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{{Infobox_gene}}
{{PBB_Controls
'''Protein Mdm4''' is a [[protein]] that in humans is encoded by the ''MDM4'' [[gene]].<ref name="pmid9226370">{{cite journal | vauthors = Shvarts A, Bazuine M, Dekker P, Ramos YF, Steegenga WT, Merckx G, van Ham RC, van der Houven van Oordt W, van der Eb AJ, Jochemsen AG | title = Isolation and identification of the human homolog of a new p53-binding protein, Mdmx | journal = Genomics | volume = 43 | issue = 1 | pages = 34–42 | date = Sep 1997 | pmid = 9226370 | pmc =  | doi = 10.1006/geno.1997.4775 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MDM4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2cr8.
| PDB = {{PDB2|2cr8}}
| Name = Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)
| HGNCid = 6974
| Symbol = MDM4
| AltSymbols =; DKFZp781B1423; MDMX; MGC132766; MRP1
| OMIM = 602704
| ECnumber = 
| Homologene = 1794
| MGIid = 107934
| GeneAtlas_image1 = PBB_GE_MDM4_205655_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0042177 |text = negative regulation of protein catabolic process}} {{GNF_GO|id=GO:0045023 |text = G0 to G1 transition}} {{GNF_GO|id=GO:0050821 |text = protein stabilization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4194
    | Hs_Ensembl = ENSG00000198625
    | Hs_RefseqProtein = NP_002384
    | Hs_RefseqmRNA = NM_002393
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 202752134
    | Hs_GenLoc_end = 202793871
    | Hs_Uniprot = O15151
    | Mm_EntrezGene = 17248
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_008575
    | Mm_RefseqProtein = NP_032601
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)''', also known as '''MDM4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The human MDM4 gene, which plays a role in [[apoptosis]], encodes a 490-amino acid protein containing a [[RING finger domain]] and a putative [[nuclear localization signal]]. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the [[C-terminal]] region of the protein. The mRNA is expressed at a high level in [[thymus]] and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the [[N-terminal]] region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2<ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The human MDM4 gene, which plays a role in apoptosis, encodes a 490-amino acid protein containing a RING finger domain and a putative nuclear localization signal. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the C-terminal region of the protein. The mRNA is expressed at a high level in thymus and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the N-terminal region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2<ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MDM4 has been shown to [[Protein-protein interaction|interact]] with [[E2F1]],<ref name=pmid12532331>{{cite journal | vauthors = Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ | title = The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein | journal = J. Cell. Biochem. | volume = 88 | issue = 3 | pages = 557–68 | date = Feb 2003 | pmid = 12532331 | doi = 10.1002/jcb.10318 }}</ref> [[Mdm2]]<ref name=pmid12483531>{{cite journal | vauthors = Kadakia M, Brown TL, McGorry MM, Berberich SJ | title = MdmX inhibits Smad transactivation | journal = Oncogene | volume = 21 | issue = 57 | pages = 8776–85 | date = Dec 2002 | pmid = 12483531 | doi = 10.1038/sj.onc.1205993 }}</ref><ref name=pmid10218570>{{cite journal | vauthors = Tanimura S, Ohtsuka S, Mitsui K, Shirouzu K, Yoshimura A, Ohtsubo M | title = MDM2 interacts with MDMX through their RING finger domains | journal = FEBS Lett. | volume = 447 | issue = 1 | pages = 5–9 | date = Mar 1999 | pmid = 10218570 | doi = 10.1016/S0014-5793(99)00254-9 }}</ref><ref name=pmid12393902>{{cite journal | vauthors = Badciong JC, Haas AL | title = MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination | journal = J. Biol. Chem. | volume = 277 | issue = 51 | pages = 49668–75 | date = Dec 2002 | pmid = 12393902 | doi = 10.1074/jbc.M208593200 }}</ref><ref name=pmid18219319>{{cite journal | vauthors = Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL | title = Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans | journal = Cell Death Differ. | volume = 15 | issue = 5 | pages = 841–8 | date = May 2008 | pmid = 18219319 | doi = 10.1038/sj.cdd.4402309 }}</ref> and [[P53]].<ref name=pmid9226370 /><ref name=pmid12393902/>
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG | title = ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. | journal = Cell Cycle | volume = 4 | issue = 9 | pages = 1166–70 | year = 2006 | pmid = 16082221 | doi = 10.4161/cc.4.9.1981 }}
| citations =
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG |title=ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1166-70 |year= 2006 |pmid= 16082221 |doi= }}
* {{cite journal | vauthors = Shvarts A, Steegenga WT, Riteco N, van Laar T, Dekker P, Bazuine M, van Ham RC, van der Houven van Oordt W, Hateboer G, van der Eb AJ, Jochemsen AG | title = MDMX: a novel p53-binding protein with some functional properties of MDM2 | journal = EMBO J. | volume = 15 | issue = 19 | pages = 5349–57 | year = 1996 | pmid = 8895579 | pmc = 452278 | doi =  }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Shvarts A, Steegenga WT, Riteco N, ''et al.'' |title=MDMX: a novel p53-binding protein with some functional properties of MDM2. |journal=EMBO J. |volume=15 |issue= 19 |pages= 5349-57 |year= 1996 |pmid= 8895579 |doi=  }}
* {{cite journal | vauthors = Tanimura S, Ohtsuka S, Mitsui K, Shirouzu K, Yoshimura A, Ohtsubo M | title = MDM2 interacts with MDMX through their RING finger domains | journal = FEBS Lett. | volume = 447 | issue = 1 | pages = 5–9 | year = 1999 | pmid = 10218570 | doi = 10.1016/S0014-5793(99)00254-9 }}
*{{cite journal | author=Shvarts A, Bazuine M, Dekker P, ''et al.'' |title=Isolation and identification of the human homolog of a new p53-binding protein, Mdmx. |journal=Genomics |volume=43 |issue= 1 |pages= 34-42 |year= 1997 |pmid= 9226370 |doi= 10.1006/geno.1997.4775 }}
* {{cite journal | vauthors = Ongkeko WM, Wang XQ, Siu WY, Lau AW, Yamashita K, Harris AL, Cox LS, Poon RY | title = MDM2 and MDMX bind and stabilize the p53-related protein p73 | journal = Curr. Biol. | volume = 9 | issue = 15 | pages = 829–32 | year = 1999 | pmid = 10469568 | doi = 10.1016/S0960-9822(99)80367-4 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Sharp DA, Kratowicz SA, Sank MJ, George DL | title = Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein | journal = J. Biol. Chem. | volume = 274 | issue = 53 | pages = 38189–96 | year = 2000 | pmid = 10608892 | doi = 10.1074/jbc.274.53.38189 }}
*{{cite journal | author=Tanimura S, Ohtsuka S, Mitsui K, ''et al.'' |title=MDM2 interacts with MDMX through their RING finger domains. |journal=FEBS Lett. |volume=447 |issue= 1 |pages= 5-9 |year= 1999 |pmid= 10218570 |doi= }}
* {{cite journal | vauthors = Jackson MW, Lindstrom MS, Berberich SJ | title = MdmX binding to ARF affects Mdm2 protein stability and p53 transactivation | journal = J. Biol. Chem. | volume = 276 | issue = 27 | pages = 25336–41 | year = 2001 | pmid = 11297540 | doi = 10.1074/jbc.M010685200 }}
*{{cite journal | author=Ongkeko WM, Wang XQ, Siu WY, ''et al.'' |title=MDM2 and MDMX bind and stabilize the p53-related protein p73. |journal=Curr. Biol. |volume=9 |issue= 15 |pages= 829-32 |year= 1999 |pmid= 10469568 |doi= }}
* {{cite journal | vauthors = Parant J, Chavez-Reyes A, Little NA, Yan W, Reinke V, Jochemsen AG, Lozano G | title = Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53 | journal = Nat. Genet. | volume = 29 | issue = 1 | pages = 92–5 | year = 2001 | pmid = 11528400 | doi = 10.1038/ng714 }}
*{{cite journal | author=Sharp DA, Kratowicz SA, Sank MJ, George DL |title=Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 38189-96 |year= 2000 |pmid= 10608892 |doi= }}
* {{cite journal | vauthors = Gentiletti F, Mancini F, D'Angelo M, Sacchi A, Pontecorvi A, Jochemsen AG, Moretti F | title = MDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblasts | journal = Oncogene | volume = 21 | issue = 6 | pages = 867–77 | year = 2002 | pmid = 11840332 | doi = 10.1038/sj.onc.1205137 }}
*{{cite journal | author=Jackson MW, Lindstrom MS, Berberich SJ |title=MdmX binding to ARF affects Mdm2 protein stability and p53 transactivation. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25336-41 |year= 2001 |pmid= 11297540 |doi= 10.1074/jbc.M010685200 }}
* {{cite journal | vauthors = Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ | title = Cluster analysis of an extensive human breast cancer cell line protein expression map database | journal = Proteomics | volume = 2 | issue = 2 | pages = 212–23 | year = 2002 | pmid = 11840567 | doi = 10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H }}
*{{cite journal | author=Parant J, Chavez-Reyes A, Little NA, ''et al.'' |title=Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. |journal=Nat. Genet. |volume=29 |issue= 1 |pages= 92-5 |year= 2001 |pmid= 11528400 |doi= 10.1038/ng714 }}
* {{cite journal | vauthors = Gu J, Kawai H, Nie L, Kitao H, Wiederschain D, Jochemsen AG, Parant J, Lozano G, Yuan ZM | title = Mutual dependence of MDM2 and MDMX in their functional inactivation of p53 | journal = J. Biol. Chem. | volume = 277 | issue = 22 | pages = 19251–4 | year = 2002 | pmid = 11953423 | doi = 10.1074/jbc.C200150200 }}
*{{cite journal | author=Gentiletti F, Mancini F, D'Angelo M, ''et al.'' |title=MDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblasts. |journal=Oncogene |volume=21 |issue= 6 |pages= 867-77 |year= 2002 |pmid= 11840332 |doi= 10.1038/sj.onc.1205137 }}
* {{cite journal | vauthors = Migliorini D, Lazzerini Denchi E, Danovi D, Jochemsen A, Capillo M, Gobbi A, Helin K, Pelicci PG, Marine JC | title = Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development | journal = Mol. Cell. Biol. | volume = 22 | issue = 15 | pages = 5527–38 | year = 2002 | pmid = 12101245 | pmc = 133932 | doi = 10.1128/MCB.22.15.5527-5538.2002 }}
*{{cite journal | author=Harris RA, Yang A, Stein RC, ''et al.'' |title=Cluster analysis of an extensive human breast cancer cell line protein expression map database. |journal=Proteomics |volume=2 |issue= 2 |pages= 212-23 |year= 2002 |pmid= 11840567 |doi= }}
* {{cite journal | vauthors = Wistow G, Bernstein SL, Wyatt MK, Fariss RN, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K | title = Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants | journal = Mol. Vis. | volume = 8 | issue = | pages = 205–20 | year = 2002 | pmid = 12107410 | doi =  }}
*{{cite journal | author=Gu J, Kawai H, Nie L, ''et al.'' |title=Mutual dependence of MDM2 and MDMX in their functional inactivation of p53. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19251-4 |year= 2002 |pmid= 11953423 |doi= 10.1074/jbc.C200150200 }}
* {{cite journal | vauthors = Sabbatini P, McCormick F | title = MDMX inhibits the p300/CBP-mediated acetylation of p53 | journal = DNA Cell Biol. | volume = 21 | issue = 7 | pages = 519–25 | year = 2002 | pmid = 12162806 | doi = 10.1089/104454902320219077 }}
*{{cite journal | author=Migliorini D, Lazzerini Denchi E, Danovi D, ''et al.'' |title=Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development. |journal=Mol. Cell. Biol. |volume=22 |issue= 15 |pages= 5527-38 |year= 2002 |pmid= 12101245 |doi=  }}
* {{cite journal | vauthors = Li C, Chen L, Chen J | title = DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms | journal = Mol. Cell. Biol. | volume = 22 | issue = 21 | pages = 7562–71 | year = 2002 | pmid = 12370303 | pmc = 135668 | doi = 10.1128/MCB.22.21.7562-7571.2002 }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue= |pages= 205-20 |year= 2002 |pmid= 12107410 |doi= }}
* {{cite journal | vauthors = Badciong JC, Haas AL | title = MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination | journal = J. Biol. Chem. | volume = 277 | issue = 51 | pages = 49668–75 | year = 2003 | pmid = 12393902 | doi = 10.1074/jbc.M208593200 }}
*{{cite journal | author=Sabbatini P, McCormick F |title=MDMX inhibits the p300/CBP-mediated acetylation of p53. |journal=DNA Cell Biol. |volume=21 |issue= 7 |pages= 519-25 |year= 2002 |pmid= 12162806 |doi= 10.1089/104454902320219077 }}
* {{cite journal | vauthors = Kadakia M, Brown TL, McGorry MM, Berberich SJ | title = MdmX inhibits Smad transactivation | journal = Oncogene | volume = 21 | issue = 57 | pages = 8776–85 | year = 2003 | pmid = 12483531 | doi = 10.1038/sj.onc.1205993 }}
*{{cite journal | author=Li C, Chen L, Chen J |title=DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms. |journal=Mol. Cell. Biol. |volume=22 |issue= 21 |pages= 7562-71 |year= 2002 |pmid= 12370303 |doi=  }}
*{{cite journal  | author=Badciong JC, Haas AL |title=MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49668-75 |year= 2003 |pmid= 12393902 |doi= 10.1074/jbc.M208593200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kadakia M, Brown TL, McGorry MM, Berberich SJ |title=MdmX inhibits Smad transactivation. |journal=Oncogene |volume=21 |issue= 57 |pages= 8776-85 |year= 2003 |pmid= 12483531 |doi= 10.1038/sj.onc.1205993 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=4194}}


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Latest revision as of 06:18, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.[1][2]

Function

The human MDM4 gene, which plays a role in apoptosis, encodes a 490-amino acid protein containing a RING finger domain and a putative nuclear localization signal. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the C-terminal region of the protein. The mRNA is expressed at a high level in thymus and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the N-terminal region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2[2]

Interactions

MDM4 has been shown to interact with E2F1,[3] Mdm2[4][5][6][7] and P53.[1][6]

References

  1. ↑ 1.0 1.1 Shvarts A, Bazuine M, Dekker P, Ramos YF, Steegenga WT, Merckx G, van Ham RC, van der Houven van Oordt W, van der Eb AJ, Jochemsen AG (Sep 1997). "Isolation and identification of the human homolog of a new p53-binding protein, Mdmx". Genomics. 43 (1): 34–42. doi:10.1006/geno.1997.4775. PMID 9226370.
  2. ↑ 2.0 2.1 "Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)".
  3. ↑ Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ (Feb 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. doi:10.1002/jcb.10318. PMID 12532331.
  4. ↑ Kadakia M, Brown TL, McGorry MM, Berberich SJ (Dec 2002). "MdmX inhibits Smad transactivation". Oncogene. 21 (57): 8776–85. doi:10.1038/sj.onc.1205993. PMID 12483531.
  5. ↑ Tanimura S, Ohtsuka S, Mitsui K, Shirouzu K, Yoshimura A, Ohtsubo M (Mar 1999). "MDM2 interacts with MDMX through their RING finger domains". FEBS Lett. 447 (1): 5–9. doi:10.1016/S0014-5793(99)00254-9. PMID 10218570.
  6. ↑ 6.0 6.1 Badciong JC, Haas AL (Dec 2002). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. 277 (51): 49668–75. doi:10.1074/jbc.M208593200. PMID 12393902.
  7. ↑ Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL (May 2008). "Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans". Cell Death Differ. 15 (5): 841–8. doi:10.1038/sj.cdd.4402309. PMID 18219319.

Further reading


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