SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q00987

- MDM2_HUMAN

UniProt

Q00987 - MDM2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

E3 ubiquitin-protein ligase Mdm2

Gene
MDM2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.13 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri299 – 32830RanBP2-typeAdd
BLAST
Zinc fingeri438 – 47942RING-typeAdd
BLAST

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. ligase activity Source: UniProtKB-KW
  4. p53 binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to acid Source: Ensembl
  2. cellular response to alkaloid Source: Ensembl
  3. cellular response to antibiotic Source: Ensembl
  4. cellular response to estrogen stimulus Source: Ensembl
  5. cellular response to hydrogen peroxide Source: Ensembl
  6. cellular response to hypoxia Source: UniProtKB
  7. cellular response to peptide hormone stimulus Source: Ensembl
  8. cellular response to UV-C Source: Ensembl
  9. cellular response to vitamin B1 Source: Ensembl
  10. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  11. epidermal growth factor receptor signaling pathway Source: Reactome
  12. establishment of protein localization Source: BHF-UCL
  13. Fc-epsilon receptor signaling pathway Source: Reactome
  14. fibroblast growth factor receptor signaling pathway Source: Reactome
  15. innate immune response Source: Reactome
  16. negative regulation of apoptotic process Source: Ensembl
  17. negative regulation of cell cycle arrest Source: BHF-UCL
  18. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  19. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  20. negative regulation of protein processing Source: Ensembl
  21. negative regulation of transcription, DNA-templated Source: UniProtKB
  22. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  23. neurotrophin TRK receptor signaling pathway Source: Reactome
  24. peptidyl-lysine modification Source: BHF-UCL
  25. phosphatidylinositol-mediated signaling Source: Reactome
  26. positive regulation of cell proliferation Source: BHF-UCL
  27. positive regulation of gene expression Source: Ensembl
  28. positive regulation of mitotic cell cycle Source: UniProtKB
  29. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  30. positive regulation of protein export from nucleus Source: Ensembl
  31. protein complex assembly Source: UniProtKB
  32. protein destabilization Source: BHF-UCL
  33. protein localization to nucleus Source: BHF-UCL
  34. protein ubiquitination Source: UniProtKB
  35. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  36. regulation of protein catabolic process Source: UniProtKB
  37. response to antibiotic Source: UniProtKB
  38. response to carbohydrate Source: Ensembl
  39. response to cocaine Source: Ensembl
  40. response to drug Source: Ensembl
  41. response to ether Source: Ensembl
  42. response to iron ion Source: Ensembl
  43. response to magnesium ion Source: Ensembl
  44. response to morphine Source: Ensembl
  45. synaptic transmission Source: Reactome
  46. traversing start control point of mitotic cell cycle Source: Ensembl
  47. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_18307. Trafficking of AMPA receptors.
REACT_309. Stabilization of p53.
SignaLinkiQ00987.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Mdm2 (EC:6.3.2.-)
Alternative name(s):
Double minute 2 protein
Short name:
Hdm2
Oncoprotein Mdm2
p53-binding protein Mdm2
Gene namesi
Name:MDM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6973. MDM2.

Subcellular locationi

Nucleusnucleoplasm. Cytoplasm. Nucleusnucleolus
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.6 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endocytic vesicle membrane Source: Reactome
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: Reactome
  8. protein complex Source: BHF-UCL
  9. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi305 – 3051C → S: No loss of ubiquitin ligase E3 activity.
Mutagenesisi374 – 3741C → T: No loss of ubiquitin ligase E3 activity.
Mutagenesisi438 – 4381C → L: No loss of ubiquitin ligase E3 activity.
Mutagenesisi441 – 4411C → G: Fails to interact with MDM4. 1 Publication
Mutagenesisi449 – 4491C → A: Loss of ubiquitin ligase E3 activity. 1 Publication
Mutagenesisi449 – 4491C → S: No substantial decrease of ubiquitin ligase E3 activity. 1 Publication
Mutagenesisi452 – 4521H → A: Loss of ubiquitin ligase E3 activity.
Mutagenesisi455 – 4551T → A: Significant decrease of ubiquitin ligase E3 activity.
Mutagenesisi457 – 4571H → S: Loss of ubiquitin ligase E3 activity.
Mutagenesisi461 – 4611C → S: Loss of ubiquitin ligase E3 activity.
Mutagenesisi464 – 4641C → 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
Mutagenesisi475 – 4751C → G: Loss of ubiquitin ligase E3 activity.
Mutagenesisi478 – 4781C → R: Fails to interact with MDM4. 1 Publication
Mutagenesisi478 – 4781C → S: Loss of ubiquitin ligase E3 activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi614401. phenotype.
Orphaneti99970. Dedifferentiated liposarcoma.
99971. Well-differentiated liposarcoma.
PharmGKBiPA30718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491E3 ubiquitin-protein ligase Mdm2PRO_0000157332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei166 – 1661Phosphoserine; by SGK12 Publications
Modified residuei240 – 2401Phosphoserine1 Publication
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei260 – 2601Phosphoserine1 Publication
Modified residuei262 – 2621Phosphoserine1 Publication
Modified residuei386 – 3861Phosphoserine; by ATM1 Publication
Modified residuei395 – 3951Phosphoserine; by ATM1 Publication
Modified residuei407 – 4071Phosphoserine; by ATM1 Publication
Modified residuei419 – 4191Phosphothreonine; by ATM1 Publication
Modified residuei425 – 4251Phosphoserine; by ATM1 Publication
Modified residuei429 – 4291Phosphoserine; by ATM1 Publication

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.4 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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ00987.
PaxDbiQ00987.
PRIDEiQ00987.

PTM databases

PhosphoSiteiQ00987.

Miscellaneous databases

PMAP-CutDBQ00987.

Expressioni

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.

Inductioni

By DNA damage.

Gene expression databases

ArrayExpressiQ00987.
BgeeiQ00987.
GenevestigatoriQ00987.

Organism-specific databases

HPAiCAB000086.
CAB016303.

Interactioni

Subunit structurei

Binds p53/TP53, TP73/p73, ARF/P14, PML, RBL5 and RP11, and specifically to RNA. Can interact with RB1, E1A-associated protein EP300 and the E2F1 transcription factor. Forms a ternary complex with p53/TP53 and WWOX. Interacts with CDKN2AIP, MTBP, RFWD3, TBRG1, USP7, PYHIN1, UBXN6, and RBBP6. Isoform Mdm2-F does not interact with p53/TP53. Interacts with and ubiquitinates HIV-1 Tat. Interacts with ARRB1 and ARRB2. Interacts (isoform 2) with PSMA3. Found in a trimeric complex with MDM2, MDM4 and UPB2. Interacts with USP2 (via N-terminus and C-terminus). Interacts with MDM4. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts directly with DAXX and USP7. Interacts (via C-terminus) with RASSF1 isoform A (via N-terminus); the interaction is independent of TP53. Interacts with APEX1; leading to its ubiquitination and degradation. Interacts with RYBP; this inhibits ubiquitination of TP53. Identified in a complex with RYBP and p53/TP53. Also component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in regulating p53/TP53 stabilization and activity. Binds directly both p53/TP53 and TRIM28. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor responses with DNA damage. Interacts directly with both 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. Interacts with herpes virus 8 protein v-IRF4.34 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-389668,EBI-389668
ADRBK1P250984EBI-389668,EBI-3904795
AKT1P317493EBI-389668,EBI-296087
ARP102752EBI-389668,EBI-608057
BTRCQ9Y2979EBI-389668,EBI-307461
CDKN2AQ8N7265EBI-389668,EBI-625922
CSNK1A1P487293EBI-389668,EBI-1383726
CSNK1A1P48729-23EBI-389668,EBI-2040168
CSNK1DP487306EBI-389668,EBI-751621
Csnk1dQ064862EBI-389668,EBI-2910316From a different organism.
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 a different organism.
GNL3Q9BVP23EBI-389668,EBI-641642
GNL3LQ9NVN88EBI-389668,EBI-746682
GORABQ5T7V86EBI-389668,EBI-3917143
HNRNPKP619782EBI-389668,EBI-304185
JMYQ8N9B52EBI-389668,EBI-866435
JUNP054123EBI-389668,EBI-852823
JUNDP175353EBI-389668,EBI-2682803
MDM4O151518EBI-389668,EBI-398437
NCLP193388EBI-389668,EBI-346967
NPM1P067485EBI-389668,EBI-78579
Npm1Q619372EBI-389668,EBI-626362From a different organism.
NR0B2Q154664EBI-389668,EBI-3910729
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
RB1P064004EBI-389668,EBI-491274
RPL11P6291311EBI-389668,EBI-354380
RPL23P628293EBI-389668,EBI-353303
RPL5P467775EBI-389668,EBI-358018
RPS27P426775EBI-389668,EBI-356336
RPS27LQ71UM56EBI-389668,EBI-355126
RPS7P6208115EBI-389668,EBI-354360
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
TP53P0463762EBI-389668,EBI-366083
UBCP0CG486EBI-389668,EBI-3390054
USP2O756044EBI-389668,EBI-743272
USP7Q9300918EBI-389668,EBI-302474
vIRF-4Q2HR732EBI-389668,EBI-9001898From a different organism.

Protein-protein interaction databases

BioGridi110358. 679 interactions.
DIPiDIP-392N.
IntActiQ00987. 179 interactions.
MINTiMINT-101583.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 169
Beta strandi17 – 193
Helixi23 – 253
Beta strandi27 – 304
Helixi32 – 409
Beta strandi46 – 494
Helixi50 – 6314
Turni64 – 674
Turni70 – 723
Beta strandi74 – 763
Beta strandi78 – 803
Helixi81 – 866
Beta strandi88 – 925
Helixi96 – 1049
Beta strandi107 – 1093
Beta strandi295 – 2973
Helixi299 – 3013
Turni306 – 3083
Beta strandi314 – 3185
Turni320 – 3223
Helixi433 – 4353
Turni439 – 4413
Beta strandi442 – 4443
Beta strandi448 – 4525
Beta strandi455 – 4606
Helixi462 – 4709
Turni476 – 4783
Beta strandi484 – 4896

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
4UMNX-ray1.99A/B6-125[»]
DisProtiDP00334.
ProteinModelPortaliQ00987.
SMRiQ00987. Positions 11-110, 290-335, 432-491.

Miscellaneous databases

EvolutionaryTraceiQ00987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 10781SWIBAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 110110Necessary for interaction with USP2Add
BLAST
Regioni150 – 23081Interaction with PYHIN1 and necessary for interaction with RFFLAdd
BLAST
Regioni170 – 306137Interaction with MTBP By similarityAdd
BLAST
Regioni210 – 30495ARF-bindingAdd
BLAST
Regioni223 – 23210Interaction with USP7
Regioni242 – 33190Region IIAdd
BLAST
Regioni276 – 491216Necessary for interaction with USP2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi179 – 1857Nuclear localization signal Reviewed prediction
Motifi190 – 20213Nuclear export signalAdd
BLAST
Motifi466 – 4738Nucleolar localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi210 – 2156Poly-Ser
Compositional biasi243 – 30159Asp/Glu-rich (acidic)Add
BLAST

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.

Sequence similaritiesi

Belongs to the MDM2/MDM4 family.
Contains 1 SWIB domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri299 – 32830RanBP2-typeAdd
BLAST
Zinc fingeri438 – 47942RING-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG46328.
HOVERGENiHBG013472.
InParanoidiQ00987.
KOiK06643.
OMAiLCVIREI.
OrthoDBiEOG7RRF7T.
PhylomeDBiQ00987.
TreeFamiTF105306.

Family and domain databases

Gene3Di1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR028340. 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.
[Graphical view]
PANTHERiPTHR10360:SF11. PTHR10360:SF11. 1 hit.
PfamiPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFiPIRSF500700. MDM2. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 2 hits.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. Align

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

MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM    50
KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY 100
TMIYRNLVVV NQQESSDSGT SVSENRCHLE GGSDQKDLVQ ELQEEKPSSS 150
HLVSRPSTSS RRRAISETEE NSDELSGERQ RKRHKSDSIS LSFDESLALC 200
VIREICCERS SSSESTGTPS NPDLDAGVSE HSGDWLDQDS VSDQFSVEFE 250
VESLDSEDYS LSEEGQELSD EDDEVYQVTV YQAGESDTDS FEEDPEISLA 300
DYWKCTSCNE MNPPLPSHCN RCWALRENWL PEDKGKDKGE ISEKAKLENS 350
TQAEEGFDVP DCKKTIVNDS RESCVEENDD KITQASQSQE SEDYSQPSTS 400
SSIIYSSQED VKEFEREETQ DKEESVESSL PLNAIEPCVI CQGRPKNGCI 450
VHGKTGHLMA CFTCAKKLKK RNKPCPVCRQ PIQMIVLTYF P 491
Length:491
Mass (Da):55,233
Last modified:April 1, 1993 - v1
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.

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

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161Missing in isoform Mdm2-alpha. VSP_003207Add
BLAST
Alternative sequencei1 – 11M → MVRSRQM in isoform 11. VSP_037997
Alternative sequencei28 – 300273Missing in isoform Mdm2-B. VSP_003209Add
BLAST
Alternative sequencei28 – 222195Missing in isoform Mdm2-A and isoform Mdm2-A1. VSP_003208Add
BLAST
Alternative sequencei30 – 388359Missing in isoform Mdm2-D. VSP_003210Add
BLAST
Alternative sequencei53 – 222170Missing in isoform Mdm2-C. VSP_003211Add
BLAST
Alternative sequencei53 – 9745Missing in isoform Mdm2-F. VSP_022578Add
BLAST
Alternative sequencei76 – 10227YCSND…KIYTM → NDCANLFPLVDLSIRELYIS NYITLGI in isoform Mdm2-E. VSP_003212Add
BLAST
Alternative sequencei103 – 491389Missing in isoform Mdm2-E. VSP_003213Add
BLAST
Alternative sequencei115 – 16955Missing in isoform Mdm2-G. VSP_022579Add
BLAST
Alternative sequencei275 – 30026Missing in isoform Mdm2-A1. VSP_003214Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171S → P in AAA82237. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005268872.2. [Q00987-1]
XP_006719462.1. XM_006719399.1. [Q00987-8]
UniGeneiHs.484551.
Hs.733536.

Genome annotation databases

EnsembliENST00000258149; ENSP00000258149; ENSG00000135679. [Q00987-10]
ENST00000299252; ENSP00000299252; ENSG00000135679. [Q00987-5]
ENST00000348801; ENSP00000335096; ENSG00000135679.
ENST00000356290; ENSP00000348637; ENSG00000135679. [Q00987-5]
ENST00000360430; ENSP00000353611; ENSG00000135679. [Q00987-2]
ENST00000393412; ENSP00000377064; ENSG00000135679. [Q00987-4]
ENST00000393413; ENSP00000377065; ENSG00000135679. [Q00987-4]
ENST00000428863; ENSP00000410694; ENSG00000135679. [Q00987-3]
ENST00000462284; ENSP00000417281; ENSG00000135679. [Q00987-11]
ENST00000540827; ENSP00000440932; ENSG00000135679. [Q00987-2]
GeneIDi4193.
KEGGihsa:4193.
UCSCiuc001sui.4. human. [Q00987-11]
uc001sun.5. human. [Q00987-5]
uc001suo.4. human. [Q00987-2]
uc009zqy.1. human. [Q00987-1]
uc009zrc.4. human. [Q00987-4]
uc009zrh.4. human. [Q00987-3]

Polymorphism databases

DMDMi266516.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

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

Mdm2 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005268872.2. [Q00987-1 ]
XP_006719462.1. XM_006719399.1. [Q00987-8 ]
UniGenei Hs.484551.
Hs.733536.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
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 [» ]
4UMN X-ray 1.99 A/B 6-125 [» ]
DisProti DP00334.
ProteinModelPortali Q00987.
SMRi Q00987. Positions 11-110, 290-335, 432-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110358. 679 interactions.
DIPi DIP-392N.
IntActi Q00987. 179 interactions.
MINTi MINT-101583.

Chemistry

BindingDBi Q00987.
ChEMBLi CHEMBL5023.

PTM databases

PhosphoSitei Q00987.

Polymorphism databases

DMDMi 266516.

Proteomic databases

MaxQBi Q00987.
PaxDbi Q00987.
PRIDEi Q00987.

Protocols and materials databases

DNASUi 4193.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258149 ; ENSP00000258149 ; ENSG00000135679 . [Q00987-10 ]
ENST00000299252 ; ENSP00000299252 ; ENSG00000135679 . [Q00987-5 ]
ENST00000348801 ; ENSP00000335096 ; ENSG00000135679 .
ENST00000356290 ; ENSP00000348637 ; ENSG00000135679 . [Q00987-5 ]
ENST00000360430 ; ENSP00000353611 ; ENSG00000135679 . [Q00987-2 ]
ENST00000393412 ; ENSP00000377064 ; ENSG00000135679 . [Q00987-4 ]
ENST00000393413 ; ENSP00000377065 ; ENSG00000135679 . [Q00987-4 ]
ENST00000428863 ; ENSP00000410694 ; ENSG00000135679 . [Q00987-3 ]
ENST00000462284 ; ENSP00000417281 ; ENSG00000135679 . [Q00987-11 ]
ENST00000540827 ; ENSP00000440932 ; ENSG00000135679 . [Q00987-2 ]
GeneIDi 4193.
KEGGi hsa:4193.
UCSCi uc001sui.4. human. [Q00987-11 ]
uc001sun.5. human. [Q00987-5 ]
uc001suo.4. human. [Q00987-2 ]
uc009zqy.1. human. [Q00987-1 ]
uc009zrc.4. human. [Q00987-4 ]
uc009zrh.4. human. [Q00987-3 ]

Organism-specific databases

CTDi 4193.
GeneCardsi GC12P069201.
HGNCi HGNC:6973. MDM2.
HPAi CAB000086.
CAB016303.
MIMi 164785. gene.
614401. phenotype.
neXtProti NX_Q00987.
Orphaneti 99970. Dedifferentiated liposarcoma.
99971. Well-differentiated liposarcoma.
PharmGKBi PA30718.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46328.
HOVERGENi HBG013472.
InParanoidi Q00987.
KOi K06643.
OMAi LCVIREI.
OrthoDBi EOG7RRF7T.
PhylomeDBi Q00987.
TreeFami TF105306.

Enzyme and pathway databases

Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_18307. Trafficking of AMPA receptors.
REACT_309. Stabilization of p53.
SignaLinki Q00987.

Miscellaneous databases

EvolutionaryTracei Q00987.
GeneWikii Mdm2.
GenomeRNAii 4193.
NextBioi 16526.
PMAP-CutDB Q00987.
PROi Q00987.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00987.
Bgeei Q00987.
Genevestigatori Q00987.

Family and domain databases

Gene3Di 1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProi 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.
[Graphical view ]
PANTHERi PTHR10360:SF11. PTHR10360:SF11. 1 hit.
Pfami PF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF500700. MDM2. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF47592. SSF47592. 2 hits.
PROSITEi PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amplification of a gene encoding a p53-associated protein in human sarcomas."
    Oliner J.D., Kinzler K.W., Meltzer P.S., George D.L., Vogelstein B.
    Nature 358:80-83(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2).
    Tissue: Colon.
  2. "Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: transforming ability and frequent detection in human cancer."
    Sigalas I., Calvert A.H., Anderson J.J., Neal D.E., Lunec J.
    Nat. Med. 2:912-917(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-A; MDM2-B; MDM2-C; MDM2-D AND MDM2-E).
    Tissue: Ovarian carcinoma.
  3. "A novel exon within the mdm2 gene modulates translation initiation in vitro and disrupts the p53-binding domain of mdm2 protein."
    Veldhoen N., Metcalfe S., Milner J.
    Oncogene 18:7026-7033(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2-ALPHA).
  4. "Analysis of the molecular species generated by MDM2 gene amplification in liposarcomas."
    Tamborini E., Della Torre G., Lavarino C., Azzarelli A., Carpinelli P., Pierotti M.A., Pilotti S.
    Int. J. Cancer 92:790-796(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-F AND MDM2-G), INTERACTION WITH TP53.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2).
    Tissue: Tongue.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2).
  7. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
    Tissue: Rhabdomyosarcoma.
  10. "A functional p53-responsive intronic promoter is contained within the human mdm2 gene."
    Zauberman A., Flusberg D., Haupt Y., Barak Y., Oren M.
    Nucleic Acids Res. 23:2584-2592(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
  11. "Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein."
    Landers J.E., Cassel S.L., George D.L.
    Cancer Res. 57:3562-3568(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  12. "Genomic organisation of the human MDM2 oncogene and relationship to its alternatively spliced mRNAs."
    Liang H., Atkins H., Abdel-Fattah R., Jones S.N., Lunec J.
    Gene 338:217-223(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-491 (ISOFORM MDM2-A1).
  13. "A MboII polymorphism in exon 11 of the human MDM2 gene occurring in normal blood donors and in soft tissue sarcoma patients: an indication for an increased cancer susceptibility?"
    Taubert H., Kappler M., Meye A., Bartel F., Schlott T., Lautenschlaeger C., Bache M., Schmidt H., Wuerl P.
    Mutat. Res. 456:39-44(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-481.
  14. "Identification and characterization of multiple mdm-2 proteins and mdm-2-p53 protein complexes."
    Olson D.C., Marechal V., Momand J., Chen J., Romocki C., Levine A.J.
    Oncogene 8:2353-2360(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53.
  15. "Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53."
    Honda R., Tanaka H., Yasuda H.
    FEBS Lett. 420:25-27(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-464.
  16. "Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein."
    Sharp D.A., Kratowicz S.A., Sank M.J., George D.L.
    J. Biol. Chem. 274:38189-38196(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-441 AND CYS-478.
  17. "Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage."
    Khosravi R., Maya R., Gottlieb T., Oren M., Shiloh Y., Shkedy D.
    Proc. Natl. Acad. Sci. U.S.A. 96:14973-14977(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ATM.
  18. "Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53."
    Fang S., Jensen J.P., Ludwig R.L., Vousden K.H., Weissman A.M.
    J. Biol. Chem. 275:8945-8951(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  19. "Identification of a cryptic nucleolar-localization signal in MDM2."
    Lohrum M.A.E., Ashcroft M., Kubbutat M.H.G., Vousden K.H.
    Nat. Cell Biol. 2:179-181(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOLAR LOCALIZATION SIGNAL.
  20. "Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase."
    Honda R., Yasuda H.
    Oncogene 19:1473-1476(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-449.
  21. "Hypophosphorylation of Mdm2 augments p53 stability."
    Blattner C., Hay T., Meek D.W., Lane D.P.
    Mol. Cell. Biol. 22:6170-6182(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-240; SER-242; SER-246; SER-260 AND SER-262.
  22. Cited for: INTERACTION WITH HIV-1 TAT.
  23. "Mdm2-dependent ubiquitination and degradation of the insulin-like growth factor 1 receptor."
    Girnita L., Girnita A., Larsson O.
    Proc. Natl. Acad. Sci. U.S.A. 100:8247-8252(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF IGF1R, INTERACTION WITH IGF1R.
  24. "Synergistic tumor suppression by coexpression of FHIT and p53 coincides with FHIT-mediated MDM2 inactivation and p53 stabilization in human non-small cell lung cancer cells."
    Nishizaki M., Sasaki J., Fang B., Atkinson E.N., Minna J.D., Roth J.A., Ji L.
    Cancer Res. 64:5745-5752(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHIT.
  25. "A single nucleotide polymorphism in the MDM2 promoter attenuates the p53 tumor suppressor pathway and accelerates tumor formation in humans."
    Bond G.L., Hu W., Bond E.E., Robins H., Lutzker S.G., Arva N.C., Bargonetti J., Bartel F., Taubert H., Wuerl P., Onel K., Yip L., Hwang S.J., Strong L.C., Lozano G., Levine A.J.
    Cell 119:591-602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ACCELERATED TUMOR FORMATION.
  26. "Negative regulation of p53 functions by Daxx and the involvement of MDM2."
    Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.
    J. Biol. Chem. 279:50566-50579(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX.
  27. "A dynamic role of HAUSP in the p53-Mdm2 pathway."
    Li M., Brooks C.L., Kon N., Gu W.
    Mol. Cell 13:879-886(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP7, DEUBIQUITINATION BY USP7.
  28. "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
    Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
    Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML AND RPL11, SUBCELLULAR LOCATION.
  29. "{beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase."
    Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R.J., Larsson O.
    J. Biol. Chem. 280:24412-24419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
  30. "WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53."
    Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.
    J. Biol. Chem. 280:43100-43108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWOX AND TP53.
  31. "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein."
    Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X.
    Mol. Cell 20:699-708(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSMA3.
  32. "Regulation of p53 and MDM2 activity by MTBP."
    Brady M., Vlatkovic N., Boyd M.T.
    Mol. Cell. Biol. 25:545-553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MTBP, MUTAGENESIS OF CYS-464.
  33. "Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2."
    Ding Y., Lee J.-F., Lu H., Lee M.-H., Yan D.-H.
    Mol. Cell. Biol. 26:1979-1996(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH PYHIN1, MUTAGENESIS OF CYS-464.
  34. Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX AND USP7, INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
  35. "CARF binds to three members (ARF, p53, and HDM2) of the p53 tumor-suppressor pathway."
    Kamrul H.M., Wadhwa R., Kaul S.C.
    Ann. N. Y. Acad. Sci. 1100:312-315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN2AIP.
  36. "The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2."
    Stevenson L.F., Sparks A., Allende-Vega N., Xirodimas D.P., Lane D.P., Saville M.K.
    EMBO J. 26:976-986(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP2, UBIQUITINATION, DEUBIQUITINATION BY USP2.
  37. "The single-nucleotide polymorphism 309 in the MDM2 gene contributes to the Li-Fraumeni syndrome and related phenotypes."
    Ruijs M.W., Schmidt M.K., Nevanlinna H., Tommiska J., Aittomaki K., Pruntel R., Verhoef S., Van't Veer L.J.
    Eur. J. Hum. Genet. 15:110-114(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ACCELERATED TUMOR FORMATION AND LI-FRAUMENI SYNDROME.
  38. Cited for: INTERACTION WITH TBRG1.
  39. "PACT is a negative regulator of p53 and essential for cell growth and embryonic development."
    Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J., Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.
    Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBBP6.
  40. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
    Yang W., Dicker D.T., Chen J., El-Deiry W.S.
    Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFFL, AUTOUBIQUITINATION.
  41. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
    Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
    EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND DAXX, SUBCELLULAR LOCATION.
  42. "AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and degradation and promote constitutive p53 turnover."
    Zweitzig D.R., Shcherbik N., Haines D.S.
    Mol. Biol. Cell 19:5029-5029(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBXN6.
  43. "ATM activates p53 by regulating MDM2 oligomerization and E3 processivity."
    Cheng Q., Chen L., Li Z., Lane W.S., Chen J.
    EMBO J. 28:3857-3867(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-386; SER-395; SER-407; THR-419; SER-425 AND SER-429.
  44. Cited for: FUNCTION, INTERACTION WITH RYBP, IDENTIFICATION IN A COMPLEX WITH RYBP AND TP53.
  45. "Sgk1 activates MDM2-dependent p53 degradation and affects cell proliferation, survival, and differentiation."
    Amato R., D'Antona L., Porciatti G., Agosti V., Menniti M., Rinaldo C., Costa N., Bellacchio E., Mattarocci S., Fuiano G., Soddu S., Paggi M.G., Lang F., Perrotti N.
    J. Mol. Med. 87:1221-1239(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-166 BY SGK1.
  46. "Kaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 targets MDM2 to deregulate the p53 tumor suppressor pathway."
    Lee H.R., Toth Z., Shin Y.C., Lee J.S., Chang H., Gu W., Oh T.K., Kim M.H., Jung J.U.
    J. Virol. 83:6739-6747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-8 PROTEIN VIRF4.
  47. "Ubiquitination of mammalian AP endonuclease (APE1) regulated by the p53-MDM2 signaling pathway."
    Busso C.S., Iwakuma T., Izumi T.
    Oncogene 28:1616-1625(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APEX1, MUTAGENESIS OF CYS-464.
  48. Cited for: IDENTIFICATION.
  49. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  50. "p53 inhibits tumor cell invasion via the degradation of snail protein in hepatocellular carcinoma."
    Lim S.O., Kim H., Jung G.
    FEBS Lett. 584:2231-2236(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNAI1.
  51. "ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage."
    Taira N., Yamamoto H., Yamaguchi T., Miki Y., Yoshida K.
    J. Biol. Chem. 285:4909-4919(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DYRK2 UBIQUITINATION, INTERACTION WITH DYRK2.
  52. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
    Gilmore-Hebert M., Ramabhadran R., Stern D.F.
    Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX AND WITH TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
  53. "RFWD3-Mdm2 ubiquitin ligase complex positively regulates p53 stability in response to DNA damage."
    Fu X., Yucer N., Liu S., Li M., Yi P., Mu J.J., Yang T., Chu J., Jung S.Y., O'Malley B.W., Gu W., Qin J., Wang Y.
    Proc. Natl. Acad. Sci. U.S.A. 107:4579-4584(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53 AND RFWD3, MUTAGENESIS OF CYS-464.
  54. "MdmX is a substrate for the deubiquitinating enzyme USP2a."
    Allende-Vega N., Sparks A., Lane D.P., Saville M.K.
    Oncogene 29:432-441(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP2 AND MDM4.
  55. "Notch1 binds and induces degradation of Snail in hepatocellular carcinoma."
    Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K., Jung G.
    BMC Biol. 9:83-83(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNAI1 AND NOTCH1.
  56. "Ret finger protein 2 enhances ionizing radiation-induced apoptosis via degradation of AKT and MDM2."
    Joo H.M., Kim J.Y., Jeong J.B., Seong K.M., Nam S.Y., Yang K.H., Kim C.S., Kim H.S., Jeong M., An S., Jin Y.W.
    Eur. J. Cell Biol. 90:420-431(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM13, UBIQUITINATION.
  57. "BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction."
    Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D.
    Oncogene 32:3156-3164(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PML.
  58. "Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain."
    Kussie P.H., Gorina S., Marechal V., Elenbaas B., Moreau J., Levine A.J., Pavletich N.P.
    Science 274:948-953(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-109 IN COMPLEX WITH P53.
  59. "Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway."
    Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y.
    PLoS Biol. 4:228-239(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 224-232 IN COMPLEX WITH USP7, INTERACTION WITH USP7.
  60. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 145-150 IN COMPLEX WITH USP7, INTERACTION WITH USP7.

Entry informationi

Entry nameiMDM2_HUMAN
AccessioniPrimary (citable) accession number: Q00987
Secondary accession number(s): A6NL51
, A8K2S6, Q13226, Q13297, Q13298, Q13299, Q13300, Q13301, Q53XW0, Q71TW9, Q8WYJ1, Q8WYJ2, Q9UGI3, Q9UMT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 3, 2014
This is version 191 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Miscellaneous

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

Caution

A report observed N-glycosylation at Asn-349 (1 Publication). However, as the protein is not extracellular, additional evidences are required to confirm this result.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi