MDM4_BOVIN
ID MDM4_BOVIN Reviewed; 491 AA.
AC Q2HJ21;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein Mdm4;
DE AltName: Full=Double minute 4 protein;
DE AltName: Full=Mdm2-like p53-binding protein;
DE AltName: Full=Protein Mdmx;
DE AltName: Full=p53-binding protein Mdm4;
GN Name=MDM4; Synonyms=MDMX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest
CC and apoptosis by binding its transcriptional activation domain.
CC Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of
CC TP53 while maintaining suppression of TP53 transactivation and
CC apoptotic functions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MDM2, TP53, TP73 and USP2. Found in a trimeric
CC complex with USP2, MDM2 and MDM4. Interacts (phosphorylated) with
CC YWHAG; negatively regulates MDM4 activity toward TP53 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-368 promotes interaction
CC with YWHAG and subsequent ubiquitination and degradation.
CC Phosphorylation at Ser-342 also induces ubiquitination and degradation
CC but to a lower extent (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on
CC the other hand stabilizes the MDM4 protein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family. {ECO:0000305}.
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DR EMBL; BC113350; AAI13351.1; -; mRNA.
DR RefSeq; NP_001039634.1; NM_001046169.1.
DR AlphaFoldDB; Q2HJ21; -.
DR SMR; Q2HJ21; -.
DR STRING; 9913.ENSBTAP00000008209; -.
DR PaxDb; Q2HJ21; -.
DR PRIDE; Q2HJ21; -.
DR GeneID; 514225; -.
DR KEGG; bta:514225; -.
DR CTD; 4194; -.
DR eggNOG; ENOG502QQNV; Eukaryota.
DR InParanoid; Q2HJ21; -.
DR OrthoDB; 1329283at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR Gene3D; 1.10.245.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015458; MDM4.
DR InterPro; IPR016495; p53_neg-reg_MDM_2/4.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13844:SF20; PTHR13844:SF20; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR PIRSF; PIRSF500699; MDM4; 1.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..491
FT /note="Protein Mdm4"
FT /id="PRO_0000331515"
FT DOMAIN 25..108
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT ZN_FING 300..329
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 438..479
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..491
FT /note="Necessary for interaction with USP2"
FT /evidence="ECO:0000250"
FT MOTIF 443..446
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 342
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:O15151"
FT MOD_RES 368
FT /note="Phosphoserine; by CHEK1 and CHEK2"
FT /evidence="ECO:0000250|UniProtKB:O15151"
SQ SEQUENCE 491 AA; 55180 MW; BF3E7B6DF2B6A8BE CRC64;
MTSFSTSAPC SAPDSARRIS PEQTNQVRPK LPLLKILQAA GAQGEMFTVK EVMHYLGQYI
MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTLA TAATDAAQTL
AIAQEHSMDI PSQDHLKQSV EESSNSRKRT EEGNIPTLPT SQYKCKNSRE DEDLVANLTQ
EETSRLDLGF EEWDVAGLPW WFLGNLRNNY TPRSNGSTDL QTNQDIGTAI VSDTTDDLWF
LNESVSEQFG VGKKVEAADP EQTSEEVGKL IDKKVTEVGK NDDLEDPKSI SDDTDIEVTS
EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP EKQESEGVDV
PDCRRTVSAP VVRPKDTYVK EESSKHFDPC NSVEFLDLAH SSESQETISS MGEQSDNLFE
QRKDTENMED CQNLLKPCSL CEKRPRNGNI IHGRTGHLVT CFHCARRLKK AGASCPICKK
EIQLVIKVFV A
