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Protein PML

 PML_MOUSE               Reviewed;         885 AA.
Q60953; Q8CEJ1; Q8VCC4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 3.
30-AUG-2017, entry version 175.
RecName: Full=Protein PML;
Name=Pml;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-839 (ISOFORM 2).
PubMed=8563172; DOI=10.1007/BF00354296;
Goddard A.D., Yuan J.Q., Fairbairn L., Dexter M., Borrow J., Kozak C.,
Solomon E.;
"Cloning of the murine homolog of the leukemia-associated PML gene.";
Mamm. Genome 6:732-737(1995).
[4]
SEQUENCE REVISION TO 130; 212; 284; 638; 731; 750; 770-772; 820 AND
839.
Goddard A.D., Howe K., Solomon E.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9806545; DOI=10.1038/3073;
Wang Z.G., Ruggero D., Ronchetti S., Zhong S., Gaboli M., Rivi R.,
Pandolfi P.P.;
"PML is essential for multiple apoptotic pathways.";
Nat. Genet. 20:266-272(1998).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9488655; DOI=10.1126/science.279.5356.1547;
Wang Z.G., Delva L., Gaboli M., Rivi R., Giorgio M., Cordon-Cardo C.,
Grosveld F., Pandolfi P.P.;
"Role of PML in cell growth and the retinoic acid pathway.";
Science 279:1547-1551(1998).
[7]
FUNCTION.
PubMed=10637504; DOI=10.1038/sj.onc.1203367;
Zhong S., Hu P., Ye T.Z., Stan R., Ellis N.A., Pandolfi P.P.;
"A role for PML and the nuclear body in genomic stability.";
Oncogene 18:7941-7947(1999).
[8]
SUMOYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=10779416;
Zhong S., Muller S., Ronchetti S., Freemont P.S., Dejean A.,
Pandolfi P.P.;
"Role of SUMO-1-modified PML in nuclear body formation.";
Blood 95:2748-2752(2000).
[9]
FUNCTION IN LCMV AND VSV RESTRICTION.
PubMed=11907221; DOI=10.1128/JVI.76.8.3810-3818.2002;
Bonilla W.V., Pinschewer D.D., Klenerman P., Rousson V., Gaboli M.,
Pandolfi P.P., Zinkernagel R.M., Salvato M.S., Hengartner H.;
"Effects of promyelocytic leukemia protein on virus-host balance.";
J. Virol. 76:3810-3818(2002).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12439746; DOI=10.1038/sj.onc.1205931;
Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P.,
De The H., Chelbi-Alix M.K.;
"Rabies virus P and small P products interact directly with PML and
reorganize PML nuclear bodies.";
Oncogene 21:7957-7970(2002).
[11]
INTERACTION WITH TRIM69.
PubMed=12837286; DOI=10.1016/S0014-4827(03)00110-1;
Shyu H.-W., Hsu S.-H., Hsieh-Li H.-M., Li H.;
"Forced expression of RNF36 induces cell apoptosis.";
Exp. Cell Res. 287:301-313(2003).
[12]
FUNCTION.
PubMed=14976551; DOI=10.1038/sj.emboj.7600109;
Insinga A., Monestiroli S., Ronzoni S., Carbone R., Pearson M.,
Pruneri G., Viale G., Appella E., Pelicci P., Minucci S.;
"Impairment of p53 acetylation, stability and function by an oncogenic
transcription factor.";
EMBO J. 23:1144-1154(2004).
[13]
INTERACTION WITH SIAH2, AND DEGRADATION.
PubMed=14645235; DOI=10.1074/jbc.M306407200;
Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S.,
Lazar M.A., Pelicci P.G., Minucci S.;
"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.";
J. Biol. Chem. 279:5374-5379(2004).
[14]
FUNCTION, INTERACTION WITH MDM2 AND RPL11, AND SUBCELLULAR LOCATION.
PubMed=15195100; DOI=10.1038/ncb1147;
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H.,
Pandolfi P.P.;
"PML regulates p53 stability by sequestering Mdm2 to the nucleolus.";
Nat. Cell Biol. 6:665-672(2004).
[15]
FUNCTION.
PubMed=15356634; DOI=10.1038/nature02783;
Lin H.K., Bergmann S., Pandolfi P.P.;
"Cytoplasmic PML function in TGF-beta signalling.";
Nature 431:205-211(2004).
[16]
DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH MTOR.
PubMed=16915281; DOI=10.1038/nature05029;
Bernardi R., Guernah I., Jin D., Grisendi S., Alimonti A.,
Teruya-Feldstein J., Cordon-Cardo C., Simon M.C., Rafii S.,
Pandolfi P.P.;
"PML inhibits HIF-1alpha translation and neoangiogenesis through
repression of mTOR.";
Nature 442:779-785(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-514 AND SER-515,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[19]
REVIEW ON FUNCTION.
PubMed=19652541; DOI=10.4161/cc.8.17.9462;
Li W., Rich T., Watson C.J.;
"PML: a tumor suppressor that regulates cell fate in mammary gland.";
Cell Cycle 8:2711-2717(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[21]
DISRUPTION PHENOTYPE, INTERACTION WITH RB1, AND FUNCTION.
PubMed=19136970; DOI=10.1038/nn.2251;
Regad T., Bellodi C., Nicotera P., Salomoni P.;
"The tumor suppressor Pml regulates cell fate in the developing
neocortex.";
Nat. Neurosci. 12:132-140(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-404; SER-503;
SER-514; SER-515; SER-528; THR-535; SER-536 AND SER-609, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[23]
FUNCTION, INTERACTION WITH ITPR3, AND SUBCELLULAR LOCATION.
PubMed=21030605; DOI=10.1126/science.1189157;
Giorgi C., Ito K., Lin H.K., Santangelo C., Wieckowski M.R.,
Lebiedzinska M., Bononi A., Bonora M., Duszynski J., Bernardi R.,
Rizzuto R., Tacchetti C., Pinton P., Pandolfi P.P.;
"PML regulates apoptosis at endoplasmic reticulum by modulating
calcium release.";
Science 330:1247-1251(2010).
[24]
FUNCTION.
PubMed=21779477; DOI=10.1177/1947601911402682;
Lunardi A., Gaboli M., Giorgio M., Rivi R., Bygrave A., Antoniou M.,
Drabek D., Dzierzak E., Fagioli M., Salmena L., Botto M.,
Cordon-Cardo C., Luzzatto L., Pelicci P.G., Grosveld F.,
Pandolfi P.P.;
"A role for PML in innate immunity.";
Genes Cancer 2:10-19(2011).
[25]
FUNCTION.
PubMed=21427174; DOI=10.1093/intimm/dxr004;
Khalfin-Rabinovich Y., Weinstein A., Levi B.Z.;
"PML is a key component for the differentiation of myeloid progenitor
cells to macrophages.";
Int. Immunol. 23:287-296(2011).
[26]
REVIEW ON FUNCTION.
PubMed=21161613; DOI=10.1007/s12035-010-8156-y;
Salomoni P., Betts-Henderson J.;
"The role of PML in the nervous system.";
Mol. Neurobiol. 43:114-123(2011).
[27]
FUNCTION IN CIRCADIAN CLOCK, SUBCELLULAR LOCATION, INTERACTION WITH
PML, AND DISRUPTION PHENOTYPE.
PubMed=22274616; DOI=10.1038/emboj.2012.1;
Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A.,
Rea M.A., Zhao Z., Lee C.C., Chang K.S.;
"PML regulates PER2 nuclear localization and circadian function.";
EMBO J. 31:1427-1439(2012).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPARGC1A AND
KAT2A.
PubMed=22886304; DOI=10.1172/JCI62129;
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.;
"A metabolic prosurvival role for PML in breast cancer.";
J. Clin. Invest. 122:3088-3100(2012).
[29]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23279884; DOI=10.1111/gbb.12014;
Butler K., Martinez L.A., Tejada-Simon M.V.;
"Impaired cognitive function and reduced anxiety-related behavior in a
promyelocytic leukemia (PML) tumor suppressor protein-deficient
mouse.";
Genes Brain Behav. 12:189-202(2013).
[30]
UBIQUITINATION.
PubMed=23530056; DOI=10.1128/MCB.01019-12;
Erker Y., Neyret-Kahn H., Seeler J.S., Dejean A., Atfi A., Levy L.;
"Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML
degradation.";
Mol. Cell. Biol. 33:2163-2177(2013).
-!- 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. Positively regulates
p53/TP53 by acting at different levels (by promoting its
acetylation and phosphorylation and by inhibiting its MDM2-
dependent degradation). Regulates phosphorylation of ITPR3 and
plays a role in the regulation of calcium homeostasis at the
endoplasmic reticulum. Regulates RB1 phosphorylation and activity.
Acts as both a negative regulator of PPARGC1A acetylation and a
potent activator of PPAR signaling and fatty acid oxidation.
Regulates translation of HIF1A by sequestering MTOR, and thereby
plays a role in neoangiogenesis and tumor vascularization.
Regulates PER2 nuclear localization and circadian function.
Cytoplasmic PML is involved in the regulation of the TGF-beta
signaling pathway. Required for normal development of the brain
cortex during embryogenesis. Plays a role in granulopoiesis or
monopoiesis of myeloid progenitor cells. May play a role
regulating stem and progenitor cell fate in tissues as diverse as
blood, brain and breast. Shows antiviral activity towards
lymphocytic choriomeningitis virus (LCMV) and the vesicular
stomatitis virus (VSV). {ECO:0000269|PubMed:10637504,
ECO:0000269|PubMed:11907221, ECO:0000269|PubMed:12439746,
ECO:0000269|PubMed:14976551, ECO:0000269|PubMed:15195100,
ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:16915281,
ECO:0000269|PubMed:19136970, ECO:0000269|PubMed:21030605,
ECO:0000269|PubMed:21427174, ECO:0000269|PubMed:21779477,
ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:22886304,
ECO:0000269|PubMed:23279884, ECO:0000269|PubMed:9488655,
ECO:0000269|PubMed:9806545}.
-!- SUBUNIT: 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 TERT, SIRT1,
TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus).
Interacts with Lassa virus Z protein and rabies virus
phosphoprotein. 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 with SMAD2, SMAD3, DAXX,
RPL11, HIPK2 and MTOR. Interacts with ITPR3, PPP1A and RB1.
Interacts with RNF4, NLRP3, MAGEA2, RBL2, PER2, E2F4 and
MAPK7/BMK1. Interacts with CSNK2A1 and CSNK2A3. Interacts with
ANKRD2; the interaction is direct. Interacts with PPARGC1A AND
KAT2A. Interacts (via SUMO-interacting motif) with sumoylated
MORC3 (By similarity). {ECO:0000250|UniProtKB:P29590,
ECO:0000269|PubMed:10779416, ECO:0000269|PubMed:12837286,
ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:15195100,
ECO:0000269|PubMed:16915281, ECO:0000269|PubMed:19136970,
ECO:0000269|PubMed:21030605, ECO:0000269|PubMed:22274616,
ECO:0000269|PubMed:22886304}.
-!- INTERACTION:
Q14DJ8:Axin1; NbExp=4; IntAct=EBI-4406901, EBI-4312125;
P25446:Fas; NbExp=6; IntAct=EBI-3895605, EBI-296206;
Q8UN00:gag-pro-pol (xeno); NbExp=4; IntAct=EBI-3895605, EBI-6692904;
Q60979:Skil; NbExp=5; IntAct=EBI-3895605, EBI-7213804;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm.
Cytoplasm. Nucleus, PML body. Nucleus, nucleolus {ECO:0000250}.
Endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Early endosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Note=Detected in the nucleolus after DNA damage.
Acetylation at Lys-497 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 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q60953-1; Sequence=Displayed;
Name=2;
IsoId=Q60953-2; Sequence=VSP_026028;
-!- DOMAIN: The coiled-coil domain mediates a strong
homo/multidimerization activity essential for core assembly of
PML-NBs. {ECO:0000250}.
-!- DOMAIN: Binds arsenic via the RING-type zinc finger.
{ECO:0000250}.
-!- DOMAIN: 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.
{ECO:0000250}.
-!- PTM: Ubiquitinated; mediated by RNF4, RNF111, UHRF1, UBE3A/E6AP,
BCR(KLHL20) E3 ubiquitin ligase complex, SIAH1 or SIAH2 and
leading to subsequent proteasomal degradation. 'Lys-6'-, 'Lys-
11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is
polysumoylation-dependent (By similarity). Ubiquitination by
RNF111 is polysumoylation-dependent (PubMed:23530056).
Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex requires
CDK1/2-mediated phosphorylation at Ser-528 which in turn is
recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed
isomerization further potentiates PML interaction with KLHL20 (By
similarity). {ECO:0000250|UniProtKB:P29590,
ECO:0000269|PubMed:23530056}.
-!- 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-70, Lys-165 and Lys-500) is required for nuclear
body formation. Sumoylation on Lys-165 is a prerequisite for
sumoylation on Lys-70. Lys-70 and Lys-165 are sumoylated by PISA1
and PIAS2. PIAS1-mediated sumoylation of PML promotes its
interaction with CSNK2A1/CK2 and phosphorylation at Ser-575 which
in turn triggers its ubiquitin-mediated degradation. Sumoylation
at Lys-500 by RANBP2 is essential for the proper assembly of PML-
NBs. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 (By
similarity). {ECO:0000250|UniProtKB:P29590}.
-!- 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. HIPK2-mediated phosphorylation at Ser-17, Ser-45
and Ser-47 leads to increased accumulation of PML protein and its
sumoylation and is required for the maximal pro-apoptotic activity
of PML after DNA damage. MAPK1- mediated phosphorylations at Ser-
404, Ser-515 and Ser-540 and CDK1/2-mediated phosphorylation at
Ser-528 promote PIN1-dependent PML degradation. CK2-mediated
phosphorylation at Ser-575 primes PML ubiquitination via an
unidentified ubiquitin ligase (By similarity).
{ECO:0000250|UniProtKB:P29590}.
-!- PTM: Acetylation at Lys-497 is essential for its nuclear
localization. Deacetylated at Lys-497 by SIRT1 and this
deacetylation promotes PML control of PER2 nuclear localization
(By similarity). {ECO:0000250|UniProtKB:P29590}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate
and are fertile. They show leukopenia with reduced levels of
circulating granulocytes and myeloid cells. They are highly
susceptible to infections, causing a reduced life span. Mice do
not exhibit normal apoptosis of hematopoietic stem cells after DNA
damage due to irradiation. They do not exhibit normal apoptosis in
response to FAS, TNF, TGFB1, interferons and ceramide, and show
impaired activation of caspases in response to pro-apoptotic
stimuli. Mice are highly susceptible to chemical carcinogens. Mice
display accelerated revascularization after ischemia. Newborns
have smaller brains with a reduced size of the brain cortex. Mice
display aberrant learning and memory, lower levels of anxiety-like
behavior and specific deficits in long-term plasticity. Mice
display a compromised endogenous ciracadian clock with reduced
precision and stability of the period length.
{ECO:0000269|PubMed:12439746, ECO:0000269|PubMed:16915281,
ECO:0000269|PubMed:19136970, ECO:0000269|PubMed:22274616,
ECO:0000269|PubMed:23279884, ECO:0000269|PubMed:9488655,
ECO:0000269|PubMed:9806545}.
-!- SEQUENCE CAUTION:
Sequence=AAA97601.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK028044; BAC25716.1; -; mRNA.
EMBL; BC020990; AAH20990.2; -; mRNA.
EMBL; U33626; AAA97601.2; ALT_INIT; mRNA.
CCDS; CCDS23239.1; -. [Q60953-1]
CCDS; CCDS23240.2; -. [Q60953-2]
RefSeq; NP_001298017.1; NM_001311088.1.
RefSeq; NP_032910.3; NM_008884.5. [Q60953-2]
RefSeq; NP_835188.2; NM_178087.4. [Q60953-1]
UniGene; Mm.392123; -.
ProteinModelPortal; Q60953; -.
SMR; Q60953; -.
BioGrid; 202265; 25.
DIP; DIP-29279N; -.
IntAct; Q60953; 12.
MINT; MINT-4108085; -.
STRING; 10090.ENSMUSP00000082816; -.
iPTMnet; Q60953; -.
PhosphoSitePlus; Q60953; -.
EPD; Q60953; -.
PaxDb; Q60953; -.
PeptideAtlas; Q60953; -.
PRIDE; Q60953; -.
Ensembl; ENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986. [Q60953-1]
Ensembl; ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986. [Q60953-2]
GeneID; 18854; -.
KEGG; mmu:18854; -.
UCSC; uc009pwp.2; mouse. [Q60953-1]
UCSC; uc009pwq.2; mouse. [Q60953-2]
CTD; 5371; -.
MGI; MGI:104662; Pml.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00510000048454; -.
HOGENOM; HOG000115586; -.
HOVERGEN; HBG000552; -.
InParanoid; Q60953; -.
KO; K10054; -.
OMA; KFRVLIQ; -.
OrthoDB; EOG091G02GY; -.
PhylomeDB; Q60953; -.
TreeFam; TF336434; -.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
PRO; PR:Q60953; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000036986; -.
CleanEx; MM_PML; -.
ExpressionAtlas; Q60953; baseline and differential.
Genevisible; Q60953; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:MGI.
GO; GO:0050897; F:cobalt ion binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0046332; F:SMAD binding; IDA:MGI.
GO; GO:0032183; F:SUMO binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0007569; P:cell aging; IMP:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IMP:UniProtKB.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IMP:MGI.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IMP:UniProtKB.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IDA:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0010761; P:fibroblast migration; IMP:CACAO.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IMP:AgBase.
GO; GO:0050711; P:negative regulation of interleukin-1 secretion; IMP:AgBase.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032938; P:negative regulation of translation in response to oxidative stress; ISO:MGI.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0030578; P:PML body organization; IDA:MGI.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; ISO:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:CACAO.
GO; GO:0031065; P:positive regulation of histone deacetylation; ISS:UniProtKB.
GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; IDA:MGI.
GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; ISO:MGI.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
GO; GO:0010522; P:regulation of calcium ion transport into cytosol; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:CACAO.
GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
GO; GO:2000779; P:regulation of double-strand break repair; ISS:UniProtKB.
GO; GO:0045343; P:regulation of MHC class I biosynthetic process; IDA:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0009411; P:response to UV; IMP:MGI.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI.
GO; GO:0007184; P:SMAD protein import into nucleus; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR021978; DUF3583.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF12126; DUF3583; 1.
Pfam; PF00643; zf-B_box; 1.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Antiviral defense;
Apoptosis; Biological rhythms; Coiled coil; Complete proteome;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Endosome;
Host-virus interaction; Immunity; Innate immunity; Isopeptide bond;
Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 885 Protein PML.
/FTId=PRO_0000056002.
ZN_FING 62 97 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 129 171 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 188 239 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
REGION 458 565 Interaction with PER2. {ECO:0000250}.
REGION 566 572 Sumo interaction motif (SIM).
{ECO:0000250}.
COILED 295 331 {ECO:0000255}.
MOTIF 486 500 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 12 38 Pro-rich.
METAL 62 62 Zinc 1. {ECO:0000250}.
METAL 65 65 Zinc 1. {ECO:0000250}.
METAL 77 77 Zinc 2. {ECO:0000250}.
METAL 79 79 Zinc 2. {ECO:0000250}.
METAL 82 82 Zinc 1. {ECO:0000250}.
METAL 85 85 Zinc 1. {ECO:0000250}.
METAL 93 93 Zinc 2. {ECO:0000250}.
METAL 96 96 Zinc 2. {ECO:0000250}.
MOD_RES 17 17 Phosphoserine; by HIPK2.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 45 45 Phosphoserine; by HIPK2 and MAPK1.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 47 47 Phosphoserine; by HIPK2 and MAPK1.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 497 497 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 515 515 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 528 528 Phosphoserine; by CDK1 and CDK2.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 535 535 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 536 536 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 540 540 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 575 575 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P29590}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 384 384 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 384 384 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 488 488 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 497 497 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
CROSSLNK 500 500 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 500 500 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P29590}.
VAR_SEQ 431 476 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8563172}.
/FTId=VSP_026028.
CONFLICT 210 210 G -> V (in Ref. 1; BAC25716).
{ECO:0000305}.
CONFLICT 414 414 A -> V (in Ref. 1; BAC25716).
{ECO:0000305}.
CONFLICT 424 424 T -> S (in Ref. 1; BAC25716).
{ECO:0000305}.
CONFLICT 429 429 E -> V (in Ref. 2; AAH20990).
{ECO:0000305}.
SEQUENCE 885 AA; 98242 MW; 6A2F93F4CD482FDD CRC64;
METEPVSVQK VPAPPGSPCR QQDSALTPTP TMPPPEEPSE DYEHSQSPAE QAIQEEFQFL
RCPSCQAQAK CPKLLPCLHT LCSGCLEAPG LQCPICKAPG QADANGEALD NVFFESLQRR
LAVFRQIVDA QAACTRCKGL ADFWCFECEQ LICSKCFEAH QWYLKHEARP LADLRDNSVS
SFLDSTRKSN IFCSNTNHRN PALTDIYCRG CAKPLCCTCA LLDRNHSHLH CDIGEEIQQW
HEELGTMTQT LEEQGRTFDS AHAQMCSAIG QLDHARADIE KQIRARVRQV VDYVQAQERE
LLEAVNDRYQ RDYQEIAGQL SCLEAVLQRI RTSGALVKRM KLYASDQEVL DMHSFLRKAL
CSLRQEEPQN QKVQLLTRGF EEFKLCLQDF ISCITQRINA AVASPEAASN QPEAASTHPV
TTSTPEDLEQ PKEVQSVQAQ ALELSKTQPV AMVKTVPGAH PVPVYAFSMQ GPTYREEASQ
TVGSMKRKCS HEDCSRKIIK MESTEENEDR LATSSPEQSW PSTFKATSPP HLDGTSNPES
TVPEKKILLP NNNHVTSDTG ETEERVVVIS SSEDSDTENL SSHELDDSSS ESSSLQLEGP
NSLKALDESL AEPHLEDRTL VFFDLKIDNE TQKISQLAAV NRESKFRVLI QPEAFSVYSK
AVSLEAGLRH FLSFLTTMHR PILACSRLWG PGLPIFFQTL SDINKLWEFQ DTISGFLAVL
PLIRERIPGA SSFKLGNLAK TYLARNMSER SALASVLAMR DLCCLLEISP GLPLAQHIYS
FSSLQCFASL QPLIQASVLP QSEARLLALH NVSFVELLNA YRTNRQEGLK KYVHYLSLQT
TPLSSSASTQ VAQFLQALST HMEGLLEGHA PAGAEGKAES KGCLA


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