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O15151

- MDM4_HUMAN

UniProt

O15151 - MDM4_HUMAN

Protein

Protein Mdm4

Gene

MDM4

Organism
Homo sapiens (Human)
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 2 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri300 – 32930RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri437 – 47842RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular response to hypoxia Source: UniProtKB
    3. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    4. G0 to G1 transition Source: UniProtKB
    5. negative regulation of apoptotic process Source: InterPro
    6. negative regulation of cell cycle arrest Source: InterPro
    7. negative regulation of cell proliferation Source: ProtInc
    8. negative regulation of protein catabolic process Source: UniProtKB
    9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. positive regulation of cell proliferation Source: Ensembl
    11. protein complex assembly Source: UniProtKB
    12. protein stabilization Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein Mdm4
    Alternative name(s):
    Double minute 4 protein
    Mdm2-like p53-binding protein
    Protein Mdmx
    p53-binding protein Mdm4
    Gene namesi
    Name:MDM4
    Synonyms:MDMX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6974. MDM4.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi437 – 4371C → G: Fails to interact with MDM2. 1 Publication

    Organism-specific databases

    PharmGKBiPA30719.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Protein Mdm4PRO_0000157336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei342 – 3421Phosphoserine; by CHEK21 Publication
    Modified residuei367 – 3671Phosphoserine; by CHEK1 and CHEK22 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent.3 Publications
    Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO15151.
    PaxDbiO15151.
    PRIDEiO15151.

    PTM databases

    PhosphoSiteiO15151.

    Miscellaneous databases

    PMAP-CutDBO15151.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested with high levels in thymus.

    Inductioni

    Down-regulated by cisplatin (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO15151.
    BgeeiO15151.
    CleanExiHS_MDM4.
    GenevestigatoriO15151.

    Organism-specific databases

    HPAiHPA018919.

    Interactioni

    Subunit structurei

    Interacts with MDM2, TP53, TP73 and USP2. Found in a trimeric complex with UPB2, MDM2 and MDM4. Interacts (phosphorylated) with YWHAG; negatively regulates MDM4 activity toward TP53.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P03255-23EBI-398437,EBI-6859460From a different organism.
    Q3YBA86EBI-398437,EBI-7852331
    BCL2P104154EBI-398437,EBI-77694
    CSNK1A1P487292EBI-398437,EBI-1383726
    MDM2Q009878EBI-398437,EBI-389668
    MKRN3Q130642EBI-398437,EBI-2340269
    RB1P064004EBI-398437,EBI-491274
    TP53P0463713EBI-398437,EBI-366083
    UBE2D2P628372EBI-398437,EBI-347677
    USP7Q9300915EBI-398437,EBI-302474
    YWHAEP622583EBI-398437,EBI-356498
    YWHAGP619817EBI-398437,EBI-359832

    Protein-protein interaction databases

    BioGridi110359. 50 interactions.
    DIPiDIP-24199N.
    IntActiO15151. 29 interactions.
    MINTiMINT-113852.
    STRINGi9606.ENSP00000356150.

    Structurei

    Secondary structure

    1
    490
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 293
    Helixi31 – 399
    Helixi49 – 6214
    Beta strandi70 – 756
    Helixi80 – 856
    Beta strandi88 – 914
    Helixi96 – 10510
    Beta strandi106 – 1094
    Beta strandi307 – 3093
    Turni321 – 3233
    Helixi431 – 4344
    Turni438 – 4403
    Beta strandi441 – 4455
    Beta strandi447 – 4515
    Beta strandi454 – 4596
    Helixi461 – 4699
    Turni475 – 4773
    Beta strandi483 – 4897

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CR8NMR-A300-339[»]
    2VJEX-ray2.20B/D428-490[»]
    2VJFX-ray2.30B/D428-490[»]
    2VYRX-ray2.00A/B/C/D16-116[»]
    3DABX-ray1.90A/C/E/G23-111[»]
    3EQYX-ray1.63A/B24-108[»]
    3FDOX-ray1.40A23-111[»]
    3FE7X-ray1.35A14-111[»]
    3FEAX-ray1.33A14-111[»]
    3JZOX-ray1.80A23-111[»]
    3JZPX-ray1.74A23-111[»]
    3JZQX-ray1.80A/B23-111[»]
    3LBJX-ray1.50E23-111[»]
    3MQRX-ray1.80B395-404[»]
    3U15X-ray1.80A/B/C/D14-111[»]
    ProteinModelPortaliO15151.
    SMRiO15151. Positions 26-108, 301-344, 429-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15151.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 10681SWIBAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni246 – 33287Region IIAdd
    BLAST
    Regioni393 – 49098Necessary for interaction with UBP2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi442 – 4454Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi243 – 30866Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.

    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 fingeri300 – 32930RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri437 – 47842RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG46328.
    HOGENOMiHOG000293341.
    HOVERGENiHBG013472.
    InParanoidiO15151.
    KOiK10127.
    OMAiLKPCSLC.
    OrthoDBiEOG7RRF7T.
    PhylomeDBiO15151.
    TreeFamiTF105306.

    Family and domain databases

    Gene3Di1.10.245.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR015458. MDM4.
    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:SF10. PTHR10360:SF10. 1 hit.
    PfamiPF02201. SWIB. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500699. MDM4. 1 hit.
    PIRSF006748. p53_MDM_2/4. 1 hit.
    SMARTiSM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47592. SSF47592. 1 hit.
    PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: O15151-1) [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

    MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK    50
    EVMHYLGQYI MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD 100
    MLRKNLVTLA TATTDAAQTL ALAQDHSMDI PSQDQLKQSA EESSTSRKRT 150
    TEDDIPTLPT SEHKCIHSRE DEDLIENLAQ DETSRLDLGF EEWDVAGLPW 200
    WFLGNLRSNY TPRSNGSTDL QTNQDVGTAI VSDTTDDLWF LNESVSEQLG 250
    VGIKVEAADT EQTSEEVGKV SDKKVIEVGK NDDLEDSKSL SDDTDVEVTS 300
    EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP 350
    EKENEGNDVP DCRRTISAPV VRPKDAYIKK ENSKLFDPCN SVEFLDLAHS 400
    SESQETISSM GEQLDNLSEQ RTDTENMEDC QNLLKPCSLC EKRPRDGNII 450
    HGRTGHLVTC FHCARRLKKA GASCPICKKE IQLVIKVFIA 490
    Length:490
    Mass (Da):54,864
    Last modified:September 27, 2005 - v2
    Checksum:i415E6FA5A0C69857
    GO
    Isoform 2 (identifier: O15151-2) [UniParc]FASTAAdd to Basket

    Also known as: MDMX-S

    The sequence of this isoform differs from the canonical sequence as follows:
         109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTARCNRILQSQKKN

    Note: No experimental confirmation available.

    Show »
    Length:127
    Mass (Da):14,185
    Checksum:i59649D26B113EFB4
    GO
    Isoform 3 (identifier: O15151-3) [UniParc]FASTAAdd to Basket

    Also known as: MDMX

    The sequence of this isoform differs from the canonical sequence as follows:
         109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTDAAQTLALAQDHT

    Note: No experimental confirmation available.

    Show »
    Length:127
    Mass (Da):13,981
    Checksum:i0A00E52B32331543
    GO
    Isoform HDMX211 (identifier: O15151-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-352: Missing.

    Note: Cancer-specific isoform, may counteract MDM2/MDM4-mediated p53 degradation.

    Show »
    Length:164
    Mass (Da):18,195
    Checksum:i1C39025CBD527C11
    GO
    Isoform 5 (identifier: O15151-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         225-274: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:440
    Mass (Da):49,541
    Checksum:iBB377C938A8C3D1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941D → N in AAB62928. (PubMed:9226370)Curated

    Mass spectrometryi

    Molecular mass is 54863.3 Da from positions 1 - 490. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751I → T.1 Publication
    Corresponds to variant rs4252716 [ dbSNP | Ensembl ].
    VAR_017106
    Natural varianti406 – 4061T → I.1 Publication
    Corresponds to variant rs4252741 [ dbSNP | Ensembl ].
    VAR_017107

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 352326Missing in isoform HDMX211. 1 PublicationVSP_042563Add
    BLAST
    Alternative sequencei109 – 490382LATAT…KVFIA → SASNNTARCNRILQSQKKN in isoform 2. CuratedVSP_035669Add
    BLAST
    Alternative sequencei109 – 490382LATAT…KVFIA → SASNNTDAAQTLALAQDHT in isoform 3. CuratedVSP_035670Add
    BLAST
    Alternative sequencei225 – 27450Missing in isoform 5. 1 PublicationVSP_043145Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF007111 mRNA. Translation: AAB62928.1.
    AY923176 mRNA. Translation: AAY22054.1.
    AK223228 mRNA. Translation: BAD96948.1.
    AY207458 Genomic DNA. Translation: AAO13494.1.
    AL512306 Genomic DNA. Translation: CAI14100.1.
    BC067299 mRNA. Translation: AAH67299.1.
    BC105106 mRNA. Translation: AAI05107.1.
    CCDSiCCDS1447.1. [O15151-1]
    CCDS55674.1. [O15151-5]
    CCDS55675.1. [O15151-4]
    RefSeqiNP_001191100.1. NM_001204171.1. [O15151-5]
    NP_001191101.1. NM_001204172.1. [O15151-4]
    NP_001265445.1. NM_001278516.1.
    NP_001265446.1. NM_001278517.1.
    NP_001265447.1. NM_001278518.1.
    NP_001265448.1. NM_001278519.1.
    NP_002384.2. NM_002393.4. [O15151-1]
    UniGeneiHs.497492.

    Genome annotation databases

    EnsembliENST00000367182; ENSP00000356150; ENSG00000198625. [O15151-1]
    ENST00000367183; ENSP00000356151; ENSG00000198625. [O15151-4]
    ENST00000454264; ENSP00000396840; ENSG00000198625. [O15151-5]
    GeneIDi4194.
    KEGGihsa:4194.
    UCSCiuc001hay.2. human. [O15151-5]
    uc001hba.3. human. [O15151-1]
    uc021phx.1. human. [O15151-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF007111 mRNA. Translation: AAB62928.1 .
    AY923176 mRNA. Translation: AAY22054.1 .
    AK223228 mRNA. Translation: BAD96948.1 .
    AY207458 Genomic DNA. Translation: AAO13494.1 .
    AL512306 Genomic DNA. Translation: CAI14100.1 .
    BC067299 mRNA. Translation: AAH67299.1 .
    BC105106 mRNA. Translation: AAI05107.1 .
    CCDSi CCDS1447.1. [O15151-1 ]
    CCDS55674.1. [O15151-5 ]
    CCDS55675.1. [O15151-4 ]
    RefSeqi NP_001191100.1. NM_001204171.1. [O15151-5 ]
    NP_001191101.1. NM_001204172.1. [O15151-4 ]
    NP_001265445.1. NM_001278516.1.
    NP_001265446.1. NM_001278517.1.
    NP_001265447.1. NM_001278518.1.
    NP_001265448.1. NM_001278519.1.
    NP_002384.2. NM_002393.4. [O15151-1 ]
    UniGenei Hs.497492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CR8 NMR - A 300-339 [» ]
    2VJE X-ray 2.20 B/D 428-490 [» ]
    2VJF X-ray 2.30 B/D 428-490 [» ]
    2VYR X-ray 2.00 A/B/C/D 16-116 [» ]
    3DAB X-ray 1.90 A/C/E/G 23-111 [» ]
    3EQY X-ray 1.63 A/B 24-108 [» ]
    3FDO X-ray 1.40 A 23-111 [» ]
    3FE7 X-ray 1.35 A 14-111 [» ]
    3FEA X-ray 1.33 A 14-111 [» ]
    3JZO X-ray 1.80 A 23-111 [» ]
    3JZP X-ray 1.74 A 23-111 [» ]
    3JZQ X-ray 1.80 A/B 23-111 [» ]
    3LBJ X-ray 1.50 E 23-111 [» ]
    3MQR X-ray 1.80 B 395-404 [» ]
    3U15 X-ray 1.80 A/B/C/D 14-111 [» ]
    ProteinModelPortali O15151.
    SMRi O15151. Positions 26-108, 301-344, 429-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110359. 50 interactions.
    DIPi DIP-24199N.
    IntActi O15151. 29 interactions.
    MINTi MINT-113852.
    STRINGi 9606.ENSP00000356150.

    Chemistry

    BindingDBi O15151.
    ChEMBLi CHEMBL2221344.

    PTM databases

    PhosphoSitei O15151.

    Proteomic databases

    MaxQBi O15151.
    PaxDbi O15151.
    PRIDEi O15151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367182 ; ENSP00000356150 ; ENSG00000198625 . [O15151-1 ]
    ENST00000367183 ; ENSP00000356151 ; ENSG00000198625 . [O15151-4 ]
    ENST00000454264 ; ENSP00000396840 ; ENSG00000198625 . [O15151-5 ]
    GeneIDi 4194.
    KEGGi hsa:4194.
    UCSCi uc001hay.2. human. [O15151-5 ]
    uc001hba.3. human. [O15151-1 ]
    uc021phx.1. human. [O15151-4 ]

    Organism-specific databases

    CTDi 4194.
    GeneCardsi GC01P204486.
    HGNCi HGNC:6974. MDM4.
    HPAi HPA018919.
    MIMi 602704. gene.
    neXtProti NX_O15151.
    PharmGKBi PA30719.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46328.
    HOGENOMi HOG000293341.
    HOVERGENi HBG013472.
    InParanoidi O15151.
    KOi K10127.
    OMAi LKPCSLC.
    OrthoDBi EOG7RRF7T.
    PhylomeDBi O15151.
    TreeFami TF105306.

    Miscellaneous databases

    ChiTaRSi MDM4. human.
    EvolutionaryTracei O15151.
    GeneWikii MDM4.
    GenomeRNAii 4194.
    NextBioi 16538.
    PMAP-CutDB O15151.
    PROi O15151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15151.
    Bgeei O15151.
    CleanExi HS_MDM4.
    Genevestigatori O15151.

    Family and domain databases

    Gene3Di 1.10.245.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR015458. MDM4.
    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:SF10. PTHR10360:SF10. 1 hit.
    Pfami PF02201. SWIB. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500699. MDM4. 1 hit.
    PIRSF006748. p53_MDM_2/4. 1 hit.
    SMARTi SM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47592. SSF47592. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon tumor.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HDMX211).
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Gastric mucosa.
    4. NIEHS SNPs program
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-175 AND ILE-406.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 5).
      Tissue: Brain and Testis.
    7. "Identification of a domain within MDMX-S that is responsible for its high affinity interaction with p53 and high-level expression in mammalian cells."
      Rallapalli R., Strachan G., Tuan R.S., Hall D.J.
      J. Cell. Biochem. 89:563-575(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
    8. "Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein."
      Sharp D.A., Kratowicz S.A., Sank M.J., George D.L.
      J. Biol. Chem. 274:38189-38196(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-437.
    9. "ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage."
      Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J.
      EMBO J. 24:3411-3422(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-342 AND SER-367 BY CHEK2, UBIQUITINATION, INTERACTION WITH MDM2.
    10. "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation."
      Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.
      EMBO J. 25:1207-1218(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-367 BY CHEK1, INTERACTION WITH YWHAG.
    11. "MdmX is a substrate for the deubiquitinating enzyme USP2a."
      Allende-Vega N., Sparks A., Lane D.P., Saville M.K.
      Oncogene 29:432-441(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP2 AND MDM2, INDUCTION, UBIQUITINATION, DEUBIQUITINATION BY USP2.
    12. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    13. "Solution structure of the ZF-RANBP domain of p53-binding protein MDM4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 300-340.

    Entry informationi

    Entry nameiMDM4_HUMAN
    AccessioniPrimary (citable) accession number: O15151
    Secondary accession number(s): Q2M2Y2
    , Q32SL2, Q6GS18, Q8IV83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3