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E3 ubiquitin-protein ligase Mdm2

 M3XEK9_FELCA            Unreviewed;       616 AA.
M3XEK9;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
10-OCT-2018, sequence version 2.
07-NOV-2018, entry version 48.
SubName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000313|Ensembl:ENSFCAP00000025067};
Name=MDM2 {ECO:0000313|Ensembl:ENSFCAP00000025067};
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000025067, ECO:0000313|Proteomes:UP000011712};
[1] {ECO:0000313|Ensembl:ENSFCAP00000025067, ECO:0000313|Proteomes:UP000011712}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025067,
ECO:0000313|Proteomes:UP000011712};
PubMed=17975172; DOI=10.1101/gr.6380007;
Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N.,
Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U.,
Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N.,
Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.;
"Initial sequence and comparative analysis of the cat genome.";
Genome Res. 17:1675-1689(2007).
[2] {ECO:0000313|Ensembl:ENSFCAP00000025067}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025067};
Hillier L.W., Warren W., Obrien S., Wilson R.K.;
"Sequence assembly of the Felis catus genome version 6.2.";
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Ensembl:ENSFCAP00000025067}
IDENTIFICATION.
STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025067};
Ensembl;
Submitted (MAR-2013) to UniProtKB.
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EMBL; AANG04003655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
Ensembl; ENSFCAT00000029807; ENSFCAP00000025067; ENSFCAG00000024456.
CTD; 4193; -.
eggNOG; ENOG410IGXG; Eukaryota.
eggNOG; ENOG41125MP; LUCA.
GeneTree; ENSGT00530000063539; -.
OMA; GELPCKL; -.
OrthoDB; EOG091G0FYK; -.
Proteomes; UP000011712; Chromosome B4.
Bgee; ENSFCAG00000024456; Expressed in 3 organ(s), highest expression level in liver.
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: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:0043130; F:ubiquitin 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.
4: Predicted;
Complete proteome {ECO:0000313|Proteomes:UP000011712};
Reference proteome {ECO:0000313|Proteomes:UP000011712}.
DOMAIN 424 453 RanBP2-type.
{ECO:0000259|PROSITE:PS50199}.
DOMAIN 563 604 RING-type. {ECO:0000259|PROSITE:PS50089}.
SEQUENCE 616 AA; 68931 MW; D09AF36D4D9A325C CRC64;
MSRGFRRAPL GQQGARIGRA SAGSGPPGAC AGPVWLERKW SKSPSLRGSP NPSDRSPAGF
AARSLFLLRT QCVRAPQWPG PREWNGRRGP RRRASARPVK GTGEPRGSPF FLLEARTTPL
GESRQMCNTN MSVSTDGAVS TSQMPASEQE TLVRPKPLLL KLLKSVGAQK DTYTMKEVIF
YLGQYIMTKR LYDEKQQHIV YCSNDLLGDL FGVPSFSVKE HRKIYTMIYR NLVVVNQHEP
SDSGTSVSEN RCHLEGGSDQ KDPVQELQEE KPSSSDLVSR PSTSSRRRTI SETEEHSDEL
PGERQRKRHK SDSISLSFDE SLALCVIREI CCERSSSSES TGTPSNPDLD AGVSEHSGDW
LDQDSVSDQF SVEFEVESLD SEDYSLSEEG QELSDEDDEV YRVTVYQAGE SDTDSFEEDP
EISLADYWKC TSCNEMNPPL PPHCNRCWAL RENWLPEDKG KDKGKMPEKA KVENSTQVEE
GFDVPDCKKT TVNDSRESCA EENDDKITQA SQSQESEDYS QPSTSNSIIH SSQEDVKEFE
REETQDKEEI VEPSFPHNAI EPCVICQGRP KNGCIVHGKT GHLMACFTCA KKLKKRNKPC
PVCRQPIQMI VLTYFP


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