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HUMAN:MDM4

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) MDM4 (synonyms: MDMX)
Protein Name(s) Protein Mdm4

Double minute 4 protein Mdm2-like p53-binding protein Protein Mdmx p53-binding protein Mdm4

External Links
UniProt O15151
EMBL AF007111
AY923176
AK223228
AY207458
AL512306
BC067299
BC105106
CCDS CCDS1447.1
CCDS55674.1
CCDS55675.1
RefSeq NP_001191100.1
NP_001191101.1
NP_001265445.1
NP_001265446.1
NP_001265447.1
NP_001265448.1
NP_002384.2
UniGene Hs.497492
PDB 2CR8
2VJE
2VJF
2VYR
3DAB
3EQY
3FDO
3FE7
3FEA
3JZO
3JZP
3JZQ
3LBJ
3MQR
3U15
PDBsum 2CR8
2VJE
2VJF
2VYR
3DAB
3EQY
3FDO
3FE7
3FEA
3JZO
3JZP
3JZQ
3LBJ
3MQR
3U15
ProteinModelPortal O15151
SMR O15151
BioGrid 110359
DIP DIP-24199N
IntAct O15151
MINT MINT-113852
STRING 9606.ENSP00000356150
BindingDB O15151
ChEMBL CHEMBL2221344
PhosphoSite O15151
MaxQB O15151
PaxDb O15151
PRIDE O15151
Ensembl ENST00000367182
ENST00000367183
ENST00000454264
GeneID 4194
KEGG hsa:4194
UCSC uc001hay.2
uc001hba.3
uc021phx.1
CTD 4194
GeneCards GC01P204486
HGNC HGNC:6974
HPA HPA018919
MIM 602704
neXtProt NX_O15151
PharmGKB PA30719
eggNOG NOG46328
GeneTree ENSGT00530000063539
HOGENOM HOG000293341
HOVERGEN HBG013472
InParanoid O15151
KO K10127
OMA TENMEDC
OrthoDB EOG7RRF7T
PhylomeDB O15151
TreeFam TF105306
ChiTaRS MDM4
EvolutionaryTrace O15151
GeneWiki MDM4
GenomeRNAi 4194
NextBio 16538
PMAP-CutDB O15151
PRO PR:O15151
Proteomes UP000005640
Bgee O15151
CleanEx HS_MDM4
ExpressionAtlas O15151
Genevestigator O15151
GO GO:0005634
GO:0019899
GO:0008270
GO:0008283
GO:0071456
GO:0030330
GO:0045023
GO:0043066
GO:0071157
GO:0008285
GO:0042177
GO:0000122
GO:0008284
GO:0006461
GO:0050821
Gene3D 1.10.245.10
3.30.40.10
InterPro IPR015458
IPR016495
IPR003121
IPR001876
IPR001841
IPR013083
PANTHER PTHR10360:SF10
Pfam PF02201
PF00641
PIRSF PIRSF500699
PIRSF006748
SMART SM00184
SM00547
SUPFAM SSF47592
PROSITE PS01358
PS50199
PS50089

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

acts_upstream_of_or_within

GO:0003281

ventricular septum development

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O35618

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0003203

endocardial cushion morphogenesis

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O35618

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0003181

atrioventricular valve morphogenesis

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O35618

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0003170

heart valve development

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O35618

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0003283

atrial septum development

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O35618

P

Seeded From UniProt

complete

involved_in

GO:0071456

cellular response to hypoxia

PMID:20810912[1]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:10608892[2]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045023

G0 to G1 transition

PMID:12101245[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0000122

negative regulation of transcription from RNA polymerase II promoter

PMID:25659040[4]

ECO:0000314

P

Figure 1. The hMDMXp60 isoform is initiated at the 7th in frame AUG codon. (A) Cartoon illustrating the hmdmx mRNA constructs and the mutated AUG sites Figure 2. hMDMXp60 and hMDMXFL are derived from cap-independent mRNA translation initiation. Figure 3. hMDMXp60 shows higher affinity toward hMDM2 as compared to hMDMXFL. Immunoprecipitation (IP) against hMDM2 shows that hMDM2 interacts with both hMDMX isoforms

complete
CACAO 10695

involved_in

GO:0042177

negative regulation of protein catabolic process

PMID:10608892[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030330

DNA damage response, signal transduction by p53 class mediator

PMID:14660608[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0019899

enzyme binding

PMID:19838211[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O75604

F

Seeded From UniProt

complete

involved_in

GO:0008283

cell population proliferation

PMID:12101245[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0065003

protein-containing complex assembly

PMID:10608892[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:9226370[7]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000122

negative regulation of transcription by RNA polymerase II

PMID:9226370[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016495

C

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016495

P

Seeded From UniProt

complete

involved_in

GO:0071157

negative regulation of cell cycle arrest

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016495

P

Seeded From UniProt

complete

involved_in

GO:0008285

negative regulation of cell population proliferation

PMID:9226370[7]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:10608892[2]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1901796

regulation of signal transduction by p53 class mediator

Reactome:R-HSA-5633007

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016579

protein deubiquitination

Reactome:R-HSA-5688426

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006977

DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Reactome:R-HSA-69563

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-6805022
Reactome:R-HSA-6804998
Reactome:R-HSA-6804996
Reactome:R-HSA-6804879
Reactome:R-HSA-6804741
Reactome:R-HSA-6804724
Reactome:R-HSA-6804253
Reactome:R-HSA-6798373
Reactome:R-HSA-5689972
Reactome:R-HSA-5689950
Reactome:R-HSA-5633460
Reactome:R-HSA-349455
Reactome:R-HSA-349426

ECO:0000304

author statement supported by traceable reference used in manual assertion













C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Chen, B et al. (2010) Hypoxia downregulates p53 but induces apoptosis and enhances expression of BAD in cultures of human syncytiotrophoblasts. Am. J. Physiol., Cell Physiol. 299 C968-76 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Sharp, DA et al. (1999) Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274 38189-96 PubMed GONUTS page
  3. ↑ 3.0 3.1 Migliorini, D et al. (2002) Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development. Mol. Cell. Biol. 22 5527-38 PubMed GONUTS page
  4. ↑ Tournillon, AS et al. (2015) The alternative translated MDMX(p60) isoform regulates MDM2 activity. Cell Cycle 14 449-58 PubMed GONUTS page
  5. ↑ Mancini, F et al. (2004) MDM4 (MDMX) overexpression enhances stabilization of stress-induced p53 and promotes apoptosis. J. Biol. Chem. 279 8169-80 PubMed GONUTS page
  6. ↑ Allende-Vega, N et al. (2010) MdmX is a substrate for the deubiquitinating enzyme USP2a. Oncogene 29 432-41 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 Shvarts, A et al. (1997) Isolation and identification of the human homolog of a new p53-binding protein, Mdmx. Genomics 43 34-42 PubMed GONUTS page
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