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Protein

E3 ubiquitin-protein ligase Mdm2

Gene

MDM2

Organism
Homo sapiens (Human)
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. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a 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 (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity).By similarity14 Publications

Miscellaneous

MDM2 RING finger mutations that failed to ubiquitinate p53 in vitro did not target p53 for degradation when expressed in cells.

Caution

Was reported to interact with UBXN6 but the corresponding article has been retracted (PubMed:18768758).
A report observed N-glycosylation at Asn-349 (PubMed:19139490). However, as the protein is not extracellular, additional evidences are required to confirm this result.1 Publication

<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 ‘Function’ 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 fingeri299 – 328RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri438 – 479RING-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 processHost-virus interaction, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
6.3.2.19 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-6804760 Regulation of TP53 Activity through Methylation
R-HSA-69541 Stabilization of p53
R-HSA-8941858 Regulation of RUNX3 expression and activity

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q00987

SIGNOR Signaling Network Open Resource

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SIGNORi
Q00987

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
Q00987 Predicted

<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
Short name:
Hdm2
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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000135679.21

Human Gene Nomenclature Database

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HGNCi
HGNC:6973 MDM2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164785 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q00987

<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; 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Seems to be amplified in certain tumors (including soft tissue sarcomas, osteosarcomas and gliomas). A higher frequency of splice variants lacking p53 binding domain sequences was found in late-stage and high-grade ovarian and bladder carcinomas. Four of the splice variants show loss of p53 binding.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi305C → S: No loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi374C → T: No loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi438C → L: No loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi441C → G: Fails to interact with MDM4. 1 Publication1
Mutagenesisi449C → A: Loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi449C → S: No substantial decrease of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi452H → A: Loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi455T → A: Significant decrease of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi457H → S: Loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi461C → S: Loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi464C → A: Loss of ubiquitin ligase E3 activity, enhances protein stability. Does not inhibit interaction with APEX1, but inhibits its ubiquitin ligase E3 activity on APEX1. 5 Publications1
Mutagenesisi475C → G: Loss of ubiquitin ligase E3 activity. 1 Publication1
Mutagenesisi478C → R: Fails to interact with MDM4. 1 Publication1
Mutagenesisi478C → S: Loss of ubiquitin ligase E3 activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
4193

MalaCards human disease database

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MalaCardsi
MDM2
MIMi614401 phenotype

Open Targets

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OpenTargetsi
ENSG00000135679

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99970 Dedifferentiated liposarcoma
524 Li-Fraumeni syndrome
99971 Well-differentiated liposarcoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30718

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5023

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

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DMDMi
266516

<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_00001573321 – 491E3 ubiquitin-protein ligase Mdm2Add BLAST491

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 residuei166Phosphoserine; by SGK1Combined sources1 Publication1
Modified residuei190PhosphoserineBy similarity1
Modified residuei240Phosphoserine1 Publication1
Modified residuei242Phosphoserine1 Publication1
Modified residuei246Phosphoserine1 Publication1
Modified residuei260Phosphoserine1 Publication1
Modified residuei262Phosphoserine1 Publication1
Modified residuei386Phosphoserine; by ATM1 Publication1
Modified residuei395Phosphoserine; by ATM1 Publication1
Modified residuei407Phosphoserine; by ATM1 Publication1
Modified residuei419Phosphothreonine; by ATM1 Publication1
Modified residuei425Phosphoserine; by ATM1 Publication1
Modified residuei429Phosphoserine; by ATM1 Publication1

<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-166 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.5 Publications
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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
Q00987

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

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PaxDbi
Q00987

PeptideAtlas

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PeptideAtlasi
Q00987

PRoteomics IDEntifications database

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PRIDEi
Q00987

ProteomicsDB human proteome resource

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ProteomicsDBi
57889
57890 [Q00987-10]
57891 [Q00987-11]
57892 [Q00987-2]
57893 [Q00987-3]
57894 [Q00987-4]
57895 [Q00987-5]
57896 [Q00987-6]
57897 [Q00987-7]
57898 [Q00987-8]
57899 [Q00987-9]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q00987

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

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PhosphoSitePlusi
Q00987

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q00987

<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

Ubiquitous. Isoform Mdm2-A, isoform Mdm2-B, isoform Mdm2-C, isoform Mdm2-D, isoform Mdm2-E, isoform Mdm2-F and isoform Mdm2-G are observed in a range of cancers but absent in normal tissues.

<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 DNA damage.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000135679 Expressed in 207 organ(s), highest expression level in oviduct epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q00987 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q00987 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000086
CAB016303

<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 (PubMed:16173922). Interacts with MTA1. Interacts with AARB2. Interacts with MTBP. Interacts with PML. Interacts with TBRG1. 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:24120868). Interacts with ADGRB1; the interaction results in inhibition of MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Interacts with RPL23A; this interaction may promote p53/TP53 polyubiquitination (PubMed:26203195).By similarity36 Publications
(Microbial infection) Interacts with herpes virus 8 protein v-IRF4.1 Publication
(Microbial infection) Interacts with and ubiquitinates HIV-1 Tat.1 Publication

<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

WithEntry#Exp.IntActNotes
itself4EBI-389668,EBI-389668
AKT1P317494EBI-389668,EBI-296087
ARP102752EBI-389668,EBI-608057
ARRB1P494073EBI-389668,EBI-743313
Arrb2P290674EBI-389668,EBI-1636616From Rattus norvegicus.
BTRCQ9Y2979EBI-389668,EBI-307461
CASP3P425742EBI-389668,EBI-524064
CDKN2AQ8N7265EBI-389668,EBI-625922
CSNK1A1P487293EBI-389668,EBI-1383726
CSNK1A1P48729-23EBI-389668,EBI-2040168
CSNK1DP487306EBI-389668,EBI-751621
Csnk1dQ064862EBI-389668,EBI-2910316From Rattus norvegicus.
CSNK1EP496743EBI-389668,EBI-749343
CUL1Q136163EBI-389668,EBI-359390
DAXXQ9UER718EBI-389668,EBI-77321
DLG4P783523EBI-389668,EBI-80389
EEF1A1P681049EBI-389668,EBI-352162
ESR1P033722EBI-389668,EBI-78473
EZRP153113EBI-389668,EBI-1056902
FBXW11Q9UKB14EBI-389668,EBI-355189
FKBP3Q006882EBI-389668,EBI-1044081
Fkbp3Q624464EBI-389668,EBI-8313562From Mus musculus.
GNL3Q9BVP23EBI-389668,EBI-641642
GNL3LQ9NVN88EBI-389668,EBI-746682
GORABQ5T7V86EBI-389668,EBI-3917143
GRK2P250984EBI-389668,EBI-3904795
HNRNPKP619782EBI-389668,EBI-304185
IGF1RP080692EBI-389668,EBI-475981
JMYQ8N9B52EBI-389668,EBI-866435
JUNP054123EBI-389668,EBI-852823
JUNDP175353EBI-389668,EBI-2682803
MDM4O1515110EBI-389668,EBI-398437
NCLP193388EBI-389668,EBI-346967
NPM1P067485EBI-389668,EBI-78579
Npm1Q619372EBI-389668,EBI-626362From Mus musculus.
NR0B2Q154664EBI-389668,EBI-3910729
NUMBP497576EBI-389668,EBI-915016
OTUB1Q96FW15EBI-389668,EBI-1058491
PLK1P533507EBI-389668,EBI-476768
PMLP295906EBI-389668,EBI-295890
PMLP29590-56EBI-389668,EBI-304008
PPM1DO152974EBI-389668,EBI-1551512
PPP2R5CQ133625EBI-389668,EBI-1266156
PSMA3P257882EBI-389668,EBI-348380
PSME3P612898EBI-389668,EBI-355546
RASSF1Q9NS235EBI-389668,EBI-367363
RB1P064005EBI-389668,EBI-491274
RFWD3Q6PCD55EBI-5279149,EBI-2129159
RPL11P6291311EBI-389668,EBI-354380
RPL23P628293EBI-389668,EBI-353303
RPL5P467775EBI-389668,EBI-358018
RPS27P426775EBI-389668,EBI-356336
RPS27LQ71UM56EBI-389668,EBI-355126
RPS3P233968EBI-389668,EBI-351193
RPS7P6208115EBI-389668,EBI-354360
RRM2BQ7LG562EBI-389668,EBI-9009083
RRM2BQ7LG56-12EBI-389668,EBI-15741413
RYBPQ8N48811EBI-389668,EBI-752324
RYR2Q927362EBI-389668,EBI-1170425
S100A1P232972EBI-389668,EBI-743686
S100A2P290342EBI-389668,EBI-752230
S100A4P264473EBI-389668,EBI-717058
S100A6P067032EBI-389668,EBI-352877
S100BP042712EBI-389668,EBI-458391
SETQ011052EBI-389668,EBI-1053182
TP53P0463793EBI-389668,EBI-366083
TP73O153504EBI-389668,EBI-389606
UBCP0CG486EBI-389668,EBI-3390054
USP2O756044EBI-389668,EBI-743272
USP7Q9300927EBI-389668,EBI-302474
vIRF-4Q2HR732EBI-389668,EBI-9001898From Human herpesvirus 8 type P (isolate GK18).
Xpo1Q6P5F94EBI-389668,EBI-2550236From Mus musculus.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110358, 484 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q00987

Database of interacting proteins

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DIPi
DIP-392N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q00987

Protein interaction database and analysis system

More...
IntActi
Q00987, 188 interactors

Molecular INTeraction database

More...
MINTi
Q00987

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000417281

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q00987

<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

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00334

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q00987

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

More...
SMRi
Q00987

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q00987

<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 USP2Add BLAST110
Regioni150 – 230Interaction with PYHIN1 and necessary for interaction with RFFL and RNF342 PublicationsAdd BLAST81
Regioni170 – 306Interaction with MTBPBy similarityAdd BLAST137
Regioni210 – 304ARF-bindingAdd BLAST95
Regioni223 – 232Interaction with USP710
Regioni242 – 331Region IIAdd BLAST90
Regioni276 – 491Necessary for interaction with USP2Add 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>Motifi179 – 185Nuclear localization signalSequence analysis7
Motifi190 – 202Nuclear export signalAdd BLAST13
Motifi466 – 473Nucleolar 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 biasi210 – 215Poly-Ser6
Compositional biasi243 – 301Asp/Glu-rich (acidic)Add BLAST59

<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 fingeri299 – 328RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri438 – 479RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IGXG Eukaryota
ENOG41125MP LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063539

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG013472

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q00987

KEGG Orthology (KO)

More...
KOi
K06643

Identification of Orthologs from Complete Genome Data

More...
OMAi
GELPCKL

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0FYK

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q00987

TreeFam database of animal gene trees

More...
TreeFami
TF105306

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.245.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
PANTHERi
PTHR13844:SF15 PTHR13844:SF15, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47592 SSF47592, 2 hits
SSF90209 SSF90209, 1 hit

PROSITE; a protein domain and family database

More...
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (11+)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 11 <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. AlignAdd to basket

This entry has 11 described isoforms and 21 potential isoforms that are computationally mapped.Show allAlign All

Isoform Mdm2 (identifier: Q00987-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM
60 70 80 90 100
KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY
110 120 130 140 150
TMIYRNLVVV NQQESSDSGT SVSENRCHLE GGSDQKDLVQ ELQEEKPSSS
160 170 180 190 200
HLVSRPSTSS RRRAISETEE NSDELSGERQ RKRHKSDSIS LSFDESLALC
210 220 230 240 250
VIREICCERS SSSESTGTPS NPDLDAGVSE HSGDWLDQDS VSDQFSVEFE
260 270 280 290 300
VESLDSEDYS LSEEGQELSD EDDEVYQVTV YQAGESDTDS FEEDPEISLA
310 320 330 340 350
DYWKCTSCNE MNPPLPSHCN RCWALRENWL PEDKGKDKGE ISEKAKLENS
360 370 380 390 400
TQAEEGFDVP DCKKTIVNDS RESCVEENDD KITQASQSQE SEDYSQPSTS
410 420 430 440 450
SSIIYSSQED VKEFEREETQ DKEESVESSL PLNAIEPCVI CQGRPKNGCI
460 470 480 490
VHGKTGHLMA CFTCAKKLKK RNKPCPVCRQ PIQMIVLTYF P
Length:491
Mass (Da):55,233
Last modified:April 1, 1993 - v1
<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:iF37CE163876BC983
GO
Isoform Mdm2-A (identifier: Q00987-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-222: Missing.

Show »
Length:296
Mass (Da):33,140
Checksum:i9772439D74A4448B
GO
Isoform Mdm2-A1 (identifier: Q00987-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-222: Missing.
     275-300: Missing.

Show »
Length:270
Mass (Da):30,265
Checksum:iA3ED7CCFF670634E
GO
Isoform Mdm2-B (identifier: Q00987-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-300: Missing.

Show »
Length:218
Mass (Da):24,467
Checksum:iBB9C602F589EEC41
GO
Isoform Mdm2-C (identifier: Q00987-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-222: Missing.

Show »
Length:321
Mass (Da):35,980
Checksum:i4BD6213CA39D15C0
GO
Isoform Mdm2-D (identifier: Q00987-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     30-388: Missing.

Show »
Length:132
Mass (Da):14,689
Checksum:i770E9B66362CA97E
GO
Isoform Mdm2-E (identifier: Q00987-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-102: YCSNDLLGDLFGVPSFSVKEHRKIYTM → NDCANLFPLVDLSIRELYISNYITLGI
     103-491: Missing.

Show »
Length:102
Mass (Da):11,587
Checksum:i75E2B91B94C786C1
GO
Isoform Mdm2-alpha (identifier: Q00987-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Show »
Length:430
Mass (Da):48,488
Checksum:iC84E1F63E39E655D
GO
Isoform Mdm2-F (identifier: Q00987-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-97: Missing.

Note: Does not interact with p53/TP53.
Show »
Length:446
Mass (Da):49,899
Checksum:i4B630B50750EADFE
GO
Isoform Mdm2-G (identifier: Q00987-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-169: Missing.

Show »
Length:436
Mass (Da):49,249
Checksum:i3C8F55E98BC4203A
GO
Isoform 11 (identifier: Q00987-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVRSRQM

Show »
Length:497
Mass (Da):55,991
Checksum:iCFEC32F36132D8FA
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 are 21 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KN53J3KN53_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
466Annotation score:

Annotation score:3 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>
A7UKY0A7UKY0_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2 mdm2
257Annotation score:

Annotation score:2 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>
A7UKX8A7UKX8_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2 mdm2
256Annotation score:

Annotation score:2 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>
G3XA89G3XA89_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2 hCG_2014981
442Annotation score:

Annotation score:2 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>
E7EPE2E7EPE2_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
229Annotation 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>
Q9H4C5Q9H4C5_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
243Annotation 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>
Q8TE47Q8TE47_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2 MDM2 isoform KB9
243Annotation 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>
A0A0C4DFR5A0A0C4DFR5_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
265Annotation 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>
Q9H4C3Q9H4C3_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
130Annotation 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>
F5H4Q8F5H4Q8_HUMAN
E3 ubiquitin-protein ligase Mdm2
MDM2
170Annotation 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>
There are more potential isoformsShow all

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 conflicti17S → P in AAA82237 (PubMed:7651818).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

A polymorphism in the MDM2 promoter is associated with susceptibility to accelerated tumor formation in both hereditary and sporadic cancers [MIMi:614401]. It also contributes to susceptibility to Li-Fraumeni syndrome, in patients carrying a TP53 germline mutation.

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0032071 – 61Missing in isoform Mdm2-alpha. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_0379971M → MVRSRQM in isoform 11. 1 Publication1
Alternative sequenceiVSP_00320928 – 300Missing in isoform Mdm2-B. 1 PublicationAdd BLAST273
Alternative sequenceiVSP_00320828 – 222Missing in isoform Mdm2-A and isoform Mdm2-A1. 2 PublicationsAdd BLAST195
Alternative sequenceiVSP_00321030 – 388Missing in isoform Mdm2-D. 1 PublicationAdd BLAST359
Alternative sequenceiVSP_00321153 – 222Missing in isoform Mdm2-C. 1 PublicationAdd BLAST170
Alternative sequenceiVSP_02257853 – 97Missing in isoform Mdm2-F. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_00321276 – 102YCSND…KIYTM → NDCANLFPLVDLSIRELYIS NYITLGI in isoform Mdm2-E. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_003213103 – 491Missing in isoform Mdm2-E. 1 PublicationAdd BLAST389
Alternative sequenceiVSP_022579115 – 169Missing in isoform Mdm2-G. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_003214275 – 300Missing in isoform Mdm2-A1. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M92424 mRNA Translation: AAA60568.1
Z12020 mRNA Translation: CAA78055.1
U33199 mRNA Translation: AAA75514.1
U33200 mRNA Translation: AAA75515.1
U33201 mRNA Translation: AAA75516.1
U33202 mRNA Translation: AAA75517.1
U33203 mRNA Translation: AAA75518.1
AF092844 mRNA Translation: AAL40179.1
AF092845 mRNA Translation: AAL40180.1
AK290341 mRNA Translation: BAF83030.1
BT007258 mRNA Translation: AAP35922.1
AF527840 Genomic DNA Translation: AAM78554.1
AC025423 Genomic DNA No translation available.
BC009893 mRNA No translation available.
U28935 Genomic DNA Translation: AAA82237.1
U39736 Genomic DNA Translation: AAA82061.1
AF201370 mRNA Translation: AAF42995.1
AJ251943 Genomic DNA Translation: CAB64448.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS61189.1 [Q00987-5]
CCDS8986.2 [Q00987-11]

Protein sequence database of the Protein Information Resource

More...
PIRi
S24354

NCBI Reference Sequences

More...
RefSeqi
NP_001138811.1, NM_001145339.2
NP_001265391.1, NM_001278462.1 [Q00987-5]
NP_002383.2, NM_002392.5 [Q00987-11]
XP_005268929.1, XM_005268872.4 [Q00987-1]
XP_006719462.1, XM_006719399.3 [Q00987-8]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.484551
Hs.733536

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000258149; ENSP00000258149; ENSG00000135679 [Q00987-11]
ENST00000299252; ENSP00000299252; ENSG00000135679 [Q00987-5]
ENST00000360430; ENSP00000353611; ENSG00000135679 [Q00987-2]
ENST00000393413; ENSP00000377065; ENSG00000135679 [Q00987-4]
ENST00000539479; ENSP00000444430; ENSG00000135679 [Q00987-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4193

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4193

UCSC genome browser

More...
UCSCi
uc001sui.6 human [Q00987-1]

Keywords - Coding sequence diversityi

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Mdm2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92424 mRNA Translation: AAA60568.1
Z12020 mRNA Translation: CAA78055.1
U33199 mRNA Translation: AAA75514.1
U33200 mRNA Translation: AAA75515.1
U33201 mRNA Translation: AAA75516.1
U33202 mRNA Translation: AAA75517.1
U33203 mRNA Translation: AAA75518.1
AF092844 mRNA Translation: AAL40179.1
AF092845 mRNA Translation: AAL40180.1
AK290341 mRNA Translation: BAF83030.1
BT007258 mRNA Translation: AAP35922.1
AF527840 Genomic DNA Translation: AAM78554.1
AC025423 Genomic DNA No translation available.
BC009893 mRNA No translation available.
U28935 Genomic DNA Translation: AAA82237.1
U39736 Genomic DNA Translation: AAA82061.1
AF201370 mRNA Translation: AAF42995.1
AJ251943 Genomic DNA Translation: CAB64448.1
CCDSiCCDS61189.1 [Q00987-5]
CCDS8986.2 [Q00987-11]
PIRiS24354
RefSeqiNP_001138811.1, NM_001145339.2
NP_001265391.1, NM_001278462.1 [Q00987-5]
NP_002383.2, NM_002392.5 [Q00987-11]
XP_005268929.1, XM_005268872.4 [Q00987-1]
XP_006719462.1, XM_006719399.3 [Q00987-8]
UniGeneiHs.484551
Hs.733536

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RV1X-ray2.30A/B/C25-109[»]
1T4EX-ray2.60A/B17-111[»]
1T4FX-ray1.90M17-125[»]
1YCRX-ray2.60A17-125[»]
1Z1MNMR-A1-118[»]
2AXIX-ray1.40A17-125[»]
2C6ANMR-A290-335[»]
2C6BNMR-A290-335[»]
2F1YX-ray1.70A224-232[»]
2FOPX-ray2.10B145-150[»]
2GV2X-ray1.80A17-125[»]
2HDPNMR-A/B429-491[»]
2LZGNMR-A1-125[»]
2M86NMR-B17-125[»]
2MPSNMR-A3-109[»]
2RUHNMR-A6-102[»]
2VJEX-ray2.20A/C428-491[»]
2VJFX-ray2.30A/C428-491[»]
3EQSX-ray1.65A25-109[»]
3G03X-ray1.80A/C18-125[»]
3IUXX-ray1.65A/C25-109[»]
3IWYX-ray1.93A/C25-109[»]
3JZKX-ray2.10A17-111[»]
3JZRX-ray2.10A17-125[»]
3JZSX-ray1.78A24-109[»]
3LBKX-ray2.30A18-111[»]
3LBLX-ray1.60A/C/E18-111[»]
3LNJX-ray2.40A/C/E25-109[»]
3LNZX-ray1.95A/C/E/G/I/K/M/O25-109[»]
3MQSX-ray2.40D394-403[»]
3TJ2X-ray2.10A/C18-111[»]
3TPXX-ray1.80A/C/E25-109[»]
3TU1X-ray1.60A18-125[»]
3V3BX-ray2.00A/B24-110[»]
3VBGX-ray2.80A/B/C/D25-109[»]
3VZVX-ray2.80A/B25-109[»]
3W69X-ray1.90A/B25-109[»]
4DIJX-ray1.90A/B17-111[»]
4EREX-ray1.80A/B17-111[»]
4ERFX-ray2.00A/C/E17-111[»]
4HBMX-ray1.90A/B/C/D/E/F/G/H6-125[»]
4HFZX-ray2.69A/C17-125[»]
4HG7X-ray1.60A17-108[»]
4JV7X-ray2.20A18-111[»]
4JV9X-ray2.50A18-111[»]
4JVEX-ray2.30A18-111[»]
4JVRX-ray1.70A/C/E18-111[»]
4JWRX-ray2.35A/B/C17-111[»]
4MDNX-ray1.90A18-110[»]
4MDQX-ray2.12A25-110[»]
4OASX-ray1.70A/C/E17-111[»]
4OBAX-ray1.60A/B/C17-111[»]
4OCCX-ray1.80A/C/E17-111[»]
4ODEX-ray1.80A6-110[»]
4ODFX-ray2.20A6-110[»]
4OGNX-ray1.38A6-110[»]
4OGTX-ray1.54A6-110[»]
4OGVX-ray2.20A/B/C17-111[»]
4OQ3X-ray2.30A/B/C/D17-111[»]
4QO4X-ray1.70A17-111[»]
4QOCX-ray1.70A/C/E/G/I/K17-111[»]
4UD7X-ray1.60A/B/C/D17-125[»]
4UE1X-ray1.45A/B/C/D17-125[»]
4UMNX-ray1.99A/B6-125[»]
4WT2X-ray1.42A6-110[»]
4XXBX-ray2.40B290-437[»]
4ZFIX-ray2.00A/B/C/D18-113[»]
4ZGKX-ray2.00A/B18-114[»]
4ZYCX-ray1.95A/B/C17-111[»]
4ZYFX-ray1.80A17-111[»]
4ZYIX-ray1.67A17-111[»]
5AFGX-ray1.90A17-108[»]
5C5AX-ray1.15A/B20-111[»]
5HMHX-ray1.79A/B21-116[»]
5HMIX-ray1.74A/B18-116[»]
5HMKX-ray2.17A/B17-125[»]
5J7FX-ray2.00A/B/C/D1-125[»]
5J7GX-ray1.85A/B/C/D18-125[»]
5LAVX-ray1.73A19-111[»]
5LAWX-ray1.64A18-111[»]
5LAYX-ray2.71A/B/C/D/E/F17-111[»]
5LAZX-ray1.66A18-111[»]
5LN2X-ray1.58A17-111[»]
5MNJX-ray2.16C/G428-491[»]
5OC8X-ray1.56A17-111[»]
5SWKX-ray1.92A/B1-150[»]
5TRFX-ray2.10A/B/C/D/E10-118[»]
5UMMX-ray1.65A/C25-109[»]
5VK0X-ray1.80A/C/E/G/I/K/M/O/Q/S/U/W25-109[»]
5WTSX-ray3.00B6-125[»]
5XXKX-ray1.66A/B6-125[»]
5Z02X-ray1.35A24-112[»]
5ZXFX-ray1.25A24-110[»]
6GGNX-ray2.00A17-111[»]
DisProtiDP00334
ProteinModelPortaliQ00987
SMRiQ00987
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110358, 484 interactors
CORUMiQ00987
DIPiDIP-392N
ELMiQ00987
IntActiQ00987, 188 interactors
MINTiQ00987
STRINGi9606.ENSP00000417281

Chemistry databases

BindingDBiQ00987
ChEMBLiCHEMBL5023

Protein family/group databases

MoonDBiQ00987 Predicted

PTM databases

iPTMnetiQ00987
PhosphoSitePlusiQ00987

Polymorphism and mutation databases

DMDMi266516

Proteomic databases

MaxQBiQ00987
PaxDbiQ00987
PeptideAtlasiQ00987
PRIDEiQ00987
ProteomicsDBi57889
57890 [Q00987-10]
57891 [Q00987-11]
57892 [Q00987-2]
57893 [Q00987-3]
57894 [Q00987-4]
57895 [Q00987-5]
57896 [Q00987-6]
57897 [Q00987-7]
57898 [Q00987-8]
57899 [Q00987-9]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4193
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258149; ENSP00000258149; ENSG00000135679 [Q00987-11]
ENST00000299252; ENSP00000299252; ENSG00000135679 [Q00987-5]
ENST00000360430; ENSP00000353611; ENSG00000135679 [Q00987-2]
ENST00000393413; ENSP00000377065; ENSG00000135679 [Q00987-4]
ENST00000539479; ENSP00000444430; ENSG00000135679 [Q00987-1]
GeneIDi4193
KEGGihsa:4193
UCSCiuc001sui.6 human [Q00987-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4193
DisGeNETi4193
EuPathDBiHostDB:ENSG00000135679.21

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MDM2
HGNCiHGNC:6973 MDM2
HPAiCAB000086
CAB016303
MalaCardsiMDM2
MIMi164785 gene
614401 phenotype
neXtProtiNX_Q00987
OpenTargetsiENSG00000135679
Orphaneti99970 Dedifferentiated liposarcoma
524 Li-Fraumeni syndrome
99971 Well-differentiated liposarcoma
PharmGKBiPA30718

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IGXG Eukaryota
ENOG41125MP LUCA
GeneTreeiENSGT00530000063539
HOVERGENiHBG013472
InParanoidiQ00987
KOiK06643
OMAiGELPCKL
OrthoDBiEOG091G0FYK
PhylomeDBiQ00987
TreeFamiTF105306

Enzyme and pathway databases

BRENDAi6.3.2.19 2681
ReactomeiR-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-6804760 Regulation of TP53 Activity through Methylation
R-HSA-69541 Stabilization of p53
R-HSA-8941858 Regulation of RUNX3 expression and activity
SignaLinkiQ00987
SIGNORiQ00987

Miscellaneous databases

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

More...
ChiTaRSi
MDM2 human
EvolutionaryTraceiQ00987

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Mdm2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4193
PMAP-CutDBiQ00987

Protein Ontology

More...
PROi
PR:Q00987

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135679 Expressed in 207 organ(s), highest expression level in oviduct epithelium
ExpressionAtlasiQ00987 baseline and differential
GenevisibleiQ00987 HS

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...

<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_HUMAN
<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: Q00987
Secondary accession number(s): A6NL51
, A8K2S6, Q13226, Q13297, Q13298, Q13299, Q13300, Q13301, Q53XW0, Q71TW9, Q8WYJ1, Q8WYJ2, Q9UGI3, Q9UMT8
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 5, 2018
This is version 240 of the entry and version 1 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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