Reviewed, UniProtKB/Swiss-Prot Q00987 (MDM2_HUMAN)

Names and origin

Protein names

Recommended name:
    E3 ubiquitin-protein ligase Mdm2
    EC=6.3.2.-
Alternative name(s):
    p53-binding protein Mdm2
    Oncoprotein Mdm2
    Double minute 2 protein
      Short name=Hdm2

Gene names

Name:

MDM2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inhibits TP53/p53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Functions as a ubiquitin ligase E3, in the presence of E1 and E2, toward p53 and itself. Permits the nuclear export of p53 and targets it for proteasome-mediated proteolysis. Functions as an ubiquitin ligase E3 toward ARRB1 By similarity. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Ref.25
Subunit structure	Binds p53, p73, ARF(P14), ribosomal protein L5 and specifically to RNA. Can interact also with retinoblastoma protein (RB), E1A-associated protein EP300 and the E2F1 transcription factor. Forms a ternary complex with TP53/p53 and WWOX. Interacts with CDKN2AIP, MTBP, TBRG1, USP7, PYHIN1 and UBXN6. Isoform Mdm2-F does not interact with TP53/p53. Interacts with and ubiquitinates HIV-1 Tat. Interacts with ARRB1 and ARRB2. Isoform 2 interacts with PSMA3. Ref.25 Ref.4 Ref.14 Ref.21 Ref.22 Ref.23 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32 Ref.33
Subcellular location	Nucleus › nucleoplasm. Cytoplasm. Nucleus › nucleolus. Note: Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Ref.14
Tissue specificity	Ubiquitous. Isoform Mdm2-A, isoform Mdm2-B, isoform Mdm2-C, isoform Mdm2-D, isoform Mdm2-E, isoform Mdm2-F and isoform Mdm2-G are observed in a range of cancers but absent in normal tissues.
Induction	By DNA damage.
Domain	Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself.
Post-translational modification	Phosphorylated in response to ionizing radiation in an ATM-dependent manner. Ref.17 Ref.30 Auto-ubiquitinated; which leads to proteasomal degradation.
Involvement in disease	Seems to be amplified in certain tumors (including soft tissue sarcomas, osteosarcomas and gliomas). A higher frequency of splice variants lacking p53 binding domain sequences was found in late-stage and high-grade ovarian and bladder carcinomas. Four of the splice variants show loss of p53 binding.
Miscellaneous	MDM2 RING finger mutations that failed to ubiquitinate p53 in vitro did not target p53 for degradation when expressed in cells.
Sequence similarities	Belongs to the MDM2/MDM4 family. Contains 1 RanBP2-type zinc finger. Contains 1 RING-type zinc finger. Contains 1 SWIB domain.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	establishment of protein localization Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of DNA damage response, signal transduction by p53 class mediator Inferred from direct assay. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of cell proliferation Traceable author statement. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: UniProtKB protein complex assembly Ref.16 Inferred from direct assay. Source: UniProtKB protein destabilization Inferred from direct assay. Source: UniProtKB protein localization in nucleus Inferred from direct assay. Source: UniProtKB protein ubiquitination during ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome endocytic vesicle membrane Inferred from Experiment. Source: Reactome insoluble fraction Inferred from direct assay. Source: UniProtKB nucleolus Ref.19 Inferred from direct assay. Source: UniProtKB nucleoplasm Ref.19 Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	basal transcription repressor activity Inferred from direct assay. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct p53 binding Inferred from physical interaction. Source: UniProtKB ubiquitin-protein ligase activity Ref.15 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.18 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-389668,EBI-389668
ACTB	P60709	1	EBI-389668,EBI-353944
AR	P10275	1	EBI-389668,EBI-608057
ARRB1	P49407	1	EBI-389668,EBI-743313
CDKN2A	Q8N726	3	EBI-389668,EBI-625922
DAXX	Q9UER7	4	EBI-389668,EBI-77321
DCD	P81605	1	EBI-389668,EBI-395625
EEF1A1	P68104	4	EBI-389668,EBI-352162
ESR1	P03372	1	EBI-389668,EBI-78473
GAPDH	P04406	1	EBI-389668,EBI-354056
GSN	P06396-2	1	EBI-389668,EBI-1018556
JMY	Q8N9B5	1	EBI-389668,EBI-866435
Jmy	Q9QXM1	1	EBI-389668,EBI-866001	From a different organism.
KRT1	P04264	1	EBI-389668,EBI-298429
KRT10	P13645	1	EBI-389668,EBI-465144
KRT14	P02533	1	EBI-389668,EBI-702178
KRT2	P35908	1	EBI-389668,EBI-1247312
KRT8	P05787	1	EBI-389668,EBI-297852
KRT9	P35527	1	EBI-389668,EBI-356382
MDM4	O15151	2	EBI-389668,EBI-398437
NPM1	P06748	3	EBI-389668,EBI-78579
Npm1	Q61937	2	EBI-389668,EBI-626362	From a different organism.
PML	P29590	2	EBI-389668,EBI-295890
PML	P29590-5	1	EBI-389668,EBI-304008
PML	Q15959	1	EBI-389668,EBI-779712
PPM1D	O15297	2	EBI-389668,EBI-1551512
RPL11	P62913	1	EBI-389668,EBI-354380
RPL5	P46777	1	EBI-389668,EBI-358018
RPS20	P60866	1	EBI-389668,EBI-353105
RPS27A	P62988	1	EBI-389668,EBI-413034
RPS7	P62081	5	EBI-389668,EBI-354360
TBP	P20226	1	EBI-389668,EBI-355371
TP53	P04637	7	EBI-389668,EBI-366083
TUBA1C	Q9BQE3	1	EBI-389668,EBI-1103245
TUBB2A	Q13885	1	EBI-389668,EBI-711595
USP7	Q93009	4	EBI-389668,EBI-302474
VIM	P08670	1	EBI-389668,EBI-353844

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Isoform Mdm2 (identifier: Q00987-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Mdm2-A (identifier: Q00987-2)

The sequence of this isoform differs from the canonical sequence as follows:
     28-222: Missing.

Isoform Mdm2-A1 (identifier: Q00987-3)

The sequence of this isoform differs from the canonical sequence as follows:
     28-222: Missing.
     275-300: Missing.

Isoform Mdm2-B (identifier: Q00987-4)

The sequence of this isoform differs from the canonical sequence as follows:
     28-300: Missing.

Isoform Mdm2-C (identifier: Q00987-5)

The sequence of this isoform differs from the canonical sequence as follows:
     53-222: Missing.

Isoform Mdm2-D (identifier: Q00987-6)

The sequence of this isoform differs from the canonical sequence as follows:
     30-388: Missing.

Isoform Mdm2-E (identifier: Q00987-7)

The sequence of this isoform differs from the canonical sequence as follows:
     76-102: YCSNDLLGDLFGVPSFSVKEHRKIYTM → NDCANLFPLVDLSIRELYISNYITLGI
     103-491: Missing.

Isoform Mdm2-alpha (identifier: Q00987-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Isoform Mdm2-F (identifier: Q00987-9)

The sequence of this isoform differs from the canonical sequence as follows:
     53-97: Missing.

Isoform Mdm2-G (identifier: Q00987-10)

The sequence of this isoform differs from the canonical sequence as follows:
     115-169: Missing.

Isoform 11 (identifier: Q00987-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVRSRQM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 491

491

E3 ubiquitin-protein ligase Mdm2

PRO_0000157332

Regions

Domain

27 – 107

81

SWIB

Zinc finger

299 – 328

30

RanBP2-type

Zinc finger

438 – 479

42

RING-type

Region

150 – 230

81

Interaction with PYHIN1

Region

170 – 306

137

Interaction with MTBP By similarity

Region

210 – 304

95

ARF-binding

Region

223 – 232

10

Interaction with USP7

Region

242 – 331

90

Region II

Motif

179 – 185

7

Nuclear localization signal Potential

Motif

190 – 202

13

Nuclear export signal

Motif

466 – 473

8

Nucleolar localization signal Potential

Compositional bias

210 – 215

6

Poly-Ser

Compositional bias

243 – 301

59

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

166

1

Phosphoserine Ref.30

Natural variations

Alternative sequence

1 – 61

61

Missing in isoform Mdm2-alpha.

VSP_003207

Alternative sequence

1

1

M → MVRSRQM in isoform 11.

VSP_037997

Alternative sequence

28 – 300

273

Missing in isoform Mdm2-B.

VSP_003209

Alternative sequence

28 – 222

195

Missing in isoform Mdm2-A and isoform Mdm2-A1.

VSP_003208

Alternative sequence

30 – 388

359

Missing in isoform Mdm2-D.

VSP_003210

Alternative sequence

53 – 222

170

Missing in isoform Mdm2-C.

VSP_003211

Alternative sequence

53 – 97

45

Missing in isoform Mdm2-F.

VSP_022578

Alternative sequence

76 – 102

27

YCSND…KIYTM → NDCANLFPLVDLSIRELYIS NYITLGI in isoform Mdm2-E.

VSP_003212

Alternative sequence

103 – 491

389

Missing in isoform Mdm2-E.

VSP_003213

Alternative sequence

115 – 169

55

Missing in isoform Mdm2-G.

VSP_022579

Alternative sequence

275 – 300

26

Missing in isoform Mdm2-A1.

VSP_003214

Experimental info

Mutagenesis

305

1

C → S: No loss of ubiquitin ligase E3 activity.

Mutagenesis

374

1

C → T: No loss of ubiquitin ligase E3 activity.

Mutagenesis

438

1

C → L: No loss of ubiquitin ligase E3 activity.

Mutagenesis

441

1

C → G: Fails to interact with MDM4. Ref.16

Mutagenesis

449

1

C → A: Loss of ubiquitin ligase E3 activity. Ref.20

Mutagenesis

449

1

C → S: No substantial decrease of ubiquitin ligase E3 activity. Ref.20

Mutagenesis

452

1

H → A: Loss of ubiquitin ligase E3 activity.

Mutagenesis

455

1

T → A: Significant decrease of ubiquitin ligase E3 activity.

Mutagenesis

457

1

H → S: Loss of ubiquitin ligase E3 activity.

Mutagenesis

461

1

C → S: Loss of ubiquitin ligase E3 activity.

Mutagenesis

464

1

C → A: Loss of ubiquitin ligase E3 activity, enhances protein stability. Ref.25 Ref.26 Ref.15

Mutagenesis

475

1

C → G: Loss of ubiquitin ligase E3 activity.

Mutagenesis

478

1

C → R: Fails to interact with MDM4. Ref.16

Mutagenesis

478

1

C → S: Loss of ubiquitin ligase E3 activity. Ref.16

Sequence conflict

17

1

S → P in AAA82237. Ref.10

Secondary structure

1

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491

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Beta strand

27 – 30

4

Helix

32 – 40

9

Helix

50 – 64

15

Beta strand

71 – 76

6

Helix

81 – 86

6

Beta strand

87 – 92

6

Helix

96 – 104

9

Beta strand

107 – 109

3

Beta strand

295 – 297

3

Helix

299 – 301

3

Turn

306 – 308

3

Turn

320 – 322

3

Beta strand

433 – 436

4

Beta strand

439 – 444

6

Beta strand

446 – 461

16

Helix

462 – 470

9

Beta strand

476 – 479

4

Beta strand

482 – 490

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mdm2 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: F37CE163876BC983	FASTA	491	55,233
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY 70 80 90 100 110 120 IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY TMIYRNLVVV NQQESSDSGT 130 140 150 160 170 180 SVSENRCHLE GGSDQKDLVQ ELQEEKPSSS HLVSRPSTSS RRRAISETEE NSDELSGERQ 190 200 210 220 230 240 RKRHKSDSIS LSFDESLALC VIREICCERS SSSESTGTPS NPDLDAGVSE HSGDWLDQDS 250 260 270 280 290 300 VSDQFSVEFE VESLDSEDYS LSEEGQELSD EDDEVYQVTV YQAGESDTDS FEEDPEISLA 310 320 330 340 350 360 DYWKCTSCNE MNPPLPSHCN RCWALRENWL PEDKGKDKGE ISEKAKLENS TQAEEGFDVP 370 380 390 400 410 420 DCKKTIVNDS RESCVEENDD KITQASQSQE SEDYSQPSTS SSIIYSSQED VKEFEREETQ 430 440 450 460 470 480 DKEESVESSL PLNAIEPCVI CQGRPKNGCI VHGKTGHLMA CFTCAKKLKK RNKPCPVCRQ 490 PIQMIVLTYF P
	Isoform Mdm2-A. Checksum: 9772439D74A4448B	FASTA	296	33,140
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLDLD AGVSEHSGDW LDQDSVSDQF SVEFEVESLD 70 80 90 100 110 120 SEDYSLSEEG QELSDEDDEV YQVTVYQAGE SDTDSFEEDP EISLADYWKC TSCNEMNPPL 130 140 150 160 170 180 PSHCNRCWAL RENWLPEDKG KDKGEISEKA KLENSTQAEE GFDVPDCKKT IVNDSRESCV 190 200 210 220 230 240 EENDDKITQA SQSQESEDYS QPSTSSSIIY SSQEDVKEFE REETQDKEES VESSLPLNAI 250 260 270 280 290 EPCVICQGRP KNGCIVHGKT GHLMACFTCA KKLKKRNKPC PVCRQPIQMI VLTYFP
	Isoform Mdm2-A1. Checksum: A3ED7CCFF670634E	FASTA	270	30,265
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLDLD AGVSEHSGDW LDQDSVSDQF SVEFEVESLD 70 80 90 100 110 120 SEDYSLSEEG QELSDEDDED YWKCTSCNEM NPPLPSHCNR CWALRENWLP EDKGKDKGEI 130 140 150 160 170 180 SEKAKLENST QAEEGFDVPD CKKTIVNDSR ESCVEENDDK ITQASQSQES EDYSQPSTSS 190 200 210 220 230 240 SIIYSSQEDV KEFEREETQD KEESVESSLP LNAIEPCVIC QGRPKNGCIV HGKTGHLMAC 250 260 270 FTCAKKLKKR NKPCPVCRQP IQMIVLTYFP
	Isoform Mdm2-B. Checksum: BB9C602F589EEC41	FASTA	218	24,467
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLDYW KCTSCNEMNP PLPSHCNRCW ALRENWLPED 70 80 90 100 110 120 KGKDKGEISE KAKLENSTQA EEGFDVPDCK KTIVNDSRES CVEENDDKIT QASQSQESED 130 140 150 160 170 180 YSQPSTSSSI IYSSQEDVKE FEREETQDKE ESVESSLPLN AIEPCVICQG RPKNGCIVHG 190 200 210 KTGHLMACFT CAKKLKKRNK PCPVCRQPIQ MIVLTYFP
	Isoform Mdm2-C. Checksum: 4BD6213CA39D15C0	FASTA	321	35,980
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEDLDAGVSE 70 80 90 100 110 120 HSGDWLDQDS VSDQFSVEFE VESLDSEDYS LSEEGQELSD EDDEVYQVTV YQAGESDTDS 130 140 150 160 170 180 FEEDPEISLA DYWKCTSCNE MNPPLPSHCN RCWALRENWL PEDKGKDKGE ISEKAKLENS 190 200 210 220 230 240 TQAEEGFDVP DCKKTIVNDS RESCVEENDD KITQASQSQE SEDYSQPSTS SSIIYSSQED 250 260 270 280 290 300 VKEFEREETQ DKEESVESSL PLNAIEPCVI CQGRPKNGCI VHGKTGHLMA CFTCAKKLKK 310 320 RNKPCPVCRQ PIQMIVLTYF P
	Isoform Mdm2-D. Checksum: 770E9B66362CA97E	FASTA	132	14,689
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRQ ESEDYSQPST SSSIIYSSQE DVKEFEREET 70 80 90 100 110 120 QDKEESVESS LPLNAIEPCV ICQGRPKNGC IVHGKTGHLM ACFTCAKKLK KRNKPCPVCR 130 QPIQMIVLTY FP
	Isoform Mdm2-E. Checksum: 75E2B91B94C786C1	FASTA	102	11,587
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY 70 80 90 100 IMTKRLYDEK QQHIVNDCAN LFPLVDLSIR ELYISNYITL GI
	Isoform Mdm2-alpha. Checksum: C84E1F63E39E655D	FASTA	430	48,488
	10 20 30 40 50 60 MTKRLYDEKQ QHIVYCSNDL LGDLFGVPSF SVKEHRKIYT MIYRNLVVVN QQESSDSGTS 70 80 90 100 110 120 VSENRCHLEG GSDQKDLVQE LQEEKPSSSH LVSRPSTSSR RRAISETEEN SDELSGERQR 130 140 150 160 170 180 KRHKSDSISL SFDESLALCV IREICCERSS SSESTGTPSN PDLDAGVSEH SGDWLDQDSV 190 200 210 220 230 240 SDQFSVEFEV ESLDSEDYSL SEEGQELSDE DDEVYQVTVY QAGESDTDSF EEDPEISLAD 250 260 270 280 290 300 YWKCTSCNEM NPPLPSHCNR CWALRENWLP EDKGKDKGEI SEKAKLENST QAEEGFDVPD 310 320 330 340 350 360 CKKTIVNDSR ESCVEENDDK ITQASQSQES EDYSQPSTSS SIIYSSQEDV KEFEREETQD 370 380 390 400 410 420 KEESVESSLP LNAIEPCVIC QGRPKNGCIV HGKTGHLMAC FTCAKKLKKR NKPCPVCRQP 430 IQMIVLTYFP
	Isoform Mdm2-F. Checksum: 4B630B50750EADFE	FASTA	446	49,899
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEKIYTMIYR 70 80 90 100 110 120 NLVVVNQQES SDSGTSVSEN RCHLEGGSDQ KDLVQELQEE KPSSSHLVSR PSTSSRRRAI 130 140 150 160 170 180 SETEENSDEL SGERQRKRHK SDSISLSFDE SLALCVIREI CCERSSSSES TGTPSNPDLD 190 200 210 220 230 240 AGVSEHSGDW LDQDSVSDQF SVEFEVESLD SEDYSLSEEG QELSDEDDEV YQVTVYQAGE 250 260 270 280 290 300 SDTDSFEEDP EISLADYWKC TSCNEMNPPL PSHCNRCWAL RENWLPEDKG KDKGEISEKA 310 320 330 340 350 360 KLENSTQAEE GFDVPDCKKT IVNDSRESCV EENDDKITQA SQSQESEDYS QPSTSSSIIY 370 380 390 400 410 420 SSQEDVKEFE REETQDKEES VESSLPLNAI EPCVICQGRP KNGCIVHGKT GHLMACFTCA 430 440 KKLKKRNKPC PVCRQPIQMI VLTYFP
	Isoform Mdm2-G. Checksum: 3C8F55E98BC4203A	FASTA	436	49,249
	10 20 30 40 50 60 MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY 70 80 90 100 110 120 IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY TMIYRNLVVV NQQEENSDEL 130 140 150 160 170 180 SGERQRKRHK SDSISLSFDE SLALCVIREI CCERSSSSES TGTPSNPDLD AGVSEHSGDW 190 200 210 220 230 240 LDQDSVSDQF SVEFEVESLD SEDYSLSEEG QELSDEDDEV YQVTVYQAGE SDTDSFEEDP 250 260 270 280 290 300 EISLADYWKC TSCNEMNPPL PSHCNRCWAL RENWLPEDKG KDKGEISEKA KLENSTQAEE 310 320 330 340 350 360 GFDVPDCKKT IVNDSRESCV EENDDKITQA SQSQESEDYS QPSTSSSIIY SSQEDVKEFE 370 380 390 400 410 420 REETQDKEES VESSLPLNAI EPCVICQGRP KNGCIVHGKT GHLMACFTCA KKLKKRNKPC 430 PVCRQPIQMI VLTYFP
	Isoform 11. Checksum: CFEC32F36132D8FA	FASTA	497	55,991
	10 20 30 40 50 60 MVRSRQMCNT NMSVPTDGAV TTSQIPASEQ ETLVRPKPLL LKLLKSVGAQ KDTYTMKEVL 70 80 90 100 110 120 FYLGQYIMTK RLYDEKQQHI VYCSNDLLGD LFGVPSFSVK EHRKIYTMIY RNLVVVNQQE 130 140 150 160 170 180 SSDSGTSVSE NRCHLEGGSD QKDLVQELQE EKPSSSHLVS RPSTSSRRRA ISETEENSDE 190 200 210 220 230 240 LSGERQRKRH KSDSISLSFD ESLALCVIRE ICCERSSSSE STGTPSNPDL DAGVSEHSGD 250 260 270 280 290 300 WLDQDSVSDQ FSVEFEVESL DSEDYSLSEE GQELSDEDDE VYQVTVYQAG ESDTDSFEED 310 320 330 340 350 360 PEISLADYWK CTSCNEMNPP LPSHCNRCWA LRENWLPEDK GKDKGEISEK AKLENSTQAE 370 380 390 400 410 420 EGFDVPDCKK TIVNDSRESC VEENDDKITQ ASQSQESEDY SQPSTSSSII YSSQEDVKEF 430 440 450 460 470 480 EREETQDKEE SVESSLPLNA IEPCVICQGR PKNGCIVHGK TGHLMACFTC AKKLKKRNKP 490 CPVCRQPIQM IVLTYFP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amplification of a gene encoding a p53-associated protein in human sarcomas." Oliner J.D., Kinzler K.W., Meltzer P.S., George D.L., Vogelstein B. Nature 358:80-83(1992) [PubMed: 1614537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2). Tissue: Colon.
[2]	"Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: transforming ability and frequent detection in human cancer." Sigalas I., Calvert A.H., Anderson J.J., Neal D.E., Lunec J. Nat. Med. 2:912-917(1996) [PubMed: 8705862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-A; MDM2-B; MDM2-C; MDM2-D AND MDM2-E). Tissue: Ovarian carcinoma.
[3]	"A novel exon within the mdm2 gene modulates translation initiation in vitro and disrupts the p53-binding domain of mdm2 protein." Veldhoen N., Metcalfe S., Milner J. Oncogene 18:7026-7033(1999) [PubMed: 10597303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDM2-ALPHA).
[4]	"Analysis of the molecular species generated by MDM2 gene amplification in liposarcomas." Tamborini E., Della Torre G., Lavarino C., Azzarelli A., Carpinelli P., Pierotti M.A., Pilotti S. Int. J. Cancer 92:790-796(2001) [PubMed: 11351297] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2-F AND MDM2-G), INTERACTION WITH TP53.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2). Tissue: Tongue.
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MDM2).
[7]	NIEHS SNPs program Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11). Tissue: Rhabdomyosarcoma.
[10]	"A functional p53-responsive intronic promoter is contained within the human mdm2 gene." Zauberman A., Flusberg D., Haupt Y., Barak Y., Oren M. Nucleic Acids Res. 23:2584-2592(1995) [PubMed: 7651818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[11]	"Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein." Landers J.E., Cassel S.L., George D.L. Cancer Res. 57:3562-3568(1997) [PubMed: 9270029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[12]	"Genomic organisation of the human MDM2 oncogene and relationship to its alternatively spliced mRNAs." Liang H., Atkins H., Abdel-Fattah R., Jones S.N., Lunec J. Gene 338:217-223(2004) [PubMed: 15315825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-491 (ISOFORM MDM2-A1).
[13]	"A MboII polymorphism in exon 11 of the human MDM2 gene occuring in normal blood donors and in soft tissue sarcoma patients: an indication for an increased cancer susceptibility?" Taubert H., Kappler M., Meye A., Bartel F., Schlott T., Lautenschlaeger C., Bache M., Schmidt H., Wuerl P. Mutat. Res. 456:39-44(2000) [PubMed: 11087894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-481.
[14]	"Identification and characterization of multiple mdm-2 proteins and mdm-2-p53 protein complexes." Olson D.C., Marechal V., Momand J., Chen J., Romocki C., Levine A.J. Oncogene 8:2353-2360(1993) [PubMed: 7689721] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53.
[15]	"Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53." Honda R., Tanaka H., Yasuda H. FEBS Lett. 420:25-27(1997) [PubMed: 9450543] [Abstract] Cited for: MUTAGENESIS OF CYS-464.
[16]	"Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein." Sharp D.A., Kratowicz S.A., Sank M.J., George D.L. J. Biol. Chem. 274:38189-38196(1999) [PubMed: 10608892] [Abstract] Cited for: MUTAGENESIS OF CYS-441 AND CYS-478.
[17]	"Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage." Khosravi R., Maya R., Gottlieb T., Oren M., Shiloh Y., Shkedy D. Proc. Natl. Acad. Sci. U.S.A. 96:14973-14977(1999) [PubMed: 10611322] [Abstract] Cited for: PHOSPHORYLATION BY ATM.
[18]	"Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53." Fang S., Jensen J.P., Ludwig R.L., Vousden K.H., Weissman A.M. J. Biol. Chem. 275:8945-8951(2000) [PubMed: 10722742] [Abstract] Cited for: MUTAGENESIS.
[19]	"Identification of a cryptic nucleolar-localization signal in MDM2." Lohrum M.A.E., Ashcroft M., Kubbutat M.H.G., Vousden K.H. Nat. Cell Biol. 2:179-181(2000) [PubMed: 10707090] [Abstract] Cited for: NUCLEOLAR LOCALIZATION SIGNAL.
[20]	"Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase." Honda R., Yasuda H. Oncogene 19:1473-1476(2000) [PubMed: 10723139] [Abstract] Cited for: MUTAGENESIS OF CYS-449.
[21]	"A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter." Bres V., Kiernan R.E., Linares L.K., Chable-Bessia C., Plechakova O., Treand C., Emiliani S., Peloponese J.-M., Jeang K.-T., Coux O., Scheffner M., Benkirane M. Nat. Cell Biol. 5:754-761(2003) [PubMed: 12883554] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[22]	"{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." Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R.J., Larsson O. J. Biol. Chem. 280:24412-24419(2005) [PubMed: 15878855] [Abstract] Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[23]	"WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53." Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q. J. Biol. Chem. 280:43100-43108(2005) [PubMed: 16219768] [Abstract] Cited for: INTERACTION WITH WWOX AND TP53.
[24]	"MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein." Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X. Mol. Cell 20:699-708(2005) [PubMed: 16337594] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSMA3.
[25]	"Regulation of p53 and MDM2 activity by MTBP." Brady M., Vlatkovic N., Boyd M.T. Mol. Cell. Biol. 25:545-553(2005) [PubMed: 15632057] [Abstract] Cited for: FUNCTION, INTERACTION WITH MTBP, MUTAGENESIS OF CYS-464.
[26]	"Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2." Ding Y., Lee J.-F., Lu H., Lee M.-H., Yan D.-H. Mol. Cell. Biol. 26:1979-1996(2006) [PubMed: 16479015] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH PYHIN1, MUTAGENESIS OF CYS-464.
[27]	"CARF binds to three members (ARF, p53, and HDM2) of the p53 tumor-suppressor pathway." Kamrul H.M., Wadhwa R., Kaul S.C. Ann. N. Y. Acad. Sci. 1100:312-315(2007) [PubMed: 17460193] [Abstract] Cited for: INTERACTION WITH CDKN2AIP.
[28]	"A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability." Tompkins V.S., Hagen J., Frazier A.A., Lushnikova T., Fitzgerald M.P., di Tommaso A.D., Ladeveze V., Domann F.E., Eischen C.M., Quelle D.E. J. Biol. Chem. 282:1322-1333(2007) [PubMed: 17110379] [Abstract] Cited for: INTERACTION WITH TBRG1.
[29]	"AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and degradation and promote constitutive p53 turnover." Zweitzig D.R., Shcherbik N., Haines D.S. Mol. Biol. Cell 19:5029-5029(2008) [PubMed: 18768758] [Abstract] Cited for: INTERACTION WITH UBXN6.
[30]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY. Tissue: T-cell.
[31]	"Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain." Kussie P.H., Gorina S., Marechal V., Elenbaas B., Moreau J., Levine A.J., Pavletich N.P. Science 274:948-953(1996) [PubMed: 8875929] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-109 IN COMPLEX WITH P53.
[32]	"Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway." Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y. PLoS Biol. 4:228-239(2006) [PubMed: 16402859] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 224-232 IN COMPLEX WITH USP7, INTERACTION WITH USP7.
[33]	"Molecular recognition of p53 and MDM2 by USP7/HAUSP." Sheng Y., Saridakis V., Sarkari F., Duan S., Wu T., Arrowsmith C.H., Frappier L. Nat. Struct. Mol. Biol. 13:285-291(2006) [PubMed: 16474402] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 145-150 IN COMPLEX WITH USP7, INTERACTION WITH USP7.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Wikipedia

Mdm2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M92424 mRNA. Translation: AAA60568.1.
Z12020 mRNA. Translation: CAA78055.1.
U33199 mRNA. Translation: AAA75514.1.
U33200 mRNA. Translation: AAA75515.1.
U33201 mRNA. Translation: AAA75516.1.
U33202 mRNA. Translation: AAA75517.1.
U33203 mRNA. Translation: AAA75518.1.
AF092844 mRNA. Translation: AAL40179.1.
AF092845 mRNA. Translation: AAL40180.1.
AK290341 mRNA. Translation: BAF83030.1.
BT007258 mRNA. Translation: AAP35922.1.
AF527840 Genomic DNA. Translation: AAM78554.1.
AC025423 Genomic DNA. No translation available.
BC009893 mRNA. No translation available.
U28935 Genomic DNA. Translation: AAA82237.1.
U39736 Genomic DNA. Translation: AAA82061.1.
AF201370 mRNA. Translation: AAF42995.1.
AJ251943 Genomic DNA. Translation: CAB64448.1.

IPI

IPI00103723.
IPI00103724.
IPI00218551.
IPI00218552.
IPI00218553.
IPI00295694.
IPI00410597.
IPI00472971.
IPI00789663.
IPI00940767.
IPI00944540.

PIR

S24354.

RefSeq

NP_001138811.1.
NP_002383.2.
NP_006869.3.
NP_006870.3.
NP_006872.3.
NP_006873.3.

UniGene

Hs.484551

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RV1	X-ray	2.30	A/B/C	25-109	[»]
1T4E	X-ray	2.60	A/B	17-111	[»]
1T4F	X-ray	1.90	M	17-125	[»]
1YCR	X-ray	2.60	A	17-125	[»]
1Z1M	NMR	-	A	1-118	[»]
2AXI	X-ray	1.40	A	17-125	[»]
2C6A	NMR	-	A	290-335	[»]
2C6B	NMR	-	A	290-335	[»]
2F1Y	X-ray	1.70	A	-	[»]
2FOP	X-ray	2.10	B	145-150	[»]
2GV2	X-ray	1.80	A	17-125	[»]
2HDP	NMR	-	A/B	429-491	[»]
2VJE	X-ray	2.20	A/C	428-491	[»]
2VJF	X-ray	2.30	A/C	428-491	[»]
3EQS	X-ray	1.65	A	25-109	[»]
3G03	X-ray	1.80	A/C	18-125	[»]
3IUX	X-ray	1.65	A/C	25-109	[»]
3JZK	X-ray	2.10	A	17-111	[»]
3JZR	X-ray	2.10	A	17-125	[»]
3JZS	X-ray	1.78	A	24-109	[»]

DisProt

DP00334.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24224N.
DIP-392N.
DIP-920N.

IntAct

Q00987. 54 interactions.

STRING

Q00987.

PTM databases

PhosphoSite

Q00987.

Proteomic databases

PRIDE

Q00987.

Genome annotation databases

Ensembl

ENST00000311420; ENSP00000310742; ENSG00000135679; Homo sapiens. [Genome view]
ENST00000350057; ENSP00000266624; ENSG00000135679; Homo sapiens. [Genome view]
ENST00000462284; ENSP00000417281; ENSG00000135679; Homo sapiens. [Genome view]

GeneID

4193.

UCSC

uc001sui.1. human.
uc001sun.2. human.
uc001suo.1. human.
uc009zqx.1. human.
uc009zrg.1. human.
uc009zrh.1. human.

Organism-specific databases

CTD

4193.

GeneCards

GC12P067488.

H-InvDB

HIX0036698.

HGNC

HGNC:6973. MDM2.

HPA

CAB000086.
CAB016303.

MIM

164785. gene.

PharmGKB

PA30718.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12752.

HOVERGEN

Q00987.

InParanoid

Q00987.

OMA

PLPSHCN.

PhylomeDB

Q00987.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
ar_tf_pathway. Regulation of Androgen receptor activity.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_11061. Signalling by NGF.
REACT_13685. Synaptic Transmission.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpress

Q00987.

Bgee

Q00987.

Genevestigator

Q00987.

GermOnline

ENSG00000135679. Homo sapiens.

Family and domain databases

InterPro

IPR016495. p53_neg-reg_MDM_2/4.
IPR003121. SWIB_MDM2_domain.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
[Graphical view]

Gene3D

G3DSA:1.10.245.10. SWIB_MDM2. 1 hit.

Pfam

PF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]

PIRSF

PIRSF006748. p53_MDM_2/4. 1 hit.

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16526.

PMAP-CutDB

Q00987.

SOURCE

Search...

Entry information

Entry name

MDM2_HUMAN

Accession

Primary (citable) accession number: Q00987
Secondary accession number(s): A6NL51 , A8K2S6, Q13226, Q13297, Q13298, Q13299, Q13300, Q13301, Q53XW0, Q71TW9, Q8WYJ1, Q8WYJ2, Q9UGI3, Q9UMT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	February 9, 2010
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.