Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

E3 ubiquitin-protein ligase Mdm2 (EC 2 3 2 27) (Double minute 2 protein) (Cdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)

 MDM2_CANLF              Reviewed;         487 AA.
P56950; Q95KN5;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 1.
28-MAR-2018, entry version 141.
RecName: Full=E3 ubiquitin-protein ligase Mdm2;
EC=2.3.2.27 {ECO:0000250|UniProtKB:P23804};
AltName: Full=Double minute 2 protein;
Short=Cdm2;
AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000305};
AltName: Full=p53-binding protein Mdm2;
Name=MDM2;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-484.
PubMed=10754200; DOI=10.1016/S0304-3835(99)00427-9;
Nasir L., Burr P.D., McFarlane S.T., Gault E., Thompson H.,
Argyle D.J.;
"Cloning, sequence analysis and expression of the cDNAs encoding the
canine and equine homologues of the mouse double minute 2 (mdm2)
proto-oncogene.";
Cancer Lett. 152:9-13(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MDM2 AND MDM2-ALPHA).
PubMed=10597303; DOI=10.1038/sj.onc.1203182;
Veldhoen N., Metcalfe S., Milner J.;
"A novel exon within the mdm2 gene modulates translation initiation in
vitro and disrupts the p53-binding domain of mdm2 protein.";
Oncogene 18:7026-7033(1999).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of p53/TP53, leading to its degradation by the proteasome.
Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and
apoptosis by binding its transcriptional activation domain. Also
acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the
nuclear export of p53/TP53. Promotes proteasome-dependent
ubiquitin-independent degradation of retinoblastoma RB1 protein.
Inhibits DAXX-mediated apoptosis by inducing its ubiquitination
and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53
complex involved in stabilizing p53/TP53. Also component of the
TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA
damage response pathways. Mediates ubiquitination and subsequent
proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R
and SNAI1 and promotes them to proteasomal degradation.
Ubiquitinates DCX, leading to DCX degradation and reduction of the
dendritic spine density of olfactory bulb granule cells.
Ubiquitinates DLG4, leading to proteasomal degradation of DLG4
which is required for AMPA receptor endocytosis.
{ECO:0000250|UniProtKB:P23804, ECO:0000250|UniProtKB:Q00987}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:P23804}.
-!- SUBUNIT: Interacts with p53/TP53, TP73/p73, RBL5 and RP11. Binds
specifically to RNA. Can interact with RB1, E1A-associated protein
EP300 and the E2F1 transcription factor. Forms a ternary complex
with p53/TP53 and WWOX. Interacts with CDKN2AIP, RFWD3, USP7,
PYHIN1 and RBBP6. Interacts with ARRB1 and ARRB2. Interacts with
PSMA3. Found in a trimeric complex with MDM2, MDM4 and USP2.
Interacts with USP2 (via N-terminus and C-terminus). Interacts
with MDM4. Part of a complex with MDM2, DAXX, RASSF1 and USP7.
Part of a complex with DAXX, MDM2 and USP7. Interacts directly
with DAXX and USP7. Interacts (via C-terminus) with RASSF1 isoform
A (via N-terminus); the interaction is independent of TP53.
Interacts with APEX1; leading to its ubiquitination and
degradation. Interacts with RYBP; this inhibits ubiquitination of
TP53. Identified in a complex with RYBP and p53/TP53. Also
component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in
regulating p53/TP53 stabilization and activity. Binds directly
both p53/TP53 and TRIM28. Component of the TRIM28/KAP1-ERBB4-MDM2
complex involved in connecting growth factor responses with DNA
damage. Interacts directly with both TRIM28 and ERBB4 in the
complex. Interacts with DYRK2. Interacts with IGF1R. Interacts
with TRIM13; the interaction ubiquitinates MDM2 leading to its
proteasomal degradation. Interacts with SNAI1; this interaction
promotes SNAI1 ubiquitination. Interacts with NOTCH1 (via
intracellular domain). Interacts with FHIT. Interacts with RFFL
and RNF34; the interaction stabilizes MDM2. Interacts with
CDK5RAP3 and CDKN2A/ARF; form a ternary complex involved in
regulation of p53/TP53. Interacts with MTA1. Interacts with AARB2.
Interacts with MTBP. Interacts with PML. Interacts with RPL11.
Interacts with TBRG1. Interacts with the 5S RNP which is composed
of the 5S RNA, RPL5 and RPL11; the interaction is direct occurs in
the nucleoplasm and negatively regulates MDM2-mediated TP53
ubiquitination and degradation. Interacts with ADGRB1; the
interaction results in inhibition of MDM2-mediated ubiquitination
and degradation of DLG4/PSD95, promoting DLG4 stability and
regulating synaptic plasticity. Interacts with RPL23A; this
interaction may promote p53/TP53 polyubiquitination (By
similarity). {ECO:0000250|UniProtKB:P23804,
ECO:0000250|UniProtKB:Q00987}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
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. Colocalizes with RASSF1 isoform A in the nucleus
(By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Mdm2;
IsoId=P56950-1; Sequence=Displayed;
Name=Mdm2-alpha;
IsoId=P56950-2; Sequence=VSP_003206;
-!- TISSUE SPECIFICITY: Isoform Mdm2-alpha is present in lymphoid and
testicular tissues.
-!- 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 (By similarity). Interacts with IGF1R (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylation on Ser-166 by SGK1 activates ubiquitination
of p53/TP53. Phosphorylated at multiple sites near the RING domain
by ATM upon DNA damage; this prevents oligomerization and E3
ligase processivity and impedes constitutive p53/TP53 degradation
(By similarity). {ECO:0000250}.
-!- PTM: Autoubiquitination leads to proteasomal degradation;
resulting in p53/TP53 activation it may be regulated by SFN. Also
ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its
accumulation and increases deubiquitination and degradation of
p53/TP53. Deubiquitinated by USP7 leading to its stabilization.
-!- SIMILARITY: Belongs to the MDM2/MDM4 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF100705; AAF67833.1; -; mRNA.
EMBL; AF322416; AAG42840.1; -; mRNA.
RefSeq; NP_001003103.1; NM_001003103.2.
UniGene; Cfa.702; -.
ProteinModelPortal; P56950; -.
SMR; P56950; -.
STRING; 9615.ENSCAFP00000000608; -.
BindingDB; P56950; -.
ChEMBL; CHEMBL3600278; -.
PaxDb; P56950; -.
GeneID; 403693; -.
KEGG; cfa:403693; -.
CTD; 4193; -.
eggNOG; ENOG410IGXG; Eukaryota.
eggNOG; ENOG41125MP; LUCA.
HOGENOM; HOG000293341; -.
HOVERGEN; HBG013472; -.
InParanoid; P56950; -.
KO; K06643; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IEA:InterPro.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
Gene3D; 1.10.245.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR028340; Mdm2.
InterPro; IPR015459; MDM2_E3_ligase.
InterPro; IPR016495; p53_neg-reg_MDM_2/4.
InterPro; IPR036885; SWIB_MDM2_dom_sf.
InterPro; IPR003121; SWIB_MDM2_domain.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR13844:SF15; PTHR13844:SF15; 1.
Pfam; PF02201; SWIB; 1.
Pfam; PF00641; zf-RanBP; 1.
PIRSF; PIRSF500700; MDM2; 1.
PIRSF; PIRSF006748; p53_MDM_2/4; 1.
SUPFAM; SSF47592; SSF47592; 2.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Cytoplasm; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 487 E3 ubiquitin-protein ligase Mdm2.
/FTId=PRO_0000157329.
DOMAIN 27 107 SWIB.
ZN_FING 299 328 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 434 475 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 150 230 Interaction with PYHIN1 and necessary for
interaction with RFFL and RNF34.
{ECO:0000250|UniProtKB:Q00987}.
REGION 170 306 Interaction with MTBP. {ECO:0000250}.
REGION 210 304 ARF-binding.
REGION 223 232 Interaction with USP7. {ECO:0000250}.
REGION 242 331 Region II.
MOTIF 179 185 Nuclear localization signal.
{ECO:0000255}.
MOTIF 190 202 Nuclear export signal.
MOTIF 462 469 Nucleolar localization signal.
{ECO:0000255}.
COMPBIAS 210 215 Poly-Ser.
COMPBIAS 243 301 Asp/Glu-rich (acidic).
MOD_RES 166 166 Phosphoserine; by SGK1.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:P23804}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 382 382 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 391 391 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 403 403 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 415 415 Phosphothreonine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
MOD_RES 425 425 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q00987}.
VAR_SEQ 1 61 Missing (in isoform Mdm2-alpha).
{ECO:0000303|PubMed:10597303}.
/FTId=VSP_003206.
CONFLICT 11 11 G -> D (in Ref. 2; AAG42840).
{ECO:0000305}.
CONFLICT 238 239 QD -> HH (in Ref. 2; AAG42840).
{ECO:0000305}.
SEQUENCE 487 AA; 54696 MW; 60CDB470A32A8E69 CRC64;
MCNTNMSVST GGAVSTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVIFYLGQY
IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY TMIYRNLVVV NQHEPSDSGT
SVSENSCHRE GGSDQKDPVQ ELQEEKPSSS DLISRPSTSS RRRTISETEE HADDLPGERQ
RKRHKSDSIS LSFDESLALC VIREICCERS SSSESTGTPS NPDLDAGVSE HSGDWLDQDS
VSDQFSVEFE VESLDSEDYS LSEEGQELSD EDDEVYRVTV YQAGESDTDS FEEDPEISLA
DYWKCTSCNE MNPPLPPHCN RCWALRENWL PEDKGKIPEK ATPENSTQVE EGFDVPDCKK
AAASDSRESC AEEIDDKITQ ASHSQESEDY SQPSTSNSII YSSQEDVKEF EREETQDKEE
IVESSFPLNA IEPCVICQGR PKNGCIVHGK TGHLMACFTC AKKLKKRNKP CPVCRQPIQM
IVLTYFP


Related products :

Catalog number Product name Quantity
15-288-21160 Ubiquitin-protein ligase E3 Mdm2 - EC 6.3.2.-; p53-binding protein Mdm2; Oncoprotein Mdm2; Double minute 2 protein; Hdm2 Polyclonal 0.1 mg
15-288-21160 Ubiquitin-protein ligase E3 Mdm2 - EC 6.3.2.-; p53-binding protein Mdm2; Oncoprotein Mdm2; Double minute 2 protein; Hdm2 Polyclonal 0.05 mg
18-783-75624 RABBIT ANTI MOUSE MDM2 (pSer185) - EC 6.3.2.-; p53-binding protein Mdm2; Oncoprotein Mdm2; Double minute 2 protein Polyclonal 0.05 mg
CSB-EL013626MO Mouse E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit SpeciesMouse 96T
CSB-EL013626HU Human E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit SpeciesHuman 96T
CSB-EL013626HO Horse E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit SpeciesHorse 96T
CSB-EL013626CA Cat E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit SpeciesCat 96T
CSB-EL013626DO Dog E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit SpeciesDog 96T
CSB-EL013626MO Mouse E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit 96T
CSB-EL013626HU Human E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit 96T
MDM2_MOUSE ELISA Kit FOR E3 ubiquitin-protein ligase Mdm2; organism: Mouse; gene name: Mdm2 96T
CSB-EL013626CA Cat E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit 96T
CSB-EL013626DO Dog E3 ubiquitin-protein ligase Mdm2(MDM2) ELISA kit 96T
18-783-76454 RABBIT ANTI HUMAN MTBP (aa122-139) - p53-binding protein Mdm2-binding protein; Double minute 2 protein-binding protein Polyclonal 0.1 mg
DL-MDM2-Mu Mouse Mdm2 p53 Binding Protein Homolog (MDM2) ELISA Kit 96T
DL-MDM2-Hu Human Mdm2 p53 Binding Protein Homolog (MDM2) ELISA Kit 96T
GWB-BF9EAB Mdm2 Transformed 3T3 Cell Double Minute 2 (MDM2 MTBP) Rabbit anti-Human Polyclonal (aa122-139) Antibody
MTBS1 MTBP Gene Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa
CSB-EL015131HU Human Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa (MTBP) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015131MO Mouse Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa (MTBP) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
20-003-40022 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Monoclonal 0.05 mg Aff Pur
20-003-40022 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Monoclonal 0.1 mg Protein A
18-003-42909 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Polyclonal 0.1 mg Protein A
18-003-42909 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Polyclonal 0.05 mg Aff Pur
CSB-EL013626DO Dog Mdm2 p53 binding protein homolog (mouse) (MDM2) ELISA kit, Species Dog, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur