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P23804 (MDM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase Mdm2

EC=6.3.2.-
Alternative name(s):
Double minute 2 protein
Oncoprotein Mdm2
p53-binding protein Mdm2
Gene names
Name:Mdm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Subunit structure

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-Fdoes 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 By similarity. Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Nucleusnucleoplasm. Cytoplasm. Nucleusnucleolus. Note: Colocalizes with RASSF1 isoform Ain 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. Ref.11

Tissue specificity

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. Ref.4

Induction

By UV light. Ref.4

Domain

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.

Post-translational modification

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. Ref.8

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.

Involvement in disease

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

Sequence similarities

Belongs to the MDM2/MDM4 family.

Contains 1 RanBP2-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 SWIB domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
   DiseaseProto-oncogene
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to UV-C

Inferred from electronic annotation. Source: Ensembl

cellular response to acid

Inferred from electronic annotation. Source: Ensembl

cellular response to alkaloid

Inferred from electronic annotation. Source: Ensembl

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

cellular response to estrogen stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin B1

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle arrest

Inferred from electronic annotation. Source: InterPro

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein processing

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine modification

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from genetic interaction PubMed 15485902. Source: MGI

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

protein catabolic process

Inferred from direct assay PubMed 12145204. Source: MGI

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein destabilization

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ether

Inferred from electronic annotation. Source: Ensembl

response to iron ion

Inferred from electronic annotation. Source: Ensembl

response to magnesium ion

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

traversing start control point of mitotic cell cycle

Inferred from direct assay Ref.9. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 14767071PubMed 19090619. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

nuclear body

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11718560PubMed 12154087PubMed 12927808PubMed 14767071PubMed 19090619PubMed 22173032. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionp53 binding

Inferred from physical interaction PubMed 20818388. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 15102471PubMed 17936560PubMed 19833129PubMed 20657550PubMed 20832751PubMed 22173032PubMed 22789538PubMed 23260144PubMed 20697359PubMed 20697359. Source: IntAct

scaffold protein binding

Inferred from physical interaction PubMed 19372219. Source: BHF-UCL

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 12145204PubMed 17591690. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform Mdm2-p90 (identifier: P23804-1)

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.
Isoform Mdm2-p76 (identifier: P23804-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489E3 ubiquitin-protein ligase Mdm2
PRO_0000018650

Regions

Domain27 – 10781SWIB
Zinc finger297 – 32630RanBP2-type
Zinc finger436 – 47742RING-type
Region1 – 110110Necessary for interaction with USP2 By similarity
Region147 – 22882Interaction with PYHIN1 and necessary for interaction with RFFL By similarity
Region167 – 304138Interaction with MTBP
Region208 – 30295ARF-binding
Region221 – 23010Interaction with USP7 By similarity
Region240 – 32990Region II
Region274 – 489216Necessary for interaction with USP2 By similarity
Motif176 – 1827Nuclear localization signal Potential
Motif183 – 19513Nuclear export signal
Motif464 – 4718Nucleolar localization signal Potential
Compositional bias203 – 21311Poly-Ser
Compositional bias221 – 29979Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue1631Phosphoserine; by SGK1 By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2401Phosphoserine By similarity
Modified residue2441Phosphoserine By similarity
Modified residue2581Phosphoserine By similarity
Modified residue2601Phosphoserine By similarity
Modified residue3941Phosphoserine; by ATM By similarity
Modified residue4061Phosphoserine; by ATM By similarity
Modified residue4171Phosphothreonine; by ATM By similarity
Modified residue4231Phosphoserine; by ATM By similarity
Modified residue4271Phosphoserine; by ATM By similarity

Natural variations

Alternative sequence1 – 4949Missing in isoform Mdm2-p76.
VSP_003215

Experimental info

Sequence conflict2031S → T in CAA41684. Ref.1
Sequence conflict4191D → H in CAA41684. Ref.1
Sequence conflict4861T → S in CAA41684. Ref.1
Sequence conflict4861T → S in AAA91167. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Mdm2-p90 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 4ABF489A82038DF4

FASTA48954,558
        10         20         30         40         50         60 
MCNTNMSVST EGAASTSQIP ASEQETLVRP KPLLLKLLKS VGAQNDTYTM KEIIFYIGQY 

        70         80         90        100        110        120 
IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY AMIYRNLVAV SQQDSGTSLS 

       130        140        150        160        170        180 
ESRRQPEGGS DLKDPLQAPP EEKPSSSDLI SRLSTSSRRR SISETEENTD ELPGERHRKR 

       190        200        210        220        230        240 
RRSLSFDPSL GLCELREMCS GGSSSSSSSS SESTETPSHQ DLDDGVSEHS GDCLDQDSVS 

       250        260        270        280        290        300 
DQFSVEFEVE SLDSEDYSLS DEGHELSDED DEVYRVTVYQ TGESDTDSFE GDPEISLADY 

       310        320        330        340        350        360 
WKCTSCNEMN PPLPSHCKRC WTLRENWLPD DKGKDKVEIS EKAKLENSAQ AEEGLDVPDG 

       370        380        390        400        410        420 
KKLTENDAKE PCAEEDSEEK AEQTPLSQES DDYSQPSTSS SIVYSSQESV KELKEETQDK 

       430        440        450        460        470        480 
DESVESSFSL NAIEPCVICQ GRPKNGCIVH GKTGHLMSCF TCAKKLKKRN KPCPVCRQPI 


QMIVLTYFN 

« Hide

Isoform Mdm2-p76 [UniParc].

Checksum: C574909560CC1A5F
Show »

FASTA44049,351

References

« Hide 'large scale' references
[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]"Genomic organization of the mouse double minute 2 gene."
Jones S.N., Ansari-Lari M.A., Hancock A.R., Jones W.J., Gibbs R.A., Donehower L.A., Bradley A.
Gene 175:209-213(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM MDM2-P90).
Strain: 129/Sv.
[3]"The organization and expression of the mdm2 gene."
de Oca Luna R.M., Tabor A.D., Eberspaecher H., Hulboy D.L., Worth L.L., Colman M.S., Finlay C.A., Lozano G.
Genomics 33:352-357(1996) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability."
Tompkins V.S., Hagen J., Frazier A.A., Lushnikova T., Fitzgerald M.P., di Tommaso A.D., Ladeveze V., Domann F.E., Eischen C.M., Quelle D.E.
J. Biol. Chem. 282:1322-1333(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBRG1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58876 mRNA. Translation: CAA41684.1.
U40145 Genomic DNA. Translation: AAA91167.1.
U47944 expand/collapse EMBL AC list , 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.
CCDSCCDS24194.1. [P23804-1]
CCDS70110.1. [P23804-2]
PIRS15349.
RefSeqNP_001275515.1. NM_001288586.1. [P23804-2]
NP_034916.1. NM_010786.4. [P23804-1]
XP_006513374.1. XM_006513311.1. [P23804-2]
UniGeneMm.22670.
Mm.447669.

3D structure databases

ProteinModelPortalP23804.
SMRP23804. Positions 26-108, 288-333, 430-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201372. 39 interactions.
DIPDIP-24174N.
DIP-24196N.
IntActP23804. 19 interactions.
MINTMINT-139756.

PTM databases

PhosphoSiteP23804.

Proteomic databases

PRIDEP23804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184. [P23804-1]
ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184. [P23804-2]
GeneID17246.
KEGGmmu:17246.
UCSCuc007hdl.1. mouse. [P23804-1]

Organism-specific databases

CTD4193.
MGIMGI:96952. Mdm2.

Phylogenomic databases

eggNOGNOG46328.
GeneTreeENSGT00530000063539.
HOGENOMHOG000293341.
HOVERGENHBG013472.
InParanoidQ91XK7.
KOK06643.
OMALCVIREI.
OrthoDBEOG7RRF7T.
TreeFamTF105306.

Gene expression databases

ArrayExpressP23804.
BgeeP23804.
CleanExMM_MDM2.
GenevestigatorP23804.

Family and domain databases

Gene3D1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR028340. 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]
PANTHERPTHR10360:SF11. PTHR10360:SF11. 1 hit.
PfamPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFPIRSF500700. MDM2. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTSM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47592. SSF47592. 2 hits.
PROSITEPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMDM2. mouse.
NextBio291706.
PMAP-CutDBQ91XK7.
PROP23804.
SOURCESearch...

Entry information

Entry nameMDM2_MOUSE
AccessionPrimary (citable) accession number: P23804
Secondary accession number(s): Q61040, Q64330, Q91XK7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot