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MDM2 proto-oncogene

 A0A0G2JVC1_RAT          Unreviewed;       483 AA.
A0A0G2JVC1;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
23-MAY-2018, entry version 28.
RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|PIRNR:PIRNR006748};
EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR006748};
Name=Mdm2 {ECO:0000313|Ensembl:ENSRNOP00000069425,
ECO:0000313|RGD:1305332};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069425, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000069425, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069425,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[3] {ECO:0000313|Ensembl:ENSRNOP00000069425}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069425};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
-!- 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; AABR07057209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_006241444.1; XM_006241382.1.
RefSeq; XP_006241445.1; XM_006241383.2.
UniGene; Rn.91829; -.
Ensembl; ENSRNOT00000086116; ENSRNOP00000069425; ENSRNOG00000006304.
GeneID; 314856; -.
CTD; 4193; -.
RGD; 1305332; Mdm2.
GeneTree; ENSGT00530000063539; -.
OMA; GELPCKL; -.
Reactome; R-RNO-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2559585; Oncogene Induced Senescence.
Reactome; R-RNO-399719; Trafficking of AMPA receptors.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-RNO-69541; Stabilization of p53.
Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000006304; -.
ExpressionAtlas; A0A0G2JVC1; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:RGD.
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:Ensembl.
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:0004842; F:ubiquitin-protein transferase activity; IMP:RGD.
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:0071312; P:cellular response to alkaloid; IEP:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:0071494; P:cellular response to UV-C; IEP:RGD.
GO; GO:0071301; P:cellular response to vitamin B1; IEP:RGD.
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:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0010955; P:negative regulation of protein processing; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
GO; GO:0018205; P:peptidyl-lysine modification; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:RGD.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IMP:RGD.
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:0016567; P:protein ubiquitination; IMP:RGD.
GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045472; P:response to ether; IEP:RGD.
GO; GO:1904404; P:response to formaldehyde; IEP:RGD.
GO; GO:0010039; P:response to iron ion; IEP:RGD.
GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:1990785; P:response to water-immersion restraint stress; IDA:RGD.
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.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Cytoplasm {ECO:0000256|PIRNR:PIRNR006748};
Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00322,
ECO:0000256|SAAS:SAAS00581830};
Nucleus {ECO:0000256|PIRNR:PIRNR006748};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
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 292 321 RanBP2-type.
{ECO:0000259|PROSITE:PS50199}.
DOMAIN 430 471 RING-type. {ECO:0000259|PROSITE:PS50089}.
SEQUENCE 483 AA; 53902 MW; 3B5FDA7044F42BA8 CRC64;
MCNTNMSVST EGAAGTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDIYTM KEIIFYIGQY
IMTKRLYDEK QQHIVYCSND LLGDVFGVPS FSVKEHRKIY AMIYRNLVVV SQQDSGTSPS
ESRCQPEGGS DLKDPVQASQ EEKPSSSDVV SRPSTSSRRR AISETEENTD ELPGERQRKR
HRALSFDESL GLCVLREICC ERSSSSEATD TPSHQDLDDG VSDHSADCLD QDSVSDQFSV
EFEVESLDSE DYSLSDEGHE LSDEDDEVYR VTVYQAGESD ADSFEGDPEI SLADYWKCTS
CNEMNPPLPS HCNRCWTLRE NWLPDDKGKD KVEISEKAKL ESSDQAEEGL DVPDGKKVTE
DDAKESSAED SEEKVAQMLL SQESDDYSQP STSSSIVYSS QESGKELKED TQDKEESMES
SFSLNAIEPC VICQGRPKNG CIVHGKTGHL MSCFTCAKKL KKRNKPCPVC RQPIQMIVLT
YFN


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