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Description:
Probable transcription factor PML (Tripartite motif protein 19) (RINGfinger protein 71).
Molecular weight: 97517
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
07-MAR-2006, entry version 71.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein PML_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M79462 | AAA60388.1 | ALT_INIT |
| EMBL | M79463 | AAA60351.1 | ALT_INIT |
| EMBL | M79464 | AAA60390.1 | ALT_INIT |
| EMBL | X63131 | CAA44841.1 | - |
| EMBL | M73778 | AAA60125.1 | - |
| EMBL | M80185 | AAA60352.1 | ALT_INIT |
| EMBL | AF230401 | AAG50180.1 | - |
| EMBL | X64800 | CAA46026.1 | - |
| PIR | A40044 | A40044. | |
| PIR | I38054 | I38054. | |
| PIR | S19244 | S19244. | |
| PDB | 1BOR | NMR | @=49-104. |
| IntAct | P29590 | -.1 | |
| TRANSFAC | T05113 | -. | |
| Ensembl | ENSG00000140464 | Homo sapiens.1 | |
| HGNC | HGNC:9113 | PML.1 | |
| MIM | 102578 | gene. | |
| LinkHub | P29590 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0003700 | F:transcription factor activity | TAS. |
| InterPro | IPR000315 | Znf_Bbox. | |
| InterPro | IPR001841 | Znf_RING. | |
| Pfam | PF00643 | zf-B_box | 2. |
| Pfam | PF00097 | zf-C3HC4 | 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. |
Keywords:
3D-structure; Activator; Alternative splicing; Chromosomal translocation; Coiled coil; DNA-binding; Metal-binding; Nuclear protein; Proto-oncogene; Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2 AND PML-3), AND
RP CHROMOMOSOMAL TRANSLOCATION WITH RARA.
RX MEDLINE=92073906; PubMed=1720570;
RA Goddard A.D., Borrow J., Freemont P.S., Solomon E.;
RT "Characterization of a zinc finger gene disrupted by the t(15;17) in
RT acute promyelocytic leukemia.";
RL Science 254:1371-1374(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-X).
RX MEDLINE=92164652; PubMed=1311253;
RA Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B.,
RA Lanotte M., Berger R., Chambon P.;
RT "Structure, localization and transcriptional properties of two classes
RT of retinoic acid receptor alpha fusion proteins in acute promyelocytic
RT leukemia (APL): structural similarities with a new family of
RT oncoproteins.";
RL EMBO J. 11:629-642(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
RX MEDLINE=91347368; PubMed=1652368; DOI=10.1016/0092-8674(91)90112-C;
RA Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr.,
RA Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M.;
RT "Chromosomal translocation t(15;17) in human acute promyelocytic
RT leukemia fuses RAR alpha with a novel putative transcription factor,
RT PML.";
RL Cell 66:663-674(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
RA Goddard A.D., Solomon E.;
RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-1).
RX MEDLINE=21231161; PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA Minucci S., Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466.
RX MEDLINE=92195661; PubMed=1312695;
RA Tong J.H., Dong S., Geng J.P., Huang W., Wang Z.Y., Sun G.L.,
RA Chen S.J., Chen Z., Larsen C.-J., Berger R.;
RT "Molecular rearrangements of the MYL gene in acute promyelocytic
RT leukemia (APL, M3) define a breakpoint cluster region as well as some
RT molecular variants.";
RL Oncogene 7:311-316(1992).
RN [7]
RP INTERACTION WITH TRIM27.
RX MEDLINE=98237715; PubMed=9570750;
RA Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.;
RT "Ret finger protein is a normal component of PML nuclear bodies and
RT interacts directly with PML.";
RL J. Cell Sci. 111:1319-1329(1998).
RN [8]
RP INTERACTION WITH SIRT1.
RX MEDLINE=22001146; PubMed=12006491; DOI=10.1093/emboj/21.10.2383;
RA Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A.,
RA Minucci S., Pelicci P.G., Kouzarides T.;
RT "Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular
RT senescence.";
RL EMBO J. 21:2383-2396(2002).
RN [9]
RP INTERACTION WITH TOPBP1.
RX PubMed=12773567; DOI=10.1128/MCB.23.12.4247-4256.2003;
RA Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S.;
RT "PML colocalizes with and stabilizes the DNA damage response protein
RT TopBP1.";
RL Mol. Cell. Biol. 23:4247-4256(2003).
RN [10]
RP INTERACTION WITH SIAH1, AND DEGRADATION.
RX PubMed=14645235; DOI=10.1074/jbc.M306407200;
RA Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S.,
RA Lazar M.A., Pelicci P.G., Minucci S.;
RT "The coiled-coil domain is the structural determinant for mammalian
RT homologues of Drosophila Sina-mediated degradation of promyelocytic
RT leukemia protein and other tripartite motif proteins by the
RT proteasome.";
RL J. Biol. Chem. 279:5374-5379(2004).
RN [11]
RP FUNCTION, INTERACTION WITH ELF4, AND SUBCELLULAR LOCATION.
RX PubMed=14976184; DOI=10.1074/jbc.M312439200;
RA Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T.,
RA Matsuzaki K., Nakao M., Li J.-D., Kai H.;
RT "Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates
RT lysozyme transcription in epithelial cells through interaction with
RT promyelocytic leukemia protein.";
RL J. Biol. Chem. 279:19091-19098(2004).
RN [12]
RP STRUCTURE BY NMR OF 49-104.
RX MEDLINE=95246746; PubMed=7729428;
RA Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S.,
RA Howe K., Solomon E., Freemont P.S.;
RT "The solution structure of the RING finger domain from the acute
RT promyelocytic leukaemia proto-oncoprotein PML.";
RL EMBO J. 14:1532-1541(1995).
RN [13]
RP INTERACTION WITH LASSA VIRUS Z PROTEIN.
RA Borden K.L., Campbell Dwyer E.J., Salvato M.S.;
RT "An arenavirus RING (zinc-binding) protein binds the oncoprotein
RT promyelocyte leukemia protein (PML) and relocates PML nuclear bodies
RT to the cytoplasm.";
RL J. Virol. 72:758-766(1998).
Feature:
CHAIN 1 882 Probable transcription factor PML.
/FTId=PRO_0000056001.
ZN_FING 57 92 RING-type.
ZN_FING 124 166 B box-type 1.
ZN_FING 183 236 B box-type 2.
COILED 228 253 Potential.
METAL 57 57 Zinc 1.
METAL 60 60 Zinc 1.
METAL 72 72 Zinc 2.
METAL 74 74 Zinc 2.
METAL 77 77 Zinc 1.
METAL 80 80 Zinc 1.
METAL 88 88 Zinc 2.
METAL 91 91 Zinc 2.
SITE 394 395 Breakpoint for translocation to form PML-
RARA oncogene in type A APL.
SITE 552 553 Breakpoint for translocation to form PML-
RARA oncogene in type B APL.
VARSPLIC 404 466 Missing (in some isoforms).
/FTId=VSP_005737.
VARSPLIC 553 560 EERVVVIS -> GRERNALW (in isoform PML-3B).
/FTId=VSP_005742.
VARSPLIC 561 882 Missing (in isoform PML-3B).
/FTId=VSP_005743.
VARSPLIC 571 882 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
FFDLKIDNETQKISQLAAVNRESKFRVVIQPEALFSIYSKA
VSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALED
INRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYL
ARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSL
QCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDR
QGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGP
ALARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQS
SPAHSSPAHSSPVQSLLRAQGASSLPCGTYHPPAWPPHQPA
EQAATPDAEPHSEPPDHQERPAVHRGIRYLLYRAQRAIRLR
HALRLHPQLHRAPIRTWSPHVVQASTPAITGPLNHPANAQE
HPAQLQRGISPPHRIRGAVRSRSRSLRGSSHLSQWLNNFFA
LPFSSMASQLDMSSVVGAGEGRAQTLGAVVPPGDSVRGSME
ASQVQVPLEASPITFPPPCAPERPPISPVPGARQAGL (in
isoform PML-3).
/FTId=VSP_005741.
VARSPLIC 571 611 SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLV
-> VSGPEVQPRTPASPHFRSQGAQPQQVTLRLALRLGNFP
VRH (in isoform PML-2).
/FTId=VSP_005739.
VARSPLIC 612 882 Missing (in isoform PML-2).
/FTId=VSP_005740.
VARSPLIC 621 633 TQKISQLAAVNRE -> SGFSWGYPHPFLI (in
isoform PML-X).
/FTId=VSP_005744.
VARSPLIC 634 882 Missing (in isoform PML-X).
/FTId=VSP_005745.
VARSPLIC 648 664 Missing (in some isoforms).
/FTId=VSP_005738.
CONFLICT 419 419 P -> A (in Ref. 1 and 4).
STRAND 51 51
STRAND 55 56
STRAND 58 60
STRAND 62 63
STRAND 65 65
STRAND 68 68
STRAND 70 70
TURN 71 72
STRAND 73 73
STRAND 76 77
TURN 78 79
STRAND 80 80
STRAND 82 87
STRAND 89 90
STRAND 93 96
STRAND 99 100
Comments:
-!- FUNCTION: Probable transcription factor. May play an important
role in recruitment of ELF4 into PML nuclear bodies.
-!- SUBUNIT: Interacts with SIRT1, TOPBP1 and TRIM27. Interacts with
the C-terminus of ELF4; this interaction enhances ELF4
transactivation of the bovine lysozyme gene. Interacts with Lassa
virus Z protein.
-!- INTERACTION:
Q9UER7:DAXX; NbExp=1; IntAct=EBI-295890, EBI-77321;
-!- SUBCELLULAR LOCATION: Nuclear; localized to PML nuclear bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist;
Name=PML-1;
IsoId=P29590-1; Sequence=Displayed;
Name=PML-2;
IsoId=P29590-2; Sequence=VSP_005739, VSP_005740;
Name=PML-3;
IsoId=P29590-3; Sequence=VSP_005741;
Name=PML-3B;
IsoId=P29590-4; Sequence=VSP_005742, VSP_005743;
Name=PML-X;
IsoId=P29590-5; Sequence=VSP_005744, VSP_005745;
-!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
subsequent proteasomal degradation.
-!- DISEASE: 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.
-!- SIMILARITY: Contains 2 B box-type zinc fingers.
-!- SIMILARITY: Contains 1 RING-type zinc finger.
-!- DATABASE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.;
WWW="http://www.infobiogen.fr/services/chromcancer/Genes/PMLID41.html".
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Sequence length: 882
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 QPEALFSIYS KAVSLEVGLQ
HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG
ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS
LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA
FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS