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E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)

 MDM2_MOUSE              Reviewed;         489 AA.
P23804; Q61040; Q64330; Q91XK7;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 186.
RecName: Full=E3 ubiquitin-protein ligase Mdm2;
EC=2.3.2.27 {ECO:0000269|PubMed:14642282};
AltName: Full=Double minute 2 protein;
AltName: Full=Oncoprotein Mdm2;
AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000305};
AltName: Full=p53-binding protein Mdm2;
Name=Mdm2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2-P90).
PubMed=2026149;
Fakharzadeh S.S., Trusko S.P., George D.L.;
"Tumorigenic potential associated with enhanced expression of a gene
that is amplified in a mouse tumor cell line.";
EMBO J. 10:1565-1569(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM MDM2-P90).
STRAIN=129/Sv;
PubMed=8917101; DOI=10.1016/0378-1119(96)00151-5;
Jones S.N., Ansari-Lari M.A., Hancock A.R., Jones W.J., Gibbs R.A.,
Donehower L.A., Bradley A.;
"Genomic organization of the mouse double minute 2 gene.";
Gene 175:209-213(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MDM2-P90).
STRAIN=129/Sv;
PubMed=8660994; DOI=10.1006/geno.1996.0210;
de Oca Luna R.M., Tabor A.D., Eberspaecher H., Hulboy D.L.,
Worth L.L., Colman M.S., Finlay C.A., Lozano G.;
"The organization and expression of the mdm2 gene.";
Genomics 33:352-357(1996).
[4]
NUCLEOTIDE SEQUENCE (ISOFORMS MDM2-P90 AND MDM2-P76), TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=10075719; DOI=10.1074/jbc.274.12.8161;
Saucedo L.J., Myers C.D., Perry M.E.;
"Multiple murine double minute gene 2 (MDM2) proteins are induced by
ultraviolet light.";
J. Biol. Chem. 274:8161-8168(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOLAR LOCALIZATION SIGNAL.
PubMed=10713175; DOI=10.1128/MCB.20.7.2517-2528.2000;
Weber J.D., Kuo M.-L., Bothner B., DiGiammarino E.L., Kriwacki R.W.,
Roussel M.F., Sherr C.J.;
"Cooperative signals governing ARF-mdm2 interaction and nucleolar
localization of the complex.";
Mol. Cell. Biol. 20:2517-2528(2000).
[8]
PHOSPHORYLATION BY ATM.
PubMed=10611322; DOI=10.1073/pnas.96.26.14973;
Khosravi R., Maya R., Gottlieb T., Oren M., Shiloh Y., Shkedy D.;
"Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation
in response to DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 96:14973-14977(1999).
[9]
INTERACTION WITH MTBP.
PubMed=10906133; DOI=10.1074/jbc.M004252200;
Boyd M.T., Vlatkovic N., Haines D.S.;
"A novel cellular protein (MTBP) binds to MDM2 and induces a G1 arrest
that is suppressed by MDM2.";
J. Biol. Chem. 275:31883-31890(2000).
[10]
FUNCTION, AND INTERACTION WITH AARB2.
PubMed=11588219; DOI=10.1126/science.1063866;
Shenoy S.K., McDonald P.H., Kohout T.A., Lefkowitz R.J.;
"Regulation of receptor fate by ubiquitination of activated beta 2-
adrenergic receptor and beta-arrestin.";
Science 294:1307-1313(2001).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=14642282;
Colledge M., Snyder E.M., Crozier R.A., Soderling J.A., Jin Y.,
Langeberg L.K., Lu H., Bear M.F., Scott J.D.;
"Ubiquitination regulates PSD-95 degradation and AMPA receptor surface
expression.";
Neuron 40:595-607(2003).
[12]
FUNCTION, INTERACTION WITH PML AND RPL11, AND SUBCELLULAR LOCATION.
PubMed=15195100; DOI=10.1038/ncb1147;
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H.,
Pandolfi P.P.;
"PML regulates p53 stability by sequestering Mdm2 to the nucleolus.";
Nat. Cell Biol. 6:665-672(2004).
[13]
INTERACTION WITH TBRG1.
PubMed=17110379; DOI=10.1074/jbc.M609612200;
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.;
"A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains
chromosomal stability.";
J. Biol. Chem. 282:1322-1333(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPL11.
PubMed=21804542; DOI=10.1038/nm.2392;
Sasaki M., Kawahara K., Nishio M., Mimori K., Kogo R., Hamada K.,
Itoh B., Wang J., Komatsu Y., Yang Y.R., Hikasa H., Horie Y.,
Yamashita T., Kamijo T., Zhang Y., Zhu Y., Prives C., Nakano T.,
Mak T.W., Sasaki T., Maehama T., Mori M., Suzuki A.;
"Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via
nucleolar RPL11.";
Nat. Med. 17:944-951(2011).
[16]
FUNCTION, AND INDUCTION.
PubMed=25088421; DOI=10.1016/j.celrep.2014.06.056;
Yoshihara S., Takahashi H., Nishimura N., Kinoshita M., Asahina R.,
Kitsuki M., Tatsumi K., Furukawa-Hibi Y., Hirai H., Nagai T.,
Yamada K., Tsuboi A.;
"Npas4 regulates Mdm2 and thus Dcx in experience-dependent dendritic
spine development of newborn olfactory bulb interneurons.";
Cell Rep. 8:843-857(2014).
[17]
INTERACTION WITH ADGRB1.
PubMed=25751059; DOI=10.1172/JCI74603;
Zhu D., Li C., Swanson A.M., Villalba R.M., Guo J., Zhang Z.,
Matheny S., Murakami T., Stephenson J.R., Daniel S., Fukata M.,
Hall R.A., Olson J.J., Neigh G.N., Smith Y., Rainnie D.G.,
Van Meir E.G.;
"BAI1 regulates spatial learning and synaptic plasticity in the
hippocampus.";
J. Clin. Invest. 125:1497-1508(2015).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of p53/TP53, leading to its degradation by the proteasome
(PubMed:15195100, PubMed:21804542). Inhibits p53/TP53- and
p73/TP73-mediated cell cycle arrest and apoptosis by binding its
transcriptional activation domain (By similarity). Also acts as a
ubiquitin ligase E3 toward itself, ARRB1 and ARBB2
(PubMed:11588219). Permits the nuclear export of p53/TP53 (By
similarity). Promotes proteasome-dependent ubiquitin-independent
degradation of retinoblastoma RB1 protein (By similarity).
Inhibits DAXX-mediated apoptosis by inducing its ubiquitination
and degradation (By similarity). Component of the TRIM28/KAP1-
MDM2-p53/TP53 complex involved in stabilizing p53/TP53 (By
similarity). Also component of the TRIM28/KAP1-ERBB4-MDM2 complex
which links growth factor and DNA damage response pathways (By
similarity). Mediates ubiquitination and subsequent proteasome
degradation of DYRK2 in nucleus (By similarity). Ubiquitinates
IGF1R and SNAI1 and promotes them to proteasomal degradation (By
similarity). Ubiquitinates DCX, leading to DCX degradation and
reduction of the dendritic spine density of olfactory bulb granule
cells (PubMed:25088421). Ubiquitinates DLG4, leading to
proteasomal degradation of DLG4 which is required for AMPA
receptor endocytosis (PubMed:14642282).
{ECO:0000250|UniProtKB:Q00987, ECO:0000269|PubMed:11588219,
ECO:0000269|PubMed:14642282, ECO:0000269|PubMed:15195100,
ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:25088421}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:14642282}.
-!- SUBUNIT: Interacts with p53/TP53, TP73/p73, RBL5 and RP11. Binds
specifically to RNA. Can interact with RB1, E1A-associated protein
EP300 and the E2F1 transcription factor. Forms a ternary complex
with p53/TP53 and WWOX. Interacts with CDKN2AIP, RFWD3, USP7,
PYHIN1 and RBBP6. Interacts with ARRB1 and ARRB2. Interacts with
PSMA3. Found in a trimeric complex with MDM2, MDM4 and USP2.
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 APEX1; leading 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 IGF1R. Interacts
with TRIM13; the interaction ubiquitinates MDM2 leading to its
proteasomal degradation. Interacts with SNAI1; this interaction
promotes SNAI1 ubiquitination. Interacts with NOTCH1 (via
intracellular domain). Interacts with FHIT. Interacts with RFFL
and RNF34; the interaction stabilizes MDM2. Interacts with
CDK5RAP3 and CDKN2A/ARF; form a ternary complex involved in
regulation of p53/TP53. Interacts with MTA1 (By similarity).
Interacts with AARB2 (PubMed:11588219). Interacts with MTBP
(PubMed:10906133). Interacts with PML (PubMed:15195100). Interacts
with TBRG1 (PubMed:17110379). Interacts with the 5S RNP which is
composed of the 5S RNA, RPL5 and RPL11; the interaction is direct
occurs in the nucleoplasm and negatively regulates MDM2-mediated
TP53 ubiquitination and degradation (PubMed:15195100,
PubMed:21804542). Interacts with ADGRB1; the interaction results
in inhibition of MDM2-mediated ubiquitination and degradation of
DLG4/PSD95, promoting DLG4 stability and regulating synaptic
plasticity (PubMed:25751059). {ECO:0000250|UniProtKB:Q00987,
ECO:0000269|PubMed:10906133, ECO:0000269|PubMed:11588219,
ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:17110379,
ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:25751059}.
-!- INTERACTION:
Q8BWG8:Arrb1; NbExp=4; IntAct=EBI-641788, EBI-641778;
Q62108:Dlg4; NbExp=3; IntAct=EBI-641788, EBI-300895;
O88904:Hipk1; NbExp=3; IntAct=EBI-641788, EBI-692945;
O35618:Mdm4; NbExp=2; IntAct=EBI-3386480, EBI-2603376;
P53350:PLK1 (xeno); NbExp=2; IntAct=EBI-641788, EBI-476768;
Q5EBH1:Rassf5; NbExp=3; IntAct=EBI-641788, EBI-960530;
Q9CXW4:Rpl11; NbExp=4; IntAct=EBI-641788, EBI-1548890;
P62830:Rpl23; NbExp=2; IntAct=EBI-641788, EBI-2365752;
P47962:Rpl5; NbExp=3; IntAct=EBI-641788, EBI-773940;
Q8BSK8:Rps6kb1; NbExp=2; IntAct=EBI-641788, EBI-646423;
P02340:Tp53; NbExp=9; IntAct=EBI-641788, EBI-474016;
P62991:Ubc; NbExp=2; IntAct=EBI-641788, EBI-413074;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}.
Cytoplasm {ECO:0000269|PubMed:15195100}. Nucleus, nucleolus
{ECO:0000269|PubMed:15195100}. 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.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=2;
Name=Mdm2-p90;
IsoId=P23804-1; Sequence=Displayed;
Name=Mdm2-p76;
IsoId=P23804-2; Sequence=VSP_003215;
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.;
-!- 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. {ECO:0000269|PubMed:10075719}.
-!- INDUCTION: By UV light (PubMed:10075719). Down-regulated by NPAS4
(PubMed:25088421). {ECO:0000269|PubMed:10075719,
ECO:0000269|PubMed:25088421}.
-!- 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.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Loss of Dlg4 ubiquitination.
{ECO:0000269|PubMed:14642282}.
-!- SIMILARITY: Belongs to the MDM2/MDM4 family. {ECO:0000305}.
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EMBL; X58876; CAA41684.1; -; mRNA.
EMBL; U40145; AAA91167.1; -; Genomic_DNA.
EMBL; U47944; AAB09030.1; -; Genomic_DNA.
EMBL; U47935; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47936; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47937; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47938; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47939; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47940; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47941; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47942; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47943; AAB09030.1; JOINED; Genomic_DNA.
EMBL; U47934; AAB09031.1; -; mRNA.
EMBL; AK004719; BAB23502.1; -; mRNA.
EMBL; AK088638; BAC40470.1; -; mRNA.
EMBL; BC050902; AAH50902.1; -; mRNA.
CCDS; CCDS24194.1; -. [P23804-1]
CCDS; CCDS70110.1; -. [P23804-2]
PIR; S15349; S15349.
RefSeq; NP_001275515.1; NM_001288586.2. [P23804-2]
RefSeq; NP_034916.1; NM_010786.4. [P23804-1]
UniGene; Mm.22670; -.
UniGene; Mm.447669; -.
ProteinModelPortal; P23804; -.
SMR; P23804; -.
BioGrid; 201372; 87.
CORUM; P23804; -.
DIP; DIP-24174N; -.
DIP; DIP-24196N; -.
IntAct; P23804; 22.
MINT; MINT-139756; -.
STRING; 10090.ENSMUSP00000020408; -.
BindingDB; P23804; -.
ChEMBL; CHEMBL3600279; -.
iPTMnet; P23804; -.
PhosphoSitePlus; P23804; -.
MaxQB; P23804; -.
PaxDb; P23804; -.
PeptideAtlas; P23804; -.
PRIDE; P23804; -.
Ensembl; ENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184. [P23804-1]
Ensembl; ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184. [P23804-2]
GeneID; 17246; -.
KEGG; mmu:17246; -.
UCSC; uc007hdl.2; mouse. [P23804-1]
CTD; 4193; -.
MGI; MGI:96952; Mdm2.
eggNOG; ENOG410IGXG; Eukaryota.
eggNOG; ENOG41125MP; LUCA.
GeneTree; ENSGT00530000063539; -.
HOGENOM; HOG000293341; -.
HOVERGEN; HBG013472; -.
InParanoid; P23804; -.
KO; K06643; -.
OMA; PCVICQS; -.
OrthoDB; EOG091G0FYK; -.
TreeFam; TF105306; -.
BRENDA; 6.3.2.19; 3474.
Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559585; Oncogene Induced Senescence.
Reactome; R-MMU-399719; Trafficking of AMPA receptors.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-MMU-69541; Stabilization of p53.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
ChiTaRS; Mdm2; mouse.
PMAP-CutDB; Q91XK7; -.
PRO; PR:P23804; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020184; -.
CleanEx; MM_MDM2; -.
ExpressionAtlas; P23804; baseline and differential.
Genevisible; P23804; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0016874; F:ligase activity; ISO:MGI.
GO; GO:0061663; F:NEDD8 ligase activity; ISO:MGI.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
GO; GO:0003283; P:atrial septum development; IGI:MGI.
GO; GO:0003181; P:atrioventricular valve morphogenesis; IGI:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0060411; P:cardiac septum morphogenesis; IGI:MGI.
GO; GO:0072717; P:cellular response to actinomycin D; ISO:MGI.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0071494; P:cellular response to UV-C; IEA:Ensembl.
GO; GO:0071301; P:cellular response to vitamin B1; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:MGI.
GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003170; P:heart valve development; IGI:MGI.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0018205; P:peptidyl-lysine modification; ISO:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
GO; GO:0006461; P:protein complex assembly; ISO:MGI.
GO; GO:0031648; P:protein destabilization; ISO:MGI.
GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0002027; P:regulation of heart rate; IGI:MGI.
GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045472; P:response to ether; IEA:Ensembl.
GO; GO:1904404; P:response to formaldehyde; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:1990785; P:response to water-immersion restraint stress; IEA:Ensembl.
GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IDA:MGI.
GO; GO:0003281; P:ventricular septum development; IGI:MGI.
Gene3D; 1.10.245.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR028340; Mdm2.
InterPro; IPR015459; MDM2_E3_ligase.
InterPro; IPR016495; p53_neg-reg_MDM_2/4.
InterPro; IPR036885; SWIB_MDM2_dom_sf.
InterPro; IPR003121; SWIB_MDM2_domain.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR13844:SF15; PTHR13844:SF15; 1.
Pfam; PF02201; SWIB; 1.
Pfam; PF00641; zf-RanBP; 1.
PIRSF; PIRSF500700; MDM2; 1.
PIRSF; PIRSF006748; p53_MDM_2/4; 1.
SUPFAM; SSF47592; SSF47592; 2.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Complete proteome;
Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 489 E3 ubiquitin-protein ligase Mdm2.
/FTId=PRO_0000018650.
DOMAIN 27 107 SWIB.
ZN_FING 297 326 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 436 477 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1 110 Necessary for interaction with USP2.
{ECO:0000250}.
REGION 147 228 Interaction with PYHIN1 and necessary for
interaction with RFFL and RNF34.
{ECO:0000250|UniProtKB:Q00987}.
REGION 167 304 Interaction with MTBP.
{ECO:0000269|PubMed:10906133}.
REGION 208 302 ARF-binding.
REGION 221 230 Interaction with USP7. {ECO:0000250}.
REGION 240 329 Region II.
REGION 274 489 Necessary for interaction with USP2.
{ECO:0000250}.
MOTIF 176 182 Nuclear localization signal.
{ECO:0000255}.
MOTIF 183 195 Nuclear export signal.
MOTIF 464 471 Nucleolar localization signal.
{ECO:0000255}.
COMPBIAS 203 213 Poly-Ser.
COMPBIAS 221 299 Asp/Glu-rich (acidic).
MOD_RES 163 163 Phosphoserine; by SGK1.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 394 394 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 406 406 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 417 417 Phosphothreonine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 423 423 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 427 427 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
VAR_SEQ 1 49 Missing (in isoform Mdm2-p76).
{ECO:0000305}.
/FTId=VSP_003215.
CONFLICT 203 203 S -> T (in Ref. 1; CAA41684).
{ECO:0000305}.
CONFLICT 419 419 D -> H (in Ref. 1; CAA41684).
{ECO:0000305}.
CONFLICT 486 486 T -> S (in Ref. 1; CAA41684 and 2;
AAA91167). {ECO:0000305}.
SEQUENCE 489 AA; 54558 MW; 4ABF489A82038DF4 CRC64;
MCNTNMSVST EGAASTSQIP ASEQETLVRP KPLLLKLLKS VGAQNDTYTM KEIIFYIGQY
IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY AMIYRNLVAV SQQDSGTSLS
ESRRQPEGGS DLKDPLQAPP EEKPSSSDLI SRLSTSSRRR SISETEENTD ELPGERHRKR
RRSLSFDPSL GLCELREMCS GGSSSSSSSS SESTETPSHQ DLDDGVSEHS GDCLDQDSVS
DQFSVEFEVE SLDSEDYSLS DEGHELSDED DEVYRVTVYQ TGESDTDSFE GDPEISLADY
WKCTSCNEMN PPLPSHCKRC WTLRENWLPD DKGKDKVEIS EKAKLENSAQ AEEGLDVPDG
KKLTENDAKE PCAEEDSEEK AEQTPLSQES DDYSQPSTSS SIVYSSQESV KELKEETQDK
DESVESSFSL NAIEPCVICQ GRPKNGCIVH GKTGHLMSCF TCAKKLKKRN KPCPVCRQPI
QMIVLTYFN


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