	Key component of PML bodies. PML bodies are formed by the interaction of PML homodimers (via SUMO-binding motif) with sumoylated PML, leading to the assembly of higher oligomers. Several types of PML bodies have been observed. PML bodies can form hollow spheres that can sequester target proteins inside. Interacts (via SUMO-binding motif) with sumoylated proteins. Interacts (via C-terminus) with p53/TP53. Recruits p53/TP53 and CHEK2 into PML bodies, which promotes p53/TP53 phosphorylation at 'Ser-20' and prevents its proteasomal degradation. Interacts with MDM2, and sequesters MDM2 in the nucleolus, thereby preventing ubiquitination of p53/TP53. Interaction with PML-RARA oncoprotein and certain viral proteins causes disassembly of PML bodies and abolishes the normal PML function. Interacts with HIPK2, TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts with ITPR3 By similarity. Interacts (in the cytoplasm) with TGFBR1, TGFBR2 and 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 By similarity. Interacts with CSNK2A1 and CSNK2A3. 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 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. Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT). Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.38 Ref.39 Ref.44 Ref.48 Ref.49 Ref.53 Ref.55 Ref.57 Ref.60 Ref.63 Ref.66 Ref.68 Ref.69 Ref.71 Ref.72 Ref.74 Ref.75 Ref.79 Ref.81 Ref.82 Ref.84 Ref.86 Ref.87 Ref.88
Subcellular location	Nucleus. Nucleus › nucleoplasm. Cytoplasm. Nucleus › PML body. Nucleus › nucleolus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Isoform PML-1 can shuttle between the nucleus and cytoplasm. Isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 are nuclear isoforms whereas isoform PML-7 and isoform PML-14 lacking the nuclear localization signal are cytoplasmic isoforms. Detected in the nucleolus after DNA damage. Acetylation at Lys-487 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein. Ref.13 Ref.18 Ref.19 Ref.20 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.38 Ref.39 Ref.42 Ref.45 Ref.66 Ref.68 Ref.69 Ref.72 Ref.74 Ref.75 Ref.79 Ref.82
Induction	By interferons alpha, beta and gamma. Up-regulated by IRF3 and p53/TP53.
Domain	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 (Ref.39). Ref.39 Ref.55 Ref.77 Ref.84 The B box-type zinc binding domain and the coiled-coil domain mediate its interaction with PIAS1 (Ref.68). Ref.39 Ref.55 Ref.77 Ref.84 Binds arsenic via the RING-type zinc finger. The RING-type zinc finger is essential for its interaction with HFV bel1/tas (Ref.20). Ref.39 Ref.55 Ref.77 Ref.84 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 (Ref.77). Ref.39 Ref.55 Ref.77 Ref.84 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 (Ref.84). Ref.39 Ref.55 Ref.77 Ref.84
Post-translational modification	Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, KLHL20-based E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. Ubiquitination by KLHL20-based 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. Ref.28 Ref.43 Ref.52 Ref.55 Ref.83 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. Ref.13 Ref.23 Ref.33 Ref.38 Ref.43 Ref.52 Ref.55 Ref.64 Ref.68 Ref.74 Ref.84 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. Ref.24 Ref.30 Ref.49 Ref.60 Ref.68 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.
Involvement in disease	A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon. Ref.1 Ref.2
Sequence similarities	Contains 2 B box-type zinc fingers. Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAA60351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA60352.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA60388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA60390.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB62809.1 differs from that shown. Reason: Chimeric cDNA. The sequence BAD92648.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Antiviral defense Apoptosis Host-virus interaction Immunity Innate immunity Transcription Transcription regulation
Cellular component	Cytoplasm Endoplasmic reticulum Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene Tumor suppressor
Domain	Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB PML body organization Inferred from direct assay PubMed 10779416PubMed 8643677. Source: UniProtKB SMAD protein import into nucleus Inferred from electronic annotation. Source: Compara activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from direct assay PubMed 9583681Ref.27. Source: UniProtKB cell fate commitment Inferred from electronic annotation. Source: Compara cellular senescence Inferred from direct assay Ref.71Ref.69Ref.88. Source: UniProtKB common-partner SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum calcium ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 9583681PubMed 11080164. Source: UniProtKB interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome intrinsic apoptotic signaling pathway in response to DNA damage Inferred from direct assay Ref.24. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from sequence or structural similarity. Source: UniProtKB maintenance of protein location in nucleus Inferred from direct assay PubMed 17332504. Source: MGI myeloid cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of angiogenesis Inferred from mutant phenotype PubMed 16915281. Source: UniProtKB negative regulation of cell growth Inferred from direct assay PubMed 9448006PubMed 7935403PubMed 9395203PubMed 9583681PubMed 9448006. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype Ref.22. Source: BHF-UCL negative regulation of mitotic cell cycle Inferred from direct assay PubMed 9395203. Source: UniProtKB negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.30. Source: UniProtKB negative regulation of telomerase activity Inferred from mutant phenotype Ref.48. Source: UniProtKB negative regulation of telomere maintenance via telomerase Inferred from mutant phenotype Ref.48. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 9448006PubMed 7935403Ref.71PubMed 11259576PubMed 9448006. Source: UniProtKB negative regulation of translation in response to oxidative stress Inferred from direct assay PubMed 16915281. Source: UniProtKB positive regulation of defense response to virus by host Inferred from mutant phenotype PubMed 16873256PubMed 16873257. Source: UniProtKB positive regulation of extrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 21803845. Source: UniProtKB positive regulation of histone deacetylation Inferred from direct assay PubMed 11259576. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.68. Source: UniProtKB protein complex assembly Inferred from direct assay PubMed 12915590. Source: UniProtKB protein stabilization Inferred from direct assay Ref.27. Source: UniProtKB protein targeting Inferred from direct assay PubMed 11080164. Source: UniProtKB regulation of MHC class I biosynthetic process Inferred from electronic annotation. Source: Compara regulation of calcium ion transport into cytosol Inferred from sequence or structural similarity. Source: UniProtKB regulation of double-strand break repair Inferred from mutant phenotype Ref.57. Source: UniProtKB regulation of protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB response to UV Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from direct assay PubMed 16915281. Source: UniProtKB retinoic acid receptor signaling pathway Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay Ref.5Ref.30Ref.38Ref.74Ref.82Ref.79Ref.88PubMed 9448006PubMed 9885291PubMed 9448006. Source: UniProtKB cytoplasm Inferred from direct assay Ref.34PubMed 9885291. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB nuclear matrix Inferred from direct assay PubMed 11080164. Source: UniProtKB nuclear membrane Inferred from direct assay PubMed 123456Ref.34. Source: UniProtKB nucleolus Inferred from direct assay Ref.30Ref.34. Source: UniProtKB nucleus Inferred from direct assay Ref.34. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from direct assay Ref.89. Source: UniProtKB protein heterodimerization activity Inferred from direct assay PubMed 7935403. Source: UniProtKB transcription coactivator activity Inferred from direct assay PubMed 11080164PubMed 15626733. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.89. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03243-1	2	EBI-304008,EBI-1927377	From a different organism.
CSNK2A1	P68400	2	EBI-295890,EBI-347804
DAXX	Q9UER7	6	EBI-295890,EBI-77321
FAS	P25445	4	EBI-295890,EBI-494743
KLHL20	Q9Y2M5	4	EBI-295890,EBI-714379
MAPK7	Q13164	6	EBI-295890,EBI-1213983
MDM2	Q00987	6	EBI-295890,EBI-389668
PSMA3	P25788	2	EBI-295890,EBI-348380
SUMO1	P63165	2	EBI-295890,EBI-80140
TP53	P04637	3	EBI-295890,EBI-366083
ZBTB16	Q05516	7	EBI-295890,EBI-711925

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Isoform PML-1 (identifier: P29590-1)

Also known as: PML-I; TRIM19alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform PML-2 (identifier: P29590-8)

Also known as: PML-II; TRIM19kappa;

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Isoform PML-3 (identifier: P29590-9)

Also known as: PML-III;

The sequence of this isoform differs from the canonical sequence as follows:
     571-641: SSRELDDSSS...RESKFRVVIQ → VSSSPQSEVL...PPSLASPPAR
     642-882: Missing.

Isoform PML-4 (identifier: P29590-5)

Also known as: PML-IV; PML-X; TRIM19zeta;

The sequence of this isoform differs from the canonical sequence as follows:
     621-633: TQKISQLAAVNRE → SGFSWGYPHPFLI
     634-882: Missing.

Isoform PML-5 (identifier: P29590-2)

Also known as: PML-2; PML-V; TRIM19beta;

The sequence of this isoform differs from the canonical sequence as follows:
     571-611: SSRELDDSSS...DPQAEDRPLV → VSGPEVQPRT...LRLGNFPVRH
     612-882: Missing.

Note: Contains a phosphoserine at position 565.

Isoform PML-6 (identifier: P29590-4)

Also known as: PML-3B; PML-VI; TRIM19epsilon;

The sequence of this isoform differs from the canonical sequence as follows:
     553-560: EERVVVIS → GRERNALW
     561-882: Missing.

Note: Contains a phosphoserine at position 518. Contains a phosphoserine at position 527. Contains a phosphoserine at position 530.

Isoform PML-7 (identifier: P29590-10)

Also known as: PML-VII; TRIM19theta;

The sequence of this isoform differs from the canonical sequence as follows:
     419-435: PEEAERVKAQVQALGLA → LPPPAHALTGPAQSSTH
     436-882: Missing.

Isoform PML-8 (identifier: P29590-3)

Also known as: PML-2G; PML-IIG; TRIM19gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Note: Non-canonical splice sites. Might alternatively represent a polymorphic variation.

Isoform PML-11 (identifier: P29590-11)

Also known as: PML-1A; PML-IA;

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.

Note: No experimental confirmation available.

Isoform PML-12 (identifier: P29590-12)

Also known as: PML-4A; PML-IVA; TRIM19lambda;

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.
     621-633: TQKISQLAAVNRE → SGFSWGYPHPFLI
     634-882: Missing.

Isoform PML-13 (identifier: P29590-13)

Also known as: PML-2A; PML-IIA;

The sequence of this isoform differs from the canonical sequence as follows:
     419-466: Missing.
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Isoform PML-14 (identifier: P29590-14)

Also known as: PML-6B; PML-VIB; TRIM19eta; TRIM19iota;

The sequence of this isoform differs from the canonical sequence as follows:
     419-423: PEEAE → RNALW
     424-882: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 882

882

Protein PML

PRO_0000056001

Regions

Zinc finger

57 – 92

36

RING-type

Zinc finger

124 – 166

43

B box-type 1; atypical

Zinc finger

183 – 236

54

B box-type 2

Region

448 – 555

108

Interaction with PER2

Region

476 – 490

15

Nuclear localization signal

Region

556 – 562

7

Sumo interaction motif (SIM)

Coiled coil

228 – 253

26

Potential

Compositional bias

3 – 46

44

Pro-rich

Sites

Metal binding

57

1

Zinc 1

Metal binding

60

1

Zinc 1

Metal binding

72

1

Zinc 2

Metal binding

74

1

Zinc 2

Metal binding

77

1

Zinc 1

Metal binding

80

1

Zinc 1

Metal binding

88

1

Zinc 2

Metal binding

91

1

Zinc 2

Site

394 – 395

2

Breakpoint for translocation to form PML-RARA oncogene in type A APL

Site

552 – 553

2

Breakpoint for translocation to form PML-RARA oncogene in type B APL

Amino acid modifications

Modified residue

8

1

Phosphoserine; by HIPK2 Ref.49

Modified residue

28

1

Phosphothreonine; by MAPK1

Modified residue

36

1

Phosphoserine; by HIPK2 and MAPK1

Modified residue

38

1

Phosphoserine; by HIPK2 and MAPK1 Ref.49

Modified residue

40

1

Phosphoserine; by MAPK1

Modified residue

42

1

Phosphothreonine

Modified residue

117

1

Phosphoserine; by CHEK2 Ref.24

Modified residue

403

1

Phosphoserine; by MAPK1 and MAPK7 Ref.35 Ref.46 Ref.60

Modified residue

409

1

Phosphothreonine; by MAPK7

Modified residue

487

1

N6-acetyllysine Ref.40 Ref.72

Modified residue

504

1

Phosphoserine By similarity

Modified residue

505

1

Phosphoserine; by MAPK1 Ref.60

Modified residue

515

1

N6-acetyllysine Probable

Modified residue

518

1

Phosphoserine; by CDK1 and CDK2 Ref.35 Ref.46 Ref.54 Ref.60 Ref.67

Modified residue

527

1

Phosphoserine; by MAPK1 Ref.35 Ref.46 Ref.54 Ref.60 Ref.67

Modified residue

530

1

Phosphoserine; by MAPK1 Ref.35 Ref.46 Ref.50 Ref.67

Modified residue

535

1

Phosphoserine

Modified residue

565

1

Phosphoserine; by CK2 Ref.35 Ref.68

Cross-link

65

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13 Ref.68

Cross-link

160

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13 Ref.68

Cross-link

380

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43

Cross-link

400

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43

Cross-link

401

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43

Cross-link

476

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.43

Cross-link

490

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13 Ref.74

Cross-link

497

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Natural variations

Alternative sequence

419 – 466

48

Missing in isoform PML-11, isoform PML-12 and isoform PML-13.

VSP_040590

Alternative sequence

419 – 435

17

PEEAE…ALGLA → LPPPAHALTGPAQSSTH in isoform PML-7.

VSP_040591

Alternative sequence

419 – 423

5

PEEAE → RNALW in isoform PML-14.

VSP_040592

Alternative sequence

424 – 882

459

Missing in isoform PML-14.

VSP_040593

Alternative sequence

436 – 882

447

Missing in isoform PML-7.

VSP_040594

Alternative sequence

553 – 560

8

EERVVVIS → GRERNALW in isoform PML-6.

VSP_005742

Alternative sequence

561 – 882

322

Missing in isoform PML-6.

VSP_005743

Alternative sequence

571 – 882

312

SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPAHSSPVQSLLRAQGAS SLPCGTYHPPAWPPHQPAEQ AATPDAEPHSEPPDHQERPA VHRGIRYLLYRAQRAIRLRH ALRLHPQLHRAPIRTWSPHV VQASTPAITGPLNHPANAQE HPAQLQRGISPPHRIRGAVR SRSRSLRGSSHLSQWLNNFF ALPFSSMASQLDMSSVVGAG ESRAQTLGAGVPPGDSVRGS MEASQVQVPLEASPITFPPP CAPERPPISPVPGARQAGL in isoform PML-2 and isoform PML-13.

VSP_040595

Alternative sequence

571 – 882

312

SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-8.

VSP_005741

Alternative sequence

571 – 641

71

SSREL…RVVIQ → VSSSPQSEVLYWKVHGAHGD RRATVLASPLLASPLLASPL LASPVSAESTRSLQPALWHI PPPSLASPPAR in isoform PML-3.

VSP_040596

Alternative sequence

571 – 611

41

SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-5.

VSP_005739

Alternative sequence

612 – 882

271

Missing in isoform PML-5.

VSP_005740

Alternative sequence

621 – 633

13

TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-4 and isoform PML-12.

VSP_005744

Alternative sequence

634 – 882

249

Missing in isoform PML-4 and isoform PML-12.

VSP_005745

Alternative sequence

642 – 882

241

Missing in isoform PML-3.

VSP_040597

Natural variant

645

1

F → L. Ref.2 Ref.5
Corresponds to variant rs5742915 [ dbSNP | Ensembl ].

VAR_052090

Experimental info

Mutagenesis

57

1

C → S: Strongly reduced sumoylation; when associated with S-60. Ref.38

Mutagenesis

60

1

C → S: Strongly reduced sumoylation; when associated with S-57. Ref.38

Mutagenesis

65

1

K → R: Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. No sumoylation nor nuclear body formation; when associated with R-160 and R-490. Ref.13

Mutagenesis

68

1

K → R: No effect on sumoylation levels.

Mutagenesis

88

1

C → S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89. Ref.33

Mutagenesis

89

1

P → R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88. Ref.33

Mutagenesis

133

1

K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.13

Mutagenesis

150

1

K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.13

Mutagenesis

160

1

K → R: Loss of 2 sumoylations; when associated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. Ref.13

Mutagenesis

487

1

K → A: Loss of nuclear localization; when associated with A-490. Ref.39 Ref.40

Mutagenesis

487

1

K → R: Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515. Ref.39 Ref.40

Mutagenesis

490

1

K → A: Loss of nuclear localization; when associated with A-487. Ref.13 Ref.39

Mutagenesis

490

1

K → R: Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160. Ref.13 Ref.39

Mutagenesis

515

1

K → R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487. Ref.40

Mutagenesis

556 – 559

4

VVVI → AAAS: Abolishes SUMO1 binding.

Sequence conflict

224

1

E → D in AAP88913. Ref.7

Sequence conflict

224

1

E → D in AAH00080. Ref.10

Sequence conflict

224

1

E → D in AAH20994. Ref.10

Sequence conflict

419

1

P → A in AAA60351. Ref.2

Sequence conflict

419

1

P → A in AAA60388. Ref.2

Sequence conflict

419

1

P → A in AAA60390. Ref.2

Sequence conflict

419

1

P → A in AAA60352. Ref.4

Sequence conflict

419

1

P → A in AAG50182. Ref.5

Sequence conflict

419

1

P → A in AAG50184. Ref.5

Sequence conflict

419

1

P → A in AAG50185. Ref.5

Isoform PML-5:

Sequence conflict

578

1

P → A in AAG50181. Ref.5

Isoform PML-7:

Sequence conflict

419

1

L → V in AAG50187. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

882

Helix Strand Turn

Details...

Beta strand

58 – 60

3

Beta strand

82 – 87

6

Beta strand

93 – 96

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform PML-1 (PML-I) (TRIM19alpha) [UniParc]. Last modified November 25, 2008. Version 3. Checksum: D50968A977E34287	FASTA	882	97,551
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 610 620 630 640 650 660 ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ 670 680 690 700 710 720 HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG 730 740 750 760 770 780 ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS 790 800 810 820 830 840 LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA 850 860 870 880 FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS
	Isoform PML-2 (PML-II) (TRIM19kappa) [UniParc]. Checksum: 25824778A4AB6AB1	FASTA	829	90,721
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS CMEPMETAEP QSSPAHSSPA HSSPAHSSPV 610 620 630 640 650 660 QSLLRAQGAS SLPCGTYHPP AWPPHQPAEQ AATPDAEPHS EPPDHQERPA VHRGIRYLLY 670 680 690 700 710 720 RAQRAIRLRH ALRLHPQLHR APIRTWSPHV VQASTPAITG PLNHPANAQE HPAQLQRGIS 730 740 750 760 770 780 PPHRIRGAVR SRSRSLRGSS HLSQWLNNFF ALPFSSMASQ LDMSSVVGAG ESRAQTLGAG 790 800 810 820 VPPGDSVRGS MEASQVQVPL EASPITFPPP CAPERPPISP VPGARQAGL
	Isoform PML-3 (PML-III) [UniParc]. Checksum: 8262393E2B00CBC7	FASTA	641	70,368
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS VSSSPQSEVL YWKVHGAHGD RRATVLASPL 610 620 630 640 LASPLLASPL LASPVSAEST RSLQPALWHI PPPSLASPPA R
	Isoform PML-4 (PML-IV) (PML-X) (TRIM19zeta) [UniParc]. Checksum: 85FBAEC9F162C8E0	FASTA	633	70,024
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 610 620 630 ADPQAEDRPL VFFDLKIDNE SGFSWGYPHP FLI
	Isoform PML-5 (PML-2) (PML-V) (TRIM19beta) [UniParc]. Checksum: 52E7FB5D57D59233	FASTA	611	67,471
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS VSGPEVQPRT PASPHFRSQG AQPQQVTLRL 610 ALRLGNFPVR H
	Isoform PML-6 (PML-3B) (PML-VI) (TRIM19epsilon) [UniParc]. Checksum: 9DC795A6542BA778	FASTA	560	62,007
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 NSNHVASGAG EAGRERNALW
	Isoform PML-7 (PML-VII) (TRIM19theta) [UniParc]. Checksum: 2565113DBF5F9229	FASTA	435	48,598
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLLP 430 PPAHALTGPA QSSTH
	Isoform PML-8 (PML-2G) (PML-IIG) (TRIM19gamma) [UniParc]. Checksum: 5DA9DD2E4EEE8492	FASTA	824	90,254
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS CMEPMETAEP QSSPAHSSPA HSSPVQSLLR 610 620 630 640 650 660 AQGASSLPCG TYHPPAWPPH QPAEQAATPD AEPHSEPPDH QERPAVHRGI RYLLYRAQRA 670 680 690 700 710 720 IRLRHALRLH PQLHRAPIRT WSPHVVQAST PAITGPLNHP ANAQEHPAQL QRGISPPHRI 730 740 750 760 770 780 RGAVRSRSRS LRGSSHLSQW LNNFFALPFS SMASQLDMSS VVGAGEGRAQ TLGAVVPPGD 790 800 810 820 SVRGSMEASQ VQVPLEASPI TFPPPCAPER PPISPVPGAR QAGL
	Isoform PML-11 (PML-1A) (PML-IA) [UniParc]. Checksum: 16772D51354CFDAC	FASTA	834	92,564
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLDV 430 440 450 460 470 480 SNTTTAQKRK CSQTQCPRKV IKMESEEGKE ARLARSSPEQ PRPSTSKAVS PPHLDGPPSP 490 500 510 520 530 540 RSPVIGSEVF LPNSNHVASG AGEAEERVVV ISSSEDSDAE NSSSRELDDS SSESSDLQLE 550 560 570 580 590 600 GPSTLRVLDE NLADPQAEDR PLVFFDLKID NETQKISQLA AVNRESKFRV VIQPEAFFSI 610 620 630 640 650 660 YSKAVSLEVG LQHFLSFLSS MRRPILACYK LWGPGLPNFF RALEDINRLW EFQEAISGFL 670 680 690 700 710 720 AALPLIRERV PGASSFKLKN LAQTYLARNM SERSAMAAVL AMRDLCRLLE VSPGPQLAQH 730 740 750 760 770 780 VYPFSSLQCF ASLQPLVQAA VLPRAEARLL ALHNVSFMEL LSAHRRDRQG GLKKYSRYLS 790 800 810 820 830 LQTTTLPPAQ PAFNLQALGT YFEGLLEGPA LARAEGVSTP LAGRGLAERA SQQS
	Isoform PML-12 (PML-4A) (PML-IVA) (TRIM19lambda) [UniParc]. Checksum: FF1E5A8D845780B2	FASTA	585	65,037
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLDV 430 440 450 460 470 480 SNTTTAQKRK CSQTQCPRKV IKMESEEGKE ARLARSSPEQ PRPSTSKAVS PPHLDGPPSP 490 500 510 520 530 540 RSPVIGSEVF LPNSNHVASG AGEAEERVVV ISSSEDSDAE NSSSRELDDS SSESSDLQLE 550 560 570 580 GPSTLRVLDE NLADPQAEDR PLVFFDLKID NESGFSWGYP HPFLI
	Isoform PML-13 (PML-2A) (PML-IIA) [UniParc]. Checksum: C6C163ECD9FA6FB2	FASTA	781	85,734
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLDV 430 440 450 460 470 480 SNTTTAQKRK CSQTQCPRKV IKMESEEGKE ARLARSSPEQ PRPSTSKAVS PPHLDGPPSP 490 500 510 520 530 540 RSPVIGSEVF LPNSNHVASG AGEAEERVVV ISSSEDSDAE NSCMEPMETA EPQSSPAHSS 550 560 570 580 590 600 PAHSSPAHSS PVQSLLRAQG ASSLPCGTYH PPAWPPHQPA EQAATPDAEP HSEPPDHQER 610 620 630 640 650 660 PAVHRGIRYL LYRAQRAIRL RHALRLHPQL HRAPIRTWSP HVVQASTPAI TGPLNHPANA 670 680 690 700 710 720 QEHPAQLQRG ISPPHRIRGA VRSRSRSLRG SSHLSQWLNN FFALPFSSMA SQLDMSSVVG 730 740 750 760 770 780 AGESRAQTLG AGVPPGDSVR GSMEASQVQV PLEASPITFP PPCAPERPPI SPVPGARQAG L
	Isoform PML-14 (PML-6B) (PML-VIB) (TRIM19eta) (TRIM19iota) [UniParc]. Checksum: EE5031BE9C3B33C8	FASTA	423	47,575
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLRN ALW

References

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[1]	"The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR." de The H., Lavau C., Marchio A., Chomienne C., Degos L., Dejean A. Cell 66:675-684(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3), DISEASE.
[2]	"Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia." Goddard A.D., Borrow J., Freemont P.S., Solomon E. Science 254:1371-1374(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-5 AND PML-8), CHROMOSOMAL TRANSLOCATION WITH RARA, DISEASE, VARIANT LEU-645.
[3]	"Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins." Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., Chambon P. EMBO J. 11:629-642(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-4).
[4]	"Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML." Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr., Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M. Cell 66:663-674(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
[5]	"The tripartite motif family identifies cell compartments." Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A. EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2; PML-4; PML-5; PML-6; PML-7; PML-8; PML-12 AND PML-14), VARIANT LEU-645.
[6]	Goddard A.D., Solomon E. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13).
[8]	"Homo sapiens protein coding cDNA." Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-11). Tissue: Brain.
[9]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13). Tissue: Kidney.
[11]	"Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants." Tong J.H., Dong S., Geng J.P., Huang W., Wang Z.Y., Sun G.L., Chen S.J., Chen Z., Larsen C.-J., Berger R. Oncogene 7:311-316(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466, CHROMOSOMAL TRANSLOCATION WITH RARA.
[12]	"Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic leukemia: structure of the fusion point in a case lacking classic t(15;17) translocation." Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K., Omine M. Leuk. Lymphoma 44:111-115(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, CHROMOSOMAL TRANSLOCATION WITH RARA.
[13]	"Identification of three major sentrinization sites in PML." Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T., Yeh E.T.H. J. Biol. Chem. 273:26675-26682(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65; LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, FUNCTION.
[14]	"Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML." Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D. J. Cell Sci. 111:1319-1329(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM27.
[15]	"An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm." Borden K.L., Campbell-Dwyer E.J., Salvato M.S. J. Virol. 72:758-766(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LASSA VIRUS Z PROTEIN.
[16]	"A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins." Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H., Kalantry S., Freedman L.P., Pandolfi P.P. Nat. Genet. 23:287-295(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RARA; RXRA AND TRIM24.
[17]	"Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis." Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P. J. Exp. Med. 191:631-640(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAXX.
[18]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
[19]	"The function of PML in p53-dependent apoptosis." Guo A., Salomoni P., Luo J., Shih A., Zhong S., Gu W., Pandolfi P.P. Nat. Cell Biol. 2:730-736(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
[20]	"PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator." Regad T., Saib A., Lallemand-Breitenbach V., Pandolfi P.P., de The H., Chelbi-Alix M.K. EMBO J. 20:3495-3505(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HFV RESTRICTION, INTERACTION WITH HFV BEL1 AND BET, SUBCELLULAR LOCATION.
[21]	"PML protein isoforms and the RBCC/TRIM motif." Jensen K., Shiels C., Freemont P.S. Oncogene 20:7223-7233(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE OF ISOFORMS PML-1 THROUGH PML-7.
[22]	"Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence." Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T. EMBO J. 21:2383-2396(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIRT1.
[23]	"SUMO-1 protease-1 regulates gene transcription through PML." Best J.L., Ganiatsas S., Agarwal S., Changou A., Salomoni P., Shirihai O., Meluh P.B., Pandolfi P.P., Zon L.I. Mol. Cell 10:843-855(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, DESUMOYLATION BY SENP2.
[24]	"PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2." Yang S., Kuo C., Bisi J.E., Kim M.K. Nat. Cell Biol. 4:865-870(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR, PHOSPHORYLATION AT SER-117 BY CHEK2, INTERACTION WITH CHEK2.
[25]	"Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies." Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P., De The H., Chelbi-Alix M.K. Oncogene 21:7957-7970(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RABIES VIRUS PHOSPHOPROTEINS, SUBCELLULAR LOCATION, FUNCTION.
[26]	"The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation." Louria-Hayon I., Grossman T., Sionov R.V., Alsheich O., Pandolfi P.P., Haupt Y. J. Biol. Chem. 278:33134-33141(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2 AND TP53.
[27]	"PML colocalizes with and stabilizes the DNA damage response protein TopBP1." Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S. Mol. Cell. Biol. 23:4247-4256(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOPBP1.
[28]	"The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome." Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S. J. Biol. Chem. 279:5374-5379(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[29]	"Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein." Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., Matsuzaki K., Nakao M., Li J.-D., Kai H. J. Biol. Chem. 279:19091-19098(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ELF4, SUBCELLULAR LOCATION.
[30]	"PML regulates p53 stability by sequestering Mdm2 to the nucleolus." Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P. Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MDM2 AND RPL11, PHOSPHORYLATION BY ATR IN RESPONSE TO DNA DAMAGE, SUBCELLULAR LOCATION.
[31]	"PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein." Daniels M.J., Marson A., Venkitaraman A.R. Nat. Struct. Mol. Biol. 11:1114-1121(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHFR.
[32]	"Cytoplasmic PML function in TGF-beta signalling." Lin H.K., Bergmann S., Pandolfi P.P. Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFBR1; TGFBR2; SMAD2; SMAD3 AND ZFYVE9/SARA.
[33]	"Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation." Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H. Biochem. Biophys. Res. Commun. 330:746-754(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF PML-RARALPHA ONCOPROTEIN WITH UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF CYS-88 AND PRO-89.
[34]	"Characterization of endogenous human promyelocytic leukemia isoforms." Condemine W., Takahashi Y., Zhu J., Puvion-Dutilleul F., Guegan S., Janin A., de The H. Cancer Res. 66:6192-6198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[35]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527 AND SER-530, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565 (ISOFORM PML-5), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR." Dellaire G., Ching R.W., Ahmed K., Jalali F., Tse K.C., Bristow R.G., Bazett-Jones D.P. J. Cell Biol. 175:55-66(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[37]	"Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense." Pampin M., Simonin Y., Blondel B., Percherancier Y., Chelbi-Alix M.K. J. Virol. 80:8582-8592(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN POLIOVIRUS RESTRICTION.
[38]	"The mechanisms of PML-nuclear body formation." Shen T.H., Lin H.K., Scaglioni P.P., Yung T.M., Pandolfi P.P. Mol. Cell 24:331-339(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUMOYLATION, SUMO-BINDING MOTIF, MUTAGENESIS OF CYS-57 AND CYS-60, SUBCELLULAR LOCATION.
[39]	"Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein." Shimada N., Shinagawa T., Ishii S. Genes Cells 13:245-254(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKM, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-487 AND LYS-490.
[40]	"Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis." Hayakawa F., Abe A., Kitabayashi I., Pandolfi P.P., Naoe T. J. Biol. Chem. 283:24420-24425(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-487 AND LYS-515, MUTAGENESIS OF LYS-487 AND LYS-515.
[41]	"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection." Tavalai N., Papior P., Rechter S., Stamminger T. J. Virol. 82:126-137(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HCMV RESTRICTION.
[42]	"The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network." Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F., Teruya-Feldstein J., Pandolfi P.P. Nature 455:813-817(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[43]	"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation." Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T. Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract] Cited for: POLYUBIQUITINATION AT LYS-380; LYS-400; LYS-401 AND LYS-476 BY RNF4, PROTEASOMAL DEGRADATION, SUMOYLATION.
[44]	"Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus." Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A., Galande S. Nat. Cell Biol. 9:45-56(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SATB1.
[45]	"A role for cytoplasmic PML in cellular resistance to viral infection." McNally B.A., Trgovcich J., Maul G.G., Liu Y., Zheng P. PLoS ONE 3:E2277-E2277(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HHV-1 RESTRICTION, SUBCELLULAR LOCATION.
[46]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527 AND SER-530, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[47]	"Differential suppressive effect of promyelocytic leukemia protein on the replication of different subtypes/strains of influenza A virus." Li W., Wang G., Zhang H., Zhang D., Zeng J., Chen X., Xu Y., Li K. Biochem. Biophys. Res. Commun. 389:84-89(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INFLUENZA A VIRUS RESTRICTION.
[48]	"PML-IV functions as a negative regulator of telomerase by interacting with TERT." Oh W., Ghim J., Lee E.W., Yang M.R., Kim E.T., Ahn J.H., Song J. J. Cell Sci. 122:2613-2622(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TERT.
[49]	"PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage." Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K., Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L. Oncogene 28:698-708(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-8 AND SER-38 BY HIPK2, INTERACTION WITH HIPK2.
[50]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[51]	"Resistance to rabies virus infection conferred by the PMLIV isoform." Blondel D., Kheddache S., Lahaye X., Dianoux L., Chelbi-Alix M.K. J. Virol. 84:10719-10726(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN RABIES VIRUS RESTRICTION.
[52]	"Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies." Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T. Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, UBIQUITINATION.
[53]	"Functional polymorphism of the CK2alpha intronless gene plays oncogenic roles in lung cancer." Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M., You L. PLoS ONE 5:E11418-E11418(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSNK2A1 AND CSNK2A3.
[54]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-527, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[55]	"Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML." Zhang X.W., Yan X.J., Zhou Z.R., Yang F.F., Wu Z.Y., Sun H.B., Liang W.X., Song A.X., Lallemand-Breitenbach V., Jeanne M., Zhang Q.Y., Yang H.Y., Huang Q.H., Zhou G.B., Tong J.H., Zhang Y., Wu J.H., Hu H.Y. , de The H., Chen S.J., Chen Z. Science 328:240-243(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBC9, SUBUNIT, UBIQUITINATION, SUMOYLATION, ARSENIC BINDING, DOMAIN, MASS SPECTROMETRY.
[56]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[57]	"Promyelocytic leukemia protein interacts with werner syndrome helicase and regulates double-strand break repair in gamma-irradiation-induced DNA damage responses." Liu J., Song Y., Qian J., Liu B., Dong Y., Tian B., Sun Z. Biokhimiia 76:550-554(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH WRN.
[58]	"The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites." Pinton P., Giorgi C., Pandolfi P.P. Cell Death Differ. 18:1450-1456(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[59]	"The nuclear bodies inside out: PML conquers the cytoplasm." Carracedo A., Ito K., Pandolfi P.P. Curr. Opin. Cell Biol. 23:360-366(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[60]	"Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover." Lim J.H., Liu Y., Reineke E., Kao H.Y. J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-403; SER-505; SER-518 AND SER-527, INTERACTION WITH PIN1 AND MAPK1.
[61]	"PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication." Cuchet D., Sykes A., Nicolas A., Orr A., Murray J., Sirma H., Heeren J., Bartelt A., Everett R.D. J. Cell Sci. 124:280-291(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[62]	"Role of promyelocytic leukemia protein in host antiviral defense." Geoffroy M.C., Chelbi-Alix M.K. J. Interferon Cytokine Res. 31:145-158(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION IN ANTIVIRAL DEFENSE.
[63]	"Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies." Maroui M.A., Pampin M., Chelbi-Alix M.K. J. Virol. 85:13164-13173(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EMCV RESTRICTION, INTERACTION WITH EMCV P3D-POL.
[64]	"The SUMO protease SENP6 is a direct regulator of PML nuclear bodies." Hattersley N., Shen L., Jaffray E.G., Hay R.T. Mol. Biol. Cell 22:78-90(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, DESUMOYLATION BY SENP6.
[65]	"The role of PML in the nervous system." Salomoni P., Betts-Henderson J. Mol. Neurobiol. 43:114-123(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[66]	"Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against Varicella-Zoster virus." Reichelt M., Wang L., Sommer M., Perrino J., Nour A.M., Sen N., Baiker A., Zerboni L., Arvin A.M. PLoS Pathog. 7:E1001266-E1001266(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN VARICELLA ZOSTER RESTRICTION, SUBCELLULAR LOCATION, INTERACTION WITH VZV VP26.
[67]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-527 AND SER-530, MASS SPECTROMETRY.
[68]	"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA." Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P. Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-65 AND LYS-160, PHOSPHORYLATION AT SER-565, SUBCELLULAR LOCATION, INTERACTION WITH PIAS1; PIAS2 AND CSNK2A1.
[69]	"MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs." Peche L.Y., Scolz M., Ladelfa M.F., Monte M., Schneider C. Cell Death Differ. 19:926-936(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MAGEA2.
[70]	"Role of the promyelocytic leukaemia protein in cell death regulation." Salomoni P., Dvorkina M., Michod D. Cell Death Dis. 3:E247-E247(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[71]	"Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence." Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M., Dejean A., Bischof O. EMBO J. 31:95-109(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TBX2; TBX3; E2F4 AND RBL2.
[72]	"PML regulates PER2 nuclear localization and circadian function." Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A., Rea M.A., Zhao Z., Lee C.C., Chang K.S. EMBO J. 31:1427-1439(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PER2, ACETYLATION AT LYS-487, DEACETYLATION BY SIRT1.
[73]	"Post-translational modifications of PML: consequences and implications." Cheng X., Kao H.Y. Front. Oncol. 2:210-210(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON PTM.
[74]	"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells." Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T. Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-490, INTERACTION WITH HDAC7; RANBP2 AND CTNNB1-TCF4 COMPLEX.
[75]	"Moloney murine leukemia virus integrase and reverse transcriptase interact with PML proteins." Okino Y., Inayoshi Y., Kojima Y., Kidani S., Kaneoka H., Honkawa A., Higuchi H., Nishijima K., Miyake K., Iijima S. J. Biochem. 152:161-169(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MOMLV IN AND RT, SUBCELLULAR LOCATION.
[76]	"Promyelocytic leukemia protein (PML) regulates endothelial cell network formation and migration in response to tumor necrosis factor alpha (TNFalpha) and interferon alpha (IFNalpha)." Cheng X., Liu Y., Chu H., Kao H.Y. J. Biol. Chem. 287:23356-23367(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[77]	"Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation." Geng Y., Monajembashi S., Shao A., Cui D., He W., Chen Z., Hemmerich P., Tang J. J. Biol. Chem. 287:30729-30742(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN C-TERMINAL.
[78]	"The role of PML ubiquitination in human malignancies." Chen R.H., Lee Y.R., Yuan W.C. J. Biomed. Sci. 19:81-81(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON UBIQUITINATION.
[79]	"PML promotes MHC class II gene expression by stabilizing the class II transactivator." Ulbricht T., Alzrigat M., Horch A., Reuter N., von Mikecz A., Steimle V., Schmitt E., Kraemer O.H., Stamminger T., Hemmerich P. J. Cell Biol. 199:49-63(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CIITA.
[80]	"A metabolic prosurvival role for PML in breast cancer." Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G., Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A., Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C., Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P. J. Clin. Invest. 122:3088-3100(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[81]	"Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation." Cuchet-Lourenco D., Vanni E., Glass M., Orr A., Everett R.D. J. Virol. 86:11209-11222(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HHV-1 ICP0.
[82]	"BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction." Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D. Oncogene 0:0-0(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MDM2 AND MAPK7.
[83]	"The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein." Guan D., Factor D., Liu Y., Wang Z., Kao H.Y. Oncogene 0:0-0(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY UHRF1.
[84]	"Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms." Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K. PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, INTERACTION WITH RNF4, DOMAIN SIM.
[85]	"PML tumor suppressor protein is required for HCV production." Kuroki M., Ariumi Y., Hijikata M., Ikeda M., Dansako H., Wakita T., Shimotohno K., Kato N. Biochem. Biophys. Res. Commun. 430:592-597(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[86]	"Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human." Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., Kuo W.C., Chuang Y.T., Jiang S.T., Shih H.M., Lai M.Z. Blood 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLRP3.
[87]	"The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription." Berscheminski J., Groitl P., Dobner T., Wimmer P., Schreiner S. J. Virol. 87:965-977(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS 2 E1A.
[88]	"MOZ increases p53 acetylation and premature senescence through its complex formation with PML." Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., Prives C. Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KAT6A.
[89]	"The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML." Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S., Howe K., Solomon E., Freemont P.S. EMBO J. 14:1532-1541(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 49-104.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S50913 mRNA. Translation: AAB19601.2.
M79462 mRNA. Translation: AAA60388.1. Different initiation.
M79463 mRNA. Translation: AAA60351.1. Different initiation.
M79464 mRNA. Translation: AAA60390.1. Different initiation.
X63131 mRNA. Translation: CAA44841.1.
M73778 mRNA. Translation: AAA60125.1.
M80185 mRNA. Translation: AAA60352.1. Different initiation.
AF230401 mRNA. Translation: AAG50180.1.
AF230402 mRNA. Translation: AAG50181.1.
AF230403 mRNA. Translation: AAG50182.1.
AF230405 mRNA. Translation: AAG50184.1.
AF230406 mRNA. Translation: AAG50185.1.
AF230407 mRNA. Translation: AAG50186.1.
AF230408 mRNA. Translation: AAG50187.1.
AF230409 mRNA. Translation: AAG50188.1.
AF230410 mRNA. Translation: AAG50189.1.
AF230411 mRNA. Translation: AAG50190.1.
BT009911 mRNA. Translation: AAP88913.1.
AB209411 mRNA. Translation: BAD92648.1. Different initiation.
AC013486 Genomic DNA. No translation available.
AC108137 Genomic DNA. No translation available.
BC000080 mRNA. Translation: AAH00080.2.
BC020994 mRNA. Translation: AAH20994.1.
X64800 Genomic DNA. Translation: CAA46026.1.
AB067754 mRNA. Translation: BAB62809.1. Sequence problems.

IPI

IPI00022348.
IPI00220453.
IPI00291097.
IPI00303999.
IPI00304000.
IPI00332110.
IPI00395707.
IPI00395893.
IPI00744329.
IPI00922350.
IPI00922504.
IPI00940182.
IPI00973909.
IPI00974368.
IPI00974373.

PIR

A40044.
I38054.
S19244.
S42516.
S44381.

RefSeq

NP_002666.1. NM_002675.3.
NP_150241.2. NM_033238.2.
NP_150242.1. NM_033239.2.
NP_150243.2. NM_033240.2.
NP_150247.2. NM_033244.3.
NP_150249.1. NM_033246.2.
NP_150250.2. NM_033247.2.
NP_150252.1. NM_033249.2.
NP_150253.2. NM_033250.2.

UniGene

Hs.526464.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOR	NMR	-	A	49-104	[»]

ProteinModelPortal

P29590.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29590. 44 interactions.

MINT

MINT-158826.

STRING

9606.ENSP00000268058.

PTM databases

PhosphoSite

P29590.

Polymorphism databases

DMDM

215274219.

Proteomic databases

PaxDb

P29590.

PRIDE

P29590.

Protocols and materials databases

DNASU

5371.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268058; ENSP00000268058; ENSG00000140464.
ENST00000268059; ENSP00000268059; ENSG00000140464.
ENST00000354026; ENSP00000315434; ENSG00000140464.
ENST00000359928; ENSP00000353004; ENSG00000140464.
ENST00000395132; ENSP00000378564; ENSG00000140464.
ENST00000395135; ENSP00000378567; ENSG00000140464.
ENST00000435786; ENSP00000395576; ENSG00000140464.
ENST00000436891; ENSP00000394642; ENSG00000140464.
ENST00000564428; ENSP00000457023; ENSG00000140464.
ENST00000565898; ENSP00000455838; ENSG00000140464.
ENST00000567543; ENSP00000456277; ENSG00000140464.
ENST00000569477; ENSP00000455612; ENSG00000140464.
ENST00000569965; ENSP00000456486; ENSG00000140464.

GeneID

5371.

KEGG

hsa:5371.

UCSC

uc002awk.3. human.
uc002awl.3. human.
uc002awm.3. human.
uc002awn.3. human.
uc002awo.3. human.
uc002awp.3. human.
uc002awr.3. human.
uc002aws.3. human.
uc002awu.3. human.
uc002awv.3. human.

Organism-specific databases

CTD

5371.

GeneCards

GC15P074287.

HGNC

HGNC:9113. PML.

HPA

CAB010194.
CAB016304.
HPA008312.

MIM

102578. gene.

neXtProt

NX_P29590.

Orphanet

520. Acute promyelocytic leukemia.

PharmGKB

PA33439.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326718.

HOVERGEN

HBG000552.

InParanoid

P29590.

KO

K10054.

OMA

VQRMKRY.

OrthoDB

EOG4H19V2.

PhylomeDB

P29590.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_6900. Immune System.

SignaLink

P29590.

Gene expression databases

ArrayExpress

P29590.

Bgee

P29590.

CleanEx

HS_PML.

Genevestigator

P29590.

GermOnline

ENSG00000140464. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]

SMART

SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PML. human.

EvolutionaryTrace

P29590.

GenomeRNAi

5371.

NextBio

20820.

PMAP-CutDB

P29590.

SOURCE

Search...

Entry information

Entry name

PML_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 169 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.