HUMAN:PML

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PML (synonyms: MYL, PP8675, RNF71, TRIM19)
Protein Name(s)	Protein PML Promyelocytic leukemia protein RING finger protein 71 Tripartite motif-containing protein 19
External Links
UniProt	P29590
EMBL	S50913 M79462 M79463 M79464 X63131 M73778 M80185 AF230401 AF230402 AF230403 AF230405 AF230406 AF230407 AF230408 AF230409 AF230410 AF230411 BT009911 AB209411 AC013486 AC108137 BC000080 BC020994 X64800 AB067754
CCDS	CCDS10255.1 CCDS10256.1 CCDS10257.1 CCDS10258.1 CCDS45297.1 CCDS45298.1 CCDS45299.1 CCDS45300.1 CCDS58386.1
PIR	A40044 I38054 S19244 S42516 S44381
RefSeq	NP_002666.1 NP_150241.2 NP_150242.1 NP_150243.2 NP_150247.2 NP_150249.1 NP_150250.2 NP_150252.1 NP_150253.2
UniGene	Hs.526464
PDB	1BOR 2MVW
PDBsum	1BOR 2MVW
ProteinModelPortal	P29590
SMR	P29590
BioGrid	111384
IntAct	P29590
MINT	MINT-158826
STRING	9606.ENSP00000268058
PhosphoSite	P29590
DMDM	215274219
MaxQB	P29590
PaxDb	P29590
PRIDE	P29590
DNASU	5371
Ensembl	ENST00000268058 ENST00000268059 ENST00000354026 ENST00000359928 ENST00000395132 ENST00000395135 ENST00000435786 ENST00000436891 ENST00000564428 ENST00000565898 ENST00000567543 ENST00000569477 ENST00000569965
GeneID	5371
KEGG	hsa:5371
UCSC	uc002awk.3 uc002awl.3 uc002awm.3 uc002awn.3 uc002awo.3 uc002awr.3 uc002aws.3 uc002awu.3 uc002awv.3
CTD	5371
GeneCards	GC15P074287
HGNC	HGNC:9113
HPA	CAB010194 CAB016304 HPA008312
MIM	102578
neXtProt	NX_P29590
Orphanet	520
PharmGKB	PA33439
eggNOG	NOG326718
GeneTree	ENSGT00510000048454
HOVERGEN	HBG000552
InParanoid	P29590
KO	K10054
OMA	CLPAVEP
OrthoDB	EOG7M98FM
PhylomeDB	P29590
TreeFam	TF336434
Reactome	REACT_25078
SignaLink	P29590
ChiTaRS	PML
EvolutionaryTrace	P29590
GeneWiki	Promyelocytic_leukemia_protein
GenomeRNAi	5371
NextBio	20820
PMAP-CutDB	P29590
PRO	PR:P29590
Proteomes	UP000005640
Bgee	P29590
CleanEx	HS_PML
ExpressionAtlas	P29590
Genevestigator	P29590
GO	GO:0005737 GO:0005829 GO:0031901 GO:0042406 GO:0016363 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0016605 GO:0050897 GO:0003677 GO:0046982 GO:0042803 GO:0032183 GO:0003713 GO:0031625 GO:0008270 GO:0006919 GO:0006915 GO:0060444 GO:0007050 GO:0045165 GO:0071353 GO:0090398 GO:0032922 GO:0007182 GO:0019221 GO:0051607 GO:0006977 GO:0032469 GO:0043153 GO:0097191 GO:0045087 GO:0060333 GO:0008630 GO:0042771 GO:0070059 GO:0008631 GO:0051457 GO:0030099 GO:0016525 GO:0030308 GO:0008285 GO:0045930 GO:2000059 GO:0051974 GO:0032211 GO:0045892 GO:0032938 GO:1902187 GO:0030578 GO:0060058 GO:0002230 GO:2001238 GO:0031065 GO:0043161 GO:0006461 GO:0050821 GO:0006605 GO:0010522 GO:0042752 GO:2000779 GO:0045343 GO:0001932 GO:0006355 GO:0034097 GO:0010332 GO:0001666 GO:0009411 GO:0048384 GO:0007184 GO:0006351 GO:0007179 GO:0016032
Gene3D	3.30.40.10
InterPro	IPR021978 IPR000315 IPR001841 IPR013083 IPR017907
Pfam	PF12126 PF00643
SMART	SM00336 SM00184
PROSITE	PS50119 PS00518 PS50089

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0051607	defense response to virus	PMID:24407287^[1]	ECO:0000314			P		Figure 5: With a PML deficiency, induction of IL-1β by HSV-1 was markedly enhanced which may lead to inflammation.	complete CACAO 9431
enables	GO:0032183	SUMO binding	PMID:17081986^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P61956	F		Seeded From UniProt	complete
involved_in	GO:0032206	positive regulation of telomere maintenance	PMID:26119943^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:26119943^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0090399)	Seeded From UniProt	complete
involved_in	GO:1902187	negative regulation of viral release from host cell	PMID:18248090^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:18248090^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:17081986^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63165	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9230084^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P29590	F		Seeded From UniProt	complete
involved_in	GO:0034097	response to cytokine	PMID:9412458^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:9412458^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:12006491^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9412458^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	PMID:21803845^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000779	regulation of double-strand break repair	PMID:21639834^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000059	negative regulation of ubiquitin-dependent protein catabolic process	PMID:15195100^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	PMID:22117195^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	PMID:22002537^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	PMID:23431171^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:22406621^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043153	entrainment of circadian clock by photoperiod	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0042771	intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
part_of	GO:0042406	extrinsic component of endoplasmic reticulum membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	C		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0032469	endoplasmic reticulum calcium ion homeostasis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:17081985^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63165	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:12915590^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00987	F		Seeded From UniProt	complete
involved_in	GO:0030578	PML body organization	PMID:17081985^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:15195100^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:23431171^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:22155184^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:23007646^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:22869143^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:11331580^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:17081985^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0016605	PML body	PMID:10910364^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016525	negative regulation of angiogenesis	PMID:16915281^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010522	regulation of calcium ion transport into cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:12915590^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:23007646^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:18298799^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:15195100^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:12915590^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22274616^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001932	regulation of protein phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q60953	P		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	PMID:16915281^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902187	negative regulation of viral release from host cell	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290	F		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002379290 UniProtKB:P29590	F		Seeded From UniProt	complete
involved_in	GO:0030578	PML body organization	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	C		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104662 PANTHER:PTN002379290 UniProtKB:P29590	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002379290 UniProtKB:P29590	C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002379290 UniProtKB:P29590	F		Seeded From UniProt	complete
involved_in	GO:0051457	maintenance of protein location in nucleus	PMID:17332504^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:12917339^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003713	P		Seeded From UniProt	complete
involved_in	GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0060444	branching involved in mammary gland duct morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0050713	negative regulation of interleukin-1 beta secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0050711	negative regulation of interleukin-1 secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0048384	retinoic acid receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0048146	positive regulation of fibroblast proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	F		Seeded From UniProt	complete
involved_in	GO:0045165	cell fate commitment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0043153	entrainment of circadian clock by photoperiod	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0042771	intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
part_of	GO:0042406	extrinsic component of endoplasmic reticulum membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0032469	endoplasmic reticulum calcium ion homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0030578	PML body organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0030155	regulation of cell adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0030099	myeloid cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
involved_in	GO:0016525	negative regulation of angiogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
involved_in	GO:0010761	fibroblast migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0010522	regulation of calcium ion transport into cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0010332	response to gamma radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0009411	response to UV	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0008631	intrinsic apoptotic signaling pathway in response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0007569	cell aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0007182	common-partner SMAD protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0006606	protein import into nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
involved_in	GO:0001932	regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
part_of	GO:0000792	heterochromatin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	C		Seeded From UniProt	complete
involved_in	GO:2001235	positive regulation of apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:1990830	cellular response to leukemia inhibitory factor	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:1902187	negative regulation of viral release from host cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0072332	intrinsic apoptotic signaling pathway by p53 class mediator	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
involved_in	GO:0071353	cellular response to interleukin-4	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q60953 ensembl:ENSMUSP00000082816	P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000315	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9885291^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002230	positive regulation of defense response to virus by host	PMID:16873256^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:7935403^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045930	negative regulation of mitotic cell cycle	PMID:9395203^[33]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:7935403^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030578	PML body organization	PMID:10779416^[34]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:9583681^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:9395203^[33]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:7935403^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:9583681^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9583681^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9294197^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0050897	cobalt ion binding	PMID:7729428^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:22002537^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030578	PML body organization	PMID:8643677^[38]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:9885291^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:7729428^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002230	positive regulation of defense response to virus by host	PMID:16873257^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904816	positive regulation of protein localization to chromosome, telomeric region	PMID:22641345^[40]	ECO:0000314	direct assay evidence used in manual assertion		P	transports_or_maintains_localization_of:(UniProtKB:Q06609)	Seeded From UniProt	complete
involved_in	GO:0032206	positive regulation of telomere maintenance	PMID:22641345^[40]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060058	positive regulation of apoptotic process involved in mammary gland involution	PMID:11080164^[41]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:12773567^[42]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:11259576^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032938	negative regulation of translation in response to oxidative stress	PMID:16915281^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031065	positive regulation of histone deacetylation	PMID:11259576^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:9448006^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	PMID:11080164^[41]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:12402044^[44]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:12773567^[42]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006605	protein targeting	PMID:15195100^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006605	protein targeting	PMID:11080164^[41]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:16778193^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:11080164^[41]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:15626733^[45]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051974	negative regulation of telomerase activity	PMID:19567472^[46]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	PMID:19567472^[46]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003713	P		Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003713	P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:9230084^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060333	interferon-gamma-mediated signaling pathway	Reactome:R-HSA-877300	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-1031716	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-8938887 Reactome:R-HSA-6805638 Reactome:R-HSA-6805620 Reactome:R-HSA-5228508 Reactome:R-HSA-3000434 Reactome:R-HSA-3000433 Reactome:R-HSA-3000411 Reactome:R-HSA-3000383 Reactome:R-HSA-1031716	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0967	C		Seeded From UniProt	complete
part_of	GO:0031901	early endosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0093	C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0465	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Dowling, JK et al. (2014) Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation. J. Biol. Chem. 289 6429-37 PubMed GONUTS page
↑ ^2.0 ^2.1 Lin, DY et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 341-54 PubMed GONUTS page
↑ ^3.0 ^3.1 Marchesini, M et al. (2016) PML is required for telomere stability in non-neoplastic human cells. Oncogene 35 1811-21 PubMed GONUTS page
↑ ^4.0 ^4.1 Uchil, PD et al. (2008) TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog. 4 e16 PubMed GONUTS page
↑ ^5.0 ^5.1 Sternsdorf, T et al. (1997) Cellular localization, expression, and structure of the nuclear dot protein 52. J. Cell Biol. 138 435-48 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Sternsdorf, T et al. (1997) Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139 1621-34 PubMed GONUTS page
↑ Langley, E et al. (2002) Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21 2383-96 PubMed GONUTS page
↑ Tao, RH et al. (2011) PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo. Blood 118 3107-18 PubMed GONUTS page
↑ Liu, J et al. (2011) Promyelocytic leukemia protein interacts with werner syndrome helicase and regulates double-strand break repair in γ-irradiation-induced DNA damage responses. Biochemistry Mosc. 76 550-4 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Bernardi, R et al. (2004) PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nat. Cell Biol. 6 665-72 PubMed GONUTS page
↑ Peche, LY et al. (2012) MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs. Cell Death Differ. 19 926-36 PubMed GONUTS page
↑ ^12.0 ^12.1 Martin, N et al. (2012) Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence. EMBO J. 31 95-109 PubMed GONUTS page
↑ ^13.0 ^13.1 Rokudai, S et al. (2013) MOZ increases p53 acetylation and premature senescence through its complex formation with PML. Proc. Natl. Acad. Sci. U.S.A. 110 3895-900 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Alcalay, M et al. (1998) The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell. Biol. 18 1084-93 PubMed GONUTS page
↑ Rabellino, A et al. (2012) The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA. Cancer Res. 72 2275-84 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Shen, TH et al. (2006) The mechanisms of PML-nuclear body formation. Mol. Cell 24 331-9 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Kurki, S et al. (2003) Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J. Cell. Sci. 116 3917-25 PubMed GONUTS page
↑ Satow, R et al. (2012) β-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells. Gastroenterology 142 572-81 PubMed GONUTS page
↑ ^19.0 ^19.1 Ulbricht, T et al. (2012) PML promotes MHC class II gene expression by stabilizing the class II transactivator. J. Cell Biol. 199 49-63 PubMed GONUTS page
↑ Yang, Q et al. (2013) BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction. Oncogene 32 3156-64 PubMed GONUTS page
↑ Reymond, A et al. (2001) The tripartite motif family identifies cell compartments. EMBO J. 20 2140-51 PubMed GONUTS page
↑ Pearson, M et al. (2000) PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406 207-10 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Bernardi, R et al. (2006) PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442 779-85 PubMed GONUTS page
↑ Shimada, N et al. (2008) Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells 13 245-54 PubMed GONUTS page
↑ Miki, T et al. (2012) PML regulates PER2 nuclear localization and circadian function. EMBO J. 31 1427-39 PubMed GONUTS page
↑ ^26.00 ^26.01 ^26.02 ^26.03 ^26.04 ^26.05 ^26.06 ^26.07 ^26.08 ^26.09 ^26.10 ^26.11 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Takahashi, K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol. Biol. Cell 18 1701-9 PubMed GONUTS page
↑ Kawai, T et al. (2003) ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol. Cell. Biol. 23 6174-86 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 ^29.6 ^29.7 Condemine, W et al. (2006) Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66 6192-8 PubMed GONUTS page
↑ ^30.0 ^30.1 Duprez, E et al. (1999) SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J. Cell. Sci. 112 ( Pt 3) 381-93 PubMed GONUTS page
↑ Everett, RD et al. (2006) PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80 7995-8005 PubMed GONUTS page
↑ ^32.0 ^32.1 ^32.2 Mu, ZM et al. (1994) PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14 6858-67 PubMed GONUTS page
↑ ^33.0 ^33.1 Mu, ZM et al. (1997) Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells. Carcinogenesis 18 2063-9 PubMed GONUTS page
↑ Zhong, S et al. (2000) Role of SUMO-1-modified PML in nuclear body formation. Blood 95 2748-52 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 Le, XF et al. (1998) Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 16 1839-49 PubMed GONUTS page
↑ Koken, MH et al. (1997) Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies. Proc. Natl. Acad. Sci. U.S.A. 94 10255-60 PubMed GONUTS page
↑ ^37.0 ^37.1 Borden, KL et al. (1995) The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 14 1532-41 PubMed GONUTS page
↑ Borden, KL et al. (1996) In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc. Natl. Acad. Sci. U.S.A. 93 1601-6 PubMed GONUTS page
↑ Tavalai, N et al. (2006) Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J. Virol. 80 8006-18 PubMed GONUTS page
↑ ^40.0 ^40.1 Hsu, JK et al. (2012) Nucleostemin prevents telomere damage by promoting PML-IV recruitment to SUMOylated TRF1. J. Cell Biol. 197 613-24 PubMed GONUTS page
↑ ^41.0 ^41.1 ^41.2 ^41.3 Fogal, V et al. (2000) Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19 6185-95 PubMed GONUTS page
↑ ^42.0 ^42.1 Xu, ZX et al. (2003) PML colocalizes with and stabilizes the DNA damage response protein TopBP1. Mol. Cell. Biol. 23 4247-56 PubMed GONUTS page
↑ ^43.0 ^43.1 Wu, WS et al. (2001) The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell. Biol. 21 2259-68 PubMed GONUTS page
↑ Yang, S et al. (2002) PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nat. Cell Biol. 4 865-70 PubMed GONUTS page
↑ Salomoni, P et al. (2005) The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage. Blood 105 3686-90 PubMed GONUTS page
↑ ^46.0 ^46.1 Oh, W et al. (2009) PML-IV functions as a negative regulator of telomerase by interacting with TERT. J. Cell. Sci. 122 2613-22 PubMed GONUTS page

[PMID:24407287-1] Dowling, JK et al. (2014) Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation. J. Biol. Chem. 289 6429-37 PubMed GONUTS page

[PMID:17081986-2] 2.0 ^2.1 Lin, DY et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 341-54 PubMed GONUTS page

[PMID:26119943-3] 3.0 ^3.1 Marchesini, M et al. (2016) PML is required for telomere stability in non-neoplastic human cells. Oncogene 35 1811-21 PubMed GONUTS page

[PMID:18248090-4] 4.0 ^4.1 Uchil, PD et al. (2008) TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog. 4 e16 PubMed GONUTS page

[PMID:9230084-5] 5.0 ^5.1 Sternsdorf, T et al. (1997) Cellular localization, expression, and structure of the nuclear dot protein 52. J. Cell Biol. 138 435-48 PubMed GONUTS page

[PMID:9412458-6] 6.0 ^6.1 ^6.2 Sternsdorf, T et al. (1997) Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139 1621-34 PubMed GONUTS page

[PMID:12006491-7] Langley, E et al. (2002) Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21 2383-96 PubMed GONUTS page

[PMID:21803845-8] Tao, RH et al. (2011) PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo. Blood 118 3107-18 PubMed GONUTS page

[PMID:21639834-9] Liu, J et al. (2011) Promyelocytic leukemia protein interacts with werner syndrome helicase and regulates double-strand break repair in γ-irradiation-induced DNA damage responses. Biochemistry Mosc. 76 550-4 PubMed GONUTS page

[PMID:15195100-10] 10.0 ^10.1 ^10.2 ^10.3 Bernardi, R et al. (2004) PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nat. Cell Biol. 6 665-72 PubMed GONUTS page

[PMID:22117195-11] Peche, LY et al. (2012) MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs. Cell Death Differ. 19 926-36 PubMed GONUTS page

[PMID:22002537-12] 12.0 ^12.1 Martin, N et al. (2012) Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence. EMBO J. 31 95-109 PubMed GONUTS page

[PMID:23431171-13] 13.0 ^13.1 Rokudai, S et al. (2013) MOZ increases p53 acetylation and premature senescence through its complex formation with PML. Proc. Natl. Acad. Sci. U.S.A. 110 3895-900 PubMed GONUTS page

[PMID:9448006-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Alcalay, M et al. (1998) The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell. Biol. 18 1084-93 PubMed GONUTS page

[PMID:22406621-15] Rabellino, A et al. (2012) The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA. Cancer Res. 72 2275-84 PubMed GONUTS page

[PMID:17081985-16] 16.0 ^16.1 ^16.2 Shen, TH et al. (2006) The mechanisms of PML-nuclear body formation. Mol. Cell 24 331-9 PubMed GONUTS page

[PMID:12915590-17] 17.0 ^17.1 ^17.2 Kurki, S et al. (2003) Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J. Cell. Sci. 116 3917-25 PubMed GONUTS page

[PMID:22155184-18] Satow, R et al. (2012) β-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells. Gastroenterology 142 572-81 PubMed GONUTS page

[PMID:23007646-19] 19.0 ^19.1 Ulbricht, T et al. (2012) PML promotes MHC class II gene expression by stabilizing the class II transactivator. J. Cell Biol. 199 49-63 PubMed GONUTS page

[PMID:22869143-20] Yang, Q et al. (2013) BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction. Oncogene 32 3156-64 PubMed GONUTS page

[PMID:11331580-21] Reymond, A et al. (2001) The tripartite motif family identifies cell compartments. EMBO J. 20 2140-51 PubMed GONUTS page

[PMID:10910364-22] Pearson, M et al. (2000) PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406 207-10 PubMed GONUTS page

[PMID:16915281-23] 23.0 ^23.1 ^23.2 Bernardi, R et al. (2006) PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442 779-85 PubMed GONUTS page

[PMID:18298799-24] Shimada, N et al. (2008) Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells 13 245-54 PubMed GONUTS page

[PMID:22274616-25] Miki, T et al. (2012) PML regulates PER2 nuclear localization and circadian function. EMBO J. 31 1427-39 PubMed GONUTS page

[PMID:21873635-26] 26.00 ^26.01 ^26.02 ^26.03 ^26.04 ^26.05 ^26.06 ^26.07 ^26.08 ^26.09 ^26.10 ^26.11 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:17332504-27] Takahashi, K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol. Biol. Cell 18 1701-9 PubMed GONUTS page

[PMID:12917339-28] Kawai, T et al. (2003) ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol. Cell. Biol. 23 6174-86 PubMed GONUTS page

[PMID:16778193-29] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 ^29.6 ^29.7 Condemine, W et al. (2006) Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66 6192-8 PubMed GONUTS page

[PMID:9885291-30] 30.0 ^30.1 Duprez, E et al. (1999) SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J. Cell. Sci. 112 ( Pt 3) 381-93 PubMed GONUTS page

[PMID:16873256-31] Everett, RD et al. (2006) PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80 7995-8005 PubMed GONUTS page

[PMID:7935403-32] 32.0 ^32.1 ^32.2 Mu, ZM et al. (1994) PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14 6858-67 PubMed GONUTS page

[PMID:9395203-33] 33.0 ^33.1 Mu, ZM et al. (1997) Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells. Carcinogenesis 18 2063-9 PubMed GONUTS page

[PMID:10779416-34] Zhong, S et al. (2000) Role of SUMO-1-modified PML in nuclear body formation. Blood 95 2748-52 PubMed GONUTS page

[PMID:9583681-35] 35.0 ^35.1 ^35.2 Le, XF et al. (1998) Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 16 1839-49 PubMed GONUTS page

[PMID:9294197-36] Koken, MH et al. (1997) Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies. Proc. Natl. Acad. Sci. U.S.A. 94 10255-60 PubMed GONUTS page

[PMID:7729428-37] 37.0 ^37.1 Borden, KL et al. (1995) The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 14 1532-41 PubMed GONUTS page

[PMID:8643677-38] Borden, KL et al. (1996) In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc. Natl. Acad. Sci. U.S.A. 93 1601-6 PubMed GONUTS page

[PMID:16873257-39] Tavalai, N et al. (2006) Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J. Virol. 80 8006-18 PubMed GONUTS page

[PMID:22641345-40] 40.0 ^40.1 Hsu, JK et al. (2012) Nucleostemin prevents telomere damage by promoting PML-IV recruitment to SUMOylated TRF1. J. Cell Biol. 197 613-24 PubMed GONUTS page

[PMID:11080164-41] 41.0 ^41.1 ^41.2 ^41.3 Fogal, V et al. (2000) Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19 6185-95 PubMed GONUTS page

[PMID:12773567-42] 42.0 ^42.1 Xu, ZX et al. (2003) PML colocalizes with and stabilizes the DNA damage response protein TopBP1. Mol. Cell. Biol. 23 4247-56 PubMed GONUTS page

[PMID:11259576-43] 43.0 ^43.1 Wu, WS et al. (2001) The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell. Biol. 21 2259-68 PubMed GONUTS page

[PMID:12402044-44] Yang, S et al. (2002) PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nat. Cell Biol. 4 865-70 PubMed GONUTS page

[PMID:15626733-45] Salomoni, P et al. (2005) The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage. Blood 105 3686-90 PubMed GONUTS page

[PMID:19567472-46] 46.0 ^46.1 Oh, W et al. (2009) PML-IV functions as a negative regulator of telomerase by interacting with TERT. J. Cell. Sci. 122 2613-22 PubMed GONUTS page

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