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Q60953

- PML_MOUSE

UniProt

Q60953 - PML_MOUSE

Protein

Protein PML

Gene

Pml

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (29 May 2007)
      Previous versions | rss
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    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 1By similarity
    Metal bindingi65 – 651Zinc 1By similarity
    Metal bindingi77 – 771Zinc 2By similarity
    Metal bindingi79 – 791Zinc 2By similarity
    Metal bindingi82 – 821Zinc 1By similarity
    Metal bindingi85 – 851Zinc 1By similarity
    Metal bindingi93 – 931Zinc 2By similarity
    Metal bindingi96 – 961Zinc 2By similarity

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    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 By similarity; Peripheral membrane protein By similarity; 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.By similarity

    GO - Cellular componenti

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

    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 PMLPRO_0000056002Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine; by HIPK21 Publication
    Modified residuei45 – 451Phosphoserine; by HIPK2 and MAPK1By similarity
    Modified residuei47 – 471Phosphoserine; by HIPK2 and MAPK1By 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 MAPK7By similarity
    Cross-linki486 – 486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei497 – 4971N6-acetyllysineBy 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 MAPK1By similarity
    Modified residuei575 – 5751Phosphoserine; by CK2By 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.By similarity
    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.By similarity
    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.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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni458 – 565108Interaction with PER2By similarityAdd
    BLAST
    Regioni486 – 50015Nuclear localization signalBy similarityAdd
    BLAST
    Regioni566 – 5727Sumo interaction motif (SIM)By similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili295 – 33137Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 3827Pro-richAdd
    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

    Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101G → V in BAC25716. (PubMed:16141072)Curated
    Sequence conflicti414 – 4141A → V in BAC25716. (PubMed:16141072)Curated
    Sequence conflicti424 – 4241T → S in BAC25716. (PubMed:16141072)Curated
    Sequence conflicti429 – 4291E → V in AAH20990. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei431 – 47646Missing in isoform 2. 2 PublicationsVSP_026028Add
    BLAST

    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

    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: October 1, 2014
    This is version 143 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