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Database: UniProt
Entry: G7PI02_MACFA
LinkDB: G7PI02_MACFA
Original site: G7PI02_MACFA 
ID   G7PI02_MACFA            Unreviewed;       442 AA.
AC   G7PI02;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|ARBA:ARBA00018786};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=Double minute 2 protein {ECO:0000256|ARBA:ARBA00032811};
DE   AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000256|ARBA:ARBA00032614};
DE   AltName: Full=p53-binding protein Mdm2 {ECO:0000256|ARBA:ARBA00030148};
GN   Name=MDM2 {ECO:0000313|Ensembl:ENSMFAP00000031284.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000031284.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000031284.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000031284.2}
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus,
CC       nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC   -!- SIMILARITY: Belongs to the MDM2/MDM4 family.
CC       {ECO:0000256|ARBA:ARBA00005803}.
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DR   AlphaFoldDB; G7PI02; -.
DR   Ensembl; ENSMFAT00000005499.2; ENSMFAP00000031284.2; ENSMFAG00000042359.2.
DR   VEuPathDB; HostDB:ENSMFAG00000042359; -.
DR   eggNOG; ENOG502QQNV; Eukaryota.
DR   GeneTree; ENSGT00530000063539; -.
DR   OrthoDB; 2916169at2759; -.
DR   Proteomes; UP000233100; Chromosome 11.
DR   Bgee; ENSMFAG00000042359; Expressed in thymus and 13 other cell types or tissues.
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; 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   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          32..115
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   DOMAIN          250..279
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          389..430
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          162..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..222
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  50021 MW;  E2CA1FA4986F758F CRC64;
     MVRSRQMCNT NMSVPTDGAV TTSQIPASEQ ETLVRPKPLL LKLLKSVGAQ KDTYTMKEVL
     FYLGQYIMTK RLYDEKQQHI VYCSNDLLGD LFGVPSFSVK EHRKIYTMIY RNLVVVNQQE
     ENSDELSGER QRKRHKSDSI SLSFDESLAL CVIREICCER SSSSESTGTP SNPDLDAGVS
     EHSGDWLDQD SVSDQFSVEF EVESLDSEDY SLSEEAQELS DEDDEVYRVT VYQAGESDTD
     SFEEDPEISL ADYWKCTSCN EMNPPLPSHC NRCWALRENW LPEDKGKDKG EISEKAKLEN
     STQAEEGFDV PDCKKTIVND SKESCVEEND DKITQASQSQ ESEDYSQPST SSSIIYSSQE
     DVKEFEREET QDKEESVESS LPLNAIEPCV ICQGRPKNGC IVHGKTGHLM ACFTCAKKLK
     KRNKPCPVCR QPIQMIVLTY FP
//
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