Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein PML (Promyelocytic leukemia protein) (RING finger protein 71) (Tripartite motif-containing protein 19)

 PML_HUMAN               Reviewed;         882 AA.
P29590; E9PBR7; P29591; P29592; P29593; Q00755; Q15959; Q59FP9;
Q8WUA0; Q96S41; Q9BPW2; Q9BWP7; Q9BZX6; Q9BZX7; Q9BZX8; Q9BZX9;
Q9BZY0; Q9BZY2; Q9BZY3;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
30-AUG-2017, entry version 216.
RecName: Full=Protein PML;
AltName: Full=Promyelocytic leukemia protein;
AltName: Full=RING finger protein 71;
AltName: Full=Tripartite motif-containing protein 19;
Name=PML; Synonyms=MYL, PP8675, RNF71, TRIM19;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3), AND DISEASE.
PubMed=1652369; DOI=10.1016/0092-8674(91)90113-D;
de The H., Lavau C., Marchio A., Chomienne C., Degos L., Dejean A.;
"The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation
in acute promyelocytic leukemia encodes a functionally altered RAR.";
Cell 66:675-684(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-5 AND PML-8),
CHROMOSOMAL TRANSLOCATION WITH RARA, DISEASE, AND VARIANT LEU-645.
PubMed=1720570; DOI=10.1126/science.1720570;
Goddard A.D., Borrow J., Freemont P.S., Solomon E.;
"Characterization of a zinc finger gene disrupted by the t(15;17) in
acute promyelocytic leukemia.";
Science 254:1371-1374(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-4).
PubMed=1311253;
Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B.,
Lanotte M., Berger R., Chambon P.;
"Structure, localization and transcriptional properties of two classes
of retinoic acid receptor alpha fusion proteins in acute promyelocytic
leukemia (APL): structural similarities with a new family of
oncoproteins.";
EMBO J. 11:629-642(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
PubMed=1652368; DOI=10.1016/0092-8674(91)90112-C;
Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr.,
Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M.;
"Chromosomal translocation t(15;17) in human acute promyelocytic
leukemia fuses RAR alpha with a novel putative transcription factor,
PML.";
Cell 66:663-674(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2; PML-4; PML-5;
PML-6; PML-7; PML-8; PML-12 AND PML-14), AND VARIANT LEU-645.
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-6).
Goddard A.D., Solomon E.;
Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-11).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PML-13).
TISSUE=Kidney;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466, AND CHROMOSOMAL
TRANSLOCATION WITH RARA.
PubMed=1312695;
Tong J.H., Dong S., Geng J.P., Huang W., Wang Z.Y., Sun G.L.,
Chen S.J., Chen Z., Larsen C.-J., Berger R.;
"Molecular rearrangements of the MYL gene in acute promyelocytic
leukemia (APL, M3) define a breakpoint cluster region as well as some
molecular variants.";
Oncogene 7:311-316(1992).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, AND CHROMOSOMAL TRANSLOCATION
WITH RARA.
PubMed=12691149;
Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K.,
Omine M.;
"Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic
leukemia: structure of the fusion point in a case lacking classic
t(15;17) translocation.";
Leuk. Lymphoma 44:111-115(2003).
[13]
SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65;
LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=9756909; DOI=10.1074/jbc.273.41.26675;
Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T.,
Yeh E.T.H.;
"Identification of three major sentrinization sites in PML.";
J. Biol. Chem. 273:26675-26682(1998).
[14]
INTERACTION WITH TRIM27.
PubMed=9570750;
Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.;
"Ret finger protein is a normal component of PML nuclear bodies and
interacts directly with PML.";
J. Cell Sci. 111:1319-1329(1998).
[15]
INTERACTION WITH LASSA VIRUS Z PROTEIN.
PubMed=9420283;
Borden K.L., Campbell-Dwyer E.J., Salvato M.S.;
"An arenavirus RING (zinc-binding) protein binds the oncoprotein
promyelocyte leukemia protein (PML) and relocates PML nuclear bodies
to the cytoplasm.";
J. Virol. 72:758-766(1998).
[16]
FUNCTION, AND INTERACTION WITH RARA; RXRA AND TRIM24.
PubMed=10610177; DOI=10.1038/15463;
Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H.,
Kalantry S., Freedman L.P., Pandolfi P.P.;
"A RA-dependent, tumour-growth suppressive transcription complex is
the target of the PML-RARalpha and T18 oncoproteins.";
Nat. Genet. 23:287-295(1999).
[17]
FUNCTION, AND INTERACTION WITH DAXX.
PubMed=10684855; DOI=10.1084/jem.191.4.631;
Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D.,
Pandolfi P.P.;
"Promyelocytic leukemia protein (PML) and Daxx participate in a novel
nuclear pathway for apoptosis.";
J. Exp. Med. 191:631-640(2000).
[18]
INTERACTION WITH DAXX, AND SUBCELLULAR LOCATION.
PubMed=10669754; DOI=10.1128/MCB.20.5.1784-1796.2000;
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
"Sequestration and inhibition of Daxx-mediated transcriptional
repression by PML.";
Mol. Cell. Biol. 20:1784-1796(2000).
[19]
FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
PubMed=11025664; DOI=10.1038/35036365;
Guo A., Salomoni P., Luo J., Shih A., Zhong S., Gu W., Pandolfi P.P.;
"The function of PML in p53-dependent apoptosis.";
Nat. Cell Biol. 2:730-736(2000).
[20]
FUNCTION IN HFV RESTRICTION, INTERACTION WITH HFV BEL1 AND BET, AND
SUBCELLULAR LOCATION.
PubMed=11432836; DOI=10.1093/emboj/20.13.3495;
Regad T., Saib A., Lallemand-Breitenbach V., Pandolfi P.P., de The H.,
Chelbi-Alix M.K.;
"PML mediates the interferon-induced antiviral state against a complex
retrovirus via its association with the viral transactivator.";
EMBO J. 20:3495-3505(2001).
[21]
NOMENCLATURE OF ISOFORMS PML-1 THROUGH PML-7.
PubMed=11704850; DOI=10.1038/sj.onc.1204765;
Jensen K., Shiels C., Freemont P.S.;
"PML protein isoforms and the RBCC/TRIM motif.";
Oncogene 20:7223-7233(2001).
[22]
INTERACTION WITH SIRT1.
PubMed=12006491; DOI=10.1093/emboj/21.10.2383;
Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A.,
Minucci S., Pelicci P.G., Kouzarides T.;
"Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular
senescence.";
EMBO J. 21:2383-2396(2002).
[23]
SUMOYLATION, AND DESUMOYLATION BY SENP2.
PubMed=12419228; DOI=10.1016/S1097-2765(02)00699-8;
Best J.L., Ganiatsas S., Agarwal S., Changou A., Salomoni P.,
Shirihai O., Meluh P.B., Pandolfi P.P., Zon L.I.;
"SUMO-1 protease-1 regulates gene transcription through PML.";
Mol. Cell 10:843-855(2002).
[24]
FUNCTION IN DNA REPAIR, PHOSPHORYLATION AT SER-117 BY CHEK2, AND
INTERACTION WITH CHEK2.
PubMed=12402044; DOI=10.1038/ncb869;
Yang S., Kuo C., Bisi J.E., Kim M.K.;
"PML-dependent apoptosis after DNA damage is regulated by the
checkpoint kinase hCds1/Chk2.";
Nat. Cell Biol. 4:865-870(2002).
[25]
INTERACTION WITH RABIES VIRUS PHOSPHOPROTEINS, SUBCELLULAR LOCATION,
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).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEK2 AND TP53.
PubMed=12810724; DOI=10.1074/jbc.M301264200;
Louria-Hayon I., Grossman T., Sionov R.V., Alsheich O., Pandolfi P.P.,
Haupt Y.;
"The promyelocytic leukemia protein protects p53 from Mdm2-mediated
inhibition and degradation.";
J. Biol. Chem. 278:33134-33141(2003).
[27]
INTERACTION WITH TOPBP1.
PubMed=12773567; DOI=10.1128/MCB.23.12.4247-4256.2003;
Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S.;
"PML colocalizes with and stabilizes the DNA damage response protein
TopBP1.";
Mol. Cell. Biol. 23:4247-4256(2003).
[28]
INTERACTION WITH SIAH1, 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).
[29]
FUNCTION, INTERACTION WITH ELF4, AND SUBCELLULAR LOCATION.
PubMed=14976184; DOI=10.1074/jbc.M312439200;
Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T.,
Matsuzaki K., Nakao M., Li J.-D., Kai H.;
"Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates
lysozyme transcription in epithelial cells through interaction with
promyelocytic leukemia protein.";
J. Biol. Chem. 279:19091-19098(2004).
[30]
INTERACTION WITH ANKRD2.
PubMed=15136035; DOI=10.1016/j.jmb.2004.03.071;
Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V.,
Valle G., Faulkner G.;
"The Ankrd2 protein, a link between the sarcomere and the nucleus in
skeletal muscle.";
J. Mol. Biol. 339:313-325(2004).
[31]
FUNCTION, INTERACTION WITH MDM2 AND RPL11, PHOSPHORYLATION BY ATR IN
RESPONSE TO DNA DAMAGE, 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).
[32]
SUBCELLULAR LOCATION, AND INTERACTION WITH CHFR.
PubMed=15467728; DOI=10.1038/nsmb837;
Daniels M.J., Marson A., Venkitaraman A.R.;
"PML bodies control the nuclear dynamics and function of the CHFR
mitotic checkpoint protein.";
Nat. Struct. Mol. Biol. 11:1114-1121(2004).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TGFBR1; TGFBR2;
SMAD2; SMAD3 AND ZFYVE9/SARA.
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).
[34]
INTERACTION OF PML-RARALPHA ONCOPROTEIN WITH UBE2I, SUBCELLULAR
LOCATION, SUMOYLATION, AND MUTAGENESIS OF CYS-88 AND PRO-89.
PubMed=15809060; DOI=10.1016/j.bbrc.2005.03.052;
Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.;
"Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for
localization, sumoylation, and inhibition of monocyte
differentiation.";
Biochem. Biophys. Res. Commun. 330:746-754(2005).
[35]
SUBCELLULAR LOCATION.
PubMed=16778193; DOI=10.1158/0008-5472.CAN-05-3792;
Condemine W., Takahashi Y., Zhu J., Puvion-Dutilleul F., Guegan S.,
Janin A., de The H.;
"Characterization of endogenous human promyelocytic leukemia
isoforms.";
Cancer Res. 66:6192-6198(2006).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527
AND SER-530, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565
(ISOFORM PML-5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518;
SER-527 AND SER-530 (ISOFORM PML-6), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[37]
FUNCTION.
PubMed=17030982; DOI=10.1083/jcb.200604009;
Dellaire G., Ching R.W., Ahmed K., Jalali F., Tse K.C., Bristow R.G.,
Bazett-Jones D.P.;
"Promyelocytic leukemia nuclear bodies behave as DNA damage sensors
whose response to DNA double-strand breaks is regulated by NBS1 and
the kinases ATM, Chk2, and ATR.";
J. Cell Biol. 175:55-66(2006).
[38]
FUNCTION IN POLIOVIRUS RESTRICTION.
PubMed=16912307; DOI=10.1128/JVI.00031-06;
Pampin M., Simonin Y., Blondel B., Percherancier Y., Chelbi-Alix M.K.;
"Cross talk between PML and p53 during poliovirus infection:
implications for antiviral defense.";
J. Virol. 80:8582-8592(2006).
[39]
SUBUNIT, SUMOYLATION, SUMO-BINDING MOTIF, MUTAGENESIS OF CYS-57 AND
CYS-60, AND SUBCELLULAR LOCATION.
PubMed=17081985; DOI=10.1016/j.molcel.2006.09.013;
Shen T.H., Lin H.K., Scaglioni P.P., Yung T.M., Pandolfi P.P.;
"The mechanisms of PML-nuclear body formation.";
Mol. Cell 24:331-339(2006).
[40]
INTERACTION WITH PKM, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND
MUTAGENESIS OF LYS-487 AND LYS-490.
PubMed=18298799; DOI=10.1111/j.1365-2443.2008.01165.x;
Shimada N., Shinagawa T., Ishii S.;
"Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML
tumor suppressor protein.";
Genes Cells 13:245-254(2008).
[41]
ACETYLATION AT LYS-487 AND LYS-515, AND MUTAGENESIS OF LYS-487 AND
LYS-515.
PubMed=18621739; DOI=10.1074/jbc.M802217200;
Hayakawa F., Abe A., Kitabayashi I., Pandolfi P.P., Naoe T.;
"Acetylation of PML is involved in histone deacetylase inhibitor-
mediated apoptosis.";
J. Biol. Chem. 283:24420-24425(2008).
[42]
FUNCTION IN HCMV RESTRICTION.
PubMed=17942542; DOI=10.1128/JVI.01685-07;
Tavalai N., Papior P., Rechter S., Stamminger T.;
"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx
independently contribute to an intrinsic antiviral defense against
human cytomegalovirus infection.";
J. Virol. 82:126-137(2008).
[43]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18716620; DOI=10.1038/nature07290;
Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F.,
Teruya-Feldstein J., Pandolfi P.P.;
"The deubiquitinylation and localization of PTEN are regulated by a
HAUSP-PML network.";
Nature 455:813-817(2008).
[44]
POLYUBIQUITINATION AT LYS-380; LYS-400; LYS-401 AND LYS-476 BY RNF4,
PROTEASOMAL DEGRADATION, AND SUMOYLATION.
PubMed=18408734; DOI=10.1038/ncb1716;
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,
Jaffray E.G., Palvimo J.J., Hay R.T.;
"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for
arsenic-induced PML degradation.";
Nat. Cell Biol. 10:538-546(2008).
[45]
FUNCTION, AND INTERACTION WITH SATB1.
PubMed=17173041; DOI=10.1038/ncb1516;
Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A.,
Galande S.;
"Functional interaction between PML and SATB1 regulates chromatin-loop
architecture and transcription of the MHC class I locus.";
Nat. Cell Biol. 9:45-56(2007).
[46]
FUNCTION IN HHV-1 RESTRICTION, AND SUBCELLULAR LOCATION.
PubMed=18509536; DOI=10.1371/journal.pone.0002277;
McNally B.A., Trgovcich J., Maul G.G., Liu Y., Zheng P.;
"A role for cytoplasmic PML in cellular resistance to viral
infection.";
PLoS ONE 3:E2277-E2277(2008).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-518; SER-527
AND SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[48]
FUNCTION IN INFLUENZA A VIRUS RESTRICTION.
PubMed=19703418; DOI=10.1016/j.bbrc.2009.08.091;
Li W., Wang G., Zhang H., Zhang D., Zeng J., Chen X., Xu Y., Li K.;
"Differential suppressive effect of promyelocytic leukemia protein on
the replication of different subtypes/strains of influenza A virus.";
Biochem. Biophys. Res. Commun. 389:84-89(2009).
[49]
FUNCTION, AND INTERACTION WITH TERT.
PubMed=19567472; DOI=10.1242/jcs.048066;
Oh W., Ghim J., Lee E.W., Yang M.R., Kim E.T., Ahn J.H., Song J.;
"PML-IV functions as a negative regulator of telomerase by interacting
with TERT.";
J. Cell Sci. 122:2613-2622(2009).
[50]
PHOSPHORYLATION AT SER-8 AND SER-38 BY HIPK2, AND INTERACTION WITH
HIPK2.
PubMed=19015637; DOI=10.1038/onc.2008.420;
Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K.,
Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L.;
"PML tumor suppressor is regulated by HIPK2-mediated phosphorylation
in response to DNA damage.";
Oncogene 28:698-708(2009).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[52]
INTERACTION WITH MORC3, AND SUBCELLULAR LOCATION.
PubMed=20501696; DOI=10.1242/jcs.063586;
Mimura Y., Takahashi K., Kawata K., Akazawa T., Inoue N.;
"Two-step colocalization of MORC3 with PML nuclear bodies.";
J. Cell Sci. 123:2014-2024(2010).
[53]
FUNCTION IN RABIES VIRUS RESTRICTION.
PubMed=20702643; DOI=10.1128/JVI.01286-10;
Blondel D., Kheddache S., Lahaye X., Dianoux L., Chelbi-Alix M.K.;
"Resistance to rabies virus infection conferred by the PMLIV
isoform.";
J. Virol. 84:10719-10726(2010).
[54]
INTERACTION OF PML-4 AND PML-5 WITH HADV5 E1B-55K.
PubMed=20639899; DOI=10.1038/onc.2010.284;
Wimmer P., Schreiner S., Everett R.D., Sirma H., Groitl P., Dobner T.;
"SUMO modification of E1B-55K oncoprotein regulates isoform-specific
binding to the tumour suppressor protein PML.";
Oncogene 29:5511-5522(2010).
[55]
SUMOYLATION, AND UBIQUITINATION.
PubMed=20943951; DOI=10.1091/mbc.E10-05-0449;
Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T.;
"Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear
bodies.";
Mol. Biol. Cell 21:4227-4239(2010).
[56]
INTERACTION WITH CSNK2A1 AND CSNK2A3.
PubMed=20625391; DOI=10.1371/journal.pone.0011418;
Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T.,
Jablons D.M., You L.;
"Functional polymorphism of the CK2alpha intronless gene plays
oncogenic roles in lung cancer.";
PLoS ONE 5:E11418-E11418(2010).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-527, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[58]
INTERACTION WITH UBC9, SUBUNIT, UBIQUITINATION, SUMOYLATION, ARSENIC
BINDING, DOMAIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20378816; DOI=10.1126/science.1183424;
Zhang X.W., Yan X.J., Zhou Z.R., Yang F.F., Wu Z.Y., Sun H.B.,
Liang W.X., Song A.X., Lallemand-Breitenbach V., Jeanne M.,
Zhang Q.Y., Yang H.Y., Huang Q.H., Zhou G.B., Tong J.H., Zhang Y.,
Wu J.H., Hu H.Y., de The H., Chen S.J., Chen Z.;
"Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by
directly binding PML.";
Science 328:240-243(2010).
[59]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[60]
FUNCTION, AND INTERACTION WITH WRN.
PubMed=21639834; DOI=10.1134/S000629791105004X;
Liu J., Song Y., Qian J., Liu B., Dong Y., Tian B., Sun Z.;
"Promyelocytic leukemia protein interacts with werner syndrome
helicase and regulates double-strand break repair in gamma-
irradiation-induced DNA damage responses.";
Biochemistry (Mosc.) 76:550-554(2011).
[61]
UBIQUITINATION, PHOSPHORYLATION AT SER-518, AND MUTAGENESIS OF
SER-518.
PubMed=21840486; DOI=10.1016/j.ccr.2011.07.008;
Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C.,
Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H.,
Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.;
"A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to
potentiate HIF-1 signaling and prostate cancer progression.";
Cancer Cell 20:214-228(2011).
[62]
REVIEW ON FUNCTION.
PubMed=21475307; DOI=10.1038/cdd.2011.31;
Pinton P., Giorgi C., Pandolfi P.P.;
"The role of PML in the control of apoptotic cell fate: a new key
player at ER-mitochondria sites.";
Cell Death Differ. 18:1450-1456(2011).
[63]
REVIEW ON FUNCTION.
PubMed=21501958; DOI=10.1016/j.ceb.2011.03.011;
Carracedo A., Ito K., Pandolfi P.P.;
"The nuclear bodies inside out: PML conquers the cytoplasm.";
Curr. Opin. Cell Biol. 23:360-366(2011).
[64]
PHOSPHORYLATION AT SER-403; SER-505; SER-518 AND SER-527, AND
INTERACTION WITH PIN1 AND MAPK1.
PubMed=22033920; DOI=10.1074/jbc.M111.289512;
Lim J.H., Liu Y., Reineke E., Kao H.Y.;
"Mitogen-activated protein kinase extracellular signal-regulated
kinase 2 phosphorylates and promotes Pin1 protein-dependent
promyelocytic leukemia protein turnover.";
J. Biol. Chem. 286:44403-44411(2011).
[65]
FUNCTION.
PubMed=21172801; DOI=10.1242/jcs.075390;
Cuchet D., Sykes A., Nicolas A., Orr A., Murray J., Sirma H.,
Heeren J., Bartelt A., Everett R.D.;
"PML isoforms I and II participate in PML-dependent restriction of
HSV-1 replication.";
J. Cell Sci. 124:280-291(2011).
[66]
REVIEW ON FUNCTION IN ANTIVIRAL DEFENSE.
PubMed=21198351; DOI=10.1089/jir.2010.0111;
Geoffroy M.C., Chelbi-Alix M.K.;
"Role of promyelocytic leukemia protein in host antiviral defense.";
J. Interferon Cytokine Res. 31:145-158(2011).
[67]
FUNCTION IN EMCV RESTRICTION, AND INTERACTION WITH EMCV P3D-POL.
PubMed=21994459; DOI=10.1128/JVI.05808-11;
Maroui M.A., Pampin M., Chelbi-Alix M.K.;
"Promyelocytic leukemia isoform IV confers resistance to
encephalomyocarditis virus via the sequestration of 3D polymerase in
nuclear bodies.";
J. Virol. 85:13164-13173(2011).
[68]
SUMOYLATION, AND DESUMOYLATION BY SENP6.
PubMed=21148299; DOI=10.1091/mbc.E10-06-0504;
Hattersley N., Shen L., Jaffray E.G., Hay R.T.;
"The SUMO protease SENP6 is a direct regulator of PML nuclear
bodies.";
Mol. Biol. Cell 22:78-90(2011).
[69]
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).
[70]
FUNCTION IN VARICELLA ZOSTER RESTRICTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH VZV VP26.
PubMed=21304940; DOI=10.1371/journal.ppat.1001266;
Reichelt M., Wang L., Sommer M., Perrino J., Nour A.M., Sen N.,
Baiker A., Zerboni L., Arvin A.M.;
"Entrapment of viral capsids in nuclear PML cages is an intrinsic
antiviral host defense against Varicella-Zoster virus.";
PLoS Pathog. 7:E1001266-E1001266(2011).
[71]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-527 AND
SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[72]
SUMOYLATION AT LYS-65 AND LYS-160, PHOSPHORYLATION AT SER-565,
SUBCELLULAR LOCATION, AND INTERACTION WITH PIAS1; PIAS2 AND CSNK2A1.
PubMed=22406621; DOI=10.1158/0008-5472.CAN-11-3159;
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
Scaglioni P.P.;
"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
oncogenic counterpart PML-RARA.";
Cancer Res. 72:2275-2284(2012).
[73]
SUBCELLULAR LOCATION, AND INTERACTION WITH MAGEA2.
PubMed=22117195; DOI=10.1038/cdd.2011.173;
Peche L.Y., Scolz M., Ladelfa M.F., Monte M., Schneider C.;
"MageA2 restrains cellular senescence by targeting the function of
PMLIV/p53 axis at the PML-NBs.";
Cell Death Differ. 19:926-936(2012).
[74]
REVIEW ON FUNCTION.
PubMed=22237204; DOI=10.1038/cddis.2011.122;
Salomoni P., Dvorkina M., Michod D.;
"Role of the promyelocytic leukaemia protein in cell death
regulation.";
Cell Death Dis. 3:E247-E247(2012).
[75]
FUNCTION, AND INTERACTION WITH TBX2; TBX3; E2F4 AND RBL2.
PubMed=22002537; DOI=10.1038/emboj.2011.370;
Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
Dejean A., Bischof O.;
"Physical and functional interaction between PML and TBX2 in the
establishment of cellular senescence.";
EMBO J. 31:95-109(2012).
[76]
FUNCTION IN CIRCADIAN CLOCK, SUBCELLULAR LOCATION, INTERACTION WITH
PER2, ACETYLATION AT LYS-487, AND DEACETYLATION BY SIRT1.
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).
[77]
REVIEW ON PTM.
PubMed=23316480; DOI=10.3389/fonc.2012.00210;
Cheng X., Kao H.Y.;
"Post-translational modifications of PML: consequences and
implications.";
Front. Oncol. 2:210-210(2012).
[78]
FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-490, AND
INTERACTION WITH HDAC7; RANBP2 AND CTNNB1-TCF7L2 COMPLEX.
PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
Satow R., Shitashige M., Jigami T., Fukami K., Honda K.,
Kitabayashi I., Yamada T.;
"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
function in colorectal cancer cells.";
Gastroenterology 142:572-581(2012).
[79]
INTERACTION WITH MOMLV IN AND RT, AND SUBCELLULAR LOCATION.
PubMed=22685230; DOI=10.1093/jb/mvs063;
Okino Y., Inayoshi Y., Kojima Y., Kidani S., Kaneoka H., Honkawa A.,
Higuchi H., Nishijima K., Miyake K., Iijima S.;
"Moloney murine leukemia virus integrase and reverse transcriptase
interact with PML proteins.";
J. Biochem. 152:161-169(2012).
[80]
FUNCTION.
PubMed=22589541; DOI=10.1074/jbc.M112.340505;
Cheng X., Liu Y., Chu H., Kao H.Y.;
"Promyelocytic leukemia protein (PML) regulates endothelial cell
network formation and migration in response to tumor necrosis factor
alpha (TNFalpha) and interferon alpha (IFNalpha).";
J. Biol. Chem. 287:23356-23367(2012).
[81]
DOMAIN C-TERMINAL.
PubMed=22773875; DOI=10.1074/jbc.M112.374769;
Geng Y., Monajembashi S., Shao A., Cui D., He W., Chen Z.,
Hemmerich P., Tang J.;
"Contribution of the C-terminal regions of promyelocytic leukemia
protein (PML) isoforms II and V to PML nuclear body formation.";
J. Biol. Chem. 287:30729-30742(2012).
[82]
REVIEW ON UBIQUITINATION.
PubMed=22935031; DOI=10.1186/1423-0127-19-81;
Chen R.H., Lee Y.R., Yuan W.C.;
"The role of PML ubiquitination in human malignancies.";
J. Biomed. Sci. 19:81-81(2012).
[83]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CIITA.
PubMed=23007646; DOI=10.1083/jcb.201112015;
Ulbricht T., Alzrigat M., Horch A., Reuter N., von Mikecz A.,
Steimle V., Schmitt E., Kraemer O.H., Stamminger T., Hemmerich P.;
"PML promotes MHC class II gene expression by stabilizing the class II
transactivator.";
J. Cell Biol. 199:49-63(2012).
[84]
FUNCTION, AND TISSUE SPECIFICITY.
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).
[85]
INTERACTION WITH HHV-1 ICP0.
PubMed=22875967; DOI=10.1128/JVI.01145-12;
Cuchet-Lourenco D., Vanni E., Glass M., Orr A., Everett R.D.;
"Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML
isoform I and induces its SUMO-independent degradation.";
J. Virol. 86:11209-11222(2012).
[86]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-38; SER-48;
SER-403; SER-505; SER-512; SER-518; SER-527; SER-530 AND THR-867, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[87]
SUBCELLULAR LOCATION, AND INTERACTION WITH MDM2 AND MAPK7.
PubMed=22869143; DOI=10.1038/onc.2012.332;
Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III,
Lee J.D.;
"BMK1 is involved in the regulation of p53 through disrupting the PML-
MDM2 interaction.";
Oncogene 32:3156-3164(2013).
[88]
UBIQUITINATION BY UHRF1.
PubMed=22945642; DOI=10.1038/onc.2012.406;
Guan D., Factor D., Liu Y., Wang Z., Kao H.Y.;
"The epigenetic regulator UHRF1 promotes ubiquitination-mediated
degradation of the tumor-suppressor protein promyelocytic leukemia
protein.";
Oncogene 32:3819-3828(2013).
[89]
SUMOYLATION, INTERACTION WITH RNF4, AND DOMAIN SIM.
PubMed=23028697; DOI=10.1371/journal.pone.0044949;
Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M.,
Chelbi-Alix M.K.;
"Requirement of PML SUMO interacting motif for RNF4- or arsenic
trioxide-induced degradation of nuclear PML isoforms.";
PLoS ONE 7:E44949-E44949(2012).
[90]
FUNCTION.
PubMed=23219818; DOI=10.1016/j.bbrc.2012.11.108;
Kuroki M., Ariumi Y., Hijikata M., Ikeda M., Dansako H., Wakita T.,
Shimotohno K., Kato N.;
"PML tumor suppressor protein is required for HCV production.";
Biochem. Biophys. Res. Commun. 430:592-597(2013).
[91]
INTERACTION WITH NLRP3.
PubMed=23430110; DOI=10.1182/blood-2012-05-432104;
Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., Kuo W.C.,
Chuang Y.T., Jiang S.T., Shih H.M., Lai M.Z.;
"Selective inhibition of the NLRP3 inflammasome by targeting to
promyelocytic leukemia protein in mouse and human.";
Blood 121:3185-3194(2013).
[92]
FUNCTION, AND INTERACTION WITH HUMAN ADENOVIRUS 2 E1A.
PubMed=23135708; DOI=10.1128/JVI.02023-12;
Berscheminski J., Groitl P., Dobner T., Wimmer P., Schreiner S.;
"The adenoviral oncogene E1A-13S interacts with a specific isoform of
the tumor suppressor PML to enhance viral transcription.";
J. Virol. 87:965-977(2013).
[93]
FUNCTION, AND INTERACTION WITH KAT6A.
PubMed=23431171; DOI=10.1073/pnas.1300490110;
Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I.,
Prives C.;
"MOZ increases p53 acetylation and premature senescence through its
complex formation with PML.";
Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013).
[94]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-36; SER-403;
SER-518; SER-527 AND SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[95]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-380 AND LYS-490, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[96]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-160 AND LYS-490, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[97]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-160; LYS-380;
LYS-394; LYS-478 AND LYS-490, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[98]
INTERACTION OF PML-4 AND PML-5 WITH HADV5 E1B-55K.
PubMed=25772236; DOI=10.1038/onc.2015.63;
Wimmer P., Berscheminski J., Blanchette P., Groitl P., Branton P.E.,
Hay R.T., Dobner T., Schreiner S.;
"PML isoforms IV and V contribute to adenovirus-mediated oncogenic
transformation by functionally inhibiting the tumor-suppressor p53.";
Oncogene 35:69-82(2016).
[99]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-160; LYS-380;
LYS-394; LYS-401; LYS-460; LYS-476; LYS-478; LYS-487; LYS-490 AND
LYS-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[100]
STRUCTURE BY NMR OF 49-104.
PubMed=7729428;
Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S.,
Howe K., Solomon E., Freemont P.S.;
"The solution structure of the RING finger domain from the acute
promyelocytic leukaemia proto-oncoprotein PML.";
EMBO J. 14:1532-1541(1995).
-!- FUNCTION: Functions via its association with PML-nuclear bodies
(PML-NBs) in a wide range of important cellular processes,
including tumor suppression, transcriptional regulation,
apoptosis, senescence, DNA damage response, and viral defense
mechanisms. Acts as the scaffold of PML-NBs allowing other
proteins to shuttle in and out, a process which is regulated by
SUMO-mediated modifications and interactions. Isoform PML-4 has a
multifaceted role in the regulation of apoptosis and growth
suppression: activates RB1 and inhibits AKT1 via interactions with
PP1 and PP2A phosphatases respectively, negatively affects the
PI3K pathway by inhibiting MTOR and activating PTEN, and
positively regulates p53/TP53 by acting at different levels (by
promoting its acetylation and phosphorylation and by inhibiting
its MDM2-dependent degradation). Isoform PML-4 also: acts as a
transcriptional repressor of TBX2 during cellular senescence and
the repression is dependent on a functional RBL2/E2F4 repressor
complex, regulates double-strand break repair in gamma-
irradiation-induced DNA damage responses via its interaction with
WRN, acts as a negative regulator of telomerase by interacting
with TERT, and regulates PER2 nuclear localization and circadian
function. Isoform PML-6 inhibits specifically the activity of the
tetrameric form of PKM. The nuclear isoforms (isoform PML-1,
isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in
concert with SATB1 are involved in local chromatin-loop remodeling
and gene expression regulation at the MHC-I locus. Isoform PML-2
is required for efficient IFN-gamma induced MHC II gene
transcription via regulation of CIITA. Cytoplasmic PML is involved
in the regulation of the TGF-beta signaling pathway. PML also
regulates transcription activity of ELF4 and can act as an
important mediator for TNF-alpha- and IFN-alpha-mediated
inhibition of endothelial cell network formation and migration.
-!- 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 (HCMV) and influenza A virus strains
PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform
PML-12 show antiviral activity against encephalomyocarditis virus
(EMCV) by promoting nuclear sequestration of viral polymerase
(P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral
activity against poliovirus by inducing apoptosis in infected
cells through the recruitment and the activation of p53/TP53 in
the PML-NBs. Isoform PML-3 represses human foamy virus (HFV)
transcription by complexing the HFV transactivator, bel1/tas,
preventing its binding to viral DNA. PML may positively regulate
infectious hepatitis C viral (HCV) production and isoform PML-2
may enhance adenovirus transcription.
-!- 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 HIPK2, TERT,
SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-
terminus). Interacts with Lassa virus Z protein and rabies virus
phosphoprotein. Interacts with ITPR3. Interacts (in the cytoplasm)
with TGFBR1, TGFBR2 and PKM. Interacts (via the coiled-coil domain
and when sumoylated) with SATB1. Interacts with UBE2I; the
interaction is enhanced by arsenic binding. Interacts (PML-RARA
oncoprotein, via the coiled-coil domain) with UBE2I; the
interaction is enhanced by arsenic binding and is required for
PML-RARA oncoprotein sumoylation and inhibition of RARA
transactivational activity. Interacts with RB1, PPP1A, SMAD2,
SMAD3, DAXX, RPL11 and MTOR. Interacts with PPARGC1A and KAT2A.
Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the
interaction is direct. Interacts (via SUMO-interacting motif) with
sumoylated MORC3 (PubMed:20501696). Isoform PML-1, isoform PML-2,
isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6
interact with RNF4. Isoform PML-1 interacts with NLRP3. Isoform
PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform
PML-5 interact with MAGEA2, RBL2, PER2 and E2F4. Isoform PML-2
interacts with CIITA. Isoform PML-2, isoform PML-3 and isoform
PML-4 interact with TBX2. Isoform PML-4 interacts with RANBP2,
HDAC7, KAT6A, WRN, PIN1, TBX3 and phosphorylated MAPK1/ERK2.
Isoform PML-4 interacts with the CTNNB1 and TCF7L2/TCF4 complex.
Isoform PML-4 preferentially interacts with MAPK7/BMK1 although
other isoforms (isoform PML-1, isoform PML-2, isoform PML-3 and
isoform PML-6) also interact with it. Isoform PML-12 interacts
with PIAS1, PIAS2 (isoform PIAS2-alpha) and CSNK2A1/CK2. Isoform
PML-3 interacts with HFV bel1/tas and bet. Isoform PML-4 interacts
with VZV capsid protein VP26/ORF23 capsid protein. Ths sumoylated
isoform PML-4 interacts with encephalomyocarditis virus (EMCV)
RNA-directed RNA polymerase 3D-POL (P3D-POL). Isoform PML-1
interacts with herpes simplex virus-1 (HHV-1) ICP0. Isoform PML-2
interacts with human adenovirus 2 E1A and this interaction
stimulates E1A-dependent transcriptional activation
(PubMed:23135708). Isoform PML-6 interacts with moloney murine
leukemia virus (MoMLV) integrase (IN) and reverse transcriptase
(RT). Isoform PML-4 and isoform PML-5 interact with human
adenovirus 5 E1B-55K protein; these interactions promote efficient
subnuclear targeting of E1B-55K to PML nuclear bodies
(PubMed:20639899, PubMed:25772236). {ECO:0000269|PubMed:10610177,
ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:10684855,
ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:11432836,
ECO:0000269|PubMed:12006491, ECO:0000269|PubMed:12402044,
ECO:0000269|PubMed:12439746, ECO:0000269|PubMed:12773567,
ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:14645235,
ECO:0000269|PubMed:14976184, ECO:0000269|PubMed:15136035,
ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:15467728, ECO:0000269|PubMed:15809060,
ECO:0000269|PubMed:17081985, ECO:0000269|PubMed:17173041,
ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:19015637,
ECO:0000269|PubMed:19567472, ECO:0000269|PubMed:20378816,
ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:20625391,
ECO:0000269|PubMed:20639899, ECO:0000269|PubMed:21304940,
ECO:0000269|PubMed:21639834, ECO:0000269|PubMed:21994459,
ECO:0000269|PubMed:22002537, ECO:0000269|PubMed:22033920,
ECO:0000269|PubMed:22117195, ECO:0000269|PubMed:22155184,
ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:22406621,
ECO:0000269|PubMed:22685230, ECO:0000269|PubMed:22869143,
ECO:0000269|PubMed:22875967, ECO:0000269|PubMed:23007646,
ECO:0000269|PubMed:23028697, ECO:0000269|PubMed:23135708,
ECO:0000269|PubMed:23430110, ECO:0000269|PubMed:23431171,
ECO:0000269|PubMed:25772236, ECO:0000269|PubMed:9420283,
ECO:0000269|PubMed:9570750}.
-!- INTERACTION:
P03243-1:- (xeno); NbExp=2; IntAct=EBI-303996, EBI-1927377;
P04489:- (xeno); NbExp=4; IntAct=EBI-8099068, EBI-6398911;
P27958:- (xeno); NbExp=6; IntAct=EBI-295890, EBI-6377335;
P68400:CSNK2A1; NbExp=2; IntAct=EBI-295890, EBI-347804;
Q9UER7:DAXX; NbExp=6; IntAct=EBI-295890, EBI-77321;
P25445:FAS; NbExp=4; IntAct=EBI-295890, EBI-494743;
Q8UN00:gag-pro-pol (xeno); NbExp=4; IntAct=EBI-295890, EBI-6692904;
Q9Y2M5:KLHL20; NbExp=9; IntAct=EBI-295890, EBI-714379;
Q13164:MAPK7; NbExp=6; IntAct=EBI-295890, EBI-1213983;
Q00987:MDM2; NbExp=6; IntAct=EBI-304008, EBI-389668;
P25788:PSMA3; NbExp=2; IntAct=EBI-295890, EBI-348380;
P63165:SUMO1; NbExp=3; IntAct=EBI-295890, EBI-80140;
Q13207:TBX2; NbExp=2; IntAct=EBI-295890, EBI-2853051;
O14746:TERT; NbExp=7; IntAct=EBI-304008, EBI-1772203;
Q15583:TGIF1; NbExp=3; IntAct=EBI-295890, EBI-714215;
P04637:TP53; NbExp=4; IntAct=EBI-295890, EBI-366083;
Q05516:ZBTB16; NbExp=7; IntAct=EBI-295890, EBI-711925;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm. Cytoplasm.
Nucleus, PML body {ECO:0000269|PubMed:20501696}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=PML-1; Synonyms=PML-I, TRIM19alpha;
IsoId=P29590-1; Sequence=Displayed;
Name=PML-2; Synonyms=PML-II, TRIM19kappa;
IsoId=P29590-8; Sequence=VSP_040595;
Name=PML-3; Synonyms=PML-III;
IsoId=P29590-9; Sequence=VSP_040596, VSP_040597;
Name=PML-4; Synonyms=PML-IV, PML-X, TRIM19zeta;
IsoId=P29590-5; Sequence=VSP_005744, VSP_005745;
Name=PML-5; Synonyms=PML-2, PML-V, TRIM19beta;
IsoId=P29590-2; Sequence=VSP_005739, VSP_005740;
Note=Ref.5 (AAG50181) sequence is in conflict in position:
578:P->A. Contains a phosphoserine at position 565.
{ECO:0000244|PubMed:17081983, ECO:0000305};
Name=PML-6; Synonyms=PML-3B, PML-VI, TRIM19epsilon;
IsoId=P29590-4; Sequence=VSP_005742, VSP_005743;
Note=Contains a phosphoserine at position 518. Contains a
phosphoserine at position 527. Contains a phosphoserine at
position 530. {ECO:0000244|PubMed:17081983};
Name=PML-7; Synonyms=PML-VII, TRIM19theta;
IsoId=P29590-10; Sequence=VSP_040591, VSP_040594;
Note=Ref.5 (AAG50187) sequence is in conflict in position:
419:L->V. {ECO:0000305};
Name=PML-8; Synonyms=PML-2G, PML-IIG, TRIM19gamma;
IsoId=P29590-3; Sequence=VSP_005741;
Note=Non-canonical splice sites. Might alternatively represent a
polymorphic variation.;
Name=PML-11; Synonyms=PML-1A, PML-IA;
IsoId=P29590-11; Sequence=VSP_040590;
Note=No experimental confirmation available.;
Name=PML-12; Synonyms=PML-4A, PML-IVA, TRIM19lambda;
IsoId=P29590-12; Sequence=VSP_040590, VSP_005744, VSP_005745;
Name=PML-13; Synonyms=PML-2A, PML-IIA;
IsoId=P29590-13; Sequence=VSP_040590, VSP_040595;
Name=PML-14; Synonyms=PML-6B, PML-VIB, TRIM19eta, TRIM19iota;
IsoId=P29590-14; Sequence=VSP_040592, VSP_040593;
-!- INDUCTION: By interferons alpha, beta and gamma. Up-regulated by
IRF3 and p53/TP53.
-!- DOMAIN: The coiled-coil domain mediates a strong
homo/multidimerization activity essential for core assembly of
PML-NBs. Interacts with PKM via its coiled-coil domain
(PubMed:18298799). {ECO:0000269|PubMed:18298799}.
-!- DOMAIN: The B box-type zinc binding domain and the coiled-coil
domain mediate its interaction with PIAS1.
{ECO:0000269|PubMed:22406621}.
-!- DOMAIN: Binds arsenic via the RING-type zinc finger. The RING-type
zinc finger is essential for its interaction with HFV bel1/tas
(PubMed:11432836). {ECO:0000269|PubMed:11432836}.
-!- DOMAIN: The unique C-terminal domains of isoform PML-2 and isoform
PML-5 play an important role in regulating the localization,
assembly dynamics, and functions of PML-NBs.
{ECO:0000269|PubMed:22773875}.
-!- 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:0000269|PubMed:23028697}.
-!- 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. DNA damage triggers
its sumoylation while some but not all viral infections can
abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5
and SENP6. Arsenic induces PML and PML-RARA polysumoylation and
their subsequent RNF4-dependent ubiquitination and proteasomal
degradation, and is used as treatment in acute promyelocytic
leukemia (APL). The nuclear isoforms (isoform PML-1, isoform PML-
2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6)
show an increased sumoylation in response to arsenic trioxide. The
cytoplasmic isoform PML-7 is not sumoylated.
{ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:22155184,
ECO:0000269|PubMed:22406621, 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. HIPK2-mediated phosphorylation at Ser-8, Ser-36
and Ser-38 leads to increased accumulation of PML protein and its
sumoylation and is required for the maximal pro-apoptotic activity
of PML after DNA damage. CHEK2-mediated phosphorylation at Ser-117
is important for PML-mediated apopotosis following DNA damage.
MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and
Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote
PIN1-dependent PML degradation. CK2-mediated phosphorylation at
Ser-565 primes PML ubiquitination via an unidentified ubiquitin
ligase. {ECO:0000269|PubMed:12402044, ECO:0000269|PubMed:15195100,
ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19015637,
ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22033920,
ECO:0000269|PubMed:22406621}.
-!- 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}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA60351.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA60352.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA60388.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA60390.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB62809.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
Sequence=BAD92648.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PMLID41.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S50913; AAB19601.2; -; mRNA.
EMBL; M79462; AAA60388.1; ALT_INIT; mRNA.
EMBL; M79463; AAA60351.1; ALT_INIT; mRNA.
EMBL; M79464; AAA60390.1; ALT_INIT; mRNA.
EMBL; X63131; CAA44841.1; -; mRNA.
EMBL; M73778; AAA60125.1; -; mRNA.
EMBL; M80185; AAA60352.1; ALT_INIT; mRNA.
EMBL; AF230401; AAG50180.1; -; mRNA.
EMBL; AF230402; AAG50181.1; -; mRNA.
EMBL; AF230403; AAG50182.1; -; mRNA.
EMBL; AF230405; AAG50184.1; -; mRNA.
EMBL; AF230406; AAG50185.1; -; mRNA.
EMBL; AF230407; AAG50186.1; -; mRNA.
EMBL; AF230408; AAG50187.1; -; mRNA.
EMBL; AF230409; AAG50188.1; -; mRNA.
EMBL; AF230410; AAG50189.1; -; mRNA.
EMBL; AF230411; AAG50190.1; -; mRNA.
EMBL; BT009911; AAP88913.1; -; mRNA.
EMBL; AB209411; BAD92648.1; ALT_INIT; mRNA.
EMBL; AC013486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000080; AAH00080.2; -; mRNA.
EMBL; BC020994; AAH20994.1; -; mRNA.
EMBL; X64800; CAA46026.1; -; Genomic_DNA.
EMBL; AB067754; BAB62809.1; ALT_SEQ; mRNA.
CCDS; CCDS10255.1; -. [P29590-1]
CCDS; CCDS10256.1; -. [P29590-10]
CCDS; CCDS10257.1; -. [P29590-8]
CCDS; CCDS10258.1; -. [P29590-13]
CCDS; CCDS45297.1; -. [P29590-5]
CCDS; CCDS45298.1; -. [P29590-2]
CCDS; CCDS45299.1; -. [P29590-4]
CCDS; CCDS45300.1; -. [P29590-14]
CCDS; CCDS58386.1; -. [P29590-12]
PIR; A40044; A40044.
PIR; I38054; I38054.
PIR; S19244; S19244.
PIR; S42516; S42516.
PIR; S44381; S44381.
RefSeq; NP_002666.1; NM_002675.3. [P29590-5]
RefSeq; NP_150241.2; NM_033238.2. [P29590-1]
RefSeq; NP_150242.1; NM_033239.2. [P29590-8]
RefSeq; NP_150243.2; NM_033240.2. [P29590-2]
RefSeq; NP_150247.2; NM_033244.3. [P29590-4]
RefSeq; NP_150249.1; NM_033246.2. [P29590-14]
RefSeq; NP_150250.2; NM_033247.2. [P29590-10]
RefSeq; NP_150252.1; NM_033249.2. [P29590-12]
RefSeq; NP_150253.2; NM_033250.2. [P29590-13]
UniGene; Hs.526464; -.
UniGene; Hs.654583; -.
PDB; 1BOR; NMR; -; A=49-104.
PDB; 2MVW; NMR; -; A/B=120-168.
PDB; 2MWX; NMR; -; A=49-104.
PDB; 4WJN; X-ray; 1.50 A; B=547-573.
PDB; 4WJO; X-ray; 1.46 A; B=547-573.
PDBsum; 1BOR; -.
PDBsum; 2MVW; -.
PDBsum; 2MWX; -.
PDBsum; 4WJN; -.
PDBsum; 4WJO; -.
ProteinModelPortal; P29590; -.
SMR; P29590; -.
BioGrid; 111384; 243.
DIP; DIP-33053N; -.
IntAct; P29590; 98.
MINT; MINT-158826; -.
STRING; 9606.ENSP00000268058; -.
iPTMnet; P29590; -.
PhosphoSitePlus; P29590; -.
BioMuta; PML; -.
DMDM; 215274219; -.
EPD; P29590; -.
MaxQB; P29590; -.
PaxDb; P29590; -.
PeptideAtlas; P29590; -.
PRIDE; P29590; -.
DNASU; 5371; -.
Ensembl; ENST00000268058; ENSP00000268058; ENSG00000140464. [P29590-1]
Ensembl; ENST00000268059; ENSP00000268059; ENSG00000140464. [P29590-8]
Ensembl; ENST00000354026; ENSP00000315434; ENSG00000140464. [P29590-13]
Ensembl; ENST00000359928; ENSP00000353004; ENSG00000140464. [P29590-14]
Ensembl; ENST00000395132; ENSP00000378564; ENSG00000140464. [P29590-10]
Ensembl; ENST00000395135; ENSP00000378567; ENSG00000140464. [P29590-5]
Ensembl; ENST00000435786; ENSP00000395576; ENSG00000140464. [P29590-2]
Ensembl; ENST00000436891; ENSP00000394642; ENSG00000140464. [P29590-4]
Ensembl; ENST00000564428; ENSP00000457023; ENSG00000140464. [P29590-12]
Ensembl; ENST00000565898; ENSP00000455838; ENSG00000140464. [P29590-11]
Ensembl; ENST00000567543; ENSP00000456277; ENSG00000140464. [P29590-14]
Ensembl; ENST00000569477; ENSP00000455612; ENSG00000140464. [P29590-9]
Ensembl; ENST00000569965; ENSP00000456486; ENSG00000140464. [P29590-4]
GeneID; 5371; -.
KEGG; hsa:5371; -.
UCSC; uc002awk.4; human. [P29590-1]
CTD; 5371; -.
DisGeNET; 5371; -.
GeneCards; PML; -.
HGNC; HGNC:9113; PML.
HPA; CAB010194; -.
HPA; CAB016304; -.
HPA; HPA008312; -.
MalaCards; PML; -.
MIM; 102578; gene.
neXtProt; NX_P29590; -.
OpenTargets; ENSG00000140464; -.
Orphanet; 520; Acute promyelocytic leukemia.
PharmGKB; PA33439; -.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00510000048454; -.
HOVERGEN; HBG000552; -.
InParanoid; P29590; -.
KO; K10054; -.
OMA; METAEPQ; -.
OrthoDB; EOG091G02GY; -.
PhylomeDB; P29590; -.
TreeFam; TF336434; -.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-877300; Interferon gamma signaling.
SignaLink; P29590; -.
SIGNOR; P29590; -.
ChiTaRS; PML; human.
EvolutionaryTrace; P29590; -.
GeneWiki; Promyelocytic_leukemia_protein; -.
GenomeRNAi; 5371; -.
PMAP-CutDB; P29590; -.
PRO; PR:P29590; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140464; -.
CleanEx; HS_PML; -.
ExpressionAtlas; P29590; baseline and differential.
Genevisible; P29590; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0032183; F:SUMO binding; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0051974; P:negative regulation of telomerase activity; IMP:UniProtKB.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032938; P:negative regulation of translation in response to oxidative stress; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0030578; P:PML body organization; IDA:UniProtKB.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:UniProtKB.
GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; IEA:Ensembl.
GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
GO; GO:0010522; P:regulation of calcium ion transport into cytosol; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2000779; P:regulation of double-strand break repair; IMP:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0009411; P:response to UV; IEA:Ensembl.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
GO; GO:0007184; P:SMAD protein import into nucleus; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
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;
3D-structure; Acetylation; Activator; Alternative splicing;
Antiviral defense; Apoptosis; Biological rhythms;
Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm;
DNA-binding; Endoplasmic reticulum; Endosome; Host-virus interaction;
Immunity; Innate immunity; Isopeptide bond; Membrane; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Repeat; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 882 Protein PML.
/FTId=PRO_0000056001.
ZN_FING 57 92 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 124 166 B box-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 183 236 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
REGION 448 555 Interaction with PER2.
{ECO:0000269|PubMed:22274616}.
REGION 556 562 Sumo interaction motif (SIM).
COILED 228 253 {ECO:0000255}.
MOTIF 476 490 Nuclear localization signal.
COMPBIAS 3 46 Pro-rich.
METAL 57 57 Zinc 1.
METAL 60 60 Zinc 1.
METAL 72 72 Zinc 2.
METAL 74 74 Zinc 2.
METAL 77 77 Zinc 1.
METAL 80 80 Zinc 1.
METAL 88 88 Zinc 2.
METAL 91 91 Zinc 2.
SITE 394 395 Breakpoint for translocation to form PML-
RARA oncogene in type A APL.
SITE 552 553 Breakpoint for translocation to form PML-
RARA oncogene in type B APL.
MOD_RES 8 8 Phosphoserine; by HIPK2.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19015637}.
MOD_RES 28 28 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:15195100}.
MOD_RES 36 36 Phosphoserine; by HIPK2 and MAPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15195100}.
MOD_RES 38 38 Phosphoserine; by HIPK2 and MAPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015637}.
MOD_RES 40 40 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:15195100}.
MOD_RES 42 42 Phosphothreonine.
{ECO:0000269|PubMed:15195100}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 117 117 Phosphoserine; by CHEK2.
{ECO:0000269|PubMed:12402044}.
MOD_RES 403 403 Phosphoserine; by MAPK1 and MAPK7.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22033920}.
MOD_RES 409 409 Phosphothreonine; by MAPK7.
{ECO:0000269|PubMed:15195100}.
MOD_RES 487 487 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18621739,
ECO:0000269|PubMed:22274616}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:Q60953}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000250|UniProtKB:Q60953}.
MOD_RES 505 505 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22033920}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 515 515 N6-acetyllysine.
{ECO:0000305|PubMed:18621739}.
MOD_RES 518 518 Phosphoserine; by CDK1 and CDK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:21840486,
ECO:0000269|PubMed:22033920}.
MOD_RES 527 527 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22033920}.
MOD_RES 530 530 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000269|PubMed:15195100}.
MOD_RES 565 565 Phosphoserine; by CK2.
{ECO:0000269|PubMed:22406621}.
MOD_RES 867 867 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 380 380 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 380 380 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:18408734}.
CROSSLNK 394 394 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 400 400 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18408734}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:18408734}.
CROSSLNK 460 460 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:18408734}.
CROSSLNK 478 478 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 487 487 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 497 497 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 497 497 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 419 466 Missing (in isoform PML-11, isoform PML-
12 and isoform PML-13).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7, ECO:0000303|Ref.8}.
/FTId=VSP_040590.
VAR_SEQ 419 435 PEEAERVKAQVQALGLA -> LPPPAHALTGPAQSSTH
(in isoform PML-7).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_040591.
VAR_SEQ 419 423 PEEAE -> RNALW (in isoform PML-14).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_040592.
VAR_SEQ 424 882 Missing (in isoform PML-14).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_040593.
VAR_SEQ 436 882 Missing (in isoform PML-7).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_040594.
VAR_SEQ 553 560 EERVVVIS -> GRERNALW (in isoform PML-6).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1652368,
ECO:0000303|Ref.6}.
/FTId=VSP_005742.
VAR_SEQ 561 882 Missing (in isoform PML-6).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1652368,
ECO:0000303|Ref.6}.
/FTId=VSP_005743.
VAR_SEQ 571 882 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
FFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKA
VSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALED
INRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYL
ARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSL
QCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDR
QGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGP
ALARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQS
SPAHSSPAHSSPAHSSPVQSLLRAQGASSLPCGTYHPPAWP
PHQPAEQAATPDAEPHSEPPDHQERPAVHRGIRYLLYRAQR
AIRLRHALRLHPQLHRAPIRTWSPHVVQASTPAITGPLNHP
ANAQEHPAQLQRGISPPHRIRGAVRSRSRSLRGSSHLSQWL
NNFFALPFSSMASQLDMSSVVGAGESRAQTLGAGVPPGDSV
RGSMEASQVQVPLEASPITFPPPCAPERPPISPVPGARQAG
L (in isoform PML-2 and isoform PML-13).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7}.
/FTId=VSP_040595.
VAR_SEQ 571 882 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
FFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKA
VSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALED
INRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYL
ARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSL
QCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDR
QGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGP
ALARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQS
SPAHSSPAHSSPVQSLLRAQGASSLPCGTYHPPAWPPHQPA
EQAATPDAEPHSEPPDHQERPAVHRGIRYLLYRAQRAIRLR
HALRLHPQLHRAPIRTWSPHVVQASTPAITGPLNHPANAQE
HPAQLQRGISPPHRIRGAVRSRSRSLRGSSHLSQWLNNFFA
LPFSSMASQLDMSSVVGAGESRAQTLGAGVPPGDSVRGSME
ASQVQVPLEASPITFPPPCAPERPPISPVPGARQAGL (in
isoform PML-8).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570}.
/FTId=VSP_005741.
VAR_SEQ 571 641 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
FFDLKIDNETQKISQLAAVNRESKFRVVIQ -> VSSSPQS
EVLYWKVHGAHGDRRATVLASPLLASPLLASPLLASPVSAE
STRSLQPALWHIPPPSLASPPAR (in isoform PML-
3). {ECO:0000303|PubMed:1652369}.
/FTId=VSP_040596.
VAR_SEQ 571 611 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
-> VSGPEVQPRTPASPHFRSQGAQPQQVTLRLALRLGNFP
VRH (in isoform PML-5).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570}.
/FTId=VSP_005739.
VAR_SEQ 612 882 Missing (in isoform PML-5).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570}.
/FTId=VSP_005740.
VAR_SEQ 621 633 TQKISQLAAVNRE -> SGFSWGYPHPFLI (in
isoform PML-4 and isoform PML-12).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1311253}.
/FTId=VSP_005744.
VAR_SEQ 634 882 Missing (in isoform PML-4 and isoform
PML-12). {ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1311253}.
/FTId=VSP_005745.
VAR_SEQ 642 882 Missing (in isoform PML-3).
{ECO:0000303|PubMed:1652369}.
/FTId=VSP_040597.
VARIANT 645 645 F -> L (in dbSNP:rs5742915).
{ECO:0000269|PubMed:11331580,
ECO:0000269|PubMed:1720570}.
/FTId=VAR_052090.
MUTAGEN 57 57 C->S: Strongly reduced sumoylation; when
associated with S-60.
{ECO:0000269|PubMed:17081985}.
MUTAGEN 60 60 C->S: Strongly reduced sumoylation; when
associated with S-57.
{ECO:0000269|PubMed:17081985}.
MUTAGEN 65 65 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.
{ECO:0000269|PubMed:9756909}.
MUTAGEN 68 68 K->R: No effect on sumoylation levels.
MUTAGEN 88 88 C->S: No nuclear microspeckle location,
no sumoylation and loss of intrinsic
transcriptional repressor activity of
PML-RARA oncoprotein; when associated
with R-89. {ECO:0000269|PubMed:15809060}.
MUTAGEN 89 89 P->R: No nuclear microspeckle location,
no sumoylation and loss of intrinsic
transcriptional repressor activity of
PML-RARA oncoprotein; when associated
with S-88. {ECO:0000269|PubMed:15809060}.
MUTAGEN 133 133 K->R: Loss of 2 sumoylations; when
associated with R-65 and R-490.
{ECO:0000269|PubMed:9756909}.
MUTAGEN 150 150 K->R: Loss of 2 sumoylations; when
associated with R-65 and R-490.
{ECO:0000269|PubMed:9756909}.
MUTAGEN 160 160 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. {ECO:0000269|PubMed:9756909}.
MUTAGEN 487 487 K->A: Loss of nuclear localization; when
associated with A-490.
{ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:18621739}.
MUTAGEN 487 487 K->R: Loss of nuclear localization.
Reduced acetylation. Further decrease in
acetylation; when associated with R-515.
{ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:18621739}.
MUTAGEN 490 490 K->A: Loss of nuclear localization; when
associated with A-487.
{ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:9756909}.
MUTAGEN 490 490 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.
{ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:9756909}.
MUTAGEN 515 515 K->R: Slightly reduced acetylation.
Further decrease in acetylation; when
associated with R-487.
{ECO:0000269|PubMed:18621739}.
MUTAGEN 518 518 S->A: Abolishes ubiquitination by the
BCR(KLHL20) E3 ubiquitin ligase complex.
{ECO:0000269|PubMed:21840486}.
MUTAGEN 556 559 VVVI->AAAS: Abolishes SUMO1 binding.
CONFLICT 224 224 E -> D (in Ref. 7; AAP88913 and 10;
AAH00080/AAH20994). {ECO:0000305}.
CONFLICT 419 419 P -> A (in Ref. 2; AAA60351/AAA60388/
AAA60390, 4; AAA60352 and 5; AAG50182/
AAG50184/AAG50185). {ECO:0000305}.
STRAND 58 60 {ECO:0000244|PDB:1BOR}.
STRAND 82 87 {ECO:0000244|PDB:1BOR}.
HELIX 90 92 {ECO:0000244|PDB:2MWX}.
STRAND 93 96 {ECO:0000244|PDB:1BOR}.
TURN 130 132 {ECO:0000244|PDB:2MVW}.
STRAND 133 140 {ECO:0000244|PDB:2MVW}.
TURN 141 143 {ECO:0000244|PDB:2MVW}.
STRAND 146 148 {ECO:0000244|PDB:2MVW}.
HELIX 149 158 {ECO:0000244|PDB:2MVW}.
STRAND 163 166 {ECO:0000244|PDB:2MVW}.
STRAND 556 558 {ECO:0000244|PDB:4WJO}.
SEQUENCE 882 AA; 97551 MW; D50968A977E34287 CRC64;
MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC
QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR
QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG
TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL
DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA
VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR
QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE
EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS
QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP
NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL
ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ
HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG
ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS
LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA
FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS


Related products :

Catalog number Product name Quantity
EIAAB31648 Homo sapiens,Human,MYL,PML,Promyelocytic leukemia protein,Protein PML,RING finger protein 71,RNF71,TRIM19,Tripartite motif-containing protein 19
EIAAB43990 BERP,Brain-expressed RING finger protein,Homo sapiens,Human,RING finger protein 22,RING finger protein 97,RNF22,RNF97,TRIM3,Tripartite motif-containing protein 3
EIAAB43957 Mouse,Mus musculus,RING finger B-box coiled-coil transcription factor,RING finger protein 36,Rnf36,Testis-specific RING finger protein,Trif,Trim69,Tripartite motif-containing protein 69
18-003-42487 Ret finger protein 2 - Leukemia-associated protein 5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Putative tumor suppressor RFP2; Tripartite motif-containing protein 13; RING finger pro 0.05 mg Aff Pur
18-003-42488 Ret finger protein 2 - Leukemia-associated protein 5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Putative tumor suppressor RFP2; Tripartite motif-containing protein 13; RING finger pro 0.1 mg Protein A
18-003-42578 Tripartite motif-containing protein 3 - RING finger protein 22; Brain-expressed RING finger protein; RING finger protein 97 Polyclonal 0.1 mg Protein A
EIAAB43873 Acid finger protein,AFP,Homo sapiens,Human,RING finger protein 95,RNF95,TRIM26,Tripartite motif-containing protein 26,Zinc finger protein 173,ZNF173
EIAAB43989 Berp,Brain-expressed RING finger protein,Rat,Rattus norvegicus,RING finger protein 22,Rnf22,Trim3,Tripartite motif-containing protein 3
EIAAB43920 Homo sapiens,Human,RING finger protein 18,RNF18,Testis-specific RING-finger protein,TRIM49,Tripartite motif-containing protein 49
EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB43875 Homo sapiens,Human,Ret finger protein,RFP,RING finger protein 76,RNF76,TRIM27,Tripartite motif-containing protein 27,Zinc finger protein RFP
EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB43999 Gerp,Glioblastoma-expressed RING finger protein,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,Rnf27,Trim8,Tripartite motif-containing protein 8
EIAAB43940 Homo sapiens,Human,RING finger protein 129,RING finger protein 33,RNF129,RNF33,TRIM60,Tripartite motif-containing protein 60
EIAAB43841 B30-RING finger protein,Homo sapiens,Human,RFB30,RING finger protein 9,RNF9,TRIM10,Tripartite motif-containing protein 10
EIAAB43844 B30-RING finger protein,Pig,RFB30,RING finger protein 9,RNF9,Sus scrofa,TRIM10,Tripartite motif-containing protein 10
EIAAB43931 Homo sapiens,Human,MuRF2,MURF2,MuRF-2,Muscle-specific RING finger protein 2,RING finger protein 29,RNF29,TRIM55,Tripartite motif-containing protein 55
EIAAB43855 Homo sapiens,Human,RING finger protein 93,RNF93,TRIM15,Tripartite motif-containing protein 15,Zinc finger protein 178,Zinc finger protein B7,ZNF178,ZNFB7
18-003-44063 GTP-binding protein ARD-1 - ADP-ribosylation factor domain-containing protein 1; Tripartite motif-containing protein 23; RING finger protein 46 Polyclonal 0.1 mg Protein A
EIAAB43930 MuRF2,Murf2,MuRF-2,Muscle-specific RING finger protein 2,Rat,Rattus norvegicus,RING finger protein 29,Rnf29,Trim55,Tripartite motif-containing protein 55
18-003-43884 Midline-1 - EC 6.3.2.-; Tripartite motif-containing protein 18; Putative transcription factor XPRF; Midin; RING finger protein 59; Midline 1 RING finger protein Polyclonal 0.1 mg Protein A
EIAAB43843 Hematopoietic RING finger 1,Herf1,Mouse,Mus musculus,RING finger protein 9,Rnf9,Trim10,Tripartite motif-containing protein 10
EIAAB43898 Mouse,Mus musculus,RING finger protein 23,Rnf23,Testis-abundant finger protein,Tfp,Trim39,Tripartite motif-containing protein 39
EIAAB43897 Homo sapiens,Human,RING finger protein 23,RNF23,Testis-abundant finger protein,TFP,TRIM39,Tripartite motif-containing protein 39
EIAAB43887 Homo sapiens,Human,IFP1,Interferon-responsive finger protein 1,RING finger protein 21,RNF21,TRIM34,Tripartite motif-containing protein 34


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur