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MDM2 proto-oncogene (Transformed mouse 3T3 cell double minute 2 homolog (Mouse) (Predicted), isoform CRA_b)

 D3ZVH5_RAT              Unreviewed;       458 AA.
D3ZVH5;
20-APR-2010, integrated into UniProtKB/TrEMBL.
20-APR-2010, sequence version 1.
12-SEP-2018, entry version 81.
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:ENSRNOP00000063449,
ECO:0000313|RGD:1305332};
Synonyms=Mdm2_predicted {ECO:0000313|EMBL:EDM16616.1};
ORFNames=rCG_48669 {ECO:0000313|EMBL:EDM16616.1};
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:ENSRNOP00000063449, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000063449, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063449,
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:0000313|EMBL:EDM16616.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM16616.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDM16616.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM16616.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000063449}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063449};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
[5] {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).
-!- 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.
EMBL; CH473960; EDM16616.1; -; Genomic_DNA.
EMBL; CH473960; EDM16617.1; -; Genomic_DNA.
RefSeq; NP_001101569.1; NM_001108099.1.
UniGene; Rn.91829; -.
STRING; 10116.ENSRNOP00000063449; -.
Ensembl; ENSRNOT00000066767; ENSRNOP00000063449; ENSRNOG00000006304.
GeneID; 314856; -.
KEGG; rno:314856; -.
UCSC; RGD:1305332; rat.
CTD; 4193; -.
RGD; 1305332; Mdm2.
eggNOG; ENOG410IGXG; Eukaryota.
eggNOG; ENOG41125MP; LUCA.
GeneTree; ENSGT00530000063539; -.
KO; K06643; -.
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-3232142; SUMOylation of ubiquitinylation proteins.
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; Expressed in 10 organ(s), highest expression level in testis.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; IPI:RGD.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:RGD.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:RGD.
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:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
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:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IEA:InterPro.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
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:InterPro.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
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:0016567; P:protein ubiquitination; IDA:UniProtKB.
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.
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; 2.
PIRSF; PIRSF006748; p53_MDM_2/4; 2.
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 267 296 RanBP2-type.
{ECO:0000259|PROSITE:PS50199}.
DOMAIN 405 446 RING-type. {ECO:0000259|PROSITE:PS50089}.
SEQUENCE 458 AA; 51051 MW; A521BF918BA6E926 CRC64;
MCNTNMSVST EGAAGTSQIP ASEQETLIIF YIGQYIMTKR LYDEKQQHIV YCSNDLLGDV
FGVPSFSVKE HRKIYAMIYR NLVVVSQQDS GTSPSESRCQ PEGGSDLKDP VQASQEEKPS
SSDVVSRPST SSRRRAISET EENTDELPGE RQRKRHRALS FDESLGLCVL REICCERSSS
SEATDTPSHQ DLDDGVSDHS ADCLDQDSVS DQFSVEFEVE SLDSEDYSLS DEGHELSDED
DEVYRVTVYQ AGESDADSFE GDPEISLADY WKCTSCNEMN PPLPSHCNRC WTLRENWLPD
DKGKDKVEIS EKAKLESSDQ AEEGLDVPDG KKVTEDDAKE SSAEDSEEKV AQMLLSQESD
DYSQPSTSSS IVYSSQESGK ELKEDTQDKE ESMESSFSLN AIEPCVICQG RPKNGCIVHG
KTGHLMSCFT CAKKLKKRNK PCPVCRQPIQ MIVLTYFN


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