HUMAN:MDM2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	MDM2
Protein Name(s)	E3 ubiquitin-protein ligase Mdm2 Double minute 2 protein Hdm2 Oncoprotein Mdm2 p53-binding protein Mdm2
External Links
UniProt	Q00987
EMBL	M92424 Z12020 U33199 U33200 U33201 U33202 U33203 AF092844 AF092845 AK290341 BT007258 AF527840 AC025423 BC009893 U28935 U39736 AF201370 AJ251943
CCDS	CCDS61189.1 CCDS8986.2
PIR	S24354
RefSeq	NP_001138811.1 NP_001265391.1 NP_002383.2 XP_005268929.1 XP_006719462.1
UniGene	Hs.484551 Hs.733536
PDB	1RV1 1T4E 1T4F 1YCR 1Z1M 2AXI 2C6A 2C6B 2F1Y 2FOP 2GV2 2HDP 2LZG 2M86 2RUH 2VJE 2VJF 3EQS 3G03 3IUX 3IWY 3JZK 3JZR 3JZS 3LBK 3LBL 3LNJ 3LNZ 3MQS 3TJ2 3TPX 3TU1 3V3B 3VBG 3VZV 3W69 4DIJ 4ERE 4ERF 4HBM 4HFZ 4HG7 4JV7 4JV9 4JVE 4JVR 4JWR 4MDN 4MDQ 4OAS 4OBA 4OCC 4ODE 4ODF 4OGN 4OGT 4OGV 4OQ3 4QO4 4UMN
PDBsum	1RV1 1T4E 1T4F 1YCR 1Z1M 2AXI 2C6A 2C6B 2F1Y 2FOP 2GV2 2HDP 2LZG 2M86 2RUH 2VJE 2VJF 3EQS 3G03 3IUX 3IWY 3JZK 3JZR 3JZS 3LBK 3LBL 3LNJ 3LNZ 3MQS 3TJ2 3TPX 3TU1 3V3B 3VBG 3VZV 3W69 4DIJ 4ERE 4ERF 4HBM 4HFZ 4HG7 4JV7 4JV9 4JVE 4JVR 4JWR 4MDN 4MDQ 4OAS 4OBA 4OCC 4ODE 4ODF 4OGN 4OGT 4OGV 4OQ3 4QO4 4UMN
DisProt	DP00334
ProteinModelPortal	Q00987
SMR	Q00987
BioGrid	110358
DIP	DIP-392N
IntAct	Q00987
MINT	MINT-101583
BindingDB	Q00987
ChEMBL	CHEMBL5023
PhosphoSite	Q00987
DMDM	266516
MaxQB	Q00987
PaxDb	Q00987
PRIDE	Q00987
DNASU	4193
Ensembl	ENST00000258149 ENST00000299252 ENST00000348801 ENST00000356290 ENST00000360430 ENST00000393413
GeneID	4193
KEGG	hsa:4193
UCSC	uc001sui.4 uc001sun.5 uc001suo.4 uc009zqy.1 uc009zrc.4 uc009zrh.4
CTD	4193
GeneCards	GC12P069201
HGNC	HGNC:6973
HPA	CAB000086 CAB016303
MIM	164785 614401
neXtProt	NX_Q00987
Orphanet	99970 524 99971
PharmGKB	PA30718
eggNOG	NOG46328
GeneTree	ENSGT00530000063539
HOVERGEN	HBG013472
InParanoid	Q00987
KO	K06643
OMA	FEREETQ
OrthoDB	EOG7RRF7T
PhylomeDB	Q00987
TreeFam	TF105306
Reactome	REACT_12564 REACT_147727 REACT_169325 REACT_169436 REACT_18307 REACT_309
SignaLink	Q00987
ChiTaRS	MDM2
EvolutionaryTrace	Q00987
GeneWiki	Mdm2
GenomeRNAi	4193
NextBio	16526
PMAP-CutDB	Q00987
PRO	PR:Q00987
Proteomes	UP000005640
Bgee	Q00987
ExpressionAtlas	Q00987
Genevestigator	Q00987
GO	GO:0005737 GO:0005829 GO:0030666 GO:0005730 GO:0005654 GO:0005634 GO:0005886 GO:0043234 GO:0045202 GO:0019899 GO:0042802 GO:0016874 GO:0002039 GO:0031625 GO:0004842 GO:0008270 GO:0071229 GO:0071312 GO:0071236 GO:0071391 GO:0070301 GO:0071456 GO:0071375 GO:0071494 GO:0071301 GO:0006977 GO:0007173 GO:0045184 GO:0038095 GO:0008543 GO:0045087 GO:0071157 GO:0043154 GO:0043518 GO:0000122 GO:0045892 GO:0048011 GO:0018205 GO:0048015 GO:0008284 GO:0045931 GO:0032436 GO:0046827 GO:0006461 GO:0031648 GO:0034504 GO:0016567 GO:0042787 GO:0042176 GO:0046677 GO:0009743 GO:0042220 GO:0042493 GO:0045472 GO:0010039 GO:0032026 GO:0043278 GO:0007268 GO:0007089 GO:0016032
Gene3D	1.10.245.10 3.30.40.10
InterPro	IPR028340 IPR015459 IPR016495 IPR003121 IPR001876 IPR001841 IPR013083
PANTHER	PTHR10360:SF11
Pfam	PF02201 PF00641
PIRSF	PIRSF500700 PIRSF006748
SMART	SM00184
SUPFAM	SSF47592
PROSITE	PS01358 PS50199 PS50089

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0031625	ubiquitin protein ligase binding	PMID:29295817^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H992	F		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:25417702^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:25417702^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008097	5S rRNA binding	PMID:24120868^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P04637)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:17237821^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P21675	P	has_input:(UniProtKB:P04637)	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:16479015^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6K0P9	F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:18560357^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061663	NEDD8 ligase activity	PMID:18560357^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:18560357^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:11718560^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q64364	F		Seeded From UniProt	complete
involved_in	GO:1990000	amyloid fibril formation	PMID:12630860^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:12630860^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8N726	F		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:11718560^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11718560^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:17237821^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043021	ribonucleoprotein complex binding	PMID:24120868^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:25417702^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H3D4	F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:25417702^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15350	F		Seeded From UniProt	complete
involved_in	GO:0072717	cellular response to actinomycin D	PMID:15314173^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:15314173^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:15314173^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:15314173^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15314173^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15314173^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:15314173^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:19656744^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04637)	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	PMID:17142452^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902254	negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator	PMID:17310983^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:17310983^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:17310983^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:17310983^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:17310983^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:18560357^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	PMID:16213212^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:16173922^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901797	negative regulation of signal transduction by p53 class mediator	PMID:16173922^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:18382127^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q969K3	F		Seeded From UniProt	complete
enables	GO:0043130	ubiquitin binding	PMID:29295817^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:29295817^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071157	negative regulation of cell cycle arrest	PMID:9529249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045184	establishment of protein localization	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043518	negative regulation of DNA damage response, signal transduction by p53 class mediator	PMID:9529249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043518	negative regulation of DNA damage response, signal transduction by p53 class mediator	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:9529249^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:11278372^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:11278372^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:9529249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018205	peptidyl-lysine modification	PMID:19372219^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q08499-6)	Seeded From UniProt	complete
colocalizes_with	GO:0016604	nuclear body	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10360174^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:19372219^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q08499-6)	Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:15053879^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:9529249^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:16479015^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071456	cellular response to hypoxia	PMID:20810912^[21]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046677	response to antibiotic	PMID:20810912^[21]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045931	positive regulation of mitotic cell cycle	PMID:17290220^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:9271120^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042176	regulation of protein catabolic process	PMID:9153395^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:18382127^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WZ73	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:18566590^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q93009	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:17290220^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75604	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15577914^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15392	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20173098^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6PCD5	F		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:15878855^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:20153724^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:9450543^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:10722742^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	PMID:21726810^[32]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:12915590^[33]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:10608892^[34]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21726810^[32]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:22869143^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:10707090^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:12915590^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:10707090^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21726810^[32]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:20173098^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:9450543^[30]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:20173098^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:9271120^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019789	SUMO transferase activity	PMID:21900752^[37]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:24506068^[38]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22493164^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00987	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17936559^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00987	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17159902^[41]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00987	F		Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0019789	P		Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	F		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	F		Seeded From UniProt	complete
involved_in	GO:0060411	cardiac septum morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0045787	positive regulation of cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0010468	regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0007507	heart development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0007089	traversing start control point of mitotic cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	F		Seeded From UniProt	complete
involved_in	GO:0003283	atrial septum development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0003281	ventricular septum development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0003203	endocardial cushion morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0003181	atrioventricular valve morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0003170	heart valve development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	F		Seeded From UniProt	complete
involved_in	GO:0002027	regulation of heart rate	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0001974	blood vessel remodeling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:0001568	blood vessel development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23804 ensembl:ENSMUSP00000020408	P		Seeded From UniProt	complete
involved_in	GO:1990785	response to water-immersion restraint stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:1904754	positive regulation of vascular associated smooth muscle cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:1904707	positive regulation of vascular smooth muscle cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:1904404	response to formaldehyde	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071494	cellular response to UV-C	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071407	cellular response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071391	cellular response to estrogen stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071375	cellular response to peptide hormone stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071363	cellular response to growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071312	cellular response to alkaloid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071310	cellular response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071301	cellular response to vitamin B1	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0071236	cellular response to antibiotic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0048545	response to steroid hormone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0046827	positive regulation of protein export from nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0045472	response to ether	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	C		Seeded From UniProt	complete
involved_in	GO:0043278	response to morphine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
enables	GO:0042975	peroxisome proliferator activated receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	F		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
enables	GO:0033612	receptor serine/threonine kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	F		Seeded From UniProt	complete
involved_in	GO:0032026	response to magnesium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0010977	negative regulation of neuron projection development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0010955	negative regulation of protein processing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0010039	response to iron ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2JVC1 ensembl:ENSRNOP00000069425	F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015459	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016495	C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015459	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016495	P		Seeded From UniProt	complete
involved_in	GO:0071157	negative regulation of cell cycle arrest	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016495	P		Seeded From UniProt	complete
involved_in	GO:0036369	transcription factor catabolic process	PMID:20181722^[42]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:P10275)	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:7791904^[43]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030666	endocytic vesicle membrane	Reactome:R-HSA-416320	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	Reactome:R-HSA-69563	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-416320	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-6795667 Reactome:R-HSA-6795460 Reactome:R-HSA-6793666 Reactome:R-HSA-2399981 Reactome:R-HSA-198599	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-8952382 Reactome:R-HSA-8952371 Reactome:R-HSA-6805022 Reactome:R-HSA-6804998 Reactome:R-HSA-6804996 Reactome:R-HSA-6804955 Reactome:R-HSA-6804942 Reactome:R-HSA-6804879 Reactome:R-HSA-6804741 Reactome:R-HSA-6804724 Reactome:R-HSA-6804253 Reactome:R-HSA-6798373 Reactome:R-HSA-6795667 Reactome:R-HSA-6793666 Reactome:R-HSA-6793661 Reactome:R-HSA-6792871 Reactome:R-HSA-6792863 Reactome:R-HSA-5689972 Reactome:R-HSA-5689950 Reactome:R-HSA-5633460 Reactome:R-HSA-5228523 Reactome:R-HSA-3700992 Reactome:R-HSA-349455 Reactome:R-HSA-349426 Reactome:R-HSA-3222072 Reactome:R-HSA-3215295 Reactome:R-HSA-3000434 Reactome:R-HSA-2997706	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Zhao, K et al. (2018) Regulation of the Mdm2-p53 pathway by the ubiquitin E3 ligase MARCH7. EMBO Rep. 19 305-319 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Stindt, MH et al. (2015) Functional interplay between MDM2, p63/p73 and mutant p53. Oncogene 34 4300-10 PubMed GONUTS page
↑ ^3.0 ^3.1 Sloan, KE et al. (2013) The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar stress. Cell Rep 5 237-47 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Ding, Y et al. (2006) Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2. Mol. Cell. Biol. 26 1979-96 PubMed GONUTS page
↑ ^5.0 ^5.1 Allende-Vega, N et al. (2007) Transcription factor TAFII250 promotes Mdm2-dependent turnover of p53. Oncogene 26 4234-42 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Horn, HF & Vousden, KH (2008) Cooperation between the ribosomal proteins L5 and L11 in the p53 pathway. Oncogene 27 5774-84 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Bothner, B et al. (2001) Defining the molecular basis of Arf and Hdm2 interactions. J. Mol. Biol. 314 263-77 PubMed GONUTS page
↑ ^8.0 ^8.1 Bothner, B et al. (2003) Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. J. Am. Chem. Soc. 125 3200-1 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Dai, MS et al. (2004) Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition. Mol. Cell. Biol. 24 7654-68 PubMed GONUTS page
↑ Yadavilli, S et al. (2009) Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) 8 1215-24 PubMed GONUTS page
↑ Nam, YJ et al. (2007) The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated degradation in response to death stimuli: identification of a degradation-resistant mutant. J. Biol. Chem. 282 5522-8 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Chen, D et al. (2007) Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function. Oncogene 26 5029-37 PubMed GONUTS page
↑ Takagi, M et al. (2005) Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin. Cell 123 49-63 PubMed GONUTS page
↑ ^14.0 ^14.1 Wang, J et al. (2006) A novel ARF-binding protein (LZAP) alters ARF regulation of HDM2. Biochem. J. 393 489-501 PubMed GONUTS page
↑ ^15.0 ^15.1 Yang, W et al. (2008) CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2. Cell Cycle 7 670-82 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 Zhang, Y et al. (1998) ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92 725-34 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Zhang, Y & Xiong, Y (1999) Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. Mol. Cell 3 579-91 PubMed GONUTS page
↑ ^18.0 ^18.1 Buschmann, T et al. (2001) Stabilization and activation of p53 by the coactivator protein TAFII31. J. Biol. Chem. 276 13852-7 PubMed GONUTS page
↑ ^19.0 ^19.1 Li, X et al. (2009) Mdm2 directs the ubiquitination of beta-arrestin-sequestered cAMP phosphodiesterase-4D5. J. Biol. Chem. 284 16170-82 PubMed GONUTS page
↑ Li, HH et al. (2004) Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for TAF1 in cell G1 progression. Mol. Cell 13 867-78 PubMed GONUTS page
↑ ^21.0 ^21.1 Chen, B et al. (2010) Hypoxia downregulates p53 but induces apoptosis and enhances expression of BAD in cultures of human syncytiotrophoblasts. Am. J. Physiol., Cell Physiol. 299 C968-76 PubMed GONUTS page
↑ ^22.0 ^22.1 Stevenson, LF et al. (2007) The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J. 26 976-86 PubMed GONUTS page
↑ ^23.0 ^23.1 Thut, CJ et al. (1997) Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 11 1974-86 PubMed GONUTS page
↑ Haupt, Y et al. (1997) Mdm2 promotes the rapid degradation of p53. Nature 387 296-9 PubMed GONUTS page
↑ Song, MS et al. (2008) The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 27 1863-74 PubMed GONUTS page
↑ Wu, C et al. (2004) Regulation of cellular response to oncogenic and oxidative stress by Seladin-1. Nature 432 640-5 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 Fu, X et al. (2010) RFWD3-Mdm2 ubiquitin ligase complex positively regulates p53 stability in response to DNA damage. Proc. Natl. Acad. Sci. U.S.A. 107 4579-84 PubMed GONUTS page
↑ Girnita, L et al. (2005) {beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase. J. Biol. Chem. 280 24412-9 PubMed GONUTS page
↑ Tang, J et al. (2010) Daxx is reciprocally regulated by Mdm2 and Hausp. Biochem. Biophys. Res. Commun. 393 542-5 PubMed GONUTS page
↑ ^30.0 ^30.1 Honda, R et al. (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420 25-7 PubMed GONUTS page
↑ Fang, S et al. (2000) Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275 8945-51 PubMed GONUTS page
↑ ^32.0 ^32.1 ^32.2 Oliver, TG et al. (2011) Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loop. Mol. Cell 43 57-71 PubMed GONUTS page
↑ ^33.0 ^33.1 Kurki, S et al. (2003) Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J. Cell. Sci. 116 3917-25 PubMed GONUTS page
↑ Sharp, DA et al. (1999) Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274 38189-96 PubMed GONUTS page
↑ Yang, Q et al. (2013) BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction. Oncogene 32 3156-64 PubMed GONUTS page
↑ ^36.0 ^36.1 Lohrum, MA et al. (2000) Identification of a cryptic nucleolar-localization signal in MDM2. Nat. Cell Biol. 2 179-81 PubMed GONUTS page
↑ Stindt, MH et al. (2011) MDM2 promotes SUMO-2/3 modification of p53 to modulate transcriptional activity. Cell Cycle 10 3176-88 PubMed GONUTS page
↑ Read, ML et al. (2014) The PTTG1-binding factor (PBF/PTTG1IP) regulates p53 activity in thyroid cells. Endocrinology 155 1222-34 PubMed GONUTS page
↑ Woodsmith, J et al. (2012) Systematic analysis of dimeric E3-RING interactions reveals increased combinatorial complexity in human ubiquitination networks. Mol. Cell Proteomics 11 M111.016162 PubMed GONUTS page
↑ Lu, X et al. (2007) The Wip1 Phosphatase acts as a gatekeeper in the p53-Mdm2 autoregulatory loop. Cancer Cell 12 342-54 PubMed GONUTS page
↑ Uldrijan, S et al. (2007) An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J. 26 102-12 PubMed GONUTS page
↑ Tavassoli, P et al. (2010) TAF1 differentially enhances androgen receptor transcriptional activity via its N-terminal kinase and ubiquitin-activating and -conjugating domains. Mol. Endocrinol. 24 696-708 PubMed GONUTS page
↑ Xiao, ZX et al. (1995) Interaction between the retinoblastoma protein and the oncoprotein MDM2. Nature 375 694-8 PubMed GONUTS page

[PMID:29295817-1] 1.0 ^1.1 ^1.2 Zhao, K et al. (2018) Regulation of the Mdm2-p53 pathway by the ubiquitin E3 ligase MARCH7. EMBO Rep. 19 305-319 PubMed GONUTS page

[PMID:25417702-2] 2.0 ^2.1 ^2.2 ^2.3 Stindt, MH et al. (2015) Functional interplay between MDM2, p63/p73 and mutant p53. Oncogene 34 4300-10 PubMed GONUTS page

[PMID:24120868-3] 3.0 ^3.1 Sloan, KE et al. (2013) The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar stress. Cell Rep 5 237-47 PubMed GONUTS page

[PMID:16479015-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Ding, Y et al. (2006) Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2. Mol. Cell. Biol. 26 1979-96 PubMed GONUTS page

[PMID:17237821-5] 5.0 ^5.1 Allende-Vega, N et al. (2007) Transcription factor TAFII250 promotes Mdm2-dependent turnover of p53. Oncogene 26 4234-42 PubMed GONUTS page

[PMID:18560357-6] 6.0 ^6.1 ^6.2 ^6.3 Horn, HF & Vousden, KH (2008) Cooperation between the ribosomal proteins L5 and L11 in the p53 pathway. Oncogene 27 5774-84 PubMed GONUTS page

[PMID:11718560-7] 7.0 ^7.1 ^7.2 Bothner, B et al. (2001) Defining the molecular basis of Arf and Hdm2 interactions. J. Mol. Biol. 314 263-77 PubMed GONUTS page

[PMID:12630860-8] 8.0 ^8.1 Bothner, B et al. (2003) Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. J. Am. Chem. Soc. 125 3200-1 PubMed GONUTS page

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