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O15151

- MDM4_HUMAN

UniProt

O15151 - MDM4_HUMAN

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Protein
Protein Mdm4
Gene
MDM4, MDMX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri300 – 32930RanBP2-type
Add
BLAST
Zinc fingeri437 – 47842RING-type
Add
BLAST

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  2. G0 to G1 transition Source: UniProtKB
  3. cell proliferation Source: UniProtKB
  4. cellular response to hypoxia Source: UniProtKB
  5. negative regulation of apoptotic process Source: InterPro
  6. negative regulation of cell cycle arrest Source: InterPro
  7. negative regulation of cell proliferation Source: ProtInc
  8. negative regulation of protein catabolic process Source: UniProtKB
  9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. positive regulation of cell proliferation Source: Ensembl
  11. protein complex assembly Source: UniProtKB
  12. protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Mdm4
Alternative name(s):
Double minute 4 protein
Mdm2-like p53-binding protein
Protein Mdmx
p53-binding protein Mdm4
Gene namesi
Name:MDM4
Synonyms:MDMX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6974. MDM4.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi437 – 4371C → G: Fails to interact with MDM2. 1 Publication

Organism-specific databases

PharmGKBiPA30719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Protein Mdm4
PRO_0000157336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei342 – 3421Phosphoserine; by CHEK21 Publication
Modified residuei367 – 3671Phosphoserine; by CHEK1 and CHEK22 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent.2 Publications
Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15151.
PaxDbiO15151.
PRIDEiO15151.

PTM databases

PhosphoSiteiO15151.

Miscellaneous databases

PMAP-CutDBO15151.

Expressioni

Tissue specificityi

Expressed in all tissues tested with high levels in thymus.

Inductioni

Down-regulated by cisplatin (at protein level).1 Publication

Gene expression databases

ArrayExpressiO15151.
BgeeiO15151.
CleanExiHS_MDM4.
GenevestigatoriO15151.

Organism-specific databases

HPAiHPA018919.

Interactioni

Subunit structurei

Interacts with MDM2, TP53, TP73 and USP2. Found in a trimeric complex with UPB2, MDM2 and MDM4. Interacts (phosphorylated) with YWHAG; negatively regulates MDM4 activity toward TP53.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03255-23EBI-398437,EBI-6859460From a different organism.
Q3YBA86EBI-398437,EBI-7852331
BCL2P104154EBI-398437,EBI-77694
CSNK1A1P487292EBI-398437,EBI-1383726
MDM2Q009878EBI-398437,EBI-389668
MKRN3Q130642EBI-398437,EBI-2340269
RB1P064004EBI-398437,EBI-491274
TP53P0463713EBI-398437,EBI-366083
UBE2D2P628372EBI-398437,EBI-347677
USP7Q9300915EBI-398437,EBI-302474
YWHAEP622583EBI-398437,EBI-356498
YWHAGP619817EBI-398437,EBI-359832

Protein-protein interaction databases

BioGridi110359. 50 interactions.
DIPiDIP-24199N.
IntActiO15151. 29 interactions.
MINTiMINT-113852.
STRINGi9606.ENSP00000356150.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293
Helixi31 – 399
Helixi49 – 6214
Beta strandi70 – 756
Helixi80 – 856
Beta strandi88 – 914
Helixi96 – 10510
Beta strandi106 – 1094
Beta strandi307 – 3093
Turni321 – 3233
Helixi431 – 4344
Turni438 – 4403
Beta strandi441 – 4455
Beta strandi447 – 4515
Beta strandi454 – 4596
Helixi461 – 4699
Turni475 – 4773
Beta strandi483 – 4897

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CR8NMR-A300-339[»]
2VJEX-ray2.20B/D428-490[»]
2VJFX-ray2.30B/D428-490[»]
2VYRX-ray2.00A/B/C/D16-116[»]
3DABX-ray1.90A/C/E/G23-111[»]
3EQYX-ray1.63A/B24-108[»]
3FDOX-ray1.40A23-111[»]
3FE7X-ray1.35A14-111[»]
3FEAX-ray1.33A14-111[»]
3JZOX-ray1.80A23-111[»]
3JZPX-ray1.74A23-111[»]
3JZQX-ray1.80A/B23-111[»]
3LBJX-ray1.50E23-111[»]
3MQRX-ray1.80B395-404[»]
3U15X-ray1.80A/B/C/D14-111[»]
ProteinModelPortaliO15151.
SMRiO15151. Positions 26-108, 301-344, 429-490.

Miscellaneous databases

EvolutionaryTraceiO15151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10681SWIB
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni246 – 33287Region II
Add
BLAST
Regioni393 – 49098Necessary for interaction with UBP2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi442 – 4454Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi243 – 30866Asp/Glu-rich (acidic)
Add
BLAST

Domaini

Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.

Sequence similaritiesi

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG46328.
HOGENOMiHOG000293341.
HOVERGENiHBG013472.
InParanoidiO15151.
KOiK10127.
OMAiLKPCSLC.
OrthoDBiEOG7RRF7T.
PhylomeDBiO15151.
TreeFamiTF105306.

Family and domain databases

Gene3Di1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR015458. MDM4.
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:SF10. PTHR10360:SF10. 1 hit.
PfamiPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFiPIRSF500699. MDM4. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTiSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 1 hit.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O15151-1) [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

MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK    50
EVMHYLGQYI MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD 100
MLRKNLVTLA TATTDAAQTL ALAQDHSMDI PSQDQLKQSA EESSTSRKRT 150
TEDDIPTLPT SEHKCIHSRE DEDLIENLAQ DETSRLDLGF EEWDVAGLPW 200
WFLGNLRSNY TPRSNGSTDL QTNQDVGTAI VSDTTDDLWF LNESVSEQLG 250
VGIKVEAADT EQTSEEVGKV SDKKVIEVGK NDDLEDSKSL SDDTDVEVTS 300
EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP 350
EKENEGNDVP DCRRTISAPV VRPKDAYIKK ENSKLFDPCN SVEFLDLAHS 400
SESQETISSM GEQLDNLSEQ RTDTENMEDC QNLLKPCSLC EKRPRDGNII 450
HGRTGHLVTC FHCARRLKKA GASCPICKKE IQLVIKVFIA 490
Length:490
Mass (Da):54,864
Last modified:September 27, 2005 - v2
Checksum:i415E6FA5A0C69857
GO
Isoform 2 (identifier: O15151-2) [UniParc]FASTAAdd to Basket

Also known as: MDMX-S

The sequence of this isoform differs from the canonical sequence as follows:
     109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTARCNRILQSQKKN

Note: No experimental confirmation available.

Show »
Length:127
Mass (Da):14,185
Checksum:i59649D26B113EFB4
GO
Isoform 3 (identifier: O15151-3) [UniParc]FASTAAdd to Basket

Also known as: MDMX

The sequence of this isoform differs from the canonical sequence as follows:
     109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTDAAQTLALAQDHT

Note: No experimental confirmation available.

Show »
Length:127
Mass (Da):13,981
Checksum:i0A00E52B32331543
GO
Isoform HDMX211 (identifier: O15151-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-352: Missing.

Note: Cancer-specific isoform, may counteract MDM2/MDM4-mediated p53 degradation.

Show »
Length:164
Mass (Da):18,195
Checksum:i1C39025CBD527C11
GO
Isoform 5 (identifier: O15151-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     225-274: Missing.

Note: No experimental confirmation available.

Show »
Length:440
Mass (Da):49,541
Checksum:iBB377C938A8C3D1C
GO

Mass spectrometryi

Molecular mass is 54863.3 Da from positions 1 - 490. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751I → T.1 Publication
Corresponds to variant rs4252716 [ dbSNP | Ensembl ].
VAR_017106
Natural varianti406 – 4061T → I.1 Publication
Corresponds to variant rs4252741 [ dbSNP | Ensembl ].
VAR_017107

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 352326Missing in isoform HDMX211.
VSP_042563Add
BLAST
Alternative sequencei109 – 490382LATAT…KVFIA → SASNNTARCNRILQSQKKN in isoform 2.
VSP_035669Add
BLAST
Alternative sequencei109 – 490382LATAT…KVFIA → SASNNTDAAQTLALAQDHT in isoform 3.
VSP_035670Add
BLAST
Alternative sequencei225 – 27450Missing in isoform 5.
VSP_043145Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941D → N in AAB62928. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007111 mRNA. Translation: AAB62928.1.
AY923176 mRNA. Translation: AAY22054.1.
AK223228 mRNA. Translation: BAD96948.1.
AY207458 Genomic DNA. Translation: AAO13494.1.
AL512306 Genomic DNA. Translation: CAI14100.1.
BC067299 mRNA. Translation: AAH67299.1.
BC105106 mRNA. Translation: AAI05107.1.
CCDSiCCDS1447.1. [O15151-1]
CCDS55674.1. [O15151-5]
CCDS55675.1. [O15151-4]
RefSeqiNP_001191100.1. NM_001204171.1. [O15151-5]
NP_001191101.1. NM_001204172.1. [O15151-4]
NP_001265445.1. NM_001278516.1.
NP_001265446.1. NM_001278517.1.
NP_001265447.1. NM_001278518.1.
NP_001265448.1. NM_001278519.1.
NP_002384.2. NM_002393.4. [O15151-1]
UniGeneiHs.497492.

Genome annotation databases

EnsembliENST00000367182; ENSP00000356150; ENSG00000198625. [O15151-1]
ENST00000367183; ENSP00000356151; ENSG00000198625. [O15151-4]
ENST00000454264; ENSP00000396840; ENSG00000198625. [O15151-5]
GeneIDi4194.
KEGGihsa:4194.
UCSCiuc001hay.2. human. [O15151-5]
uc001hba.3. human. [O15151-1]
uc021phx.1. human. [O15151-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007111 mRNA. Translation: AAB62928.1 .
AY923176 mRNA. Translation: AAY22054.1 .
AK223228 mRNA. Translation: BAD96948.1 .
AY207458 Genomic DNA. Translation: AAO13494.1 .
AL512306 Genomic DNA. Translation: CAI14100.1 .
BC067299 mRNA. Translation: AAH67299.1 .
BC105106 mRNA. Translation: AAI05107.1 .
CCDSi CCDS1447.1. [O15151-1 ]
CCDS55674.1. [O15151-5 ]
CCDS55675.1. [O15151-4 ]
RefSeqi NP_001191100.1. NM_001204171.1. [O15151-5 ]
NP_001191101.1. NM_001204172.1. [O15151-4 ]
NP_001265445.1. NM_001278516.1.
NP_001265446.1. NM_001278517.1.
NP_001265447.1. NM_001278518.1.
NP_001265448.1. NM_001278519.1.
NP_002384.2. NM_002393.4. [O15151-1 ]
UniGenei Hs.497492.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CR8 NMR - A 300-339 [» ]
2VJE X-ray 2.20 B/D 428-490 [» ]
2VJF X-ray 2.30 B/D 428-490 [» ]
2VYR X-ray 2.00 A/B/C/D 16-116 [» ]
3DAB X-ray 1.90 A/C/E/G 23-111 [» ]
3EQY X-ray 1.63 A/B 24-108 [» ]
3FDO X-ray 1.40 A 23-111 [» ]
3FE7 X-ray 1.35 A 14-111 [» ]
3FEA X-ray 1.33 A 14-111 [» ]
3JZO X-ray 1.80 A 23-111 [» ]
3JZP X-ray 1.74 A 23-111 [» ]
3JZQ X-ray 1.80 A/B 23-111 [» ]
3LBJ X-ray 1.50 E 23-111 [» ]
3MQR X-ray 1.80 B 395-404 [» ]
3U15 X-ray 1.80 A/B/C/D 14-111 [» ]
ProteinModelPortali O15151.
SMRi O15151. Positions 26-108, 301-344, 429-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110359. 50 interactions.
DIPi DIP-24199N.
IntActi O15151. 29 interactions.
MINTi MINT-113852.
STRINGi 9606.ENSP00000356150.

Chemistry

BindingDBi O15151.
ChEMBLi CHEMBL2221344.

PTM databases

PhosphoSitei O15151.

Proteomic databases

MaxQBi O15151.
PaxDbi O15151.
PRIDEi O15151.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367182 ; ENSP00000356150 ; ENSG00000198625 . [O15151-1 ]
ENST00000367183 ; ENSP00000356151 ; ENSG00000198625 . [O15151-4 ]
ENST00000454264 ; ENSP00000396840 ; ENSG00000198625 . [O15151-5 ]
GeneIDi 4194.
KEGGi hsa:4194.
UCSCi uc001hay.2. human. [O15151-5 ]
uc001hba.3. human. [O15151-1 ]
uc021phx.1. human. [O15151-4 ]

Organism-specific databases

CTDi 4194.
GeneCardsi GC01P204486.
HGNCi HGNC:6974. MDM4.
HPAi HPA018919.
MIMi 602704. gene.
neXtProti NX_O15151.
PharmGKBi PA30719.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46328.
HOGENOMi HOG000293341.
HOVERGENi HBG013472.
InParanoidi O15151.
KOi K10127.
OMAi LKPCSLC.
OrthoDBi EOG7RRF7T.
PhylomeDBi O15151.
TreeFami TF105306.

Miscellaneous databases

ChiTaRSi MDM4. human.
EvolutionaryTracei O15151.
GeneWikii MDM4.
GenomeRNAii 4194.
NextBioi 16538.
PMAP-CutDB O15151.
PROi O15151.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15151.
Bgeei O15151.
CleanExi HS_MDM4.
Genevestigatori O15151.

Family and domain databases

Gene3Di 1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR015458. MDM4.
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:SF10. PTHR10360:SF10. 1 hit.
Pfami PF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF500699. MDM4. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTi SM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47592. SSF47592. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon tumor.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HDMX211).
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Gastric mucosa.
  4. NIEHS SNPs program
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-175 AND ILE-406.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 5).
    Tissue: Brain and Testis.
  7. "Identification of a domain within MDMX-S that is responsible for its high affinity interaction with p53 and high-level expression in mammalian cells."
    Rallapalli R., Strachan G., Tuan R.S., Hall D.J.
    J. Cell. Biochem. 89:563-575(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
  8. "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-437.
  9. "ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage."
    Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J.
    EMBO J. 24:3411-3422(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-342 AND SER-367 BY CHEK2, UBIQUITINATION, INTERACTION WITH MDM2.
  10. "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-367 BY CHEK1, INTERACTION WITH YWHAG.
  11. "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 MDM2, INDUCTION, UBIQUITINATION, DEUBIQUITINATION BY USP2.
  12. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  13. "Solution structure of the ZF-RANBP domain of p53-binding protein MDM4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 300-340.

Entry informationi

Entry nameiMDM4_HUMAN
AccessioniPrimary (citable) accession number: O15151
Secondary accession number(s): Q2M2Y2
, Q32SL2, Q6GS18, Q8IV83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 27, 2005
Last modified: July 9, 2014
This is version 151 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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