Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P29590 (PML_HUMAN)

Last modified July 7, 2009. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Nucleusnucleoplasm. 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 processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processDNA 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 componentPML 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 functionDNA 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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 882882Probable transcription factor PML
PRO_0000056001

Regions

Zinc finger57 – 9236RING-type
Zinc finger124 – 16643B box-type 1; atypical
Zinc finger183 – 23654B box-type 2
Region476 – 49015Nuclear localization signal
Coiled coil228 – 25326 Potential
Compositional bias3 – 4644Pro-rich

Sites

Metal binding571Zinc 1
Metal binding601Zinc 1
Metal binding721Zinc 2
Metal binding741Zinc 2
Metal binding771Zinc 1
Metal binding801Zinc 1
Metal binding881Zinc 2
Metal binding911Zinc 2
Site394 – 3952Breakpoint for translocation to form PML-RARA oncogene in type A APL
Site552 – 5532Breakpoint for translocation to form PML-RARA oncogene in type B APL

Amino acid modifications

Modified residue81Phosphoserine Ref.16
Modified residue4031Phosphoserine Ref.16 Ref.18
Modified residue4091Phosphothreonine Ref.18
Modified residue5041Phosphoserine By similarity
Modified residue5051Phosphoserine Ref.17
Modified residue5121Phosphoserine Ref.17
Modified residue5181Phosphoserine Ref.16 Ref.18
Modified residue5271Phosphoserine Ref.16 Ref.18
Modified residue5301Phosphoserine Ref.16 Ref.18
Modified residue5351Phosphoserine Ref.16
Modified residue5601Phosphoserine Ref.16
Modified residue5611Phosphoserine Ref.16
Modified residue5621Phosphoserine Ref.16
Modified residue5651Phosphoserine Ref.16
Cross-link65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Natural variations

Alternative sequence404 – 46663Missing in isoform PML-4.
VSP_005737
Alternative sequence553 – 5608EERVVVIS → GRERNALW in isoform PML-3B.
VSP_005742
Alternative sequence561 – 882322Missing in isoform PML-3B.
VSP_005743
Alternative sequence571 – 882312SSREL…ASQQS → CMEPMETAEPQSSPAHSSPA HSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPD AEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLH PQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQL QRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFS SMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQ VQVPLEASPITFPPPCAPER PPISPVPGARQAGL in isoform PML-3.
VSP_005741
Alternative sequence571 – 61141SSREL…DRPLV → VSGPEVQPRTPASPHFRSQG AQPQQVTLRLALRLGNFPVR H in isoform PML-2.
VSP_005739
Alternative sequence612 – 882271Missing in isoform PML-2.
VSP_005740
Alternative sequence621 – 63313TQKIS…AVNRE → SGFSWGYPHPFLI in isoform PML-X.
VSP_005744
Alternative sequence634 – 882249Missing in isoform PML-X.
VSP_005745
Alternative sequence648 – 66417Missing in isoform PML-5.
VSP_005738
Natural variant6451F → L: dbSNP rs5742915. Ref.1 Ref.5
VAR_052090

Experimental info

Mutagenesis651K → 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
Mutagenesis681K → R: No effect on sumoylation levels.
Mutagenesis1331K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.9
Mutagenesis1501K → R: Loss of 2 sumoylations; when associated with R-65 and R-490. Ref.9
Mutagenesis1601K → 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
Mutagenesis4901K → 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 conflict4191P → A in AAA60351. Ref.1
Sequence conflict4191P → A in AAA60388. Ref.1
Sequence conflict4191P → A in AAA60390. Ref.1
Sequence conflict4191P → A in AAA60352. Ref.3

Secondary structure

....... 882
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PML-1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: D50968A977E34287

FASTA88297,551
        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 

« Hide

Isoform PML-2.

Checksum: 52E7FB5D57D59233
Show »

FASTA61167,471
Isoform PML-3.

Checksum: 5DA9DD2E4EEE8492
Show »

FASTA82490,254
Isoform PML-3B.

Checksum: 9DC795A6542BA778
Show »

FASTA56062,007
Isoform PML-X.

Checksum: 85FBAEC9F162C8E0
Show »

FASTA63370,024
Isoform PML-4.

Checksum: 08A61429A471F3EA
Show »

FASTA81990,986
Isoform PML-5.

Checksum: FF6BC26D338E89CB
Show »

FASTA86595,677

References

« Hide '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. expand/collapse author list , 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.

Cross-references

Sequence databases

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.
IPIIPI00022348.
IPI00220453.
IPI00303999.
IPI00304000.
IPI00337754.
IPI00922350.
IPI00922504.
PIRA40044.
I38054.
S19244.
S42516.
S44381.
RefSeqNP_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.
UniGeneHs.526464

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BORNMR-A49-104[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP29590. 19 interactions.

PTM databases

PhosphoSiteP29590.

Proteomic databases

PRIDEP29590.

Genome annotation databases

EnsemblENSG00000140464. Homo sapiens. [Contig view]
GeneID5371.
KEGGhsa:5371.
UCSCuc002awm.1. human.
uc002awn.1. human.
uc002awr.1. human.
uc002awv.1. human.

Organism-specific databases

GeneCardsGC15P072074.
HGNCHGNC:9113. PML.
HPACAB010194.
CAB016304.
HPA008312.
MIM102578. gene.
Orphanet520. Leukemia, promyelocytic, acute.
PharmGKBPA33439.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP29590.
HOVERGENP29590.
OMAP29590. RVLIQPE.

Enzyme and pathway databases

Pathway_Interaction_DBtgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpressP29590.
BgeeP29590.
CleanExHS_PML.
GermOnlineENSG00000140464. Homo sapiens.

Family and domain databases

InterProIPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00643. zf-B_box. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20820.
PMAP-CutDBP29590.
SOURCESearch...

Entry information

Entry namePML_HUMAN
AccessionPrimary (citable) accession number: P29590
Secondary accession number(s): P29591 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents