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E3 ubiquitin-protein ligase Mdm2 isoform MDM2 (MDM2 proto-oncogene)

 H9FUJ1_MACMU            Unreviewed;       497 AA.
H9FUJ1; F7AKS9;
16-MAY-2012, integrated into UniProtKB/TrEMBL.
16-MAY-2012, sequence version 1.
25-APR-2018, entry version 51.
RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|PIRNR:PIRNR006748};
EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR006748};
Name=MDM2 {ECO:0000313|EMBL:AFE78300.1,
ECO:0000313|Ensembl:ENSMMUP00000018645};
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE78300.1};
[1] {ECO:0000313|Ensembl:ENSMMUP00000018645, ECO:0000313|Proteomes:UP000006718}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000018645,
ECO:0000313|Proteomes:UP000006718};
PubMed=17431167; DOI=10.1126/science.1139247;
Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
Zwieg A.S.;
"Evolutionary and biomedical insights from the rhesus macaque
genome.";
Science 316:222-234(2007).
[2] {ECO:0000313|Ensembl:ENSMMUP00000018645}
IDENTIFICATION.
STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000018645};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
[3] {ECO:0000313|EMBL:AFE78300.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Caudate {ECO:0000313|EMBL:AFE78300.1}, and
Thymus {ECO:0000313|EMBL:AFH32437.1};
PubMed=25319552; DOI=10.1186/1745-6150-9-20;
Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
"A new rhesus macaque assembly and annotation for next-generation
sequencing analyses.";
Biol. Direct 9:20-20(2014).
-!- 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. {ECO:0000256|PIRNR:PIRNR006748}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000256|PIRNR:PIRNR006748}. Cytoplasm
{ECO:0000256|PIRNR:PIRNR006748}. Nucleus, nucleolus
{ECO:0000256|PIRNR:PIRNR006748}.
-!- SIMILARITY: Belongs to the MDM2/MDM4 family.
{ECO:0000256|PIRNR:PIRNR006748}.
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EMBL; JSUE03007143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; JSUE03007144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; JU334547; AFE78300.1; -; mRNA.
EMBL; JU475633; AFH32437.1; -; mRNA.
RefSeq; NP_001253331.1; NM_001266402.1.
UniGene; Mmu.31140; -.
Ensembl; ENSMMUT00000019919; ENSMMUP00000018645; ENSMMUG00000014193.
GeneID; 718284; -.
KEGG; mcc:718284; -.
CTD; 4193; -.
eggNOG; ENOG410IGXG; Eukaryota.
eggNOG; ENOG41125MP; LUCA.
GeneTree; ENSGT00530000063539; -.
KO; K06643; -.
Proteomes; UP000006718; Chromosome 11.
Bgee; ENSMMUG00000014193; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0008097; F:5S rRNA binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0061663; F:NEDD8 ligase activity; IEA:Ensembl.
GO; GO:0002039; F:p53 binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0003283; P:atrial septum development; IEA:Ensembl.
GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0060411; P:cardiac septum morphogenesis; IEA:Ensembl.
GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0018205; P:peptidyl-lysine modification; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
Gene3D; 1.10.245.10; -; 1.
Gene3D; 3.30.40.10; -; 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.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR13844:SF15; PTHR13844:SF15; 1.
Pfam; PF02201; SWIB; 1.
Pfam; PF00641; zf-RanBP; 1.
PIRSF; PIRSF500700; MDM2; 1.
PIRSF; PIRSF006748; p53_MDM_2/4; 1.
SUPFAM; SSF47592; SSF47592; 2.
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;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006718};
Cytoplasm {ECO:0000256|PIRNR:PIRNR006748};
Ligase {ECO:0000313|EMBL:AFE78300.1};
Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00322,
ECO:0000256|SAAS:SAAS00581830};
Nucleus {ECO:0000256|PIRNR:PIRNR006748};
Reference proteome {ECO:0000313|Proteomes:UP000006718};
Transferase {ECO:0000256|PIRNR:PIRNR006748};
Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR006748};
Zinc {ECO:0000256|PROSITE-ProRule:PRU00322,
ECO:0000256|SAAS:SAAS00581830};
Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322,
ECO:0000256|SAAS:SAAS00581830}.
DOMAIN 305 334 RanBP2-type.
{ECO:0000259|PROSITE:PS50199}.
DOMAIN 444 485 RING-type. {ECO:0000259|PROSITE:PS50089}.
COILED 171 191 {ECO:0000256|SAM:Coils}.
SEQUENCE 497 AA; 56005 MW; 175E7044DA4974CE CRC64;
MVRSRQMCNT NMSVPTDGAV TTSQIPASEQ ETLVRPKPLL LKLLKSVGAQ KDTYTMKEVL
FYLGQYIMTK RLYDEKQQHI VYCSNDLLGD LFGVPSFSVK EHRKIYTMIY RNLVVVNQQE
SSDSGTSVSE NRCHLEGGSD QKDLVQELQE EKPSSSHLVS RPSTSSRRRA ISETEENSDE
LSGERQRKRH KSDSISLSFD ESLALCVIRE ICCERSSSSE STGTPSNPDL DAGVSEHSGD
WLDQDSVSDQ FSVEFEVESL DSEDYSLSEE AQELSDEDDE VYRVTVYQAG ESDTDSFEED
PEISLADYWK CTSCNEMNPP LPSHCNRCWA LRENWLPEDK GKDKGEISEK AKLENSTQAE
EGFDVPDCKK TIVNDSKESC VEENDDKITQ ASQSQESEDY SQPSTSSSII YSSQEDVKEF
EREETQDKEE SVESSLPLNA IEPCVICQGR PKNGCIVHGK TGHLMACFTC AKKLKKRNKP
CPVCRQPIQM IVLTYFP


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