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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.
17-JUN-2020, entry version 242.
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; DOI=10.1002/j.1460-2075.1992.tb05095.x;
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; DOI=10.1080/1042819021000040305;
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 (MICROBIAL INFECTION).
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]
SUMOYLATION AT LYS-65; LYS-160 AND LYS-490.
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).
[18]
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).
[19]
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).
[20]
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).
[21]
FUNCTION IN HUMAN FOAMY VIRUS RESTRICTION, INTERACTION WITH HUMAN FOAMY
VIRUS BEL1 AND BET (MICROBIAL INFECTION), 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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
INTERACTION OF PML-4 AND PML-5 WITH HADV5 E1B-55K (MICROBIAL INFECTION).
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).
[56]
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).
[57]
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).
[58]
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).
[59]
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).
[60]
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).
[61]
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).
[62]
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).
[63]
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).
[64]
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).
[65]
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).
[66]
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).
[67]
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).
[68]
FUNCTION IN EMCV RESTRICTION, AND INTERACTION WITH EMCV P3D-POL (MICROBIAL
INFECTION).
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).
[69]
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).
[70]
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).
[71]
FUNCTION IN VARICELLA ZOSTER RESTRICTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH VZV VP26 (MICROBIAL INFECTION).
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).
[72]
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).
[73]
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).
[74]
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).
[75]
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).
[76]
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).
[77]
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).
[78]
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).
[79]
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).
[80]
INTERACTION WITH MOMLV IN AND RT (MICROBIAL INFECTION), 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).
[81]
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).
[82]
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).
[83]
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).
[84]
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).
[85]
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).
[86]
INTERACTION WITH HHV-1 ICP0 (MICROBIAL INFECTION).
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).
[87]
INTERACTION WITH TRIM16.
PubMed=22629402; DOI=10.1371/journal.pone.0037470;
Bell J.L., Malyukova A., Holien J.K., Koach J., Parker M.W., Kavallaris M.,
Marshall G.M., Cheung B.B.;
"TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other
TRIM family members.";
PLoS ONE 7:E37470-E37470(2012).
[88]
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).
[89]
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).
[90]
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).
[91]
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).
[92]
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).
[93]
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).
[94]
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).
[95]
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).
[96]
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).
[97]
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).
[98]
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).
[99]
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).
[100]
INTERACTION OF PML-4 AND PML-5 WITH HADV5 E1B-55K (MICROBIAL INFECTION).
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).
[101]
SUMOYLATION AT LYS-160; LYS-380; LYS-400; LYS-490 AND LYS-497, MUTAGENESIS
OF LYS-65; LYS-160; LYS-380; LYS-400; LYS-490 AND LYS-497, AND SUBCELLULAR
LOCATION.
PubMed=27211601; DOI=10.1038/srep26509;
Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
"SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
Sci. Rep. 6:26509-26509(2016).
[102]
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).
[103]
STRUCTURE BY NMR OF 49-104.
PubMed=7729428; DOI=10.1002/j.1460-2075.1995.tb07139.x;
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 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. Interacts with TRIM16.
{ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:10669754,
ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:11025664,
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:21639834, 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:22629402,
ECO:0000269|PubMed:22869143, ECO:0000269|PubMed:23007646,
ECO:0000269|PubMed:23028697, ECO:0000269|PubMed:23430110,
ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:9570750}.
-!- SUBUNIT: (Microbial infection) Interacts with Lassa virus Z protein and
rabies virus phosphoprotein. {ECO:0000269|PubMed:9420283}.
-!- SUBUNIT: (Microbial infection) Isoform PML-1 interacts with herpes
simplex virus-1/HHV-1 ICP0. {ECO:0000269|PubMed:22875967}.
-!- SUBUNIT: (Microbial infection) Isoform PML-2 interacts with human
adenovirus 2 E1A and this interaction stimulates E1A-dependent
transcriptional activation. {ECO:0000269|PubMed:23135708}.
-!- SUBUNIT: (Microbial infection) Isoform PML-4 interacts with VZV capsid
protein VP26/ORF23 capsid protein. {ECO:0000269|PubMed:21304940}.
-!- SUBUNIT: (Microbial infection) The sumoylated isoform PML-4 interacts
with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-
POL (P3D-POL). {ECO:0000269|PubMed:21994459}.
-!- SUBUNIT: (Microbial infection) Isoform PML-6 interacts with moloney
murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase
(RT). {ECO:0000269|PubMed:22685230}.
-!- SUBUNIT: (Microbial infection) 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.
{ECO:0000269|PubMed:20639899, ECO:0000269|PubMed:23135708,
ECO:0000269|PubMed:25772236}.
-!- SUBUNIT: (Microbial infection) Isoform PML-3 interacts with human foamy
virus bel1/tas and bet. {ECO:0000269|PubMed:11432836}.
-!- INTERACTION:
P29590; P68400: CSNK2A1; NbExp=2; IntAct=EBI-295890, EBI-347804;
P29590; Q9UER7: DAXX; NbExp=6; IntAct=EBI-295890, EBI-77321;
P29590; P25445: FAS; NbExp=4; IntAct=EBI-295890, EBI-494743;
P29590; Q9Y2M5: KLHL20; NbExp=9; IntAct=EBI-295890, EBI-714379;
P29590; Q13164: MAPK7; NbExp=6; IntAct=EBI-295890, EBI-1213983;
P29590; Q00987: MDM2; NbExp=6; IntAct=EBI-295890, EBI-389668;
P29590; O15055: PER2; NbExp=3; IntAct=EBI-295890, EBI-1054296;
P29590; P25788: PSMA3; NbExp=2; IntAct=EBI-295890, EBI-348380;
P29590; P63165: SUMO1; NbExp=6; IntAct=EBI-295890, EBI-80140;
P29590; Q13207: TBX2; NbExp=2; IntAct=EBI-295890, EBI-2853051;
P29590; Q6N021: TET2; NbExp=2; IntAct=EBI-295890, EBI-310727;
P29590; Q15583: TGIF1; NbExp=3; IntAct=EBI-295890, EBI-714215;
P29590; P04637: TP53; NbExp=4; IntAct=EBI-295890, EBI-366083;
P29590; Q05516: ZBTB16; NbExp=7; IntAct=EBI-295890, EBI-711925;
P29590; Q8UN00: gag-pro-pol; Xeno; NbExp=4; IntAct=EBI-295890, EBI-6692904;
P29590; P03243-1; Xeno; NbExp=3; IntAct=EBI-295890, EBI-1927377;
P29590; PRO_0000037566 [P27958]; Xeno; NbExp=6; IntAct=EBI-295890, EBI-6377335;
P29590-2; P03243-1; Xeno; NbExp=3; IntAct=EBI-303996, EBI-1927377;
P29590-3; P04489; Xeno; NbExp=4; IntAct=EBI-8099068, EBI-6398911;
P29590-5; Q00987: MDM2; NbExp=6; IntAct=EBI-304008, EBI-389668;
P29590-5; O14746: TERT; NbExp=7; IntAct=EBI-304008, EBI-1772203;
P29590-5; Q05516: ZBTB16; NbExp=2; IntAct=EBI-304008, EBI-711925;
P29590-5; P03243-1; Xeno; NbExp=3; IntAct=EBI-304008, EBI-1927377;
P29590-5; PRO_0000039791 [P03304]; Xeno; NbExp=3; IntAct=EBI-304008, EBI-6726189;
P29590-9; P63165: SUMO1; NbExp=2; IntAct=EBI-6861318, EBI-80140;
P29590-13; P29590-13: PML; NbExp=3; IntAct=EBI-12368281, EBI-12368281;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm. Cytoplasm
{ECO:0000269|PubMed:27211601}. Nucleus, PML body
{ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:27211601}. 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;
Name=PML-6; Synonyms=PML-3B, PML-VI, TRIM19epsilon;
IsoId=P29590-4; Sequence=VSP_005742, VSP_005743;
Name=PML-7; Synonyms=PML-VII, TRIM19theta;
IsoId=P29590-10; Sequence=VSP_040591, VSP_040594;
Name=PML-8; Synonyms=PML-2G, PML-IIG, TRIM19gamma;
IsoId=P29590-3; Sequence=VSP_005741;
Name=PML-11; Synonyms=PML-1A, PML-IA;
IsoId=P29590-11; Sequence=VSP_040590;
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. SUMO1P1/SUMO5 conjugated PML at
Lys-160, Lys-380, Lys-400, Lys-490 and Lys-497, but Lys-380, Lys-400
and Lys-497 are not key acceptor lysines. SUMO1P1/SUMO5 forms polymeric
chain on Lys-160 of PML by successive conjugation at 'Lys-18';
facilitating recruitment of PML-NB components, which enlarges PML.
SUMO1P1/SUMO5 conjugation of PML increases SUMO2/3 conjugation, which
leads to the recruitment of RNF4 and ubiquitin-dependent disintegration
of PML-NBs. SUMO1P1/SUMO5 monoconjugated Lys-490 (PubMed:27211601). DNA
damage triggers its sumoylation while some but not all viral infections
can abolish sumoylation. Desumoylated by SENP1, SENP2, SENP3, SENP5 and
SENP6 (PubMed:27211601, PubMed:12419228, PubMed:21148299). Arsenic
induces PML and PML-RARA polysumoylation and their subsequent RNF4-
dependent ubiquitination and proteasomal degradation, and is used as
treatment in acute promyelocytic leukemia (APL). The nuclear isoforms
(isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform
PML-5 and isoform PML-6) show an increased sumoylation in response to
arsenic trioxide. The cytoplasmic isoform PML-7 is not sumoylated.
{ECO:0000269|PubMed:12419228, ECO:0000269|PubMed:18408734,
ECO:0000269|PubMed:21148299, ECO:0000269|PubMed:22155184,
ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:27211601,
ECO:0000269|PubMed:9756909}.
-!- PTM: Phosphorylation is a major regulatory mechanism that controls PML
protein abundance and the number and size of PML nuclear bodies (PML-
NBs). Phosphorylated in response to DNA damage, probably by ATR. 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 apoptosis
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}.
-!- MISCELLANEOUS: [Isoform PML-8]: Non-canonical splice sites. Might
alternatively represent a polymorphic variation. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA60351.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAA60352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAA60388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAA60390.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAB62809.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
Sequence=BAD92648.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PMLID41.html";
---------------------------------------------------------------------------
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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]
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.
PDB; 5YUF; X-ray; 1.60 A; A/B/C/D=49-99.
PDB; 6IMQ; X-ray; 2.06 A; A/B/C/D=120-168.
PDB; 6UYO; X-ray; 1.64 A; B/D=547-574.
PDB; 6UYP; X-ray; 1.42 A; B=547-574.
PDB; 6UYQ; X-ray; 1.50 A; B=547-574.
PDB; 6UYR; X-ray; 1.30 A; B=547-574.
PDB; 6UYS; X-ray; 1.59 A; B/D=547-574.
PDB; 6UYT; X-ray; 1.66 A; B=547-574.
PDB; 6UYU; X-ray; 1.66 A; B/D=547-574.
PDB; 6UYV; X-ray; 1.40 A; B=547-574.
PDBsum; 1BOR; -.
PDBsum; 2MVW; -.
PDBsum; 2MWX; -.
PDBsum; 4WJN; -.
PDBsum; 4WJO; -.
PDBsum; 5YUF; -.
PDBsum; 6IMQ; -.
PDBsum; 6UYO; -.
PDBsum; 6UYP; -.
PDBsum; 6UYQ; -.
PDBsum; 6UYR; -.
PDBsum; 6UYS; -.
PDBsum; 6UYT; -.
PDBsum; 6UYU; -.
PDBsum; 6UYV; -.
SMR; P29590; -.
BioGRID; 111384; 272.
CORUM; P29590; -.
DIP; DIP-33053N; -.
IntAct; P29590; 123.
MINT; P29590; -.
STRING; 9606.ENSP00000268058; -.
DrugBank; DB01169; Arsenic trioxide.
iPTMnet; P29590; -.
PhosphoSitePlus; P29590; -.
BioMuta; PML; -.
DMDM; 215274219; -.
EPD; P29590; -.
jPOST; P29590; -.
MassIVE; P29590; -.
MaxQB; P29590; -.
PaxDb; P29590; -.
PeptideAtlas; P29590; -.
PRIDE; P29590; -.
ProteomicsDB; 19281; -.
ProteomicsDB; 54589; -. [P29590-1]
ProteomicsDB; 54590; -. [P29590-10]
ProteomicsDB; 54591; -. [P29590-11]
ProteomicsDB; 54592; -. [P29590-12]
ProteomicsDB; 54593; -. [P29590-13]
ProteomicsDB; 54594; -. [P29590-14]
ProteomicsDB; 54595; -. [P29590-2]
ProteomicsDB; 54596; -. [P29590-3]
ProteomicsDB; 54597; -. [P29590-4]
ProteomicsDB; 54598; -. [P29590-5]
ProteomicsDB; 54599; -. [P29590-8]
ProteomicsDB; 54600; -. [P29590-9]
Antibodypedia; 1737; 572 antibodies.
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; -.
EuPathDB; HostDB:ENSG00000140464.19; -.
GeneCards; PML; -.
HGNC; HGNC:9113; PML.
HPA; ENSG00000140464; Low tissue specificity.
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; -.
HOGENOM; CLU_009136_1_0_1; -.
InParanoid; P29590; -.
KO; K10054; -.
OMA; CCICALL; -.
OrthoDB; 421875at2759; -.
PhylomeDB; P29590; -.
TreeFam; TF336434; -.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8948747; Regulation of PTEN localization.
Reactome; R-HSA-9609690; HCMV Early Events.
Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. [P29590-4]
SignaLink; P29590; -.
SIGNOR; P29590; -.
BioGRID-ORCS; 5371; 8 hits in 791 CRISPR screens.
ChiTaRS; PML; human.
EvolutionaryTrace; P29590; -.
GeneWiki; Promyelocytic_leukemia_protein; -.
GenomeRNAi; 5371; -.
Pharos; P29590; Tbio.
PRO; PR:P29590; -.
Proteomes; UP000005640; Chromosome 15.
RNAct; P29590; protein.
Bgee; ENSG00000140464; Expressed in left lobe of thyroid gland and 198 other tissues.
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; IBA:GO_Central.
GO; GO:0032183; F:SUMO binding; IPI:UniProtKB.
GO; GO:0140037; F:sumo-dependent protein 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 population 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: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:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP: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: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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; 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: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; 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
/note="Protein PML"
/id="PRO_0000056001"
ZN_FING 57..92
/note="RING-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 124..166
/note="B box-type 1; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
ZN_FING 183..236
/note="B box-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
REGION 448..555
/note="Interaction with PER2"
/evidence="ECO:0000269|PubMed:22274616"
REGION 556..562
/note="Sumo interaction motif (SIM)"
COILED 228..253
/evidence="ECO:0000255"
MOTIF 476..490
/note="Nuclear localization signal"
COMPBIAS 3..46
/note="Pro-rich"
METAL 57
/note="Zinc 1"
METAL 60
/note="Zinc 1"
METAL 72
/note="Zinc 2"
METAL 74
/note="Zinc 2"
METAL 77
/note="Zinc 1"
METAL 80
/note="Zinc 1"
METAL 88
/note="Zinc 2"
METAL 91
/note="Zinc 2"
SITE 394..395
/note="Breakpoint for translocation to form PML-RARA
oncogene in type A APL"
SITE 552..553
/note="Breakpoint for translocation to form PML-RARA
oncogene in type B APL"
MOD_RES 8
/note="Phosphoserine; by HIPK2"
/evidence="ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19015637"
MOD_RES 36
/note="Phosphoserine; by HIPK2 and MAPK1"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 38
/note="Phosphoserine; by HIPK2 and MAPK1"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015637"
MOD_RES 48
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 117
/note="Phosphoserine; by CHEK2"
/evidence="ECO:0000269|PubMed:12402044"
MOD_RES 403
/note="Phosphoserine; by MAPK1 and MAPK7"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569, ECO:0000269|PubMed:22033920"
MOD_RES 487
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000269|PubMed:18621739,
ECO:0000269|PubMed:22274616"
MOD_RES 493
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q60953"
MOD_RES 504
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q60953"
MOD_RES 505
/note="Phosphoserine; by MAPK1"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22033920"
MOD_RES 512
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 515
/note="N6-acetyllysine"
/evidence="ECO:0000305|PubMed:18621739"
MOD_RES 518
/note="Phosphoserine; by CDK1 and CDK2"
/evidence="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
/note="Phosphoserine; by MAPK1"
/evidence="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
/note="Phosphoserine; by MAPK1"
/evidence="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 565
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:22406621"
MOD_RES 867
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 65
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0000269|PubMed:10779416"
CROSSLNK 65
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 160
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0000269|PubMed:10779416"
CROSSLNK 160
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1P1/SUMO5); alternate"
/evidence="ECO:0000269|PubMed:27211601"
CROSSLNK 160
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733"
CROSSLNK 380
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in /SUMO5); alternate"
/evidence="ECO:0000269|PubMed:27211601"
CROSSLNK 380
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
CROSSLNK 380
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:18408734"
CROSSLNK 394
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733"
CROSSLNK 400
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1P1/SUMO5); alternate"
/evidence="ECO:0000269|PubMed:27211601"
CROSSLNK 400
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:18408734"
CROSSLNK 401
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 401
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:18408734"
CROSSLNK 460
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 476
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 476
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:18408734"
CROSSLNK 478
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733"
CROSSLNK 487
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 490
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0000269|PubMed:10779416"
CROSSLNK 490
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1P1/SUMO5); alternate"
/evidence="ECO:0000269|PubMed:27211601"
CROSSLNK 490
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 497
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
CROSSLNK 497
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1P1/SUMO5); alternate"
/evidence="ECO:0000269|PubMed:27211601"
CROSSLNK 497
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 419..466
/note="Missing (in isoform PML-11, isoform PML-12 and
isoform PML-13)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7,
ECO:0000303|Ref.8"
/id="VSP_040590"
VAR_SEQ 419..435
/note="PEEAERVKAQVQALGLA -> LPPPAHALTGPAQSSTH (in isoform
PML-7)"
/evidence="ECO:0000303|PubMed:11331580"
/id="VSP_040591"
VAR_SEQ 419..423
/note="PEEAE -> RNALW (in isoform PML-14)"
/evidence="ECO:0000303|PubMed:11331580"
/id="VSP_040592"
VAR_SEQ 424..882
/note="Missing (in isoform PML-14)"
/evidence="ECO:0000303|PubMed:11331580"
/id="VSP_040593"
VAR_SEQ 436..882
/note="Missing (in isoform PML-7)"
/evidence="ECO:0000303|PubMed:11331580"
/id="VSP_040594"
VAR_SEQ 553..560
/note="EERVVVIS -> GRERNALW (in isoform PML-6)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1652368, ECO:0000303|Ref.6"
/id="VSP_005742"
VAR_SEQ 561..882
/note="Missing (in isoform PML-6)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1652368, ECO:0000303|Ref.6"
/id="VSP_005743"
VAR_SEQ 571..882
/note="SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQ
KISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWG
PGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSE
RSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLA
LHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPA
LARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQSSPAHSSPAHSSPAHSSPVQ
SLLRAQGASSLPCGTYHPPAWPPHQPAEQAATPDAEPHSEPPDHQERPAVHRGIRYLLY
RAQRAIRLRHALRLHPQLHRAPIRTWSPHVVQASTPAITGPLNHPANAQEHPAQLQRGI
SPPHRIRGAVRSRSRSLRGSSHLSQWLNNFFALPFSSMASQLDMSSVVGAGESRAQTLG
AGVPPGDSVRGSMEASQVQVPLEASPITFPPPCAPERPPISPVPGARQAGL (in
isoform PML-2 and isoform PML-13)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7"
/id="VSP_040595"
VAR_SEQ 571..882
/note="SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQ
KISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWG
PGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSE
RSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLA
LHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPA
LARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQSSPAHSSPAHSSPVQSLLRA
QGASSLPCGTYHPPAWPPHQPAEQAATPDAEPHSEPPDHQERPAVHRGIRYLLYRAQRA
IRLRHALRLHPQLHRAPIRTWSPHVVQASTPAITGPLNHPANAQEHPAQLQRGISPPHR
IRGAVRSRSRSLRGSSHLSQWLNNFFALPFSSMASQLDMSSVVGAGESRAQTLGAGVPP
GDSVRGSMEASQVQVPLEASPITFPPPCAPERPPISPVPGARQAGL (in isoform
PML-8)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570"
/id="VSP_005741"
VAR_SEQ 571..641
/note="SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQ
KISQLAAVNRESKFRVVIQ -> VSSSPQSEVLYWKVHGAHGDRRATVLASPLLASPLL
ASPLLASPVSAESTRSLQPALWHIPPPSLASPPAR (in isoform PML-3)"
/evidence="ECO:0000303|PubMed:1652369"
/id="VSP_040596"
VAR_SEQ 571..611
/note="SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV -> VSGPEVQ
PRTPASPHFRSQGAQPQQVTLRLALRLGNFPVRH (in isoform PML-5)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570"
/id="VSP_005739"
VAR_SEQ 612..882
/note="Missing (in isoform PML-5)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1720570"
/id="VSP_005740"
VAR_SEQ 621..633
/note="TQKISQLAAVNRE -> SGFSWGYPHPFLI (in isoform PML-4 and
isoform PML-12)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1311253"
/id="VSP_005744"
VAR_SEQ 634..882
/note="Missing (in isoform PML-4 and isoform PML-12)"
/evidence="ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:1311253"
/id="VSP_005745"
VAR_SEQ 642..882
/note="Missing (in isoform PML-3)"
/evidence="ECO:0000303|PubMed:1652369"
/id="VSP_040597"
VARIANT 645
/note="F -> L (in dbSNP:rs5742915)"
/evidence="ECO:0000269|PubMed:11331580,
ECO:0000269|PubMed:1720570"
/id="VAR_052090"
MUTAGEN 57
/note="C->S: Strongly reduced sumoylation; when associated
with S-60."
/evidence="ECO:0000269|PubMed:17081985"
MUTAGEN 60
/note="C->S: Strongly reduced sumoylation; when associated
with S-57."
/evidence="ECO:0000269|PubMed:17081985"
MUTAGEN 65
/note="K->R: Loss of one sumoylation. No effect on nuclear
body formation. Loss of 2 sumoylations; when associated
with R-490 with or without R-133 or R-150. No effect on
nuclear body formation; when associated with R-490. Loss
the ability to be conjugated by SUMO1P1/SUMO5 but could be
conjugated by SUMO1; when associated with R-160 and R-490."
/evidence="ECO:0000269|PubMed:27211601,
ECO:0000269|PubMed:9756909"
MUTAGEN 65
/note="K->R: Loss of one sumoylation. No effect on nuclear
body formation. Loss of 2 sumoylations; when associated
with R-490 with or without R-133 or R-150. No effect on
nuclear body formation; when associated with R-490. No
sumoylation nor nuclear body formation; when associated
with R-160 and R-490."
/evidence="ECO:0000269|PubMed:9756909"
MUTAGEN 68
/note="K->R: No effect on sumoylation levels."
MUTAGEN 88
/note="C->S: No nuclear microspeckle location, no
sumoylation and loss of intrinsic transcriptional repressor
activity of PML-RARA oncoprotein; when associated with R-
89."
/evidence="ECO:0000269|PubMed:15809060"
MUTAGEN 89
/note="P->R: No nuclear microspeckle location, no
sumoylation and loss of intrinsic transcriptional repressor
activity of PML-RARA oncoprotein; when associated with S-
88."
/evidence="ECO:0000269|PubMed:15809060"
MUTAGEN 133
/note="K->R: Loss of 2 sumoylations; when associated with
R-65 and R-490."
/evidence="ECO:0000269|PubMed:9756909"
MUTAGEN 150
/note="K->R: Loss of 2 sumoylations; when associated with
R-65 and R-490."
/evidence="ECO:0000269|PubMed:9756909"
MUTAGEN 160
/note="K->R: Compromised the formation of high molecular
weight species of SUMO1P1/SUMO5 conjugation on PML. Loss of
2 sumoylations; when associated with or without R-65. No
sumoylation nor nuclear body formation; when associated
with or without R-65 and R-490. Loss the ability to be
conjugated by SUMO1P1/SUMO5 but could be conjugated by
SUMO1; when associated with R-65 and R-490."
/evidence="ECO:0000269|PubMed:27211601,
ECO:0000269|PubMed:9756909"
MUTAGEN 160
/note="K->R: Loss of 2 sumoylations; when associated with
or without R-65. No sumoylation nor nuclear body formation;
when associated with or without R-65 and R-490."
/evidence="ECO:0000269|PubMed:9756909"
MUTAGEN 380
/note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."
/evidence="ECO:0000269|PubMed:27211601"
MUTAGEN 400
/note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."
/evidence="ECO:0000269|PubMed:27211601"
MUTAGEN 487
/note="K->A: Loss of nuclear localization; when associated
with A-490."
/evidence="ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:18621739"
MUTAGEN 487
/note="K->R: Loss of nuclear localization. Reduced
acetylation. Further decrease in acetylation; when
associated with R-515."
/evidence="ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:18621739"
MUTAGEN 490
/note="K->A: Loss of nuclear localization; when associated
with A-487."
/evidence="ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:9756909"
MUTAGEN 490
/note="K->R: Abolished conjugation of one SUMO1P1/SUMO5.
Loss of 2 sumoylations; when associated with R-65 with or
without R-133. No effect on nuclear body formation; when
associated with R-65. No sumoylation nor nuclear body
formation; when associated with R-65 and R-160. Loss the
ability to be conjugated by SUMO1P1/SUMO5 but could be
conjugated by SUMO1; when associated with R-65 and R-160."
/evidence="ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9756909"
MUTAGEN 490
/note="K->R: Loss of 2 sumoylations; when associated with
R-65 with or without R-133. No effect on nuclear body
formation; when associated with R-65. No sumoylation nor
nuclear body formation; when associated with R-65 and R-
160."
/evidence="ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:9756909"
MUTAGEN 497
/note="K->R: Does not affect SUMO1P1/SUMO5 conjugation."
/evidence="ECO:0000269|PubMed:27211601"
MUTAGEN 515
/note="K->R: Slightly reduced acetylation. Further decrease
in acetylation; when associated with R-487."
/evidence="ECO:0000269|PubMed:18621739"
MUTAGEN 518
/note="S->A: Abolishes ubiquitination by the BCR(KLHL20) E3
ubiquitin ligase complex."
/evidence="ECO:0000269|PubMed:21840486"
MUTAGEN 556..559
/note="VVVI->AAAS: Abolishes SUMO1 binding."
CONFLICT 224
/note="E -> D (in Ref. 7; AAP88913 and 10; AAH00080/
AAH20994)"
/evidence="ECO:0000305"
CONFLICT 419
/note="P -> A (in Ref. 2; AAA60351/AAA60388/AAA60390, 4;
AAA60352 and 5; AAG50182/AAG50184/AAG50185)"
/evidence="ECO:0000305"
STRAND 54..56
/evidence="ECO:0000244|PDB:5YUF"
TURN 58..60
/evidence="ECO:0000244|PDB:5YUF"
STRAND 62..66
/evidence="ECO:0000244|PDB:5YUF"
HELIX 78..82
/evidence="ECO:0000244|PDB:5YUF"
TURN 89..91
/evidence="ECO:0000244|PDB:5YUF"
STRAND 93..96
/evidence="ECO:0000244|PDB:1BOR"
STRAND 121..126
/evidence="ECO:0000244|PDB:6IMQ"
TURN 130..132
/evidence="ECO:0000244|PDB:6IMQ"
STRAND 138..140
/evidence="ECO:0000244|PDB:6IMQ"
TURN 141..144
/evidence="ECO:0000244|PDB:6IMQ"
STRAND 145..147
/evidence="ECO:0000244|PDB:6IMQ"
HELIX 149..158
/evidence="ECO:0000244|PDB:6IMQ"
STRAND 163..165
/evidence="ECO:0000244|PDB:6IMQ"
STRAND 556..558
/evidence="ECO:0000244|PDB:6UYR"
MOD_RES P29590-2:565
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983"
CONFLICT P29590-2:578
/note="P -> A (in Ref. 5; AAG50181)"
/evidence="ECO:0000305"
MOD_RES P29590-4:518
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983"
MOD_RES P29590-4:527
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983"
MOD_RES P29590-4:530
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983"
CONFLICT P29590-10:419
/note="L -> V (in Ref. 5; AAG50187)"
/evidence="ECO:0000305"
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


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EIAAB43875 Homo sapiens,Human,Ret finger protein,RFP,RING finger protein 76,RNF76,TRIM27,Tripartite motif-containing protein 27,Zinc finger protein RFP
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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
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Pathways :
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP2371: Parkinsons Disease Pathway
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1675: Nitrogen metabolism
WP813: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP1616: ABC transporters
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection
WP1692: Protein export
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP2324: AGE/RAGE pathway
WP1663: Homologous recombination
WP35: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways

Related Genes :
[PML MYL PP8675 RNF71 TRIM19] Protein PML (Promyelocytic leukemia protein) (RING finger protein 71) (Tripartite motif-containing protein 19)
[TRIM13 LEU5 RFP2 RNF77] E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (B-cell chronic lymphocytic leukemia tumor suppressor Leu5) (Leukemia-associated protein 5) (Putative tumor suppressor RFP2) (RING finger protein 77) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13)
[ZBTB16 PLZF ZNF145] Zinc finger and BTB domain-containing protein 16 (Promyelocytic leukemia zinc finger protein) (Zinc finger protein 145) (Zinc finger protein PLZF)
[TRIM27 RFP RNF76] Zinc finger protein RFP (EC 2.3.2.27) (RING finger protein 76) (RING-type E3 ubiquitin transferase TRIM27) (Ret finger protein) (Tripartite motif-containing protein 27)
[TRIM5 RNF88] Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING finger protein 88) (RING-type E3 ubiquitin transferase TRIM5)
[Pml] Protein PML
[TRIM8 GERP RNF27] E3 ubiquitin-protein ligase TRIM8 (EC 2.3.2.27) (Glioblastoma-expressed RING finger protein) (RING finger protein 27) (RING-type E3 ubiquitin transferase TRIM8) (Tripartite motif-containing protein 8)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[TRIM11 RNF92] E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (Protein BIA1) (RING finger protein 92) (RING-type E3 ubiquitin transferase TRIM11) (Tripartite motif-containing protein 11)
[TRIM22 RNF94 STAF50] E3 ubiquitin-protein ligase TRIM22 (EC 2.3.2.27) (50 kDa-stimulated trans-acting factor) (RING finger protein 94) (RING-type E3 ubiquitin transferase TRIM22) (Staf-50) (Tripartite motif-containing protein 22)
[TRIM9 KIAA0282 RNF91] E3 ubiquitin-protein ligase TRIM9 (EC 2.3.2.27) (RING finger protein 91) (RING-type E3 ubiquitin transferase TRIM9) (Tripartite motif-containing protein 9)
[TRIM63 IRF MURF1 RNF28 SMRZ] E3 ubiquitin-protein ligase TRIM63 (EC 2.3.2.27) (Iris RING finger protein) (Muscle-specific RING finger protein 1) (MuRF-1) (MuRF1) (RING finger protein 28) (RING-type E3 ubiquitin transferase TRIM63) (Striated muscle RING zinc finger protein) (Tripartite motif-containing protein 63)
[MID2 FXY2 RNF60 TRIM1] Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midin-2) (Midline defect 2) (Midline-2) (RING finger protein 60) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1)
[MID1 FXY RNF59 TRIM18 XPRF] E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (Putative transcription factor XPRF) (RING finger protein 59) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)
[Trim27 Rfp] Zinc finger protein RFP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM27) (Ret finger protein) (Tripartite motif-containing protein 27)
[TRIM2 KIAA0517 RNF86] Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING finger protein 86) (RING-type E3 ubiquitin transferase TRIM2)
[TRIM55 MURF2 RNF29] Tripartite motif-containing protein 55 (Muscle-specific RING finger protein 2) (MuRF-2) (MuRF2) (RING finger protein 29)
[TRIM24 RNF82 TIF1 TIF1A] Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)
[TRIM5] Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM5) (TRIM5alpha)
[SIAH1 HUMSIAH] E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.27) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (Msx-interacting zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (RING-type E3 ubiquitin transferase PIAS2)
[Trim11] E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM11) (Tripartite motif-containing protein 11)
[Trim71 Gm1127 Lin41] E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (mLin41) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)
[Trim28 Kap1 Krip1 Tif1b] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-A-interacting protein) (KRIP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[Mid1 Fxy Trim18] E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)
[TRIM36 RBCC728 RNF98] E3 ubiquitin-protein ligase TRIM36 (EC 2.3.2.27) (RING finger protein 98) (RING-type E3 ubiquitin transferase TRIM36) (Tripartite motif-containing protein 36) (Zinc-binding protein Rbcc728)
[Rnf4 Snurf] E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) (Small nuclear ring finger protein) (Protein SNURF)
[Trim24 Tif1 Tif1a] Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase Trim24) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)
[Siah2] E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (mSiah2)

Bibliography :