Reviewed, UniProtKB/Swiss-Prot P29590 (PML_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable transcription factor PML
Alternative name(s):
    Tripartite motif-containing protein 19
    RING finger protein 71

Gene names

Name:	PML
Synonyms:	MYL, RNF71, TRIM19

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	882 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable transcription factor. May play an important role in recruitment of ELF4 into PML nuclear bodies. Ref.9 Ref.15
Subunit structure	Interacts with SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with the C-terminus of ELF4. Interacts with Lassa virus Z protein and rabies virus phosphoprotein By similarity.
Subcellular location	Nucleus › nucleoplasm. Cytoplasm. Note: Sumoylated forms localize to the PML nuclear bodies. The B1 box and the RING finger are also required for this nuclear localization. Isoforms lacking a nuclear localization signal are cytoplasmic. Ref.9 Ref.15
Post-translational modification	Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. Ref.14 Sumoylated on all three sites is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. The PML-RARA fusion protein is not sumoylated. Ref.9
Involvement in 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.
Sequence similarities	Contains 2 B box-type zinc fingers. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW maintenance of protein location in nucleus Inferred from direct assay. Source: MGI negative regulation of angiogenesis Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell growth Inferred from direct assay. Source: UniProtKB negative regulation of cell proliferation Ref.12 Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription Inferred from direct assay. Source: UniProtKB protein complex assembly Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to cytokine stimulus Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	PML body Ref.5 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA insoluble fraction Inferred from direct assay. Source: UniProtKB nuclear membrane Inferred from direct assay. Source: UniProtKB nucleolus Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO polymer binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSNK2A1	P68400	2	EBI-295890,EBI-347804
DAXX	Q9UER7	1	EBI-295890,EBI-77321
MDM2	Q00987	1	EBI-304008,EBI-389668
MDM2	Q00987	2	EBI-295890,EBI-389668
TP53	P04637	1	EBI-295890,EBI-366083
ZBTB16	Q05516	1	EBI-304008,EBI-711925

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform PML-1 (identifier: P29590-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform PML-2 (identifier: P29590-2)

The sequence of this isoform differs from the canonical sequence as follows:
     571-611: SSRELDDSSS...DPQAEDRPLV → VSGPEVQPRT...LRLGNFPVRH
     612-882: Missing.

Isoform PML-3 (identifier: P29590-3)

The sequence of this isoform differs from the canonical sequence as follows:
     571-882: SSRELDDSSS...GLAERASQQS → CMEPMETAEP...PVPGARQAGL

Isoform PML-3B (identifier: P29590-4)

The sequence of this isoform differs from the canonical sequence as follows:
     553-560: EERVVVIS → GRERNALW
     561-882: Missing.

Isoform PML-X (identifier: P29590-5)

The sequence of this isoform differs from the canonical sequence as follows:
     621-633: TQKISQLAAVNRE → SGFSWGYPHPFLI
     634-882: Missing.

Isoform PML-4 (identifier: P29590-6)

The sequence of this isoform differs from the canonical sequence as follows:
     404-466: Missing.

Isoform PML-5 (identifier: P29590-7)

The sequence of this isoform differs from the canonical sequence as follows:
     648-664: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 882

882

Probable transcription factor PML

PRO_0000056001

Regions

Zinc finger

57 – 92

36

RING-type

Zinc finger

124 – 166

43

B box-type 1; atypical

Zinc finger

183 – 236

54

B box-type 2

Region

476 – 490

15

Nuclear localization signal

Coiled coil

228 – 253

26

Potential

Compositional bias

3 – 46

44

Pro-rich

Sites

Metal binding

57

1

Zinc 1

Metal binding

60

1

Zinc 1

Metal binding

72

1

Zinc 2

Metal binding

74

1

Zinc 2

Metal binding

77

1

Zinc 1

Metal binding

80

1

Zinc 1

Metal binding

88

1

Zinc 2

Metal binding

91

1

Zinc 2

Site

394 – 395

2

Breakpoint for translocation to form PML-RARA oncogene in type A APL

Site

552 – 553

2

Breakpoint for translocation to form PML-RARA oncogene in type B APL

Amino acid modifications

Modified residue

8

1

Phosphoserine Ref.16

Modified residue

403

1

Phosphoserine Ref.16 Ref.18

Modified residue

409

1

Phosphothreonine Ref.18

Modified residue

504

1

Phosphoserine By similarity

Modified residue

505

1

Phosphoserine Ref.17

Modified residue

512

1

Phosphoserine Ref.17

Modified residue

518

1

Phosphoserine Ref.16 Ref.18

Modified residue

527

1

Phosphoserine Ref.16 Ref.18

Modified residue

530

1

Phosphoserine Ref.16 Ref.18

Modified residue

535

1

Phosphoserine Ref.16

Modified residue

560

1

Phosphoserine Ref.16

Modified residue

561

1

Phosphoserine Ref.16

Modified residue

562

1

Phosphoserine Ref.16

Modified residue

565

1

Phosphoserine Ref.16

Cross-link

65

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Cross-link

160

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Cross-link

490

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Natural variations

Alternative sequence

404 – 466

63

Missing in isoform PML-4.

VSP_005737

Alternative sequence

553 – 560

8

EERVVVIS → GRERNALW in isoform PML-3B.

VSP_005742

Alternative sequence

561 – 882

322

Missing in isoform PML-3B.

VSP_005743

Alternative sequence

571 – 882

312

SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-3.

VSP_005741

Alternative sequence

571 – 611

41

SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-2.

VSP_005739

Alternative sequence

612 – 882

271

Missing in isoform PML-2.

VSP_005740

Alternative sequence

621 – 633

13

TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-X.

VSP_005744

Alternative sequence

634 – 882

249

Missing in isoform PML-X.

VSP_005745

Alternative sequence

648 – 664

17

Missing in isoform PML-5.

VSP_005738

Natural variant

645

1

F → L: dbSNP rs5742915. Ref.1 Ref.5

VAR_052090

Experimental info

Mutagenesis

65

1

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. Ref.9

Mutagenesis

68

1

K → R: No effect on sumoylation levels.

Mutagenesis

133

1

K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.9

Mutagenesis

150

1

K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.9

Mutagenesis

160

1

K → R: Loss of 2 sumoylations; when asociated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. Ref.9

Mutagenesis

490

1

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. Ref.9

Sequence conflict

419

1

P → A in AAA60351. Ref.1

Sequence conflict

419

1

P → A in AAA60388. Ref.1

Sequence conflict

419

1

P → A in AAA60390. Ref.1

Sequence conflict

419

1

P → A in AAA60352. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

882

Helix Strand Turn

Details...

Beta strand

58 – 60

3

Beta strand

82 – 87

6

Beta strand

93 – 96

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform PML-1 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: D50968A977E34287	FASTA	882	97,551
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 610 620 630 640 650 660 ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ 670 680 690 700 710 720 HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG 730 740 750 760 770 780 ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS 790 800 810 820 830 840 LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA 850 860 870 880 FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS
	Isoform PML-2. Checksum: 52E7FB5D57D59233	FASTA	611	67,471
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS VSGPEVQPRT PASPHFRSQG AQPQQVTLRL 610 ALRLGNFPVR H
	Isoform PML-3. Checksum: 5DA9DD2E4EEE8492	FASTA	824	90,254
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS CMEPMETAEP QSSPAHSSPA HSSPVQSLLR 610 620 630 640 650 660 AQGASSLPCG TYHPPAWPPH QPAEQAATPD AEPHSEPPDH QERPAVHRGI RYLLYRAQRA 670 680 690 700 710 720 IRLRHALRLH PQLHRAPIRT WSPHVVQAST PAITGPLNHP ANAQEHPAQL QRGISPPHRI 730 740 750 760 770 780 RGAVRSRSRS LRGSSHLSQW LNNFFALPFS SMASQLDMSS VVGAGEGRAQ TLGAVVPPGD 790 800 810 820 SVRGSMEASQ VQVPLEASPI TFPPPCAPER PPISPVPGAR QAGL
	Isoform PML-3B. Checksum: 9DC795A6542BA778	FASTA	560	62,007
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 NSNHVASGAG EAGRERNALW
	Isoform PML-X. Checksum: 85FBAEC9F162C8E0	FASTA	633	70,024
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 610 620 630 ADPQAEDRPL VFFDLKIDNE SGFSWGYPHP FLI
	Isoform PML-4. Checksum: 08A61429A471F3EA	FASTA	819	90,986
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASDVSNTTT AQKRKCSQTQ 430 440 450 460 470 480 CPRKVIKMES EEGKEARLAR SSPEQPRPST SKAVSPPHLD GPPSPRSPVI GSEVFLPNSN 490 500 510 520 530 540 HVASGAGEAE ERVVVISSSE DSDAENSSSR ELDDSSSESS DLQLEGPSTL RVLDENLADP 550 560 570 580 590 600 QAEDRPLVFF DLKIDNETQK ISQLAAVNRE SKFRVVIQPE AFFSIYSKAV SLEVGLQHFL 610 620 630 640 650 660 SFLSSMRRPI LACYKLWGPG LPNFFRALED INRLWEFQEA ISGFLAALPL IRERVPGASS 670 680 690 700 710 720 FKLKNLAQTY LARNMSERSA MAAVLAMRDL CRLLEVSPGP QLAQHVYPFS SLQCFASLQP 730 740 750 760 770 780 LVQAAVLPRA EARLLALHNV SFMELLSAHR RDRQGGLKKY SRYLSLQTTT LPPAQPAFNL 790 800 810 QALGTYFEGL LEGPALARAE GVSTPLAGRG LAERASQQS
	Isoform PML-5. Checksum: FF6BC26D338E89CB	FASTA	865	95,677
	10 20 30 40 50 60 MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 70 80 90 100 110 120 QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 130 140 150 160 170 180 QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 190 200 210 220 230 240 TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 250 260 270 280 290 300 DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 310 320 330 340 350 360 VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 370 380 390 400 410 420 QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 430 440 450 460 470 480 EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 490 500 510 520 530 540 QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 550 560 570 580 590 600 NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 610 620 630 640 650 660 ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSFLS SMRRPILACY 670 680 690 700 710 720 KLWGPGLPNF FRALEDINRL WEFQEAISGF LAALPLIRER VPGASSFKLK NLAQTYLARN 730 740 750 760 770 780 MSERSAMAAV LAMRDLCRLL EVSPGPQLAQ HVYPFSSLQC FASLQPLVQA AVLPRAEARL 790 800 810 820 830 840 LALHNVSFME LLSAHRRDRQ GGLKKYSRYL SLQTTTLPPA QPAFNLQALG TYFEGLLEGP 850 860 ALARAEGVST PLAGRGLAER ASQQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia." Goddard A.D., Borrow J., Freemont P.S., Solomon E. Science 254:1371-1374(1991) [PubMed: 1720570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2 AND PML-3), CHROMOSOMAL TRANSLOCATION WITH RARA, VARIANT LEU-645.
[2]	"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." Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., Chambon P. EMBO J. 11:629-642(1992) [PubMed: 1311253] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-X).
[3]	"Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML." Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr., Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M. Cell 66:663-674(1991) [PubMed: 1652368] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
[4]	Goddard A.D., Solomon E. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
[5]	"The tripartite motif family identifies cell compartments." 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. EMBO J. 20:2140-2151(2001) [PubMed: 11331580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-1), VARIANT LEU-645.
[6]	"Analysis of the DNA sequence and duplication history of human chromosome 15." 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. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants." 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. Oncogene 7:311-316(1992) [PubMed: 1312695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466, CHROMOSOMAL TRANSLOCATION WITH RARA.
[8]	"Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic leukemia: structure of the fusion point in a case lacking classic t(15;17) translocation." Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K., Omine M. Leuk. Lymphoma 44:111-115(2003) [PubMed: 12691149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, CHROMOSOMAL TRANSLOCATION WITH RARA.
[9]	"Identification of three major sentrinization sites in PML." Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T., Yeh E.T.H. J. Biol. Chem. 273:26675-26682(1998) [PubMed: 9756909] [Abstract] Cited for: SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65; LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, FUNCTION.
[10]	"Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML." Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D. J. Cell Sci. 111:1319-1329(1998) [PubMed: 9570750] [Abstract] Cited for: INTERACTION WITH TRIM27.
[11]	"An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm." Borden K.L., Campbell-Dwyer E.J., Salvato M.S. J. Virol. 72:758-766(1998) [PubMed: 9420283] [Abstract] Cited for: INTERACTION WITH LASSA VIRUS Z PROTEIN.
[12]	"Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence." Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T. EMBO J. 21:2383-2396(2002) [PubMed: 12006491] [Abstract] Cited for: INTERACTION WITH SIRT1.
[13]	"PML colocalizes with and stabilizes the DNA damage response protein TopBP1." Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S. Mol. Cell. Biol. 23:4247-4256(2003) [PubMed: 12773567] [Abstract] Cited for: INTERACTION WITH TOPBP1.
[14]	"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." Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S. J. Biol. Chem. 279:5374-5379(2004) [PubMed: 14645235] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[15]	"Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein." Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., Matsuzaki K., Nakao M., Li J.-D., Kai H. J. Biol. Chem. 279:19091-19098(2004) [PubMed: 14976184] [Abstract] Cited for: FUNCTION, INTERACTION WITH ELF4, SUBCELLULAR LOCATION.
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-403; SER-518; SER-527; SER-530; SER-535; SER-560; SER-561; SER-562 AND SER-565, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-512, MASS SPECTROMETRY.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; THR-409; SER-518; SER-527 AND SER-530, MASS SPECTROMETRY.
[19]	"The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML." Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S., Howe K., Solomon E., Freemont P.S. EMBO J. 14:1532-1541(1995) [PubMed: 7729428] [Abstract] Cited for: STRUCTURE BY NMR OF 49-104.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

M79462 mRNA. Translation: AAA60388.1. Different initiation.
M79463 mRNA. Translation: AAA60351.1. Different initiation.
M79464 mRNA. Translation: AAA60390.1. Different initiation.
X63131 mRNA. Translation: CAA44841.1.
M73778 mRNA. Translation: AAA60125.1.
M80185 mRNA. Translation: AAA60352.1. Different initiation.
AF230401 mRNA. Translation: AAG50180.1.
AC013486 Genomic DNA. No translation available.
AC108137 Genomic DNA. No translation available.
X64800 Genomic DNA. Translation: CAA46026.1.
AB067754 mRNA. Translation: BAB62809.1. Different termination.

IPI

IPI00022348.
IPI00220453.
IPI00303999.
IPI00304000.
IPI00337754.
IPI00922350.
IPI00922504.

PIR

A40044.
I38054.
S19244.
S42516.
S44381.

RefSeq

NP_002666.1.
NP_150241.2.
NP_150242.1.
NP_150243.2.
NP_150247.2.
NP_150249.1.
NP_150250.2.
NP_150252.1.
NP_150253.2.

UniGene

Hs.526464

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOR	NMR	-	A	49-104	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P29590. 19 interactions.

PTM databases

PhosphoSite

P29590.

Proteomic databases

PRIDE

P29590.

Genome annotation databases

Ensembl

ENSG00000140464. Homo sapiens. [Contig view]

GeneID

5371.

KEGG

hsa:5371.

UCSC

uc002awm.1. human.
uc002awn.1. human.
uc002awr.1. human.
uc002awv.1. human.

Organism-specific databases

GeneCards

GC15P072074.

HGNC

HGNC:9113. PML.

HPA

CAB010194.
CAB016304.
HPA008312.

MIM

102578. gene.

Orphanet

520. Leukemia, promyelocytic, acute.

PharmGKB

PA33439.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P29590.

HOVERGEN

P29590.

OMA

P29590. RVLIQPE.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpress

P29590.

Bgee

P29590.

CleanEx

HS_PML.

GermOnline

ENSG00000140464. Homo sapiens.

Family and domain databases

InterPro

IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00643. zf-B_box. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

SMART

SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

20820.

PMAP-CutDB

P29590.

SOURCE

Search...

Entry information

Entry name

PML_HUMAN

Accession

Primary (citable) accession number: P29590
Secondary accession number(s): P29591 , P29592, P29593, Q00755, Q96S41

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 25, 2008
Last modified:	July 7, 2009
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)