ID A0A2K6KDT4_RHIBE Unreviewed; 466 AA.
AC A0A2K6KDT4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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|Ensembl:ENSRBIP00000009431.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000009431.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000009431.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000009431.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6KDT4; -.
DR Ensembl; ENSRBIT00000033047.1; ENSRBIP00000009431.1; ENSRBIG00000028561.1.
DR GeneTree; ENSGT00530000063539; -.
DR Proteomes; UP000233180; Unplaced.
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:0006915; P:apoptotic process; 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 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; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR PIRSF; PIRSF500700; MDM2; 2.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 2.
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 3: Inferred from homology;
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:UP000233180};
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 1..84
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 274..303
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 413..454
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 116..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 52407 MW; 5788C92A08B35D93 CRC64;
MCNTNMSVPT DGAVTTSQIP ASEQETLVLF YLGQYIMTKR LYDEKQQHIV YCSNDLLGDL
FGVPSFSVKE HRKIYTMIYR NLVVVNQQES SDSGTSVSEN RCHLEGGSDQ KDLVQELQEE
KPSSSHLVSR PSTSSRRRAI SETEENSDEL SGERQRKRHK SDSISLSFDE SLALCVIREI
CCERSSSSES TGTPSNPDLD AGVSEHSGDW LDQDSVSDQF SVEFEVESLD SEDYSLSEEA
QELSDEDDEV YRVTVYQAGE SDTDSFEEDP EISLADYWKC TSCNEMNPPL PSHCNRCWAL
RENWLPEDKG KDKGEISEKA KLENSTQAEE GFDVPDCKKT IVNDSKESCV EENDDKITQA
SQSQESEDYS QPSTSSSIIY SSQEDVKEFE REETQDKEES VESSLPLNAI EPCVICQGRP
KNGCIVHGKT GHLMACFTCA KKLKKRNKPC PVCRQPIQMI VLTYFP
//
