UniProtKB - Q00987 (MDM2_HUMAN)
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E3 ubiquitin-protein ligase Mdm2
MDM2
Functioni
Miscellaneous
Catalytic activityi
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 299 – 328 | RanBP2-typePROSITE-ProRule annotationAdd BLAST | 30 | |
| Zinc fingeri | 438 – 479 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
GO - Molecular functioni
- 5S rRNA binding Source: UniProtKB
- disordered domain specific binding Source: CAFA
- enzyme binding Source: UniProtKB
- identical protein binding Source: IntAct
- ligase activity Source: UniProtKB
- NEDD8 ligase activity Source: CAFA
- p53 binding Source: UniProtKB
- peroxisome proliferator activated receptor binding Source: Ensembl
- protein N-terminus binding Source: CAFA
- ribonucleoprotein complex binding Source: UniProtKB
- scaffold protein binding Source: Ensembl
- SUMO transferase activity Source: Reactome
- ubiquitin protein ligase activity Source: CAFA
- ubiquitin protein ligase binding Source: UniProtKB
- ubiquitin-protein transferase activity Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- amyloid fibril formation Source: CAFA
- atrial septum development Source: Ensembl
- atrioventricular valve morphogenesis Source: Ensembl
- blood vessel development Source: Ensembl
- blood vessel remodeling Source: Ensembl
- cardiac septum morphogenesis Source: Ensembl
- cellular response to actinomycin D Source: CAFA
- cellular response to alkaloid Source: Ensembl
- cellular response to estrogen stimulus Source: Ensembl
- cellular response to gamma radiation Source: CAFA
- cellular response to growth factor stimulus Source: Ensembl
- cellular response to hydrogen peroxide Source: Ensembl
- cellular response to hypoxia Source: UniProtKB
- cellular response to peptide hormone stimulus Source: Ensembl
- cellular response to UV-C Source: Ensembl
- cellular response to vitamin B1 Source: Ensembl
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
- endocardial cushion morphogenesis Source: Ensembl
- establishment of protein localization Source: BHF-UCL
- negative regulation of cell cycle arrest Source: BHF-UCL
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
- negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
- negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: CAFA
- negative regulation of neuron projection development Source: Ensembl
- negative regulation of protein processing Source: Ensembl
- negative regulation of signal transduction by p53 class mediator Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
- peptidyl-lysine modification Source: BHF-UCL
- positive regulation of cell proliferation Source: BHF-UCL
- positive regulation of gene expression Source: Ensembl
- positive regulation of mitotic cell cycle Source: UniProtKB
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
- positive regulation of protein export from nucleus Source: Ensembl
- positive regulation of vascular associated smooth muscle cell migration Source: Ensembl
- positive regulation of vascular smooth muscle cell proliferation Source: Ensembl
- protein autoubiquitination Source: ParkinsonsUK-UCL
- protein complex assembly Source: UniProtKB
- protein destabilization Source: BHF-UCL
- protein deubiquitination Source: Reactome
- protein localization to nucleus Source: BHF-UCL
- protein ubiquitination Source: UniProtKB
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
- proteolysis involved in cellular protein catabolic process Source: CAFA
- regulation of heart rate Source: Ensembl
- regulation of protein catabolic process Source: UniProtKB
- regulation of signal transduction by p53 class mediator Source: Reactome
- response to antibiotic Source: UniProtKB
- response to cocaine Source: Ensembl
- response to drug Source: Ensembl
- response to ether Source: Ensembl
- response to formaldehyde Source: Ensembl
- response to iron ion Source: Ensembl
- response to magnesium ion Source: Ensembl
- response to morphine Source: Ensembl
- response to steroid hormone Source: Ensembl
- response to toxic substance Source: Ensembl
- response to water-immersion restraint stress Source: Ensembl
- transcription factor catabolic process Source: ParkinsonsUK-UCL
- traversing start control point of mitotic cell cycle Source: Ensembl
- ventricular septum development Source: Ensembl
- viral process Source: UniProtKB-KW
Keywordsi
| Molecular function | Transferase |
| Biological process | Host-virus interaction, Ubl conjugation pathway |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
| BRENDAi | 6.3.2.19. 2681. |
| 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-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. |
| SignaLinki | Q00987. |
| SIGNORi | Q00987. |
Names & Taxonomyi
| Protein namesi | Recommended name: E3 ubiquitin-protein ligase Mdm2 (EC:2.3.2.27)Alternative name(s): Double minute 2 protein Short name: Hdm2 Oncoprotein Mdm2 RING-type E3 ubiquitin transferase Mdm2Curated p53-binding protein Mdm2 |
| Gene namesi | Name:MDM2 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:6973. MDM2. |
Subcellular locationi
- Nucleus › nucleoplasm
- Cytoplasm
- Nucleus › nucleolus
Note: Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus.
GO - Cellular componenti
- cytoplasm Source: UniProtKB
- cytosol Source: Reactome
- endocytic vesicle membrane Source: Reactome
- nucleolus Source: UniProtKB
- nucleoplasm Source: UniProtKB
- nucleus Source: BHF-UCL
- plasma membrane Source: Reactome
- protein complex Source: CAFA
- synapse Source: Ensembl
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Involvement in diseasei
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 305 | C → S: No loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 374 | C → T: No loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 438 | C → L: No loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 441 | C → G: Fails to interact with MDM4. 1 Publication | 1 | |
| Mutagenesisi | 449 | C → A: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 449 | C → S: No substantial decrease of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 452 | H → A: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 455 | T → A: Significant decrease of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 457 | H → S: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 461 | C → S: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 464 | C → 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 Publications | 1 | |
| Mutagenesisi | 475 | C → G: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 | |
| Mutagenesisi | 478 | C → R: Fails to interact with MDM4. 1 Publication | 1 | |
| Mutagenesisi | 478 | C → S: Loss of ubiquitin ligase E3 activity. 1 Publication | 1 |
Keywords - Diseasei
Proto-oncogeneOrganism-specific databases
| DisGeNETi | 4193. |
| MalaCardsi | MDM2. |
| MIMi | 614401. phenotype. |
| OpenTargetsi | ENSG00000135679. |
| Orphaneti | 99970. Dedifferentiated liposarcoma. 524. Li-Fraumeni syndrome. 99971. Well-differentiated liposarcoma. |
| PharmGKBi | PA30718. |
Chemistry databases
| ChEMBLi | CHEMBL5023. |
Polymorphism and mutation databases
| DMDMi | 266516. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000157332 | 1 – 491 | E3 ubiquitin-protein ligase Mdm2Add BLAST | 491 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 166 | Phosphoserine; by SGK1Combined sources1 Publication | 1 | |
| Modified residuei | 190 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 240 | Phosphoserine1 Publication | 1 | |
| Modified residuei | 242 | Phosphoserine1 Publication | 1 | |
| Modified residuei | 246 | Phosphoserine1 Publication | 1 | |
| Modified residuei | 260 | Phosphoserine1 Publication | 1 | |
| Modified residuei | 262 | Phosphoserine1 Publication | 1 | |
| Modified residuei | 386 | Phosphoserine; by ATM1 Publication | 1 | |
| Modified residuei | 395 | Phosphoserine; by ATM1 Publication | 1 | |
| Modified residuei | 407 | Phosphoserine; by ATM1 Publication | 1 | |
| Modified residuei | 419 | Phosphothreonine; by ATM1 Publication | 1 | |
| Modified residuei | 425 | Phosphoserine; by ATM1 Publication | 1 | |
| Modified residuei | 429 | Phosphoserine; by ATM1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
| EPDi | Q00987. |
| MaxQBi | Q00987. |
| PaxDbi | Q00987. |
| PeptideAtlasi | Q00987. |
| PRIDEi | Q00987. |
PTM databases
| iPTMneti | Q00987. |
| PhosphoSitePlusi | Q00987. |
Miscellaneous databases
| PMAP-CutDBi | Q00987. |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
| Bgeei | ENSG00000135679. |
| ExpressionAtlasi | Q00987. baseline and differential. |
| Genevisiblei | Q00987. HS. |
Organism-specific databases
| HPAi | CAB000086. CAB016303. |
Interactioni
Subunit structurei
Binary interactionsi
GO - Molecular functioni
- disordered domain specific binding Source: CAFA
- enzyme binding Source: UniProtKB
- identical protein binding Source: IntAct
- p53 binding Source: UniProtKB
- peroxisome proliferator activated receptor binding Source: Ensembl
- protein N-terminus binding Source: CAFA
- scaffold protein binding Source: Ensembl
- ubiquitin protein ligase binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 110358. 458 interactors. |
| DIPi | DIP-392N. |
| IntActi | Q00987. 182 interactors. |
| MINTi | MINT-101583. |
| STRINGi | 9606.ENSP00000417281. |
Chemistry databases
| BindingDBi | Q00987. |
Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 7 – 10 | Combined sources | 4 | |
| Beta strandi | 13 – 15 | Combined sources | 3 | |
| Beta strandi | 17 – 19 | Combined sources | 3 | |
| Helixi | 23 – 25 | Combined sources | 3 | |
| Beta strandi | 27 – 30 | Combined sources | 4 | |
| Helixi | 32 – 41 | Combined sources | 10 | |
| Beta strandi | 46 – 49 | Combined sources | 4 | |
| Helixi | 50 – 64 | Combined sources | 15 | |
| Beta strandi | 71 – 76 | Combined sources | 6 | |
| Beta strandi | 78 – 80 | Combined sources | 3 | |
| Helixi | 81 – 86 | Combined sources | 6 | |
| Beta strandi | 88 – 92 | Combined sources | 5 | |
| Helixi | 96 – 104 | Combined sources | 9 | |
| Beta strandi | 107 – 109 | Combined sources | 3 | |
| Beta strandi | 295 – 297 | Combined sources | 3 | |
| Helixi | 299 – 301 | Combined sources | 3 | |
| Turni | 306 – 308 | Combined sources | 3 | |
| Beta strandi | 314 – 318 | Combined sources | 5 | |
| Turni | 320 – 322 | Combined sources | 3 | |
| Helixi | 433 – 435 | Combined sources | 3 | |
| Turni | 439 – 441 | Combined sources | 3 | |
| Beta strandi | 442 – 444 | Combined sources | 3 | |
| Beta strandi | 448 – 452 | Combined sources | 5 | |
| Beta strandi | 455 – 460 | Combined sources | 6 | |
| Helixi | 462 – 470 | Combined sources | 9 | |
| Turni | 476 – 478 | Combined sources | 3 | |
| Beta strandi | 484 – 489 | Combined sources | 6 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1RV1 | X-ray | 2.30 | A/B/C | 25-109 | [»] | |
| 1T4E | X-ray | 2.60 | A/B | 17-111 | [»] | |
| 1T4F | X-ray | 1.90 | M | 17-125 | [»] | |
| 1YCR | X-ray | 2.60 | A | 17-125 | [»] | |
| 1Z1M | NMR | - | A | 1-118 | [»] | |
| 2AXI | X-ray | 1.40 | A | 17-125 | [»] | |
| 2C6A | NMR | - | A | 290-335 | [»] | |
| 2C6B | NMR | - | A | 290-335 | [»] | |
| 2F1Y | X-ray | 1.70 | A | 224-232 | [»] | |
| 2FOP | X-ray | 2.10 | B | 145-150 | [»] | |
| 2GV2 | X-ray | 1.80 | A | 17-125 | [»] | |
| 2HDP | NMR | - | A/B | 429-491 | [»] | |
| 2LZG | NMR | - | A | 1-125 | [»] | |
| 2M86 | NMR | - | B | 17-125 | [»] | |
| 2MPS | NMR | - | A | 3-109 | [»] | |
| 2RUH | NMR | - | A | 6-102 | [»] | |
| 2VJE | X-ray | 2.20 | A/C | 428-491 | [»] | |
| 2VJF | X-ray | 2.30 | A/C | 428-491 | [»] | |
| 3EQS | X-ray | 1.65 | A | 25-109 | [»] | |
| 3G03 | X-ray | 1.80 | A/C | 18-125 | [»] | |
| 3IUX | X-ray | 1.65 | A/C | 25-109 | [»] | |
| 3IWY | X-ray | 1.93 | A/C | 25-109 | [»] | |
| 3JZK | X-ray | 2.10 | A | 17-111 | [»] | |
| 3JZR | X-ray | 2.10 | A | 17-125 | [»] | |
| 3JZS | X-ray | 1.78 | A | 24-109 | [»] | |
| 3LBK | X-ray | 2.30 | A | 18-111 | [»] | |
| 3LBL | X-ray | 1.60 | A/C/E | 18-111 | [»] | |
| 3LNJ | X-ray | 2.40 | A/C/E | 25-109 | [»] | |
| 3LNZ | X-ray | 1.95 | A/C/E/G/I/K/M/O | 25-109 | [»] | |
| 3MQS | X-ray | 2.40 | D | 394-403 | [»] | |
| 3TJ2 | X-ray | 2.10 | A/C | 18-111 | [»] | |
| 3TPX | X-ray | 1.80 | A/C/E | 25-109 | [»] | |
| 3TU1 | X-ray | 1.60 | A | 18-125 | [»] | |
| 3V3B | X-ray | 2.00 | A/B | 24-110 | [»] | |
| 3VBG | X-ray | 2.80 | A/B/C/D | 25-109 | [»] | |
| 3VZV | X-ray | 2.80 | A/B | 25-109 | [»] | |
| 3W69 | X-ray | 1.90 | A/B | 25-109 | [»] | |
| 4DIJ | X-ray | 1.90 | A/B | 17-111 | [»] | |
| 4ERE | X-ray | 1.80 | A/B | 17-111 | [»] | |
| 4ERF | X-ray | 2.00 | A/C/E | 17-111 | [»] | |
| 4HBM | X-ray | 1.90 | A/B/C/D/E/F/G/H | 6-125 | [»] | |
| 4HFZ | X-ray | 2.69 | A/C | 17-125 | [»] | |
| 4HG7 | X-ray | 1.60 | A | 17-108 | [»] | |
| 4JV7 | X-ray | 2.20 | A | 18-111 | [»] | |
| 4JV9 | X-ray | 2.50 | A | 18-111 | [»] | |
| 4JVE | X-ray | 2.30 | A | 18-111 | [»] | |
| 4JVR | X-ray | 1.70 | A/C/E | 18-111 | [»] | |
| 4JWR | X-ray | 2.35 | A/B/C | 17-111 | [»] | |
| 4MDN | X-ray | 1.90 | A | 18-110 | [»] | |
| 4MDQ | X-ray | 2.12 | A | 25-110 | [»] | |
| 4OAS | X-ray | 1.70 | A/C/E | 17-111 | [»] | |
| 4OBA | X-ray | 1.60 | A/B/C | 17-111 | [»] | |
| 4OCC | X-ray | 1.80 | A/C/E | 17-111 | [»] | |
| 4ODE | X-ray | 1.80 | A | 6-110 | [»] | |
| 4ODF | X-ray | 2.20 | A | 6-110 | [»] | |
| 4OGN | X-ray | 1.38 | A | 6-110 | [»] | |
| 4OGT | X-ray | 1.54 | A | 6-110 | [»] | |
| 4OGV | X-ray | 2.20 | A/B/C | 17-111 | [»] | |
| 4OQ3 | X-ray | 2.30 | A/B/C/D | 17-111 | [»] | |
| 4QO4 | X-ray | 1.70 | A | 17-111 | [»] | |
| 4QOC | X-ray | 1.70 | A/C/E/G/I/K | 17-111 | [»] | |
| 4UD7 | X-ray | 1.60 | A/B/C/D | 17-125 | [»] | |
| 4UE1 | X-ray | 1.45 | A/B/C/D | 17-125 | [»] | |
| 4UMN | X-ray | 1.99 | A/B | 6-125 | [»] | |
| 4WT2 | X-ray | 1.42 | A | 6-110 | [»] | |
| 4XXB | X-ray | 2.40 | B | 290-437 | [»] | |
| 4ZFI | X-ray | 2.00 | A/B/C/D | 18-113 | [»] | |
| 4ZGK | X-ray | 2.00 | A/B | 18-114 | [»] | |
| 4ZYC | X-ray | 1.95 | A/B/C | 17-111 | [»] | |
| 4ZYF | X-ray | 1.80 | A | 17-111 | [»] | |
| 4ZYI | X-ray | 1.67 | A | 17-111 | [»] | |
| 5AFG | X-ray | 1.90 | A | 17-108 | [»] | |
| 5C5A | X-ray | 1.15 | A/B | 20-111 | [»] | |
| 5HMH | X-ray | 1.79 | A/B | 21-116 | [»] | |
| 5HMI | X-ray | 1.74 | A/B | 18-116 | [»] | |
| 5HMK | X-ray | 2.17 | A/B | 17-125 | [»] | |
| 5J7F | X-ray | 2.00 | A/B/C/D | 1-125 | [»] | |
| 5J7G | X-ray | 1.85 | A/B/C/D | 18-125 | [»] | |
| 5LAV | X-ray | 1.73 | A | 19-111 | [»] | |
| 5LAW | X-ray | 1.64 | A | 18-111 | [»] | |
| 5LAY | X-ray | 2.71 | A/B/C/D/E/F | 17-111 | [»] | |
| 5LAZ | X-ray | 1.66 | A | 18-111 | [»] | |
| 5LN2 | X-ray | 1.58 | A | 17-111 | [»] | |
| 5TRF | X-ray | 2.10 | A/B/C/D/E | 10-118 | [»] | |
| DisProti | DP00334. | |||||
| ProteinModelPortali | Q00987. | |||||
| SMRi | Q00987. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | Q00987. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 27 – 107 | SWIBAdd BLAST | 81 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 1 – 110 | Necessary for interaction with USP2Add BLAST | 110 | |
| Regioni | 150 – 230 | Interaction with PYHIN1 and necessary for interaction with RFFL and RNF342 PublicationsAdd BLAST | 81 | |
| Regioni | 170 – 306 | Interaction with MTBPBy similarityAdd BLAST | 137 | |
| Regioni | 210 – 304 | ARF-bindingAdd BLAST | 95 | |
| Regioni | 223 – 232 | Interaction with USP7 | 10 | |
| Regioni | 242 – 331 | Region IIAdd BLAST | 90 | |
| Regioni | 276 – 491 | Necessary for interaction with USP2Add BLAST | 216 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 179 – 185 | Nuclear localization signalSequence analysis | 7 | |
| Motifi | 190 – 202 | Nuclear export signalAdd BLAST | 13 | |
| Motifi | 466 – 473 | Nucleolar localization signalSequence analysis | 8 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Compositional biasi | 210 – 215 | Poly-Ser | 6 | |
| Compositional biasi | 243 – 301 | Asp/Glu-rich (acidic)Add BLAST | 59 |
Domaini
Sequence similaritiesi
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 299 – 328 | RanBP2-typePROSITE-ProRule annotationAdd BLAST | 30 | |
| Zinc fingeri | 438 – 479 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
| eggNOGi | ENOG410IGXG. Eukaryota. ENOG41125MP. LUCA. |
| GeneTreei | ENSGT00530000063539. |
| HOVERGENi | HBG013472. |
| InParanoidi | Q00987. |
| KOi | K06643. |
| OMAi | PCVICQS. |
| OrthoDBi | EOG091G0FYK. |
| PhylomeDBi | Q00987. |
| TreeFami | TF105306. |
Family and domain databases
| CDDi | cd00162. RING. 1 hit. |
| Gene3Di | 1.10.245.10. 1 hit. 3.30.40.10. 1 hit. |
| InterProi | View protein in InterPro IPR028340. Mdm2. IPR015459. MDM2_E3_ligase. IPR016495. p53_neg-reg_MDM_2/4. IPR003121. SWIB_MDM2_domain. IPR001876. Znf_RanBP2. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. |
| PANTHERi | PTHR13844:SF33. PTHR13844:SF33. 1 hit. |
| Pfami | View protein in Pfam PF02201. SWIB. 1 hit. PF00641. zf-RanBP. 1 hit. |
| PIRSFi | PIRSF500700. MDM2. 1 hit. PIRSF006748. p53_MDM_2/4. 1 hit. |
| SUPFAMi | SSF47592. SSF47592. 2 hits. SSF90209. SSF90209. 1 hit. |
| PROSITEi | View protein in PROSITE PS01358. ZF_RANBP2_1. 1 hit. PS50199. ZF_RANBP2_2. 1 hit. PS50089. ZF_RING_2. 1 hit. |
Sequences (11)i
Sequence statusi: Complete.
This entry describes 11 isoformsi produced by alternative splicing. AlignAdd 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.
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
The sequence of this isoform differs from the canonical sequence as follows:
28-222: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
28-222: Missing.
275-300: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
28-300: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
53-222: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
30-388: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
76-102: YCSNDLLGDLFGVPSFSVKEHRKIYTM → NDCANLFPLVDLSIRELYISNYITLGI
103-491: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-61: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
53-97: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
115-169: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MVRSRQM
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 17 | S → P in AAA82237 (PubMed:7651818).Curated | 1 |
Polymorphismi
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_003207 | 1 – 61 | Missing in isoform Mdm2-alpha. 1 PublicationAdd BLAST | 61 | |
| Alternative sequenceiVSP_037997 | 1 | M → MVRSRQM in isoform 11. 1 Publication | 1 | |
| Alternative sequenceiVSP_003209 | 28 – 300 | Missing in isoform Mdm2-B. 1 PublicationAdd BLAST | 273 | |
| Alternative sequenceiVSP_003208 | 28 – 222 | Missing in isoform Mdm2-A and isoform Mdm2-A1. 2 PublicationsAdd BLAST | 195 | |
| Alternative sequenceiVSP_003210 | 30 – 388 | Missing in isoform Mdm2-D. 1 PublicationAdd BLAST | 359 | |
| Alternative sequenceiVSP_003211 | 53 – 222 | Missing in isoform Mdm2-C. 1 PublicationAdd BLAST | 170 | |
| Alternative sequenceiVSP_022578 | 53 – 97 | Missing in isoform Mdm2-F. 1 PublicationAdd BLAST | 45 | |
| Alternative sequenceiVSP_003212 | 76 – 102 | YCSND…KIYTM → NDCANLFPLVDLSIRELYIS NYITLGI in isoform Mdm2-E. 1 PublicationAdd BLAST | 27 | |
| Alternative sequenceiVSP_003213 | 103 – 491 | Missing in isoform Mdm2-E. 1 PublicationAdd BLAST | 389 | |
| Alternative sequenceiVSP_022579 | 115 – 169 | Missing in isoform Mdm2-G. 1 PublicationAdd BLAST | 55 | |
| Alternative sequenceiVSP_003214 | 275 – 300 | Missing in isoform Mdm2-A1. 1 PublicationAdd BLAST | 26 |
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. |
| CCDSi | CCDS61189.1. [Q00987-5] CCDS8986.2. [Q00987-11] |
| PIRi | S24354. |
| 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] |
| UniGenei | Hs.484551. Hs.733536. |
Genome annotation databases
| Ensembli | ENST00000258149; ENSP00000258149; ENSG00000135679. [Q00987-11] ENST00000299252; ENSP00000299252; ENSG00000135679. [Q00987-5] ENST00000360430; ENSP00000353611; ENSG00000135679. [Q00987-2] ENST00000393413; ENSP00000377065; ENSG00000135679. [Q00987-4] |
| GeneIDi | 4193. |
| KEGGi | hsa:4193. |
| UCSCi | uc001sui.6. human. [Q00987-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | MDM2_HUMAN | |
| Accessioni | Q00987Primary (citable) accession number: Q00987 Secondary accession number(s): A6NL51 Q9UMT8 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
| Last sequence update: | April 1, 1993 | |
| Last modified: | July 5, 2017 | |
| This is version 224 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
Miscellaneousi
Caution
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
