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Entry version 202 (03 Jul 2019)
Sequence version 3 (27 Jul 2011)
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Protein

E3 ubiquitin-protein ligase Mdm2

Gene

Mdm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri297 – 326RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri436 – 477RING-typePROSITE-ProRule annotationAdd BLAST42

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
6.3.2.19 3474

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-198323 AKT phosphorylates targets in the cytosol
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-399719 Trafficking of AMPA receptors
R-MMU-5689880 Ub-specific processing proteases
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-69541 Stabilization of p53
R-MMU-8941858 Regulation of RUNX3 expression and activity

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Mdm2 (EC:2.3.2.271 Publication)
Alternative name(s):
Double minute 2 protein
Oncoprotein Mdm2
RING-type E3 ubiquitin transferase Mdm2Curated
p53-binding protein Mdm2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mdm2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:96952 Mdm2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of Dlg4 ubiquitination.1 Publication

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3600279

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000186501 – 489E3 ubiquitin-protein ligase Mdm2Add BLAST489

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei163Phosphoserine; by SGK1By similarity1
Modified residuei183PhosphoserineCombined sources1
Modified residuei238PhosphoserineBy similarity1
Modified residuei240PhosphoserineBy similarity1
Modified residuei244PhosphoserineBy similarity1
Modified residuei258PhosphoserineBy similarity1
Modified residuei260PhosphoserineBy similarity1
Modified residuei394Phosphoserine; by ATMBy similarity1
Modified residuei406Phosphoserine; by ATMBy similarity1
Modified residuei417Phosphothreonine; by ATMBy similarity1
Modified residuei423Phosphoserine; by ATMBy similarity1
Modified residuei427Phosphoserine; by ATMBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity
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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P23804

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P23804

PeptideAtlas

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PeptideAtlasi
P23804

PRoteomics IDEntifications database

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PRIDEi
P23804

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P23804

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P23804

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By UV light (PubMed:10075719). Down-regulated by NPAS4 (PubMed:25088421).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000020184 Expressed in 313 organ(s), highest expression level in embryonic stem cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P23804 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P23804 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).

Interacts with RPL23A; this interaction may promote p53/TP53 polyubiquitination (By similarity).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
201372, 88 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P23804

Database of interacting proteins

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DIPi
DIP-24174N
DIP-24196N

Protein interaction database and analysis system

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IntActi
P23804, 22 interactors

Molecular INTeraction database

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MINTi
P23804

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000020408

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P23804

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P23804

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 107SWIBAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 110Necessary for interaction with USP2By similarityAdd BLAST110
Regioni147 – 228Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34By similarityAdd BLAST82
Regioni167 – 304Interaction with MTBP1 PublicationAdd BLAST138
Regioni208 – 302ARF-bindingAdd BLAST95
Regioni221 – 230Interaction with USP7By similarity10
Regioni240 – 329Region IIAdd BLAST90
Regioni274 – 489Necessary for interaction with USP2By similarityAdd BLAST216

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi176 – 182Nuclear localization signalSequence analysis7
Motifi183 – 195Nuclear export signalAdd BLAST13
Motifi464 – 471Nucleolar localization signalSequence analysis8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi203 – 213Poly-SerAdd BLAST11
Compositional biasi221 – 299Asp/Glu-rich (acidic)Add BLAST79

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MDM2/MDM4 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri297 – 326RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri436 – 477RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IGXG Eukaryota
ENOG41125MP LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063539

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000293341

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P23804

KEGG Orthology (KO)

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KOi
K06643

Identification of Orthologs from Complete Genome Data

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OMAi
GELPCKL

Database of Orthologous Groups

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OrthoDBi
1329283at2759

TreeFam database of animal gene trees

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TreeFami
TF105306

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.245.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR028340 Mdm2
IPR015459 MDM2_E3_ligase
IPR016495 p53_neg-reg_MDM_2/4
IPR036885 SWIB_MDM2_dom_sf
IPR003121 SWIB_MDM2_domain
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

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PANTHERi
PTHR13844:SF15 PTHR13844:SF15, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02201 SWIB, 1 hit
PF00641 zf-RanBP, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF500700 MDM2, 1 hit
PIRSF006748 p53_MDM_2/4, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47592 SSF47592, 2 hits
SSF90209 SSF90209, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01358 ZF_RANBP2_1, 1 hit
PS50199 ZF_RANBP2_2, 1 hit
PS50089 ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Mdm2-p90 (identifier: P23804-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MCNTNMSVST EGAASTSQIP ASEQETLVRP KPLLLKLLKS VGAQNDTYTM
60 70 80 90 100
KEIIFYIGQY IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY
110 120 130 140 150
AMIYRNLVAV SQQDSGTSLS ESRRQPEGGS DLKDPLQAPP EEKPSSSDLI
160 170 180 190 200
SRLSTSSRRR SISETEENTD ELPGERHRKR RRSLSFDPSL GLCELREMCS
210 220 230 240 250
GGSSSSSSSS SESTETPSHQ DLDDGVSEHS GDCLDQDSVS DQFSVEFEVE
260 270 280 290 300
SLDSEDYSLS DEGHELSDED DEVYRVTVYQ TGESDTDSFE GDPEISLADY
310 320 330 340 350
WKCTSCNEMN PPLPSHCKRC WTLRENWLPD DKGKDKVEIS EKAKLENSAQ
360 370 380 390 400
AEEGLDVPDG KKLTENDAKE PCAEEDSEEK AEQTPLSQES DDYSQPSTSS
410 420 430 440 450
SIVYSSQESV KELKEETQDK DESVESSFSL NAIEPCVICQ GRPKNGCIVH
460 470 480
GKTGHLMSCF TCAKKLKKRN KPCPVCRQPI QMIVLTYFN
Length:489
Mass (Da):54,558
Last modified:July 27, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4ABF489A82038DF4
GO
Isoform Mdm2-p76 (identifier: P23804-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:440
Mass (Da):49,351
Checksum:iC574909560CC1A5F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QP04J3QP04_MOUSE
E3 ubiquitin-protein ligase Mdm2
Mdm2
162Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti203S → T in CAA41684 (PubMed:2026149).Curated1
Sequence conflicti419D → H in CAA41684 (PubMed:2026149).Curated1
Sequence conflicti486T → S in CAA41684 (PubMed:2026149).Curated1
Sequence conflicti486T → S in AAA91167 (PubMed:8917101).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0032151 – 49Missing in isoform Mdm2-p76. CuratedAdd BLAST49

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS24194.1 [P23804-1]
CCDS70110.1 [P23804-2]

Protein sequence database of the Protein Information Resource

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PIRi
S15349

NCBI Reference Sequences

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RefSeqi
NP_001275515.1, NM_001288586.2 [P23804-2]
NP_034916.1, NM_010786.4 [P23804-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184 [P23804-1]
ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184 [P23804-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
17246

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:17246

UCSC genome browser

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UCSCi
uc007hdl.2 mouse [P23804-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS24194.1 [P23804-1]
CCDS70110.1 [P23804-2]
PIRiS15349
RefSeqiNP_001275515.1, NM_001288586.2 [P23804-2]
NP_034916.1, NM_010786.4 [P23804-1]

3D structure databases

SMRiP23804
ModBaseiSearch...

Protein-protein interaction databases

BioGridi201372, 88 interactors
CORUMiP23804
DIPiDIP-24174N
DIP-24196N
IntActiP23804, 22 interactors
MINTiP23804
STRINGi10090.ENSMUSP00000020408

Chemistry databases

BindingDBiP23804
ChEMBLiCHEMBL3600279

PTM databases

iPTMnetiP23804
PhosphoSitePlusiP23804

Proteomic databases

MaxQBiP23804
PaxDbiP23804
PeptideAtlasiP23804
PRIDEiP23804

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020408; ENSMUSP00000020408; ENSMUSG00000020184 [P23804-1]
ENSMUST00000105263; ENSMUSP00000100898; ENSMUSG00000020184 [P23804-2]
GeneIDi17246
KEGGimmu:17246
UCSCiuc007hdl.2 mouse [P23804-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4193
MGIiMGI:96952 Mdm2

Phylogenomic databases

eggNOGiENOG410IGXG Eukaryota
ENOG41125MP LUCA
GeneTreeiENSGT00530000063539
HOGENOMiHOG000293341
InParanoidiP23804
KOiK06643
OMAiGELPCKL
OrthoDBi1329283at2759
TreeFamiTF105306

Enzyme and pathway databases

BRENDAi6.3.2.19 3474
ReactomeiR-MMU-198323 AKT phosphorylates targets in the cytosol
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-399719 Trafficking of AMPA receptors
R-MMU-5689880 Ub-specific processing proteases
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-69541 Stabilization of p53
R-MMU-8941858 Regulation of RUNX3 expression and activity

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Mdm2 mouse

Protein Ontology

More...
PROi
PR:P23804

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020184 Expressed in 313 organ(s), highest expression level in embryonic stem cell
ExpressionAtlasiP23804 baseline and differential
GenevisibleiP23804 MM

Family and domain databases

Gene3Di1.10.245.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR028340 Mdm2
IPR015459 MDM2_E3_ligase
IPR016495 p53_neg-reg_MDM_2/4
IPR036885 SWIB_MDM2_dom_sf
IPR003121 SWIB_MDM2_domain
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR13844:SF15 PTHR13844:SF15, 1 hit
PfamiView protein in Pfam
PF02201 SWIB, 1 hit
PF00641 zf-RanBP, 1 hit
PIRSFiPIRSF500700 MDM2, 1 hit
PIRSF006748 p53_MDM_2/4, 1 hit
SUPFAMiSSF47592 SSF47592, 2 hits
SSF90209 SSF90209, 1 hit
PROSITEiView protein in PROSITE
PS01358 ZF_RANBP2_1, 1 hit
PS50199 ZF_RANBP2_2, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMDM2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23804
Secondary accession number(s): Q61040, Q64330, Q91XK7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 27, 2011
Last modified: July 3, 2019
This is version 202 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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