Mdm2
entrez
17246
canonical
uniprot
P23804
canonical
ensembl
ENSMUSG00000020184
resolver
ensp
ENSMUSP00000020408
resolver
ensp
ENSMUSP00000100898
resolver
genesymbol
Mdm2
resolver
uniprot
Q61040
resolver
uniprot
Q64330
resolver
uniprot
Q91XK7
resolver
uniprot_entry
MDM2_MOUSE
resolver
uniprot_sec
Q61040
resolver
uniprot_sec
Q64330
resolver
uniprot_sec
Q91XK7
resolver
amino_acid_sequence
MCNTNMSVSTEGAASTSQIPASEQETLVRPKPLLLKLLKSVGAQNDTYTMKEIIFYIGQYIMTKRLYDEKQQHIVYCSNDLLGDVFGVPSFSVKEHRKIYAMIYRNLVAVSQQDSGTSLSESRRQPEGGSDLKDPLQAPPEEKPSSSDLISRLSTSSRRRSISETEENTDELPGERHRKRRRSLSFDPSLGLCELREMCSGGSSSSSSSSSESTETPSHQDLDDGVSEHSGDCLDQDSVSDQFSVEFEVESLDSEDYSLSDEGHELSDEDDEVYRVTVYQTGESDTDSFEGDPEISLADYWKCTSCNEMNPPLPSHCKRCWTLRENWLPDDKGKDKVEISEKAKLENSAQAEEGLDVPDGKKLTENDAKEPCAEEDSEEKAEQTPLSQESDDYSQPSTSSSIVYSSQESVKELKEETQDKDESVESSFSLNAIEPCVICQGRPKNGCIVHGKTGHLMSCFTCAKKLKKRNKPCPVCRQPIQMIVLTYFN
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
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 a 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). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903). {ECO:0000250|UniProtKB:Q00987, ECO:0000269|PubMed:11588219, ECO:0000269|PubMed:14642282, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:25088421, ECO:0000269|PubMed:30879903}.
uniprot
proteins
mass_dalton
54558
uniprot
proteins
mutagenesis
MUTAGEN 58; /note="G->I: Reduced interaction with NDUFS1, ROS production and apoptosis."; /evidence="ECO:0000269|PubMed:30879903
uniprot
proteins
post_translational_modification
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 promotes its ubiquitination and degradation, preventing 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. ATM-phosphorylated MDM2 is ubiquitinated by the SCF(FBXO31) complex in response to genotoxic stress, promoting its degradation and p53/TP53-mediated DNA damage response. 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|UniProtKB:Q00987}.
uniprot
proteins
protein_family
MDM2/MDM4 family
uniprot
proteins
pubmed
10075719
uniprot
proteins
pubmed
10611322
uniprot
proteins
pubmed
10713175
uniprot
proteins
pubmed
10906133
uniprot
proteins
pubmed
11588219
uniprot
proteins
pubmed
14642282
uniprot
proteins
pubmed
15195100
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17110379
uniprot
proteins
pubmed
2026149
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21804542
uniprot
proteins
pubmed
25088421
uniprot
proteins
pubmed
25751059
uniprot
proteins
pubmed
30879903
uniprot
proteins
pubmed
8660994
uniprot
proteins
pubmed
8917101
uniprot
proteins
sequence_length
489
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. Cytoplasm {ECO:0000269|PubMed:15195100}. Nucleus, nucleolus {ECO:0000269|PubMed:15195100}. Nucleus {ECO:0000250|UniProtKB:Q00987}. 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|UniProtKB:Q00987}.
uniprot
proteins