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P23804

- MDM2_MOUSE

UniProt

P23804 - MDM2_MOUSE

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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

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. scaffold protein binding Source: BHF-UCL
  4. ubiquitin-protein transferase activity Source: MGI
  5. 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
Complete GO annotation...

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.
REACT_256790. Stabilization of p53.

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
Complete GO annotation...

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

BgeeiP23804.
CleanExiMM_MDM2.
ExpressionAtlasiP23804. baseline and differential.
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 and RNF34; the interaction stabilizes MDM2. 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
Tp53P023405EBI-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 RFFL and RNF34By 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.
InParanoidiP23804.
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

        10         20         30         40         50
MCNTNMSVST EGAASTSQIP ASEQETLVRP KPLLLKLLKS VGAQNDTYTM
60 70 80 90 100
KEIIFYIGQY IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY
110 120 130 140 150
AMIYRNLVAV SQQDSGTSLS ESRRQPEGGS DLKDPLQAPP EEKPSSSDLI
160 170 180 190 200
SRLSTSSRRR SISETEENTD ELPGERHRKR RRSLSFDPSL GLCELREMCS
210 220 230 240 250
GGSSSSSSSS SESTETPSHQ DLDDGVSEHS GDCLDQDSVS DQFSVEFEVE
260 270 280 290 300
SLDSEDYSLS DEGHELSDED DEVYRVTVYQ TGESDTDSFE GDPEISLADY
310 320 330 340 350
WKCTSCNEMN PPLPSHCKRC WTLRENWLPD DKGKDKVEIS EKAKLENSAQ
360 370 380 390 400
AEEGLDVPDG KKLTENDAKE PCAEEDSEEK AEQTPLSQES DDYSQPSTSS
410 420 430 440 450
SIVYSSQESV KELKEETQDK DESVESSFSL NAIEPCVICQ GRPKNGCIVH
460 470 480
GKTGHLMSCF TCAKKLKKRN KPCPVCRQPI QMIVLTYFN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 P23804.
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.
REACT_256790. Stabilization of p53.

Miscellaneous databases

ChiTaRSi Mdm2. mouse.
NextBioi 291706.
PMAP-CutDB Q91XK7.
PROi P23804.
SOURCEi Search...

Gene expression databases

Bgeei P23804.
CleanExi MM_MDM2.
ExpressionAtlasi P23804. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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