UniProt: A0A8D2ILV5

Database: UniProt
Entry: A0A8D2ILV5_UROPR

LinkDB:  A0A8D2ILV5_UROPR 
Original site:  A0A8D2ILV5_UROPR

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Ontology (17)   
   GO (17)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (4)   
All databases (37)   

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ID   A0A8D2ILV5_UROPR        Unreviewed;       437 AA.
AC   A0A8D2ILV5;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|ARBA:ARBA00018786};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=Double minute 2 protein {ECO:0000256|ARBA:ARBA00032811};
DE   AltName: Full=Oncoprotein Mdm2 {ECO:0000256|ARBA:ARBA00083112};
DE   AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000256|ARBA:ARBA00032614};
DE   AltName: Full=p53-binding protein Mdm2 {ECO:0000256|ARBA:ARBA00030148};
GN   Name=MDM2 {ECO:0000313|Ensembl:ENSUPAP00010029679.1};
OS   Urocitellus parryii (Arctic ground squirrel) (Spermophilus parryii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Urocitellus.
OX   NCBI_TaxID=9999 {ECO:0000313|Ensembl:ENSUPAP00010029679.1, ECO:0000313|Proteomes:UP000694417};
RN   [1] {ECO:0000313|Ensembl:ENSUPAP00010029679.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSUPAP00010029679.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus,
CC       nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC   -!- SIMILARITY: Belongs to the MDM2/MDM4 family.
CC       {ECO:0000256|ARBA:ARBA00005803}.
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DR   AlphaFoldDB; A0A8D2ILV5; -.
DR   Ensembl; ENSUPAT00010033756.1; ENSUPAP00010029679.1; ENSUPAG00010023340.1.
DR   GeneTree; ENSGT00530000063539; -.
DR   Proteomes; UP000694417; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0002039; F:p53 binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0003283; P:atrial septum development; IEA:UniProtKB-ARBA.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:UniProtKB-ARBA.
DR   GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:UniProtKB-ARBA.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:UniProtKB-ARBA.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR   GO; GO:0002027; P:regulation of heart rate; IEA:UniProtKB-ARBA.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd17672; MDM2; 1.
DR   CDD; cd16783; mRING-HC-C2H2C4_MDM2; 1.
DR   FunFam; 1.10.245.10:FF:000002; E3 ubiquitin-protein ligase Mdm2; 1.
DR   FunFam; 2.30.30.380:FF:000005; E3 ubiquitin-protein ligase Mdm2; 1.
DR   FunFam; 3.30.40.10:FF:000076; E3 ubiquitin-protein ligase Mdm2; 1.
DR   Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR028340; Mdm2.
DR   InterPro; IPR044080; MDM2_mRING-HC-C2H2C4.
DR   InterPro; IPR016495; p53_neg-reg_MDM_2/4.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46858:SF13; E3 UBIQUITIN-PROTEIN LIGASE MDM2; 1.
DR   PANTHER; PTHR46858; OS05G0521000 PROTEIN; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   Pfam; PF00641; Zn_ribbon_RanBP; 1.
DR   PIRSF; PIRSF500700; MDM2; 1.
DR   PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF47592; SWIB/MDM2 domain; 2.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694417};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          29..112
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   DOMAIN          246..275
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          384..425
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          159..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  49499 MW;  0AFE0D164D1B83F8 CRC64;
     LVPMCNTNMS VSTDGAVSTS QIPASEQETL VRPKPLLLKL LKSVGAQKDT YTMKEVIFYL
     GQYIMTKRLY DEKQQHIVYC SNDLLGDLFG VPSFSVKEHR KIYTMIYKNL VVVNQQEDNS
     DELSGERRKR HKSDSISLSF DESLALCVIR EICCERSSSS ESIETPSNPD IEDGVSEHSS
     DWLDQDSVSD QFSVEFEVES LDSEDYSLSE EGQELSDEDD EVYRVTVYQA GESDTDSFEE
     DPEISLADYW KCTSCNEMNP PLPPHCNRCW TLRENWLPED KGKDKGEISE KAKLESSKQA
     EEGLDVPDGK KITANDSKES CFEENDKITQ ASQSQESEDY SQPSTSNSII YSSQEDVKEF
     EKEETQDKEE SMESSFPLNA IEPCVICQGR PKNGCIVHGK TGHLMSCFTC AKKLKKRNKP
     CPVCRQPIQM IVLTYFN
//

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