O15151 (MDM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein Mdm4

Alternative name(s):
Double minute 4 protein
Mdm2-like p53-binding protein
Protein Mdmx
p53-binding protein Mdm4

Gene names

Name:	MDM4
Synonyms:	MDMX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. Ref.9 Ref.10
Subunit structure	Interacts with MDM2, TP53, TP73 and USP2. Found in a trimeric complex with UPB2, MDM2 and MDM4. Interacts (phosphorylated) with YWHAG; negatively regulates MDM4 activity toward TP53. Ref.9 Ref.10 Ref.11
Subcellular location	Nucleus.
Tissue specificity	Expressed in all tissues tested with high levels in thymus.
Induction	Down-regulated by cisplatin (at protein level). Ref.11
Domain	Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.
Post-translational modification	Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent. Ref.9 Ref.10 Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein. Ref.9 Ref.11
Sequence similarities	Belongs to the MDM2/MDM4 family. Contains 1 RanBP2-type zinc finger. Contains 1 RING-type zinc finger. Contains 1 SWIB domain.
Mass spectrometry	Molecular mass is 54863.3 Da from positions 1 - 490. Determined by MALDI. Ref.12

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G0 to G1 transition Inferred from expression pattern PubMed 12101245. Source: UniProtKB apoptotic process Inferred from expression pattern PubMed 14660608. Source: UniProtKB cell proliferation Inferred from expression pattern PubMed 12101245. Source: UniProtKB cellular response to hypoxia Inferred from expression pattern PubMed 20810912. Source: UniProtKB negative regulation of apoptotic process Inferred from electronic annotation. Source: InterPro negative regulation of cell cycle arrest Inferred from electronic annotation. Source: InterPro negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc negative regulation of protein catabolic process Inferred from mutant phenotype Ref.8. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara protein complex assembly Inferred from direct assay Ref.8. Source: UniProtKB protein stabilization Inferred from expression pattern Ref.8. Source: UniProtKB
Cellular_component	nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	zinc ion binding Traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	6	EBI-398437,EBI-389668
MKRN3	Q13064	2	EBI-398437,EBI-2340269
TP53	P04637	4	EBI-398437,EBI-366083
UBE2D2	P62837	2	EBI-398437,EBI-347677

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O15151-1)

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 2 (identifier: O15151-2)

Also known as: MDMX-S;

The sequence of this isoform differs from the canonical sequence as follows:
     109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTARCNRILQSQKKN

Note: No experimental confirmation available.

Isoform 3 (identifier: O15151-3)

Also known as: MDMX;

The sequence of this isoform differs from the canonical sequence as follows:
     109-490: LATATTDAAQ...IQLVIKVFIA → SASNNTDAAQTLALAQDHT

Note: No experimental confirmation available.

Isoform HDMX211 (identifier: O15151-4)

The sequence of this isoform differs from the canonical sequence as follows:
     27-352: Missing.

Note: Cancer-specific isoform, may counteract MDM2/MDM4-mediated p53 degradation.

Isoform 5 (identifier: O15151-5)

The sequence of this isoform differs from the canonical sequence as follows:
     225-274: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Protein Mdm4

PRO_0000157336

Regions

Domain

26 – 106

81

SWIB

Zinc finger

300 – 329

30

RanBP2-type

Zinc finger

437 – 478

42

RING-type

Region

246 – 332

87

Region II

Region

393 – 490

98

Necessary for interaction with UBP2

Motif

442 – 445

4

Nuclear localization signal Potential

Compositional bias

243 – 308

66

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

342

1

Phosphoserine; by CHEK2 Ref.9

Modified residue

367

1

Phosphoserine; by CHEK1 and CHEK2 Ref.9 Ref.10

Natural variations

Alternative sequence

27 – 352

326

Missing in isoform HDMX211.

VSP_042563

Alternative sequence

109 – 490

382

LATAT…KVFIA → SASNNTARCNRILQSQKKN in isoform 2.

VSP_035669

Alternative sequence

109 – 490

382

LATAT…KVFIA → SASNNTDAAQTLALAQDHT in isoform 3.

VSP_035670

Alternative sequence

225 – 274

50

Missing in isoform 5.

VSP_043145

Natural variant

175

1

I → T. Ref.4
Corresponds to variant rs4252716 [ dbSNP | Ensembl ].

VAR_017106

Natural variant

406

1

T → I. Ref.4
Corresponds to variant rs4252741 [ dbSNP | Ensembl ].

VAR_017107

Experimental info

Mutagenesis

437

1

C → G: Fails to interact with MDM2. Ref.8

Sequence conflict

94

1

D → N in AAB62928. Ref.1

Secondary structure

1

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490

Helix Strand Turn

Details...

Beta strand

27 – 29

3

Helix

31 – 39

9

Helix

49 – 62

14

Beta strand

70 – 75

6

Helix

80 – 85

6

Beta strand

88 – 91

4

Helix

96 – 105

10

Beta strand

106 – 109

4

Beta strand

307 – 309

3

Turn

321 – 323

3

Helix

431 – 434

4

Turn

438 – 440

3

Beta strand

441 – 445

5

Beta strand

447 – 451

5

Beta strand

454 – 459

6

Helix

461 – 469

9

Turn

475 – 477

3

Beta strand

483 – 489

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 415E6FA5A0C69857	FASTA	490	54,864
	10 20 30 40 50 60 MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK EVMHYLGQYI 70 80 90 100 110 120 MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTLA TATTDAAQTL 130 140 150 160 170 180 ALAQDHSMDI PSQDQLKQSA EESSTSRKRT TEDDIPTLPT SEHKCIHSRE DEDLIENLAQ 190 200 210 220 230 240 DETSRLDLGF EEWDVAGLPW WFLGNLRSNY TPRSNGSTDL QTNQDVGTAI VSDTTDDLWF 250 260 270 280 290 300 LNESVSEQLG VGIKVEAADT EQTSEEVGKV SDKKVIEVGK NDDLEDSKSL SDDTDVEVTS 310 320 330 340 350 360 EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP EKENEGNDVP 370 380 390 400 410 420 DCRRTISAPV VRPKDAYIKK ENSKLFDPCN SVEFLDLAHS SESQETISSM GEQLDNLSEQ 430 440 450 460 470 480 RTDTENMEDC QNLLKPCSLC EKRPRDGNII HGRTGHLVTC FHCARRLKKA GASCPICKKE 490 IQLVIKVFIA
	Isoform 2 (MDMX-S) [UniParc]. Checksum: 59649D26B113EFB4	FASTA	127	14,185
	10 20 30 40 50 60 MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK EVMHYLGQYI 70 80 90 100 110 120 MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTSA SNNTARCNRI LQSQKKN
	Isoform 3 (MDMX) [UniParc]. Checksum: 0A00E52B32331543	FASTA	127	13,981
	10 20 30 40 50 60 MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK EVMHYLGQYI 70 80 90 100 110 120 MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTSA SNNTDAAQTL ALAQDHT
	Isoform HDMX211 [UniParc]. Checksum: 1C39025CBD527C11	FASTA	164	18,195
	10 20 30 40 50 60 MTSFSTSAQC STSDSACRIS PGQINQENEG NDVPDCRRTI SAPVVRPKDA YIKKENSKLF 70 80 90 100 110 120 DPCNSVEFLD LAHSSESQET ISSMGEQLDN LSEQRTDTEN MEDCQNLLKP CSLCEKRPRD 130 140 150 160 GNIIHGRTGH LVTCFHCARR LKKAGASCPI CKKEIQLVIK VFIA
	Isoform 5 [UniParc]. Checksum: BB377C938A8C3D1C	FASTA	440	49,541
	10 20 30 40 50 60 MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK EVMHYLGQYI 70 80 90 100 110 120 MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTLA TATTDAAQTL 130 140 150 160 170 180 ALAQDHSMDI PSQDQLKQSA EESSTSRKRT TEDDIPTLPT SEHKCIHSRE DEDLIENLAQ 190 200 210 220 230 240 DETSRLDLGF EEWDVAGLPW WFLGNLRSNY TPRSNGSTDL QTNQVIEVGK NDDLEDSKSL 250 260 270 280 290 300 SDDTDVEVTS EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP 310 320 330 340 350 360 EKENEGNDVP DCRRTISAPV VRPKDAYIKK ENSKLFDPCN SVEFLDLAHS SESQETISSM 370 380 390 400 410 420 GEQLDNLSEQ RTDTENMEDC QNLLKPCSLC EKRPRDGNII HGRTGHLVTC FHCARRLKKA 430 440 GASCPICKKE IQLVIKVFIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and identification of the human homolog of a new p53-binding protein, Mdmx." Shvarts A., Bazuine M., Dekker P., Ramos Y.F.M., Steegenga W.T., Merckx G., van Ham R.C.A., van der Houven van Oordt W., van der Eb A.J., Jochemsen A.G. Genomics 43:34-42(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon tumor.
[2]	"Identification of an aberrantly spliced form of HDMX in human tumors: a new mechanism for HDM2 stabilization." Giglio S., Mancini F., Gentiletti F., Sparaco G., Felicioni L., Barassi F., Martella C., Prodosmo A., Iacovelli S., Buttitta F., Farsetti A., Soddu S., Marchetti A., Sacchi A., Pontecorvi A., Moretti F. Cancer Res. 65:9687-9694(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HDMX211).
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Gastric mucosa.
[4]	NIEHS SNPs program Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-175 AND ILE-406.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). Tissue: Brain and Testis.
[7]	"Identification of a domain within MDMX-S that is responsible for its high affinity interaction with p53 and high-level expression in mammalian cells." Rallapalli R., Strachan G., Tuan R.S., Hall D.J. J. Cell. Biochem. 89:563-575(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
[8]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-437.
[9]	"ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage." Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J. EMBO J. 24:3411-3422(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-342 AND SER-367 BY CHEK2, UBIQUITINATION, INTERACTION WITH MDM2.
[10]	"14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation." Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H. EMBO J. 25:1207-1218(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TP53 ACTIVATION, PHOSPHORYLATION AT SER-367 BY CHEK1, INTERACTION WITH YWHAG.
[11]	"MdmX is a substrate for the deubiquitinating enzyme USP2a." Allende-Vega N., Sparks A., Lane D.P., Saville M.K. Oncogene 29:432-441(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH USP2 AND MDM2, INDUCTION, UBIQUITINATION, DEUBIQUITINATION BY USP2.
[12]	"Cluster analysis of an extensive human breast cancer cell line protein expression map database." Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J. Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Mammary cancer.
[13]	"Solution structure of the ZF-RANBP domain of p53-binding protein MDM4." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 300-340.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF007111 mRNA. Translation: AAB62928.1.
AY923176 mRNA. Translation: AAY22054.1.
AK223228 mRNA. Translation: BAD96948.1.
AY207458 Genomic DNA. Translation: AAO13494.1.
AL512306 Genomic DNA. Translation: CAI14100.1.
BC067299 mRNA. Translation: AAH67299.1.
BC105106 mRNA. Translation: AAI05107.1.

IPI

IPI00005170.
IPI00513968.
IPI00655963.
IPI00914644.
IPI00914667.

RefSeq

NP_001191100.1. NM_001204171.1.
NP_001191101.1. NM_001204172.1.
NP_002384.2. NM_002393.4.

UniGene

Hs.497492.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CR8	NMR	-	A	300-339	[»]
2VJE	X-ray	2.20	B/D	428-490	[»]
2VJF	X-ray	2.30	B/D	428-490	[»]
2VYR	X-ray	2.00	A/B/C/D	16-116	[»]
3DAB	X-ray	1.90	A/C/E/G	23-111	[»]
3EQY	X-ray	1.63	A/B	24-108	[»]
3FDO	X-ray	1.40	A	23-111	[»]
3FE7	X-ray	1.35	A	14-111	[»]
3FEA	X-ray	1.33	A	14-111	[»]
3JZO	X-ray	1.80	A	23-111	[»]
3JZP	X-ray	1.74	A	23-111	[»]
3JZQ	X-ray	1.80	A/B	23-111	[»]
3LBJ	X-ray	1.50	E	23-111	[»]
3U15	X-ray	1.80	A/B/C/D	14-111	[»]

ProteinModelPortal

O15151.

SMR

O15151. Positions 26-108, 301-344, 429-490.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24199N.

IntAct

O15151. 12 interactions.

MINT

MINT-113852.

STRING

9606.ENSP00000356150.

PTM databases

PhosphoSite

O15151.

Proteomic databases

PaxDb

O15151.

PRIDE

O15151.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367182; ENSP00000356150; ENSG00000198625.
ENST00000367183; ENSP00000356151; ENSG00000198625.
ENST00000454264; ENSP00000396840; ENSG00000198625.

GeneID

4194.

KEGG

hsa:4194.

UCSC

uc001hba.3. human.

Organism-specific databases

CTD

4194.

GeneCards

GC01P204486.

HGNC

HGNC:6974. MDM4.

HPA

HPA018919.

MIM

602704. gene.

neXtProt

NX_O15151.

PharmGKB

PA30719.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46328.

HOGENOM

HOG000293341.

HOVERGEN

HBG013472.

InParanoid

O15151.

KO

K10127.

OMA

CNSVEFL.

OrthoDB

EOG4CZBFT.

PhylomeDB

O15151.

Gene expression databases

ArrayExpress

O15151.

Bgee

O15151.

CleanEx

HS_MDM4.

Genevestigator

O15151.

GermOnline

ENSG00000198625. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR015458. MDM4.
IPR016495. p53_neg-reg_MDM_2/4.
IPR003121. SWIB_MDM2_domain.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

PANTHER

PTHR10360:SF10. PTHR10360:SF10. 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.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

SUPFAM

SSF47592. MDM2. 1 hit.

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

BindingDB

O15151.

ChEMBL

CHEMBL1255126.

ChiTaRS

MDM4. human.

EvolutionaryTrace

O15151.

GenomeRNAi

4194.

NextBio

16538.

PMAP-CutDB

O15151.

SOURCE

Search...

Entry information

Entry name

MDM4_HUMAN

Accession

Primary (citable) accession number: O15151
Secondary accession number(s): Q2M2Y2 , Q32SL2, Q6GS18, Q8IV83

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	September 27, 2005
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.