ID Q6P3Q9_XENTR Unreviewed; 482 AA.
AC Q6P3Q9; F6WMQ0; F7C835;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|ARBA:ARBA00018786, ECO:0000256|PIRNR:PIRNR006748};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|PIRNR:PIRNR006748};
GN Name=mdm2 {ECO:0000313|EMBL:AAH63898.1,
GN ECO:0000313|RefSeq:NP_989243.1, ECO:0000313|Xenbase:XB-GENE-482711};
GN Synonyms=hdm2 {ECO:0000313|RefSeq:NP_989243.1}, xdm-2
GN {ECO:0000313|RefSeq:NP_989243.1}, Xdm2
GN {ECO:0000313|RefSeq:NP_989243.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH63898.1, ECO:0000313|Proteomes:UP000008143};
RN [1] {ECO:0000313|RefSeq:NP_989243.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH63898.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH63898.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 414-482 IN COMPLEX WITH ZN(2+).
RX PubMed=33450248; DOI=10.1016/j.jmb.2021.166807;
RA Magnussen H.M., Huang D.T.;
RT "Identification of a Catalytic Active but Non-Aggregating MDM2 RING Domain
RT Variant.";
RL J. Mol. Biol. 433:166807-166807(2021).
RN [4] {ECO:0000313|RefSeq:NP_989243.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|PIRNR:PIRNR006748};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006748}. Nucleus, nucleoplasm
CC {ECO:0000256|PIRNR:PIRNR006748}. Nucleus, nucleolus
CC {ECO:0000256|PIRNR:PIRNR006748}.
CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family.
CC {ECO:0000256|ARBA:ARBA00005803, ECO:0000256|PIRNR:PIRNR006748}.
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DR EMBL; BC063898; AAH63898.1; -; mRNA.
DR RefSeq; NP_001231689.1; NM_001244760.1.
DR RefSeq; NP_989243.1; NM_203912.2.
DR PDB; 7AHY; X-ray; 2.53 A; AAA/BBB=414-482.
DR PDB; 7AHZ; X-ray; 1.82 A; AAA/DDD/GGG/JJJ=414-482.
DR GeneID; 394853; -.
DR KEGG; xtr:394853; -.
DR AGR; Xenbase:XB-GENE-482711; -.
DR Xenbase; XB-GENE-482711; mdm2.
DR HOGENOM; CLU_043544_2_0_1; -.
DR OrthoDB; 2916169at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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 CDD; cd17672; MDM2; 1.
DR CDD; cd16783; mRING-HC-C2H2C4_MDM2; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR028340; Mdm2.
DR InterPro; IPR044080; MDM2_mRING-HC-C2H2C4.
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; PTHR46858:SF13; E3 UBIQUITIN-PROTEIN LIGASE MDM2; 1.
DR PANTHER; PTHR46858; OS05G0521000 PROTEIN; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR PIRSF; PIRSF500700; MDM2; 1.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 2.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR006748};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006748}; Nucleus {ECO:0000256|PIRNR:PIRNR006748};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006748};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR006748};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006748};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 22..105
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 299..328
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 429..470
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 208..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7AHY, ECO:0007829|PDB:7AHZ"
SQ SEQUENCE 482 AA; 54657 MW; 4CD1ED6DE5C01EF0 CRC64;
MNLTSTTNCL ENSHIMASDQ EKLVKPTPLL LSLLKSAGAQ KETFTMKEVI YHLGQYIMAK
QLYDEKQQHI VHCSNDPLGE LFGVQEFSVK EPRRLYAMIS RNLVSAAVKE SSEDVYGNHV
CSFPDKQKSQ KELLQELPEK VIAPAYDSKP CNSSQRKSNN ETVCVEEISS VDHPAEQQRK
RHKSDSISLT FDESLSWWVI SGLRCDRNSS ESTDTSSNPD PEKHTVDDNS EQDSDSDQFS
VEFEVESVYS DDYSPSGDEH CISEEEEEDE INDEVYQVTI YEAEDSETNA FDVDTEISEA
DYWKCSECEE INPPLPSHCH RCWALRKDWL PEESKKELHP SKRKRMETEE DEGFDVPDCK
KSKLTSSQDT NIDKKEAESI QISESQETED CSQPSTSGSI ASCSQEATKE DTRDESMEPS
LPLTSVEPCV ICQTRPKNGC IVHGRTGHLM ACYTCAKKLK KRNKPCPVCR EPIQMIVLTY
FS
//
