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P23804

- MDM2_MOUSE

UniProt

P23804 - MDM2_MOUSE

Protein

E3 ubiquitin-protein ligase Mdm2

Gene

Mdm2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri297 – 32630RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri436 – 47742RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. p53 binding Source: BHF-UCL
    3. protein binding Source: IntAct
    4. scaffold protein binding Source: BHF-UCL
    5. ubiquitin-protein transferase activity Source: MGI
    6. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. cellular response to acid chemical Source: Ensembl
    2. cellular response to alkaloid Source: Ensembl
    3. cellular response to antibiotic Source: Ensembl
    4. cellular response to estrogen stimulus Source: Ensembl
    5. cellular response to growth factor stimulus Source: Ensembl
    6. cellular response to hydrogen peroxide Source: Ensembl
    7. cellular response to hypoxia Source: Ensembl
    8. cellular response to peptide hormone stimulus Source: Ensembl
    9. cellular response to UV-C Source: Ensembl
    10. cellular response to vitamin B1 Source: Ensembl
    11. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Ensembl
    12. establishment of protein localization Source: Ensembl
    13. negative regulation of apoptotic process Source: Ensembl
    14. negative regulation of cell cycle arrest Source: InterPro
    15. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    16. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: Ensembl
    17. negative regulation of protein processing Source: Ensembl
    18. negative regulation of transcription from RNA polymerase II promoter Source: InterPro
    19. peptidyl-lysine modification Source: Ensembl
    20. positive regulation of cell cycle Source: MGI
    21. positive regulation of gene expression Source: Ensembl
    22. positive regulation of mitotic cell cycle Source: Ensembl
    23. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    24. positive regulation of protein export from nucleus Source: Ensembl
    25. protein catabolic process Source: MGI
    26. protein complex assembly Source: Ensembl
    27. protein destabilization Source: Ensembl
    28. protein localization to nucleus Source: Ensembl
    29. protein ubiquitination Source: UniProtKB
    30. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
    31. response to carbohydrate Source: Ensembl
    32. response to cocaine Source: Ensembl
    33. response to drug Source: Ensembl
    34. response to ether Source: Ensembl
    35. response to iron ion Source: Ensembl
    36. response to magnesium ion Source: Ensembl
    37. response to morphine Source: Ensembl
    38. traversing start control point of mitotic cell cycle Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_220918. AKT phosphorylates targets in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase Mdm2 (EC:6.3.2.-)
    Alternative name(s):
    Double minute 2 protein
    Oncoprotein Mdm2
    p53-binding protein Mdm2
    Gene namesi
    Name:Mdm2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:96952. Mdm2.

    Subcellular locationi

    Nucleusnucleoplasm 1 Publication. Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication
    Note: Colocalizes with RASSF1 isoform A in the nucleus By similarity. Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: Ensembl
    3. nuclear body Source: Ensembl
    4. nucleolus Source: UniProtKB
    5. nucleus Source: MGI
    6. plasma membrane Source: Ensembl
    7. protein complex Source: Ensembl
    8. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    The gene for this protein is amplified in a mouse tumor cell line.

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489E3 ubiquitin-protein ligase Mdm2PRO_0000018650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei163 – 1631Phosphoserine; by SGK1By similarity
    Modified residuei238 – 2381PhosphoserineBy similarity
    Modified residuei240 – 2401PhosphoserineBy similarity
    Modified residuei244 – 2441PhosphoserineBy similarity
    Modified residuei258 – 2581PhosphoserineBy similarity
    Modified residuei260 – 2601PhosphoserineBy similarity
    Modified residuei394 – 3941Phosphoserine; by ATMBy similarity
    Modified residuei406 – 4061Phosphoserine; by ATMBy similarity
    Modified residuei417 – 4171Phosphothreonine; by ATMBy similarity
    Modified residuei423 – 4231Phosphoserine; by ATMBy similarity
    Modified residuei427 – 4271Phosphoserine; by ATMBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-163 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation By similarity.By similarity
    Autoubiquitination leads to proteasomal degradation; resulting in p53/TP53 activation it may be regulated by SFN. Also ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its accumulation and increases deubiquitination and degradation of p53/TP53. Deubiquitinated by USP7 leading to its stabilization By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP23804.

    PTM databases

    PhosphoSiteiP23804.

    Miscellaneous databases

    PMAP-CutDBQ91XK7.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed at low-level throughout embryo development and in adult tissues. MDM2-p90 is much more abundant than MDM2-p76 in testis, brain, heart, and kidney, but in the thymus, spleen, and intestine, the levels of the MDM2 proteins are roughly equivalent.1 Publication

    Inductioni

    By UV light.1 Publication

    Gene expression databases

    ArrayExpressiP23804.
    BgeeiP23804.
    CleanExiMM_MDM2.
    GenevestigatoriP23804.

    Interactioni

    Subunit structurei

    Binds p53/TP53, TP73/p73, ARF/P14, PML, RBL5 and RP11, and specifically to RNA. Can interact also with retinoblastoma protein (RB), E1A-associated protein EP300 and the E2F1 transcription factor. Forms a ternary complex with p53/TP53 and WWOX. Interacts with CDKN2AIP, RFWD3, USP7, PYHIN1, UBXN6, and RBBP6. Isoform Mdm2-F does not interact with p53/TP53. Interacts with AARB1. Interacts (isoform 2) with PSMA3. Found in a trimeric complex with MDM2, MDM4 and UPB2. Interacts with USP2 (via N-terminus and C-terminus). Interacts with MDM4. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts directly with DAXX and USP7. Interacts (via C-terminus) with RASSF1 isoform A (via N-terminus); the interaction is independent of TP53. Interacts with DAXX. Interacts with APEX1; the interaction leads to its ubiquitination and degradation. Interacts with RYBP; this inhibits ubiquitination of TP53. Identified in a complex with RYBP and p53/TP53. Also component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in regulating p53/TP53 stabilization and activity. Binds directly both p53/TP53 and TRIM28. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor responses with DNA damage. Interacts directly with both TRIM28 and ERBB4 in the complex. Interacts with DYRK2. Interacts with TRIM13; the interaction ubiquitinates MDM2 leading to its proteasomal degradation. Interacts with IGF1R. Interacts with SNAI1; this interaction promotes SNAI1 ubiquitination. Interacts with NOTCH1 (via intracellular domain). Interacts with FHIT By similarity. Interacts with AARB2, MTBP and TBRG1. Interacts with RFFL. Interacts with MTA1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Arrb1Q8BWG84EBI-641788,EBI-641778
    Dlg4Q621083EBI-641788,EBI-300895
    Hipk1O889043EBI-641788,EBI-692945
    Mdm4O356182EBI-3386480,EBI-2603376
    PLK1P533502EBI-641788,EBI-476768From a different organism.
    Rassf5Q5EBH13EBI-641788,EBI-960530
    Rpl11Q9CXW44EBI-641788,EBI-1548890
    Rpl23P628302EBI-641788,EBI-2365752
    Rpl5P479623EBI-641788,EBI-773940
    Rps6kb1Q8BSK82EBI-641788,EBI-646423
    Tp53P023403EBI-641788,EBI-474016

    Protein-protein interaction databases

    BioGridi201372. 39 interactions.
    DIPiDIP-24174N.
    DIP-24196N.
    IntActiP23804. 19 interactions.
    MINTiMINT-139756.

    Structurei

    3D structure databases

    ProteinModelPortaliP23804.
    SMRiP23804. Positions 26-108, 288-333, 430-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 10781SWIBAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 110110Necessary for interaction with USP2By similarityAdd
    BLAST
    Regioni147 – 22882Interaction with PYHIN1 and necessary for interaction with RFFLBy similarityAdd
    BLAST
    Regioni167 – 304138Interaction with MTBPAdd
    BLAST
    Regioni208 – 30295ARF-bindingAdd
    BLAST
    Regioni221 – 23010Interaction with USP7By similarity
    Regioni240 – 32990Region IIAdd
    BLAST
    Regioni274 – 489216Necessary for interaction with USP2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi176 – 1827Nuclear localization signalSequence Analysis
    Motifi183 – 19513Nuclear export signalAdd
    BLAST
    Motifi464 – 4718Nucleolar localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi203 – 21311Poly-SerAdd
    BLAST
    Compositional biasi221 – 29979Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself.

    Sequence similaritiesi

    Belongs to the MDM2/MDM4 family.Curated
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SWIB domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri297 – 32630RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri436 – 47742RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG46328.
    GeneTreeiENSGT00530000063539.
    HOGENOMiHOG000293341.
    HOVERGENiHBG013472.
    InParanoidiQ91XK7.
    KOiK06643.
    OMAiLCVIREI.
    OrthoDBiEOG7RRF7T.
    TreeFamiTF105306.

    Family and domain databases

    Gene3Di1.10.245.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR028340. Mdm2.
    IPR015459. MDM2_E3_ligase.
    IPR016495. p53_neg-reg_MDM_2/4.
    IPR003121. SWIB_MDM2_domain.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PANTHERiPTHR10360:SF11. PTHR10360:SF11. 1 hit.
    PfamiPF02201. SWIB. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500700. MDM2. 1 hit.
    PIRSF006748. p53_MDM_2/4. 1 hit.
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47592. SSF47592. 2 hits.
    PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 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 and alternative initiation. Align

    Isoform Mdm2-p90 (identifier: P23804-1) [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

    MCNTNMSVST EGAASTSQIP ASEQETLVRP KPLLLKLLKS VGAQNDTYTM    50
    KEIIFYIGQY IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY 100
    AMIYRNLVAV SQQDSGTSLS ESRRQPEGGS DLKDPLQAPP EEKPSSSDLI 150
    SRLSTSSRRR SISETEENTD ELPGERHRKR RRSLSFDPSL GLCELREMCS 200
    GGSSSSSSSS SESTETPSHQ DLDDGVSEHS GDCLDQDSVS DQFSVEFEVE 250
    SLDSEDYSLS DEGHELSDED DEVYRVTVYQ TGESDTDSFE GDPEISLADY 300
    WKCTSCNEMN PPLPSHCKRC WTLRENWLPD DKGKDKVEIS EKAKLENSAQ 350
    AEEGLDVPDG KKLTENDAKE PCAEEDSEEK AEQTPLSQES DDYSQPSTSS 400
    SIVYSSQESV KELKEETQDK DESVESSFSL NAIEPCVICQ GRPKNGCIVH 450
    GKTGHLMSCF TCAKKLKKRN KPCPVCRQPI QMIVLTYFN 489
    Length:489
    Mass (Da):54,558
    Last modified:July 27, 2011 - v3
    Checksum:i4ABF489A82038DF4
    GO
    Isoform Mdm2-p76 (identifier: P23804-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: Missing.

    Note: Does not bind to p53. Can be produced by alternative initiation at Met-50 of isoform Mdm2-p90, but is produced more efficiently by alternative splicing.

    Show »
    Length:440
    Mass (Da):49,351
    Checksum:iC574909560CC1A5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031S → T in CAA41684. (PubMed:2026149)Curated
    Sequence conflicti419 – 4191D → H in CAA41684. (PubMed:2026149)Curated
    Sequence conflicti486 – 4861T → S in CAA41684. (PubMed:2026149)Curated
    Sequence conflicti486 – 4861T → S in AAA91167. (PubMed:8917101)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949Missing in isoform Mdm2-p76. CuratedVSP_003215Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58876 mRNA. Translation: CAA41684.1.
    U40145 Genomic DNA. Translation: AAA91167.1.
    U47944
    , U47935, U47936, U47937, U47938, U47939, U47940, U47941, U47942, U47943 Genomic DNA. Translation: AAB09030.1.
    U47934 mRNA. Translation: AAB09031.1.
    AK004719 mRNA. Translation: BAB23502.1.
    AK088638 mRNA. Translation: BAC40470.1.
    BC050902 mRNA. Translation: AAH50902.1.
    CCDSiCCDS24194.1. [P23804-1]
    CCDS70110.1. [P23804-2]
    PIRiS15349.
    RefSeqiNP_001275515.1. NM_001288586.1. [P23804-2]
    NP_034916.1. NM_010786.4. [P23804-1]
    XP_006513374.1. XM_006513311.1. [P23804-2]
    UniGeneiMm.22670.
    Mm.447669.

    Genome annotation databases

    EnsembliENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184. [P23804-1]
    ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184. [P23804-2]
    GeneIDi17246.
    KEGGimmu:17246.
    UCSCiuc007hdl.1. mouse. [P23804-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58876 mRNA. Translation: CAA41684.1 .
    U40145 Genomic DNA. Translation: AAA91167.1 .
    U47944
    , U47935 , U47936 , U47937 , U47938 , U47939 , U47940 , U47941 , U47942 , U47943 Genomic DNA. Translation: AAB09030.1 .
    U47934 mRNA. Translation: AAB09031.1 .
    AK004719 mRNA. Translation: BAB23502.1 .
    AK088638 mRNA. Translation: BAC40470.1 .
    BC050902 mRNA. Translation: AAH50902.1 .
    CCDSi CCDS24194.1. [P23804-1 ]
    CCDS70110.1. [P23804-2 ]
    PIRi S15349.
    RefSeqi NP_001275515.1. NM_001288586.1. [P23804-2 ]
    NP_034916.1. NM_010786.4. [P23804-1 ]
    XP_006513374.1. XM_006513311.1. [P23804-2 ]
    UniGenei Mm.22670.
    Mm.447669.

    3D structure databases

    ProteinModelPortali P23804.
    SMRi P23804. Positions 26-108, 288-333, 430-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201372. 39 interactions.
    DIPi DIP-24174N.
    DIP-24196N.
    IntActi P23804. 19 interactions.
    MINTi MINT-139756.

    PTM databases

    PhosphoSitei P23804.

    Proteomic databases

    PRIDEi P23804.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020408 ; ENSMUSP00000020408 ; ENSMUSG00000020184 . [P23804-1 ]
    ENSMUST00000105263 ; ENSMUSP00000100898 ; ENSMUSG00000020184 . [P23804-2 ]
    GeneIDi 17246.
    KEGGi mmu:17246.
    UCSCi uc007hdl.1. mouse. [P23804-1 ]

    Organism-specific databases

    CTDi 4193.
    MGIi MGI:96952. Mdm2.

    Phylogenomic databases

    eggNOGi NOG46328.
    GeneTreei ENSGT00530000063539.
    HOGENOMi HOG000293341.
    HOVERGENi HBG013472.
    InParanoidi Q91XK7.
    KOi K06643.
    OMAi LCVIREI.
    OrthoDBi EOG7RRF7T.
    TreeFami TF105306.

    Enzyme and pathway databases

    Reactomei REACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_220918. AKT phosphorylates targets in the cytosol.

    Miscellaneous databases

    ChiTaRSi MDM2. mouse.
    NextBioi 291706.
    PMAP-CutDB Q91XK7.
    PROi P23804.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23804.
    Bgeei P23804.
    CleanExi MM_MDM2.
    Genevestigatori P23804.

    Family and domain databases

    Gene3Di 1.10.245.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR028340. Mdm2.
    IPR015459. MDM2_E3_ligase.
    IPR016495. p53_neg-reg_MDM_2/4.
    IPR003121. SWIB_MDM2_domain.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    PANTHERi PTHR10360:SF11. PTHR10360:SF11. 1 hit.
    Pfami PF02201. SWIB. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500700. MDM2. 1 hit.
    PIRSF006748. p53_MDM_2/4. 1 hit.
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47592. SSF47592. 2 hits.
    PROSITEi PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line."
      Fakharzadeh S.S., Trusko S.P., George D.L.
      EMBO J. 10:1565-1569(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2-P90).
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM MDM2-P90).
      Strain: 129/Sv.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MDM2-P90).
      Strain: 129/Sv.
    4. "Multiple murine double minute gene 2 (MDM2) proteins are induced by ultraviolet light."
      Saucedo L.J., Myers C.D., Perry M.E.
      J. Biol. Chem. 274:8161-8168(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS MDM2-P90 AND MDM2-P76), TISSUE SPECIFICITY, INDUCTION.
    5. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Lung and Thymus.
    6. "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].
      Strain: C57BL/6.
    7. "Cooperative signals governing ARF-mdm2 interaction and nucleolar localization of the complex."
      Weber J.D., Kuo M.-L., Bothner B., DiGiammarino E.L., Kriwacki R.W., Roussel M.F., Sherr C.J.
      Mol. Cell. Biol. 20:2517-2528(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOLAR LOCALIZATION SIGNAL.
    8. "Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage."
      Khosravi R., Maya R., Gottlieb T., Oren M., Shiloh Y., Shkedy D.
      Proc. Natl. Acad. Sci. U.S.A. 96:14973-14977(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ATM.
    9. "A novel cellular protein (MTBP) binds to MDM2 and induces a G1 arrest that is suppressed by MDM2."
      Boyd M.T., Vlatkovic N., Haines D.S.
      J. Biol. Chem. 275:31883-31890(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTBP.
    10. "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin."
      Shenoy S.K., McDonald P.H., Kohout T.A., Lefkowitz R.J.
      Science 294:1307-1313(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AARB2.
    11. "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 PML AND RPL11, SUBCELLULAR LOCATION.
    12. Cited for: INTERACTION WITH TBRG1.

    Entry informationi

    Entry nameiMDM2_MOUSE
    AccessioniPrimary (citable) accession number: P23804
    Secondary accession number(s): Q61040, Q64330, Q91XK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 152 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