PML
entrez
5371
canonical
uniprot
P29590
canonical
ensembl
ENSG00000140464
resolver
ensp
ENSP00000268058
resolver
ensp
ENSP00000268059
resolver
ensp
ENSP00000315434
resolver
ensp
ENSP00000353004
resolver
ensp
ENSP00000378564
resolver
ensp
ENSP00000378567
resolver
ensp
ENSP00000394642
resolver
ensp
ENSP00000395576
resolver
ensp
ENSP00000457023
resolver
genesymbol
PML
resolver
genesymbol_syn
MYL
resolver
genesymbol_syn
PP8675
resolver
genesymbol_syn
RNF71
resolver
genesymbol_syn
TRIM19
resolver
hgnc
HGNC:9113
resolver
uniprot
E9PBR7
resolver
uniprot
P29591
resolver
uniprot
P29592
resolver
uniprot
P29593
resolver
uniprot
Q00755
resolver
uniprot
Q15959
resolver
uniprot
Q59FP9
resolver
uniprot
Q8WUA0
resolver
uniprot
Q96S41
resolver
uniprot
Q9BPW2
resolver
uniprot
Q9BWP7
resolver
uniprot
Q9BZX6
resolver
uniprot
Q9BZX7
resolver
uniprot
Q9BZX8
resolver
uniprot
Q9BZX9
resolver
uniprot
Q9BZY0
resolver
uniprot
Q9BZY2
resolver
uniprot
Q9BZY3
resolver
uniprot_entry
PML_HUMAN
resolver
uniprot_sec
E9PBR7
resolver
uniprot_sec
P29591
resolver
uniprot_sec
P29592
resolver
uniprot_sec
P29593
resolver
uniprot_sec
Q00755
resolver
uniprot_sec
Q15959
resolver
uniprot_sec
Q59FP9
resolver
uniprot_sec
Q8WUA0
resolver
uniprot_sec
Q96S41
resolver
uniprot_sec
Q9BPW2
resolver
uniprot_sec
Q9BWP7
resolver
uniprot_sec
Q9BZX6
resolver
uniprot_sec
Q9BZX7
resolver
uniprot_sec
Q9BZX8
resolver
uniprot_sec
Q9BZX9
resolver
uniprot_sec
Q9BZY0
resolver
uniprot_sec
Q9BZY2
resolver
uniprot_sec
Q9BZY3
resolver
amino_acid_sequence
MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon. {ECO:0000269|PubMed:1652369, ECO:0000269|PubMed:1720570}.
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
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. Inhibits EIF4E-mediated mRNA nuclear export by reducing EIF4E affinity for the 5' 7-methylguanosine (m7G) cap of target mRNAs (PubMed:11500381, PubMed:11575918, PubMed:18391071). 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- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration. {ECO:0000269|PubMed:11500381, ECO:0000269|PubMed:11575918, ECO:0000269|PubMed:18391071}.; FUNCTION: 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 (HHV-5) 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. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response (PubMed:20972456, PubMed:28250117). Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity (PubMed:20972456, PubMed:28250117). {ECO:0000269|PubMed:20972456, ECO:0000269|PubMed:28250117}.
uniprot
proteins
mass_dalton
97551
uniprot
proteins
mutagenesis
MUTAGEN 57; /note="C->S: Strongly reduced sumoylation; when associated with S-60."; /evidence="ECO:0000269|PubMed:17081985"; MUTAGEN 60; /note="C->S: Strongly reduced sumoylation; when associated with S-57."; /evidence="ECO:0000269|PubMed:17081985"; MUTAGEN 65; /note="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. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-160 and R-490."; /evidence="ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9756909"; MUTAGEN 65; /note="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."; /evidence="ECO:0000269|PubMed:9756909"; MUTAGEN 68; /note="K->R: No effect on sumoylation levels."; MUTAGEN 88; /note="C->S: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89."; /evidence="ECO:0000269|PubMed:15809060"; MUTAGEN 89; /note="P->R: No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88."; /evidence="ECO:0000269|PubMed:15809060"; MUTAGEN 133; /note="K->R: Loss of 2 sumoylations; when associated with R-65 and R-490."; /evidence="ECO:0000269|PubMed:9756909"; MUTAGEN 150; /note="K->R: Loss of 2 sumoylations; when associated with R-65 and R-490."; /evidence="ECO:0000269|PubMed:9756909"; MUTAGEN 160; /note="K->R: Compromised the formation of high molecular weight species of SUMO1P1/SUMO5 conjugation on PML. Loss of 2 sumoylations; when associated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-490."; /evidence="ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9756909"; MUTAGEN 160; /note="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."; /evidence="ECO:0000269|PubMed:9756909"; MUTAGEN 380; /note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."; /evidence="ECO:0000269|PubMed:27211601"; MUTAGEN 400; /note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."; /evidence="ECO:0000269|PubMed:27211601"; MUTAGEN 430; /note="Q->A: Loss of cleavage by enterovirus 71 protease 3C."; /evidence="ECO:0000269|PubMed:34930370"; MUTAGEN 444; /note="Q->A: Loss of cleavage by enterovirus 71 protease 3C."; /evidence="ECO:0000269|PubMed:34930370"; MUTAGEN 487; /note="K->A: Loss of nuclear localization; when associated with A-490."; /evidence="ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:18621739"; MUTAGEN 487; /note="K->R: Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515."; /evidence="ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:18621739"; MUTAGEN 490; /note="K->A: Loss of nuclear localization; when associated with A-487."; /evidence="ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:9756909"; MUTAGEN 490; /note="K->R: Abolished conjugation of one SUMO1P1/SUMO5. Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-160."; /evidence="ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9756909"; MUTAGEN 490; /note="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."; /evidence="ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:9756909"; MUTAGEN 497; /note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."; /evidence="ECO:0000269|PubMed:27211601"; MUTAGEN 515; /note="K->R: Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487."; /evidence="ECO:0000269|PubMed:18621739"; MUTAGEN 518; /note="S->A: Abolishes ubiquitination by the BCR(KLHL20) E3 ubiquitin ligase complex."; /evidence="ECO:0000269|PubMed:21840486"; MUTAGEN 556..559; /note="VVVI->AAAS: Abolishes SUMO1 binding.
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:20972456, ECO:0000269|PubMed:28250117}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; mediated by RNF4, RNF111, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation (PubMed:18408734, PubMed:21840486, PubMed:22033920). Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-518 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20 (PubMed:21840486, PubMed:22033920). 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent (PubMed:18408734). Ubiquitination by RNF111 is polysumoylation-dependent (By similarity). {ECO:0000250|UniProtKB:Q60953, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22033920}.; PTM: Sumoylation regulates PML's: stability in response to extracellular or intracellular stimuli, transcription directly and indirectly, through sequestration of or dissociation of the transcription factors from PML-NBs, ability to regulate apoptosis and its anti-viral activities. It is also essential for: maintaining proper PML nuclear bodies (PML-NBs) structure and normal function, recruitment of components of PML-NBs, the turnover and retention of PML in PML-NBs and the integrity of PML-NBs. Undergoes 'Lys-11'-linked sumoylation. Sumoylation on all three sites (Lys-65, Lys-160 and Lys-490) is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. Lys-65 and Lys-160 are sumoylated by PISA1 and PIAS2. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-565 which in turn triggers its ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML-RARA promotes its ubiquitin-mediated degradation. The PML-RARA fusion protein requires the coiled-coil domain for sumoylation. Sumoylation at Lys-490 by RANBP2 is essential for the proper assembly of PML-NBs. SUMO1P1/SUMO5 conjugated PML at Lys-160, Lys-380, Lys-400, Lys-490 and Lys-497, but Lys-380, Lys-400 and Lys-497 are not key acceptor lysines. SUMO1P1/SUMO5 forms polymeric chain on Lys-160 of PML by successive conjugation at 'Lys-18'; facilitating recruitment of PML-NB components, which enlarges PML. SUMO1P1/SUMO5 conjugation of PML increases SUMO2/3 conjugation, which leads to the recruitment of RNF4 and ubiquitin-dependent disintegration of PML-NBs. SUMO1P1/SUMO5 monoconjugated Lys-490 (PubMed:27211601). DNA damage triggers its sumoylation while some but not all viral infections can abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 (PubMed:12419228, PubMed:21148299, PubMed:27211601). 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. {ECO:0000269|PubMed:12419228, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:21148299, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9756909}.; PTM: 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 (PubMed:15195100). 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 (PubMed:19015637). CHEK2-mediated phosphorylation at Ser-117 is important for PML-mediated apoptosis following DNA damage (PubMed:12402044). 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 (PubMed:21840486, PubMed:22033920). CK2-mediated phosphorylation at Ser-565 primes PML ubiquitination via an unidentified ubiquitin ligase (PubMed:20719947, PubMed:22406621). {ECO:0000269|PubMed:12402044, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:19015637, ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22033920, ECO:0000269|PubMed:22406621}.; PTM: (Microbial infection) Upon infection with Epstein-Barr virus, phosphorylated by CK2. Viral EBNA1 increases the association of CK2 with PML proteins, which increases PML phosphorylation by CK2, triggering the USP7-dependent polyubiquitylation and degradation of PML. {ECO:0000269|PubMed:20719947}.; PTM: 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. {ECO:0000269|PubMed:18621739, ECO:0000269|PubMed:22274616}.; PTM: (Microbial infection) Immediate early protein IE1 of human cytomegalovirus (HHV-5) interferes with the sumoylation of PML (PubMed:10233977, PubMed:15163746, PubMed:27903803). Immediate early protein IE1 inhibits PML de novo sumoylation (PubMed:27903803). {ECO:0000269|PubMed:10233977, ECO:0000269|PubMed:15163746, ECO:0000269|PubMed:27903803}.; PTM: (Microbial infection) Cleaved at two different sites by enterovirus 71 protease 3C, leading to impaired PML-Nuclear bodies formation. {ECO:0000269|PubMed:34930370}.
uniprot
proteins
pubmed
10233977
uniprot
proteins
pubmed
10610177
uniprot
proteins
pubmed
10669754
uniprot
proteins
pubmed
10684855
uniprot
proteins
pubmed
10779416
uniprot
proteins
pubmed
11025664
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
11432836
uniprot
proteins
pubmed
11500381
uniprot
proteins
pubmed
11575918
uniprot
proteins
pubmed
11704850
uniprot
proteins
pubmed
12006491
uniprot
proteins
pubmed
12402044
uniprot
proteins
pubmed
12419228
uniprot
proteins
pubmed
12439746
uniprot
proteins
pubmed
12691149
uniprot
proteins
pubmed
12773567
uniprot
proteins
pubmed
12810724
uniprot
proteins
pubmed
1311253
uniprot
proteins
pubmed
1312695
uniprot
proteins
pubmed
14645235
uniprot
proteins
pubmed
14976184
uniprot
proteins
pubmed
15136035
uniprot
proteins
pubmed
15163746
uniprot
proteins
pubmed
15195100
uniprot
proteins
pubmed
15356634
uniprot
proteins
pubmed
15467728
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15809060
uniprot
proteins
pubmed
1652368
uniprot
proteins
pubmed
1652369
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16778193
uniprot
proteins
pubmed
16912307
uniprot
proteins
pubmed
17030982
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17081985
uniprot
proteins
pubmed
17173041
uniprot
proteins
pubmed
1720570
uniprot
proteins
pubmed
17942542
uniprot
proteins
pubmed
18298799
uniprot
proteins
pubmed
18391071
uniprot
proteins
pubmed
18408734
uniprot
proteins
pubmed
18509536
uniprot
proteins
pubmed
18621739
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18716620
uniprot
proteins
pubmed
19015637
uniprot
proteins
pubmed
19567472
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19703418
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20378816
uniprot
proteins
pubmed
20501696
uniprot
proteins
pubmed
20625391
uniprot
proteins
pubmed
20639899
uniprot
proteins
pubmed
20702643
uniprot
proteins
pubmed
20719947
uniprot
proteins
pubmed
20943951
uniprot
proteins
pubmed
20972456
uniprot
proteins
pubmed
21148299
uniprot
proteins
pubmed
21161613
uniprot
proteins
pubmed
21172801
uniprot
proteins
pubmed
21198351
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21304940
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21475307
uniprot
proteins
pubmed
21501958
uniprot
proteins
pubmed
21639834
uniprot
proteins
pubmed
21840486
uniprot
proteins
pubmed
21994459
uniprot
proteins
pubmed
22002537
uniprot
proteins
pubmed
22033920
uniprot
proteins
pubmed
22117195
uniprot
proteins
pubmed
22155184
uniprot
proteins
pubmed
22237204
uniprot
proteins
pubmed
22274616
uniprot
proteins
pubmed
22406621
uniprot
proteins
pubmed
22589541
uniprot
proteins
pubmed
22629402
uniprot
proteins
pubmed
22685230
uniprot
proteins
pubmed
22773875
uniprot
proteins
pubmed
22869143
uniprot
proteins
pubmed
22875967
uniprot
proteins
pubmed
22886304
uniprot
proteins
pubmed
22935031
uniprot
proteins
pubmed
22945642
uniprot
proteins
pubmed
23007646
uniprot
proteins
pubmed
23028697
uniprot
proteins
pubmed
23135708
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23219818
uniprot
proteins
pubmed
23316480
uniprot
proteins
pubmed
23430110
uniprot
proteins
pubmed
23431171
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772236
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27211601
uniprot
proteins
pubmed
27903803
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28250117
uniprot
proteins
pubmed
28842558
uniprot
proteins
pubmed
34930370
uniprot
proteins
pubmed
36373674
uniprot
proteins
pubmed
7729428
uniprot
proteins
pubmed
9420283
uniprot
proteins
pubmed
9570750
uniprot
proteins
pubmed
9756909
uniprot
proteins
sequence_length
882
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm. Cytoplasm {ECO:0000269|PubMed:27211601}. Nucleus, PML body {ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:36373674}. Nucleus, nucleolus. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. 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.
uniprot
proteins