P23804 (MDM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Mdm2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Evidence 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 an 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-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. Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Nucleus › nucleoplasm. Cytoplasm. Nucleus › nucleolus. 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. 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	Phosphorylated in response to ionizing radiation in an ATM-dependent manner. Phosphorylation on Ser-163 by SGK1 activates ubiquitination of p53/TP53 By similarity. Ref.8 Auto-ubiquitinated; which leads to proteasomal degradation. 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from electronic annotation. Source: Compara cellular response to UV-C Inferred from electronic annotation. Source: Compara cellular response to acid Inferred from electronic annotation. Source: Compara cellular response to alkaloid Inferred from electronic annotation. Source: Compara cellular response to antibiotic Inferred from electronic annotation. Source: Compara cellular response to estrogen stimulus Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to vitamin B1 Inferred from electronic annotation. Source: Compara establishment of protein localization Inferred from electronic annotation. Source: Compara negative regulation of DNA damage response, signal transduction by p53 class mediator Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of protein processing Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara peptidyl-lysine modification Inferred from electronic annotation. Source: Compara positive regulation of cell cycle Inferred from genetic interaction PubMed 15485902. Source: MGI positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of protein export from nucleus Inferred from electronic annotation. Source: Compara protein catabolic process Inferred from direct assay PubMed 12145204. Source: MGI protein complex assembly Inferred from electronic annotation. Source: Compara protein destabilization Inferred from electronic annotation. Source: Compara protein localization to nucleus Inferred from electronic annotation. Source: Compara protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara response to carbohydrate stimulus Inferred from electronic annotation. Source: Compara response to cocaine Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ether Inferred from electronic annotation. Source: Compara response to iron ion Inferred from electronic annotation. Source: Compara response to magnesium ion Inferred from electronic annotation. Source: Compara response to morphine Inferred from electronic annotation. Source: Compara traversing start control point of mitotic cell cycle Inferred from direct assay Ref.9. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 14767071. Source: MGI cytosol Inferred from electronic annotation. Source: Compara nuclear body Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay Ref.11. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara synapse Inferred from electronic annotation. Source: Compara
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay PubMed 12145204PubMed 17591690. Source: MGI zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arrb1	Q8BWG8	4	EBI-641788,EBI-641778
Mdm4	O35618	2	EBI-3386480,EBI-2603376
Rpl11	Q9CXW4	4	EBI-641788,EBI-1548890
Rpl23	P62830	2	EBI-641788,EBI-2365752
Rpl5	P47962	3	EBI-641788,EBI-773940
Tp53	P02340	3	EBI-641788,EBI-474016

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	E3 ubiquitin-protein ligase Mdm2		PRO_0000018650
Regions
	Domain	27 – 107	81	SWIB
	Zinc finger	297 – 326	30	RanBP2-type
	Zinc finger	436 – 477	42	RING-type
	Region	1 – 110	110	Necessary for interaction with USP2 By similarity
	Region	147 – 228	82	Interaction with PYHIN1 By similarity
	Region	167 – 304	138	Interaction with MTBP
	Region	208 – 302	95	ARF-binding
	Region	221 – 230	10	Interaction with USP7 By similarity
	Region	240 – 329	90	Region II
	Region	274 – 489	216	Necessary for interaction with USP2 By similarity
	Motif	176 – 182	7	Nuclear localization signal Potential
	Motif	183 – 195	13	Nuclear export signal
	Motif	464 – 471	8	Nucleolar localization signal Potential
	Compositional bias	203 – 213	11	Poly-Ser
	Compositional bias	221 – 299	79	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	163	1	Phosphoserine; by SGK1 By similarity
	Modified residue	238	1	Phosphoserine By similarity
	Modified residue	240	1	Phosphoserine By similarity
	Modified residue	244	1	Phosphoserine By similarity
	Modified residue	258	1	Phosphoserine By similarity
	Modified residue	260	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 49	49	Missing in isoform Mdm2-p76.		VSP_003215
Experimental info
	Sequence conflict	203	1	S → T in CAA41684. Ref.1
	Sequence conflict	419	1	D → H in CAA41684. Ref.1
	Sequence conflict	486	1	T → S in CAA41684. Ref.1
	Sequence conflict	486	1	T → S in AAA91167. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mdm2-p90 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 4ABF489A82038DF4	FASTA	489	54,558
	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
	Isoform Mdm2-p76 [UniParc]. Checksum: C574909560CC1A5F	FASTA	440	49,351
	10 20 30 40 50 60 MKEIIFYIGQ YIMTKRLYDE KQQHIVYCSN DLLGDVFGVP SFSVKEHRKI YAMIYRNLVA 70 80 90 100 110 120 VSQQDSGTSL SESRRQPEGG SDLKDPLQAP PEEKPSSSDL ISRLSTSSRR RSISETEENT 130 140 150 160 170 180 DELPGERHRK RRRSLSFDPS LGLCELREMC SGGSSSSSSS SSESTETPSH QDLDDGVSEH 190 200 210 220 230 240 SGDCLDQDSV SDQFSVEFEV ESLDSEDYSL SDEGHELSDE DDEVYRVTVY QTGESDTDSF 250 260 270 280 290 300 EGDPEISLAD YWKCTSCNEM NPPLPSHCKR CWTLRENWLP DDKGKDKVEI SEKAKLENSA 310 320 330 340 350 360 QAEEGLDVPD GKKLTENDAK EPCAEEDSEE KAEQTPLSQE SDDYSQPSTS SSIVYSSQES 370 380 390 400 410 420 VKELKEETQD KDESVESSFS LNAIEPCVIC QGRPKNGCIV HGKTGHLMSC FTCAKKLKKR 430 440 NKPCPVCRQP IQMIVLTYFN

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
IPI	IPI00129226. IPI00323397.
PIR	S15349.
RefSeq	NP_034916.1. NM_010786.3.
UniGene	Mm.22670. Mm.447669.
3D structure databases
ProteinModelPortal	P23804.
SMR	P23804. Positions 26-108, 288-333, 430-488.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24174N. DIP-24196N.
IntAct	P23804. 9 interactions.
MINT	MINT-139756.
PTM databases
PhosphoSite	P23804.
Proteomic databases
PRIDE	P23804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184. ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184.
GeneID	17246.
KEGG	mmu:17246.
Organism-specific databases
CTD	4193.
MGI	MGI:96952. Mdm2.
Phylogenomic databases
eggNOG	NOG46328.
GeneTree	ENSGT00530000063539.
HOGENOM	HOG000293341.
HOVERGEN	HBG013472.
InParanoid	Q91XK7.
KO	K06643.
OMA	LCVIREI.
OrthoDB	EOG4P8FK2.
Gene expression databases
ArrayExpress	P23804.
Bgee	P23804.
CleanEx	MM_MDM2.
Genevestigator	P23804.
GermOnline	ENSMUSG00000020184. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	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]
PANTHER	PTHR10360:SF9. PTHR10360:SF9. 1 hit.
Pfam	PF02201. SWIB. 1 hit. PF00641. zf-RanBP. 1 hit. [Graphical view]
PIRSF	PIRSF006748. p53_MDM_2/4. 1 hit.
SMART	SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47592. MDM2. 2 hits.
PROSITE	PS01358. ZF_RANBP2_1. 1 hit. PS50199. ZF_RANBP2_2. 1 hit. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MDM2. mouse.
NextBio	291706.
PMAP-CutDB	Q91XK7.
SOURCE	Search...

Entry information

Entry name

MDM2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program