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Q60953 (PML_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PML
Gene names
Name:Pml
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length885 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV). Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28

Subunit structure

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 TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. 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 with SMAD2, SMAD3, DAXX, RPL11, HIPK2 and MTOR. Interacts with ITPR3, PPP1A and RB1. Interacts with RNF4, NLRP3, MAGEA2, RBL2, PER2, E2F4 and MAPK7/BMK1. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Interacts with PPARGC1A AND KAT2A. Ref.8 Ref.11 Ref.13 Ref.14 Ref.16 Ref.21 Ref.22 Ref.26 Ref.27

Subcellular location

Nucleus By similarity. Nucleusnucleoplasm. Cytoplasm. NucleusPML body. Nucleusnucleolus By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Detected in the nucleolus after DNA damage. Acetylation at Lys-497 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 By similarity. Ref.8 Ref.14 Ref.22 Ref.26 Ref.27

Domain

The coiled-coil domain mediates a strong homo/multidimerization activity essential for core assembly of PML-NBs By similarity.

Binds arsenic via the RING-type zinc finger By similarity.

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 By similarity.

Post-translational modification

Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent. Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex requires CDK1/2-mediated phosphorylation at Ser-528 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20 By similarity. Ref.13

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-70, Lys-165 and Lys-500) is required for nuclear body formation. Sumoylation on Lys-165 is a prerequisite for sumoylation on Lys-70. Lys-70 and Lys-165 are sumoylated by PISA1 and PIAS2. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-575 which in turn triggers its ubiquitin-mediated degradation. Sumoylation at Lys-500 by RANBP2 is essential for the proper assembly of PML-NBs. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 By similarity. Ref.8

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-17, Ser-45 and Ser-47 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage. MAPK1- mediated phosphorylations at Ser-404, Ser-515 and Ser-540 and CDK1/2-mediated phosphorylation at Ser-528 promote PIN1-dependent PML degradation. CK2-mediated phosphorylation at Ser-575 primes PML ubiquitination via an unidentified ubiquitin ligase By similarity.

Acetylation at Lys-497 is essential for its nuclear localization. Deacetylated at Lys-497 by SIRT1 and this deacetylation promotes PML control of PER2 nuclear localization By similarity.

Disruption phenotype

Mice are born at the expected Mendelian rate and are fertile. They show leukopenia with reduced levels of circulating granulocytes and myeloid cells. They are highly susceptible to infections, causing a reduced life span. Mice do not exhibit normal apoptosis of hematopoietic stem cells after DNA damage due to irradiation. They do not exhibit normal apoptosis in response to FAS, TNF, TGFB1, interferons and ceramide, and show impaired activation of caspases in response to pro-apoptotic stimuli. Mice are highly susceptible to chemical carcinogens. Mice display accelerated revascularization after ischemia. Newborns have smaller brains with a reduced size of the brain cortex. Mice display aberrant learning and memory, lower levels of anxiety-like behavior and specific deficits in long-term plasticity. Mice display a compromised endogenous ciracadian clock with reduced precision and stability of the period length. Ref.5 Ref.6 Ref.10 Ref.16 Ref.21 Ref.26 Ref.28

Sequence similarities

Contains 2 B box-type zinc fingers.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAA97601.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAntiviral defense
Apoptosis
Biological rhythms
Host-virus interaction
Immunity
Innate immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainCoiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from mutant phenotype PubMed 15626733. Source: UniProtKB

PML body organization

Inferred from direct assay PubMed 12529400. Source: MGI

SMAD protein import into nucleus

Inferred from mutant phenotype Ref.15. Source: MGI

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.5. Source: MGI

branching involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 19261859. Source: MGI

cell aging

Inferred from mutant phenotype PubMed 10910364. Source: UniProtKB

cell cycle arrest

Inferred from mutant phenotype PubMed 10910364. Source: UniProtKB

cell fate commitment

Inferred from mutant phenotype PubMed 19261859. Source: MGI

cellular response to interleukin-4

Inferred from direct assay PubMed 9798653. Source: MGI

cellular senescence

Inferred from sequence or structural similarity. Source: UniProtKB

circadian regulation of gene expression

Inferred from direct assay Ref.26. Source: UniProtKB

common-partner SMAD protein phosphorylation

Inferred from mutant phenotype Ref.15. Source: MGI

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum calcium ion homeostasis

Inferred from mutant phenotype Ref.22. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from direct assay Ref.26. Source: UniProtKB

extrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.5. Source: MGI

innate immune response

Inferred from direct assay PubMed 18248090. Source: UniProt

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from mutant phenotype PubMed 14992722. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype PubMed 15626733Ref.5. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 15626733. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.22. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype Ref.22. Source: MGI

maintenance of protein location in nucleus

Inferred from sequence orthology PubMed 17332504. Source: MGI

myeloid cell differentiation

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of telomerase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of telomere maintenance via telomerase

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of viral release from host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

positive regulation of apoptotic process involved in mammary gland involution

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from mutant phenotype PubMed 10684855. Source: MGI

positive regulation of defense response to virus by host

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein stabilization

Inferred from electronic annotation. Source: Ensembl

protein targeting

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of MHC class I biosynthetic process

Inferred from direct assay PubMed 9845074. Source: MGI

regulation of calcium ion transport into cytosol

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of circadian rhythm

Inferred from direct assay Ref.26. Source: UniProtKB

regulation of double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein phosphorylation

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9845074. Source: MGI

response to UV

Inferred from mutant phenotype PubMed 15626733. Source: MGI

response to gamma radiation

Inferred from mutant phenotype PubMed 11025664Ref.5. Source: MGI

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

retinoic acid receptor signaling pathway

Inferred from mutant phenotype Ref.6. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype Ref.15. Source: MGI

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cytosol

Inferred from direct assay Ref.22. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of endoplasmic reticulum membrane

Inferred from direct assay Ref.22. Source: UniProtKB

nuclear matrix

Inferred from direct assay PubMed 15252119. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.22Ref.26. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

SMAD binding

Inferred from direct assay Ref.15. Source: MGI

cobalt ion binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 21057547. Source: IntAct

transcription coactivator activity

Traceable author statement PubMed 15626733. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q60953-1)

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 2 (identifier: Q60953-2)

The sequence of this isoform differs from the canonical sequence as follows:
     431-476: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 885885Protein PML
PRO_0000056002

Regions

Zinc finger62 – 9736RING-type
Zinc finger129 – 17143B box-type 1
Zinc finger188 – 23952B box-type 2
Region458 – 565108Interaction with PER2 By similarity
Region486 – 50015Nuclear localization signal By similarity
Region566 – 5727Sumo interaction motif (SIM) By similarity
Coiled coil295 – 33137 Potential
Compositional bias12 – 3827Pro-rich

Sites

Metal binding621Zinc 1 By similarity
Metal binding651Zinc 1 By similarity
Metal binding771Zinc 2 By similarity
Metal binding791Zinc 2 By similarity
Metal binding821Zinc 1 By similarity
Metal binding851Zinc 1 By similarity
Metal binding931Zinc 2 By similarity
Metal binding961Zinc 2 By similarity

Amino acid modifications

Modified residue171Phosphoserine; by HIPK2 Ref.17
Modified residue451Phosphoserine; by HIPK2 and MAPK1 By similarity
Modified residue471Phosphoserine; by HIPK2 and MAPK1 By similarity
Modified residue4041Phosphoserine; by MAPK1 and MAPK7 By similarity
Modified residue4971N6-acetyllysine By similarity
Modified residue5141Phosphoserine Ref.17
Modified residue5151Phosphoserine; by MAPK1 Ref.17
Modified residue5281Phosphoserine; by CDK1 and CDK2 Ref.20
Modified residue5401Phosphoserine; by MAPK1 By similarity
Modified residue5751Phosphoserine; by CK2 By similarity
Cross-link70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence431 – 47646Missing in isoform 2.
VSP_026028

Experimental info

Sequence conflict2101G → V in BAC25716. Ref.1
Sequence conflict4141A → V in BAC25716. Ref.1
Sequence conflict4241T → S in BAC25716. Ref.1
Sequence conflict4291E → V in AAH20990. Ref.2

Sequences

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

Last modified May 29, 2007. Version 3.
Checksum: 6A2F93F4CD482FDD

FASTA88598,242
        10         20         30         40         50         60 
METEPVSVQK VPAPPGSPCR QQDSALTPTP TMPPPEEPSE DYEHSQSPAE QAIQEEFQFL 

        70         80         90        100        110        120 
RCPSCQAQAK CPKLLPCLHT LCSGCLEAPG LQCPICKAPG QADANGEALD NVFFESLQRR 

       130        140        150        160        170        180 
LAVFRQIVDA QAACTRCKGL ADFWCFECEQ LICSKCFEAH QWYLKHEARP LADLRDNSVS 

       190        200        210        220        230        240 
SFLDSTRKSN IFCSNTNHRN PALTDIYCRG CAKPLCCTCA LLDRNHSHLH CDIGEEIQQW 

       250        260        270        280        290        300 
HEELGTMTQT LEEQGRTFDS AHAQMCSAIG QLDHARADIE KQIRARVRQV VDYVQAQERE 

       310        320        330        340        350        360 
LLEAVNDRYQ RDYQEIAGQL SCLEAVLQRI RTSGALVKRM KLYASDQEVL DMHSFLRKAL 

       370        380        390        400        410        420 
CSLRQEEPQN QKVQLLTRGF EEFKLCLQDF ISCITQRINA AVASPEAASN QPEAASTHPV 

       430        440        450        460        470        480 
TTSTPEDLEQ PKEVQSVQAQ ALELSKTQPV AMVKTVPGAH PVPVYAFSMQ GPTYREEASQ 

       490        500        510        520        530        540 
TVGSMKRKCS HEDCSRKIIK MESTEENEDR LATSSPEQSW PSTFKATSPP HLDGTSNPES 

       550        560        570        580        590        600 
TVPEKKILLP NNNHVTSDTG ETEERVVVIS SSEDSDTENL SSHELDDSSS ESSSLQLEGP 

       610        620        630        640        650        660 
NSLKALDESL AEPHLEDRTL VFFDLKIDNE TQKISQLAAV NRESKFRVLI QPEAFSVYSK 

       670        680        690        700        710        720 
AVSLEAGLRH FLSFLTTMHR PILACSRLWG PGLPIFFQTL SDINKLWEFQ DTISGFLAVL 

       730        740        750        760        770        780 
PLIRERIPGA SSFKLGNLAK TYLARNMSER SALASVLAMR DLCCLLEISP GLPLAQHIYS 

       790        800        810        820        830        840 
FSSLQCFASL QPLIQASVLP QSEARLLALH NVSFVELLNA YRTNRQEGLK KYVHYLSLQT 

       850        860        870        880 
TPLSSSASTQ VAQFLQALST HMEGLLEGHA PAGAEGKAES KGCLA 

« Hide

Isoform 2 [UniParc].

Checksum: AA1B497B0C2559E3
Show »

FASTA83993,263

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Lung.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Salivary gland.
[3]"Cloning of the murine homolog of the leukemia-associated PML gene."
Goddard A.D., Yuan J.Q., Fairbairn L., Dexter M., Borrow J., Kozak C., Solomon E.
Mamm. Genome 6:732-737(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-839 (ISOFORM 2).
[4]Goddard A.D., Howe K., Solomon E.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 130; 212; 284; 638; 731; 750; 770-772; 820 AND 839.
[5]"PML is essential for multiple apoptotic pathways."
Wang Z.G., Ruggero D., Ronchetti S., Zhong S., Gaboli M., Rivi R., Pandolfi P.P.
Nat. Genet. 20:266-272(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]"Role of PML in cell growth and the retinoic acid pathway."
Wang Z.G., Delva L., Gaboli M., Rivi R., Giorgio M., Cordon-Cardo C., Grosveld F., Pandolfi P.P.
Science 279:1547-1551(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]"A role for PML and the nuclear body in genomic stability."
Zhong S., Hu P., Ye T.Z., Stan R., Ellis N.A., Pandolfi P.P.
Oncogene 18:7941-7947(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Role of SUMO-1-modified PML in nuclear body formation."
Zhong S., Muller S., Ronchetti S., Freemont P.S., Dejean A., Pandolfi P.P.
Blood 95:2748-2752(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, SUBCELLULAR LOCATION, SUBUNIT.
[9]"Effects of promyelocytic leukemia protein on virus-host balance."
Bonilla W.V., Pinschewer D.D., Klenerman P., Rousson V., Gaboli M., Pandolfi P.P., Zinkernagel R.M., Salvato M.S., Hengartner H.
J. Virol. 76:3810-3818(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LCMV AND VSV RESTRICTION.
[10]"Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies."
Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P., De The H., Chelbi-Alix M.K.
Oncogene 21:7957-7970(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[11]"Forced expression of RNF36 induces cell apoptosis."
Shyu H.-W., Hsu S.-H., Hsieh-Li H.-M., Li H.
Exp. Cell Res. 287:301-313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM69.
[12]"Impairment of p53 acetylation, stability and function by an oncogenic transcription factor."
Insinga A., Monestiroli S., Ronzoni S., Carbone R., Pearson M., Pruneri G., Viale G., Appella E., Pelicci P., Minucci S.
EMBO J. 23:1144-1154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH2, DEGRADATION.
[14]"PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2 AND RPL11, SUBCELLULAR LOCATION.
[15]"Cytoplasmic PML function in TGF-beta signalling."
Lin H.K., Bergmann S., Pandolfi P.P.
Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR."
Bernardi R., Guernah I., Jin D., Grisendi S., Alimonti A., Teruya-Feldstein J., Cordon-Cardo C., Simon M.C., Rafii S., Pandolfi P.P.
Nature 442:779-785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH MTOR.
[17]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-514 AND SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[19]"PML: a tumor suppressor that regulates cell fate in mammary gland."
Li W., Rich T., Watson C.J.
Cell Cycle 8:2711-2717(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[20]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[21]"The tumor suppressor Pml regulates cell fate in the developing neocortex."
Regad T., Bellodi C., Nicotera P., Salomoni P.
Nat. Neurosci. 12:132-140(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH RB1, FUNCTION.
[22]"PML regulates apoptosis at endoplasmic reticulum by modulating calcium release."
Giorgi C., Ito K., Lin H.K., Santangelo C., Wieckowski M.R., Lebiedzinska M., Bononi A., Bonora M., Duszynski J., Bernardi R., Rizzuto R., Tacchetti C., Pinton P., Pandolfi P.P.
Science 330:1247-1251(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITPR3, SUBCELLULAR LOCATION.
[23]"A role for PML in innate immunity."
Lunardi A., Gaboli M., Giorgio M., Rivi R., Bygrave A., Antoniou M., Drabek D., Dzierzak E., Fagioli M., Salmena L., Botto M., Cordon-Cardo C., Luzzatto L., Pelicci P.G., Grosveld F., Pandolfi P.P.
Genes Cancer 2:10-19(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"PML is a key component for the differentiation of myeloid progenitor cells to macrophages."
Khalfin-Rabinovich Y., Weinstein A., Levi B.Z.
Int. Immunol. 23:287-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"The role of PML in the nervous system."
Salomoni P., Betts-Henderson J.
Mol. Neurobiol. 43:114-123(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[26]"PML regulates PER2 nuclear localization and circadian function."
Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A., Rea M.A., Zhao Z., Lee C.C., Chang K.S.
EMBO J. 31:1427-1439(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK, SUBCELLULAR LOCATION, INTERACTION WITH PML, DISRUPTION PHENOTYPE.
[27]"A metabolic prosurvival role for PML in breast cancer."
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.
J. Clin. Invest. 122:3088-3100(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARGC1A AND KAT2A.
[28]"Impaired cognitive function and reduced anxiety-related behavior in a promyelocytic leukemia (PML) tumor suppressor protein-deficient mouse."
Butler K., Martinez L.A., Tejada-Simon M.V.
Genes Brain Behav. 12:189-202(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK028044 mRNA. Translation: BAC25716.1.
BC020990 mRNA. Translation: AAH20990.2.
U33626 mRNA. Translation: AAA97601.2. Different initiation.
CCDSCCDS23239.1. [Q60953-1]
CCDS23240.2. [Q60953-2]
RefSeqNP_032910.3. NM_008884.5. [Q60953-2]
NP_835188.2. NM_178087.4. [Q60953-1]
UniGeneMm.392123.

3D structure databases

ProteinModelPortalQ60953.
SMRQ60953. Positions 54-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202265. 25 interactions.
DIPDIP-29279N.
IntActQ60953. 12 interactions.
MINTMINT-4108085.

PTM databases

PhosphoSiteQ60953.

Proteomic databases

MaxQBQ60953.
PaxDbQ60953.
PRIDEQ60953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986. [Q60953-1]
ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986. [Q60953-2]
GeneID18854.
KEGGmmu:18854.
UCSCuc009pwp.2. mouse. [Q60953-1]
uc009pwq.2. mouse. [Q60953-2]

Organism-specific databases

CTD5371.
MGIMGI:104662. Pml.

Phylogenomic databases

eggNOGNOG326718.
GeneTreeENSGT00510000048454.
HOGENOMHOG000115586.
HOVERGENHBG000552.
InParanoidQ60953.
KOK10054.
OMAKFRVLIQ.
OrthoDBEOG7M98FM.
PhylomeDBQ60953.
TreeFamTF336434.

Gene expression databases

ArrayExpressQ60953.
BgeeQ60953.
CleanExMM_PML.
GenevestigatorQ60953.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 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

ChiTaRSPML. mouse.
NextBio295230.
PROQ60953.
SOURCESearch...

Entry information

Entry namePML_MOUSE
AccessionPrimary (citable) accession number: Q60953
Secondary accession number(s): Q8CEJ1, Q8VCC4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot