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Q60953

- PML_MOUSE

UniProt

Q60953 - PML_MOUSE

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Protein
Protein PML
Gene
Pml
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).16 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Zinc 1 By similarity
Metal bindingi65 – 651Zinc 1 By similarity
Metal bindingi77 – 771Zinc 2 By similarity
Metal bindingi79 – 791Zinc 2 By similarity
Metal bindingi82 – 821Zinc 1 By similarity
Metal bindingi85 – 851Zinc 1 By similarity
Metal bindingi93 – 931Zinc 2 By similarity
Metal bindingi96 – 961Zinc 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri62 – 9736RING-type
Add
BLAST
Zinc fingeri129 – 17143B box-type 1
Add
BLAST
Zinc fingeri188 – 23952B box-type 2
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. SMAD binding Source: MGI
  3. cobalt ion binding Source: Ensembl
  4. protein binding Source: IntAct
  5. transcription coactivator activity Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  2. PML body organization Source: MGI
  3. SMAD protein import into nucleus Source: MGI
  4. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  5. branching involved in mammary gland duct morphogenesis Source: MGI
  6. cell aging Source: UniProtKB
  7. cell cycle arrest Source: UniProtKB
  8. cell fate commitment Source: MGI
  9. cellular response to interleukin-4 Source: MGI
  10. cellular senescence Source: UniProtKB
  11. circadian regulation of gene expression Source: UniProtKB
  12. common-partner SMAD protein phosphorylation Source: MGI
  13. defense response to virus Source: UniProtKB-KW
  14. endoplasmic reticulum calcium ion homeostasis Source: UniProtKB
  15. entrainment of circadian clock by photoperiod Source: UniProtKB
  16. extrinsic apoptotic signaling pathway Source: MGI
  17. innate immune response Source: UniProt
  18. intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  19. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  20. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  21. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
  22. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  23. maintenance of protein location in nucleus Source: MGI
  24. myeloid cell differentiation Source: MGI
  25. negative regulation of angiogenesis Source: UniProtKB
  26. negative regulation of cell growth Source: UniProtKB
  27. negative regulation of cell proliferation Source: MGI
  28. negative regulation of mitotic cell cycle Source: Ensembl
  29. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  30. negative regulation of telomerase activity Source: Ensembl
  31. negative regulation of telomere maintenance via telomerase Source: Ensembl
  32. negative regulation of transcription, DNA-templated Source: UniProtKB
  33. negative regulation of translation in response to oxidative stress Source: Ensembl
  34. negative regulation of viral release from host cell Source: UniProt
  35. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
  36. positive regulation of apoptotic signaling pathway Source: MGI
  37. positive regulation of defense response to virus by host Source: Ensembl
  38. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  39. positive regulation of histone deacetylation Source: UniProtKB
  40. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  41. protein complex assembly Source: UniProtKB
  42. protein stabilization Source: Ensembl
  43. protein targeting Source: UniProtKB
  44. regulation of MHC class I biosynthetic process Source: MGI
  45. regulation of calcium ion transport into cytosol Source: UniProtKB
  46. regulation of circadian rhythm Source: UniProtKB
  47. regulation of double-strand break repair Source: UniProtKB
  48. regulation of protein phosphorylation Source: UniProtKB
  49. regulation of transcription, DNA-templated Source: MGI
  50. response to UV Source: MGI
  51. response to gamma radiation Source: MGI
  52. response to hypoxia Source: UniProtKB
  53. retinoic acid receptor signaling pathway Source: MGI
  54. transcription, DNA-templated Source: UniProtKB-KW
  55. transforming growth factor beta receptor signaling pathway Source: MGI
  56. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Antiviral defense, Apoptosis, Biological rhythms, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198660. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PML
Gene namesi
Name:Pml
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:104662. Pml.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. early endosome membrane Source: UniProtKB-SubCell
  4. extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  5. nuclear matrix Source: MGI
  6. nuclear membrane Source: Ensembl
  7. nucleolus Source: UniProtKB
  8. nucleoplasm Source: UniProtKB
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.7 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885Protein PML
PRO_0000056002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine; by HIPK21 Publication
Modified residuei45 – 451Phosphoserine; by HIPK2 and MAPK1 By similarity
Modified residuei47 – 471Phosphoserine; by HIPK2 and MAPK1 By similarity
Cross-linki70 – 70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki165 – 165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki384 – 384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei404 – 4041Phosphoserine; by MAPK1 and MAPK7 By similarity
Cross-linki486 – 486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei497 – 4971N6-acetyllysine By similarity
Cross-linki500 – 500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei514 – 5141Phosphoserine1 Publication
Modified residuei515 – 5151Phosphoserine; by MAPK11 Publication
Modified residuei528 – 5281Phosphoserine; by CDK1 and CDK21 Publication
Modified residuei540 – 5401Phosphoserine; by MAPK1 By similarity
Modified residuei575 – 5751Phosphoserine; by CK2 By similarity

Post-translational modificationi

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.1 Publication
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.1 Publication
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ60953.
PaxDbiQ60953.
PRIDEiQ60953.

PTM databases

PhosphoSiteiQ60953.

Expressioni

Gene expression databases

ArrayExpressiQ60953.
BgeeiQ60953.
CleanExiMM_PML.
GenevestigatoriQ60953.

Interactioni

Subunit structurei

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Axin1Q14DJ84EBI-4406901,EBI-4312125
FasP254466EBI-3895605,EBI-296206
SkilQ609795EBI-3895605,EBI-7213804

Protein-protein interaction databases

BioGridi202265. 25 interactions.
DIPiDIP-29279N.
IntActiQ60953. 12 interactions.
MINTiMINT-4108085.

Structurei

3D structure databases

ProteinModelPortaliQ60953.
SMRiQ60953. Positions 54-109.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni458 – 565108Interaction with PER2 By similarity
Add
BLAST
Regioni486 – 50015Nuclear localization signal By similarity
Add
BLAST
Regioni566 – 5727Sumo interaction motif (SIM) By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili295 – 33137 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 3827Pro-rich
Add
BLAST

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG326718.
GeneTreeiENSGT00510000048454.
HOGENOMiHOG000115586.
HOVERGENiHBG000552.
InParanoidiQ60953.
KOiK10054.
OMAiKFRVLIQ.
OrthoDBiEOG7M98FM.
PhylomeDBiQ60953.
TreeFamiTF336434.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q60953-1) [UniParc]FASTAAdd to Basket

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.

« Hide

METEPVSVQK VPAPPGSPCR QQDSALTPTP TMPPPEEPSE DYEHSQSPAE    50
QAIQEEFQFL RCPSCQAQAK CPKLLPCLHT LCSGCLEAPG LQCPICKAPG 100
QADANGEALD NVFFESLQRR LAVFRQIVDA QAACTRCKGL ADFWCFECEQ 150
LICSKCFEAH QWYLKHEARP LADLRDNSVS SFLDSTRKSN IFCSNTNHRN 200
PALTDIYCRG CAKPLCCTCA LLDRNHSHLH CDIGEEIQQW HEELGTMTQT 250
LEEQGRTFDS AHAQMCSAIG QLDHARADIE KQIRARVRQV VDYVQAQERE 300
LLEAVNDRYQ RDYQEIAGQL SCLEAVLQRI RTSGALVKRM KLYASDQEVL 350
DMHSFLRKAL CSLRQEEPQN QKVQLLTRGF EEFKLCLQDF ISCITQRINA 400
AVASPEAASN QPEAASTHPV TTSTPEDLEQ PKEVQSVQAQ ALELSKTQPV 450
AMVKTVPGAH PVPVYAFSMQ GPTYREEASQ TVGSMKRKCS HEDCSRKIIK 500
MESTEENEDR LATSSPEQSW PSTFKATSPP HLDGTSNPES TVPEKKILLP 550
NNNHVTSDTG ETEERVVVIS SSEDSDTENL SSHELDDSSS ESSSLQLEGP 600
NSLKALDESL AEPHLEDRTL VFFDLKIDNE TQKISQLAAV NRESKFRVLI 650
QPEAFSVYSK AVSLEAGLRH FLSFLTTMHR PILACSRLWG PGLPIFFQTL 700
SDINKLWEFQ DTISGFLAVL PLIRERIPGA SSFKLGNLAK TYLARNMSER 750
SALASVLAMR DLCCLLEISP GLPLAQHIYS FSSLQCFASL QPLIQASVLP 800
QSEARLLALH NVSFVELLNA YRTNRQEGLK KYVHYLSLQT TPLSSSASTQ 850
VAQFLQALST HMEGLLEGHA PAGAEGKAES KGCLA 885
Length:885
Mass (Da):98,242
Last modified:May 29, 2007 - v3
Checksum:i6A2F93F4CD482FDD
GO
Isoform 2 (identifier: Q60953-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:839
Mass (Da):93,263
Checksum:iAA1B497B0C2559E3
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei431 – 47646Missing in isoform 2.
VSP_026028Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101G → V in BAC25716. 1 Publication
Sequence conflicti414 – 4141A → V in BAC25716. 1 Publication
Sequence conflicti424 – 4241T → S in BAC25716. 1 Publication
Sequence conflicti429 – 4291E → V in AAH20990. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK028044 mRNA. Translation: BAC25716.1.
BC020990 mRNA. Translation: AAH20990.2.
U33626 mRNA. Translation: AAA97601.2. Different initiation.
CCDSiCCDS23239.1. [Q60953-1]
CCDS23240.2. [Q60953-2]
RefSeqiNP_032910.3. NM_008884.5. [Q60953-2]
NP_835188.2. NM_178087.4. [Q60953-1]
UniGeneiMm.392123.

Genome annotation databases

EnsembliENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986. [Q60953-1]
ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986. [Q60953-2]
GeneIDi18854.
KEGGimmu:18854.
UCSCiuc009pwp.2. mouse. [Q60953-1]
uc009pwq.2. mouse. [Q60953-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK028044 mRNA. Translation: BAC25716.1 .
BC020990 mRNA. Translation: AAH20990.2 .
U33626 mRNA. Translation: AAA97601.2 . Different initiation.
CCDSi CCDS23239.1. [Q60953-1 ]
CCDS23240.2. [Q60953-2 ]
RefSeqi NP_032910.3. NM_008884.5. [Q60953-2 ]
NP_835188.2. NM_178087.4. [Q60953-1 ]
UniGenei Mm.392123.

3D structure databases

ProteinModelPortali Q60953.
SMRi Q60953. Positions 54-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202265. 25 interactions.
DIPi DIP-29279N.
IntActi Q60953. 12 interactions.
MINTi MINT-4108085.

PTM databases

PhosphoSitei Q60953.

Proteomic databases

MaxQBi Q60953.
PaxDbi Q60953.
PRIDEi Q60953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000085673 ; ENSMUSP00000082816 ; ENSMUSG00000036986 . [Q60953-1 ]
ENSMUST00000114136 ; ENSMUSP00000109771 ; ENSMUSG00000036986 . [Q60953-2 ]
GeneIDi 18854.
KEGGi mmu:18854.
UCSCi uc009pwp.2. mouse. [Q60953-1 ]
uc009pwq.2. mouse. [Q60953-2 ]

Organism-specific databases

CTDi 5371.
MGIi MGI:104662. Pml.

Phylogenomic databases

eggNOGi NOG326718.
GeneTreei ENSGT00510000048454.
HOGENOMi HOG000115586.
HOVERGENi HBG000552.
InParanoidi Q60953.
KOi K10054.
OMAi KFRVLIQ.
OrthoDBi EOG7M98FM.
PhylomeDBi Q60953.
TreeFami TF336434.

Enzyme and pathway databases

Reactomei REACT_198660. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSi PML. mouse.
NextBioi 295230.
PROi Q60953.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q60953.
Bgeei Q60953.
CleanExi MM_PML.
Genevestigatori Q60953.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR021978. DUF3583.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF12126. DUF3583. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view ]
SMARTi SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. 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. 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. 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. Cited for: FUNCTION, INTERACTION WITH ITPR3, SUBCELLULAR LOCATION.
  23. 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. Cited for: REVIEW ON FUNCTION.
  26. Cited for: FUNCTION IN CIRCADIAN CLOCK, SUBCELLULAR LOCATION, INTERACTION WITH PML, DISRUPTION PHENOTYPE.
  27. 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.

Entry informationi

Entry nameiPML_MOUSE
AccessioniPrimary (citable) accession number: Q60953
Secondary accession number(s): Q8CEJ1, Q8VCC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 29, 2007
Last modified: September 3, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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