E3 ubiquitin-protein ligase Mdm2 (Protein name
), MDM2_HUMAN from NCBI database.
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Gene name:
MDM2;
Protein name:
E3 ubiquitin-protein ligase Mdm2;
Alternative:
Oncoprotein Mdm2;Double minute 2 protein(Hdm2);p53-binding protein Mdm2;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Binds p53/TP53, TP73/p73, ARF/P14, PML, RBL5 and RP11, and 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, MTBP, RFWD3, TBRG1, USP7, PYHIN1, UBXN6, and RBBP6. Isoform Mdm2-F does not interact with p53/TP53. Interacts with and ubiquitinates HIV-1 Tat. Interacts with ARRB1 and ARRB2. 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 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 MDM2 and ERBB4 in the complex.
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.
Subcellular Location:
Nucleus
nucleoplasm
Cytoplasm
Nucleus
nucleolus
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. Colocalizes with RASSF1 isoform A in the nucleus.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-A; MDM2-B; MDM2-C; MDM2-D AND MDM2-E)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2-ALPHA)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-F AND MDM2-G);INTERACTION WITH TP53
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2)
7.
NIEHS SNPs program
Submitted (2002-07) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-491 (ISOFORM MDM2-A1)
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Cited for: PHOSPHORYLATION AT SER-240; SER-242; SER-246; SER-260 AND SER-262
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Cited for: FUNCTION IN UBIQUITINATION OF IGF1R;INTERACTION WITH IGF1R
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Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ACCELERATED TUMOR FORMATION
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Cited for: FUNCTION;INTERACTION WITH USP7;DEUBIQUITINATION BY USP7
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Cited for: FUNCTION;INTERACTION WITH PML AND RPL11;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH MTBP;MUTAGENESIS OF CYS-464
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Cited for: PHOSPHORYLATION AT SER-386; SER-395; SER-407; THR-419; SER-425 AND SER-429
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Cited for: FUNCTION;INTERACTION WITH RYBP;IDENTIFICATION IN A COMPLEX WITH RYBP AND TP53
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Cited for: FUNCTION;INTERACTION WITH APEX1;MUTAGENESIS OF CYS-464
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION IN DYRK2 UBIQUITINATION;INTERACTION WITH DYRK2
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Cited for: INTERACTION WITH TRIM28 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX AND WITH TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX;FUNCTION;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH TP53 AND RFWD3;MUTAGENESIS OF CYS-464
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Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-109 IN COMPLEX WITH P53
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Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 224-232 IN COMPLEX WITH USP7;INTERACTION WITH USP7
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Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 145-150 IN COMPLEX WITH USP7;INTERACTION WITH USP7
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Cited for: UBIQUITINATION;INTERACTION WITH PYHIN1;MUTAGENESIS OF CYS-464
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Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX AND USP7;INTERACTION WITH DAXX;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH USP2;UBIQUITINATION;DEUBIQUITINATION BY USP2
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Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ACCELERATED TUMOR FORMATION AND LI-FRAUMENI SYNDROME
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Cited for: INTERACTION WITH RFFL AND RNF34;AUTOUBIQUITINATION
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Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX; RASSF1 AND USP7;INTERACTION WITH RASSF1; USP7 AND DAXX;SUBCELLULAR LOCATION
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