ID   NUB1_BOVIN              Reviewed;         221 AA.
AC   Q8MJ87;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=NEDD8 ultimate buster 1;
DE   AltName: Full=Negative regulator of ubiquitin-like proteins 1;
DE   Flags: Fragment;
GN   Name=NUB1;
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 [MRNA], AND INTERACTION WITH AIPL1.
RC   TISSUE=Retina;
RX   PubMed=12374762; DOI=10.1093/hmg/11.22.2723;
RA   Akey D.T., Zhu X., Dyer M., Li A., Sorensen A., Blackshaw S.,
RA   Fukuda-Kamitani T., Daiger S.P., Craft C.M., Kamitani T., Sohocki M.M.;
RT   "The inherited blindness associated protein AIPL1 interacts with the cell
RT   cycle regulator protein NUB1.";
RL   Hum. Mol. Genet. 11:2723-2733(2002).
CC   -!- FUNCTION: Specific down-regulator of the NEDD8 conjugation system.
CC       Recruits NEDD8 and its conjugates to the proteasome for degradation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Directly interacts with NEDD8 and PSMD4/S5a, a member of the
CC       regulatory subunit of the 26S proteasome. Interacts with AIPL1.
CC       {ECO:0000269|PubMed:12374762}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Predominantly
CC       nuclear. {ECO:0000250}.
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DR   EMBL; AF514279; AAM74162.1; -; mRNA.
DR   AlphaFoldDB; Q8MJ87; -.
DR   SMR; Q8MJ87; -.
DR   IntAct; Q8MJ87; 1.
DR   STRING; 9913.ENSBTAP00000005970; -.
DR   PaxDb; Q8MJ87; -.
DR   PRIDE; Q8MJ87; -.
DR   eggNOG; KOG2561; Eukaryota.
DR   HOGENOM; CLU_030806_0_0_1; -.
DR   InParanoid; Q8MJ87; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR039749; NUB1.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12948; PTHR12948; 1.
DR   Pfam; PF00627; UBA; 2.
DR   SMART; SM00165; UBA; 2.
DR   SUPFAM; SSF46934; SSF46934; 2.
DR   PROSITE; PS50030; UBA; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repeat.
FT   CHAIN           <1..221
FT                   /note="NEDD8 ultimate buster 1"
FT                   /id="PRO_0000210991"
FT   DOMAIN          <1..19
FT                   /note="UBA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          30..76
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          95..135
FT                   /note="UBA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          136..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..193
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   221 AA;  24617 MW;  B417FBD4CC269FD1 CRC64;
     LGLRACDGNV DHAAVHIANR REELDQIKKE EREKKKRRLE NINHLKGMGY SMRAARQALH
     QAAGNLEEAL KILLHNPQLW WLNDSAPESN NRQQSPSQEK IDQLVYMGFD AVAAKAALRV
     FRDNVQLAAQ TLVHNGGRLP PDLQLSAEDS SSTPSTSPSD SAGTSSASTD EDMETEAVNE
     ILEDIPEHEE DYLDSTLEDE EIIIAEYLSY VENIKSAAKK N