ID   MTBP_XENLA              Reviewed;         860 AA.
AC   Q6NRW0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Mdm2-binding protein;
GN   Name=mtbp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in mdm2-dependent p53/TP53 homeostasis in
CC       unstressed cells. Inhibits autoubiquitination of mdm2, thereby
CC       enhancing mdm2 stability. This promotes mdm2-mediated ubiquitination of
CC       p53/TP53 and its subsequent degradation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MTBP family. {ECO:0000305}.
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DR   EMBL; BC070600; AAH70600.1; -; mRNA.
DR   RefSeq; NP_001084870.1; NM_001091401.1.
DR   AlphaFoldDB; Q6NRW0; -.
DR   PRIDE; Q6NRW0; -.
DR   DNASU; 431919; -.
DR   GeneID; 431919; -.
DR   KEGG; xla:431919; -.
DR   CTD; 431919; -.
DR   Xenbase; XB-GENE-990926; mtbp.S.
DR   OrthoDB; 1334548at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 431919; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IEA:InterPro.
DR   InterPro; IPR039061; MTBP.
DR   InterPro; IPR029418; MTBP_C.
DR   InterPro; IPR029420; MTBP_central.
DR   InterPro; IPR029421; MTBP_N.
DR   PANTHER; PTHR14382; PTHR14382; 1.
DR   Pfam; PF14920; MTBP_C; 1.
DR   Pfam; PF14919; MTBP_mid; 1.
DR   Pfam; PF14918; MTBP_N; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Growth arrest; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..860
FT                   /note="Mdm2-binding protein"
FT                   /id="PRO_0000323747"
FT   REGION          671..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  96308 MW;  279019BF58BDDBEE CRC64;
     MERFVLCIHW ERRAEQQQPV PQGLVYAQDI YTQLKEYSTN CTSTFPACSL TGNPGIRKWF
     FALQSLYGFS QFCSSDWEDL CPAVTTDDSE EPVQTALDEC LDALQFPDGE DDNSRDSISQ
     TNLFEEAAEL LHQLSDKLPA PGRALVDVLL FPSEAPKLKD CLSAIGAIKH LKEWHTAKIT
     IVSKDCKGWQ KIGKFLSANV VVSDCPRQLI DPQELWRGTI EIKERKFTSE VEFPEFCLRS
     VSDDKVPYFE NNGDDKNKTV LSEVFHYYGA SLEYVQMVAL SEIPSYFVSD SVFELSITRN
     GLQGKSKLML DQLCSLTEKV GAIFMLPCNV CSLPNPPALQ RSSKKWREYM SRKPKDIKVP
     GVELKGEYCS YYFLIQGKGS GLCKATLLHS ASQISGAASL LLLHQRLNNN HPVNMAESTS
     DILDSLPHFN GEQIALREQI LARAQVLAVK EYLKRQEAQP HASVSQSNNL GRLLALTREH
     VIGDCESRLD SVSYKNMQNI TVSTPAFPES EAMISNPADW PERNVLQNLE NFEKIKQRLR
     ASILSGSAEQ LLGRKDGLKE GMTLLDAKEL LKYFTPQGLA VGELQPLQVQ RGDNAFLVTP
     KLTPRKLKGL PFEKAAECHY HGLEYCLDNR KALDRDVAFS ELQSRLIRYE TQTTCTRECC
     PIPFALSPIP SPAVLSEPGS VPDGESIQTE LRGDPLRLKR RSKDIEGLYP SKRLAKSGSS
     DSLVSLASEG SGHQQPTRLR TERTASSVSG AQPSSTRVRT APSVPAQSKP SSHLELEQKE
     SRSQKHNRML KEVVSKTLQK HSIGVEHPCY AACNQRLFEI SKFFLKDLKT SRGLLDEMKK
     AASNNAKQVI QWELDKLKKN