Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein Mdm4  

UniProtKB / Swiss-Prot ID :  MDM4_HUMAN

Gene Name (Synonyms) : 
MDM4, MDMX  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. 

Protein Sequence MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCEEECCCHHHHHHHHHHCCCCCEEEHHHHHHHHHHHHHHHHHHHCCC...
Protein Variant
LocationDescription
175I -> T (in dbSNP:rs4252716). VAR_017106
406T -> I (in dbSNP:rs4252741). VAR_017107
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
55PhosphotyrosineEVMHYLGQY
HHHHHHHHH
8.40Phosphositeplus
Link-
96PhosphoserineVKDPSPLYD
CCCCHHHHH
37.36Phosphositeplus
Link-
99PhosphotyrosinePSPLYDMLR
CHHHHHHHH
11.59Phosphositeplus
Link-
161PhosphoserineTLPTSEHKC
CCCCCCCCC
35.45HPRD
Link-
254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GVGIKVEAA
EEEEEEEEC
28.26Phosphositeplus
Link-
289PhosphoserineEDSKSLSDD
CCCCCCCCC
36.74Phosphositeplus
Link-
342PhosphoserineTHSLSTSDI
CCCCCHHHC
28.96Phosphositeplus
Link-
342Phosphoserine (AKT1)THSLSTSDI
CCCCCHHHC
28.96HPRD
Link-
342Phosphoserine (CHEK1)THSLSTSDI
CCCCCHHHC
28.96HPRD
Link-
342Phosphoserine (CHEK2)THSLSTSDI
CCCCCHHHC
28.96HPRD
Link-
342Phosphoserine; by CHEK2.THSLSTSDI
CCCCCHHHC
28.96UniProtKB
Link-
361noneNDVPDCRRT
CCCCCCCCH
38.10HPRD
Link-
365PhosphothreonineDCRRTISAP
CCCCHHHHH
10.42HPRD
Link-
365PhosphothreonineDCRRTISAP
CCCCHHHHH
10.42Phosphositeplus
Link-
367PhosphoserineRRTISAPVV
CCHHHHHCC
26.38HPRD
Link-
367PhosphoserineRRTISAPVV
CCHHHHHCC
26.38Phosphositeplus
Link-
367Phosphoserine (CHEK1)RRTISAPVV
CCHHHHHCC
26.38HPRD
Link-
367Phosphoserine (CHEK2)RRTISAPVV
CCHHHHHCC
26.38HPRD
Link-
367Phosphoserine; by CHEK1 and CHEK2.RRTISAPVV
CCHHHHHCC
26.38UniProtKB
Link-
379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)DAYIKKENS
HHHHCCCCH
41.16Phosphositeplus
Link-
391PhosphoserineDPCNSVEFL
HCCCCCCCC
29.73HPRD
Link-
403PhosphoserineHSSESQETI
CCCCCCHHH
34.95Phosphositeplus
Link-
403Phosphoserine (ATM)HSSESQETI
CCCCCCHHH
34.95HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CHK1_HUMANphosphorylation reactionMINT-1958287MINT16511572
1433B_HUMANphysical interactionMINT-1958529MINT16511560
1433G_HUMANphysical interactionMINT-1958118MINT16511572
1433G_HUMANphysical interactionMINT-1958602MINT16511560
1433G_HUMANphysical interactionMINT-1957780MINT16511572
1433G_HUMANphysical interactionMINT-1957996MINT16511572
1433G_HUMANphysical interactionMINT-1958362MINT16511572
1433G_HUMANphysical interactionMINT-1958145MINT16511572
1433E_HUMANphysical interactionMINT-1958547MINT16511560
UBIQ_HUMANphysical interactionMINT-3391197MINT17110929
MDM2_HUMANphysical interactionMINT-4054707MINT17159902
MDM2_HUMANphysical interactionMINT-15116MINT10608892
1433F_HUMANphysical interactionMINT-1958584MINT16511560
MDM2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
DIP:40080EDIP10608892
10218570
10608892
10218570
10218570
10608892
MDM4_HUMANphysical interactionDIP:40084EDIP10218570
P53_HUMANphysical interactionDIP:40086EDIP11223036
P73_HUMANphysical interactionDIP:40087EDIP11223036
MDM2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-398450
EBI-399556
EBI-399
intact10608892
10608892
10608892
10608892
ARF1_HUMANin vitro
in vivo
HPRD:04082HPRD11297540
MDM2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04082HPRD10218570
12393902
12483531
10608892
P53_HUMANin vitro
in vivo
HPRD:04082HPRD8895579
9226370
12393902
11528400
RB_HUMANin vivoHPRD:04082HPRD16510145
E2F1_HUMANin vitro
yeast 2-hybrid
HPRD:04082HPRD12532331
EP300_HUMANin vitro
in vivo
HPRD:04082HPRD12483531
UBP7_HUMANin vitroHPRD:04082HPRD15916963
P73_HUMANin vitroHPRD:04082HPRD11223036
KC1A_HUMANin vivoHPRD:04082HPRD16511560
1433G_HUMANin vivoHPRD:04082HPRD16511560
1433T_HUMANin vivoHPRD:04082HPRD16511560
1433B_HUMANin vivoHPRD:04082HPRD16511560
1433Z_HUMANin vivoHPRD:04082HPRD16511560
1433E_HUMANin vivoHPRD:04082HPRD16511560
1433F_HUMANin vivoHPRD:04082HPRD16511560
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"14-3-3gamma binds to MDMX that is phosphorylated by UV-activatedChk1, resulting in p53 activation.";
Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.;
EMBO J. 25:1207-1218(2006).
Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-367 BY CHEK1, ANDINTERACTION WITH YWHAG.
"ATM and Chk2-dependent phosphorylation of MDMX contribute to p53activation after DNA damage.";
Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J.;
EMBO J. 24:3411-3422(2005).
Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-342 AND SER-367 BYCHEK2, UBIQUITINATION, AND INTERACTION WITH MDM2.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures