Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P56273 (MDM2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase Mdm2

EC=6.3.2.-
Alternative name(s):
Double minute 2 protein
Short name=Xdm2
p53-binding protein Mdm2
Gene names
Name:mdm2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degration by the proteasome By similarity.

Subcellular location

Nucleusnucleoplasm By similarity. Cytoplasm By similarity. Nucleusnucleolus By similarity.

Developmental stage

Expression increases from oocyte stage I/II to reach its maximum in oocyte stage v/vi in unfertilized eggs, and then progressively decreases to become undetectable at the gastrula stage.

Sequence similarities

Belongs to the MDM2/MDM4 family.

Contains 1 RanBP2-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 SWIB domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473E3 ubiquitin-protein ligase Mdm2
PRO_0000157334

Regions

Domain23 – 10381SWIB
Zinc finger290 – 31930RanBP2-type
Zinc finger420 – 46142RING-type
Region230 – 32293Region II
Motif173 – 1797Nuclear localization signal Potential
Compositional bias216 – 29277Asp/Glu-rich (acidic)

Secondary structure

................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56273 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 7DA668DE8B3BEE01

FASTA47353,464
        10         20         30         40         50         60 
MNLTSTTNCL ENNHISTSDQ EKLVQPTPLL LSLLKSAGAQ KETFTMKEVI YHLGQYIMAK 

        70         80         90        100        110        120 
QLYDEKQQHI VHCSNDPLGE LFGVQEFSVK EPRRLYAMIS RNLVSANVKE SSEDIFGNVC 

       130        140        150        160        170        180 
CFPDKQSSQK EKLQELPDKL IAPASDSKPC NLSQRKSSNE TEEISSVDHP AEQQRKRHKS 

       190        200        210        220        230        240 
DSFSLTFDES LSWWVISGLR CDRNSSESTD SSSNSDPERH STNDNSEHDS DQFSVEFEVE 

       250        260        270        280        290        300 
SVCSDDYSPS GDEHGVSEEE EINDEVYQVT IYETEESETD SFDVDTEISE ADYWKCPECG 

       310        320        330        340        350        360 
EVNPPLPSYC PRCWTVRKDW LPEQRRKEPP PSKRKLLEIE EDEGFDVPDC KKSKLTSSQD 

       370        380        390        400        410        420 
TNVDKKEAEN IQNSESQETE DCSQPSTSGS IASCSQEVTK EDSSKESMES SLPLTSIDPC 

       430        440        450        460        470 
VICQTRPKNG CIVHGRTGHL MACYTCAKKL KKRNKPCPVC REPIQMIVLT YFS 

« Hide

References

[1]"Conservation of structural domains and biochemical activities of the MDM2 protein from Xenopus laevis."
Marechal V., Elenbaas B., Taneyhill L., Piette J., Mechali M., Nicolas J.-C., Levine A.J., Moreau J.
Oncogene 14:1427-1433(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"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 (2.3 ANGSTROMS) OF 13-119 IN COMPLEX WITH P53.
+Additional computationally mapped references.

Cross-references

Sequence databases

UniGeneXl.80570.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TTVNMR-A13-119[»]
1YCQX-ray2.30A13-119[»]
4IPFX-ray1.70A21-105[»]
4J3EX-ray1.91A21-105[»]
4J74X-ray1.20A21-105[»]
4J7DX-ray1.25A21-105[»]
4J7EX-ray1.63A21-105[»]
4JRGX-ray1.90A/B21-105[»]
4JSCX-ray2.50A/B21-105[»]
ProteinModelPortalP56273.
SMRP56273. Positions 21-108, 281-325, 410-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP56273. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-6255114. mdm2.

Phylogenomic databases

HOVERGENHBG013472.

Family and domain databases

Gene3D1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR028340. 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]
PANTHERPTHR10360:SF9. PTHR10360:SF9. 1 hit.
PfamPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFPIRSF500700. MDM2. 1 hit.
PIRSF006748. p53_MDM_2/4. 1 hit.
SMARTSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMSSF47592. SSF47592. 2 hits.
PROSITEPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56273.

Entry information

Entry nameMDM2_XENLA
AccessionPrimary (citable) accession number: P56273
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references