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E3 ubiquitin-protein ligase Mdm2 (EC 2 3 2 27) (Double minute 2 protein) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)

 MDM2_DANRE              Reviewed;         445 AA.
O42354;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=E3 ubiquitin-protein ligase Mdm2;
EC=2.3.2.27;
AltName: Full=Double minute 2 protein;
AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000305};
AltName: Full=p53-binding protein Mdm2;
Name=mdm2;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Neel H., Piette J.;
"Partial cDNA nucleotide sequence of the zebrafish homolog of Mdm2.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Lin Y.T., Chou C.M., Leu J.H., Tsai S.C., Huang C.J.;
"A gene encoding MDM2-like protein from zebrafish.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of p53/TP53, leading to its degration by the proteasome.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
-!- SIMILARITY: Belongs to the MDM2/MDM4 family. {ECO:0000305}.
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EMBL; AF010255; AAB64176.1; -; mRNA.
EMBL; AF356346; AAM00198.1; -; mRNA.
UniGene; Dr.75764; -.
ProteinModelPortal; O42354; -.
SMR; O42354; -.
PRIDE; O42354; -.
ZFIN; ZDB-GENE-990415-153; mdm2.
HOGENOM; HOG000293341; -.
HOVERGEN; HBG013472; -.
InParanoid; O42354; -.
PRO; PR:O42354; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ZFIN.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IMP:ZFIN.
GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:ZFIN.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IGI:ZFIN.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0035775; P:pronephric glomerulus morphogenesis; IMP:ZFIN.
GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
GO; GO:0031647; P:regulation of protein stability; IGI:ZFIN.
GO; GO:0010165; P:response to X-ray; IGI:ZFIN.
Gene3D; 1.10.245.10; -; 1.
InterPro; IPR028340; Mdm2.
InterPro; IPR015459; MDM2_E3_ligase.
InterPro; IPR016495; p53_neg-reg_MDM_2/4.
InterPro; IPR036885; SWIB_MDM2_dom_sf.
InterPro; IPR003121; SWIB_MDM2_domain.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
InterPro; IPR001841; Znf_RING.
PANTHER; PTHR13844:SF15; PTHR13844:SF15; 1.
Pfam; PF02201; SWIB; 1.
PIRSF; PIRSF500700; MDM2; 1.
PIRSF; PIRSF006748; p53_MDM_2/4; 1.
SUPFAM; SSF47592; SSF47592; 1.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Metal-binding; Nucleus;
Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 445 E3 ubiquitin-protein ligase Mdm2.
/FTId=PRO_0000157335.
DOMAIN 20 100 SWIB.
ZN_FING 274 303 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 392 433 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 190 279 ARF-binding.
REGION 222 306 Region II.
MOTIF 160 166 Nuclear localization signal.
{ECO:0000255}.
MOTIF 171 183 Nuclear export signal.
MOTIF 420 427 Nucleolar localization signal.
{ECO:0000255}.
COMPBIAS 141 145 Poly-Arg.
COMPBIAS 210 276 Asp/Glu-rich (acidic).
SEQUENCE 445 AA; 49950 MW; 6FA8175A8A8E6261 CRC64;
MATESCLSSS QISKVDNEKL VRPKVQLKSL LEDAGADKDV FTMKEVMFYL GKYIMSKELY
DKQQQHIVHC GEDPLGAVLG VKSFSVKEPR ALFALINRNL VTVKNPESQS TFSEPRSQSE
PDRGPGDTDS DSRSSTSQQQ RRRRRSSDPE SSSAEDESRE RRKRHKSDSF SLTFDDSLSW
CVIGGLHRER GNSESSDANS NSDVGISRSE GSEESEDSDS DSDNFSVEFE VESINSDAYS
ENDVDSVPGE NEIYEVTIFA EDEDSFDEDT EITEADYWKC PKCDQFNPPL PRHCKSCWTV
RADWLPETHS NWENLSRNTR TNPEDTSVTT TPNTTFEKKL SKPSSPLPET DDGVDVPTPP
LLRRGSSQEE TPELERFNSL EACLPATCLE PCVICQSRPK NGCIVHGRTG HLMACYTCAK
KLKNRNKLCP VCREPIQSVV LTYMS


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