ID   NEDD8_BOVIN             Reviewed;          81 AA.
AC   P61282; Q3T0P8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=NEDD8;
DE   AltName: Full=Neddylin;
DE   AltName: Full=Ubiquitin-like protein Nedd8;
DE   Flags: Precursor;
GN   Name=NEDD8;
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].
RX   PubMed=11118368; DOI=10.1006/viro.2000.0644;
RA   Baroth M., Orlich M., Thiel H.J., Becher P.;
RT   "Insertion of cellular NEDD8 coding sequences in a pestivirus.";
RL   Virology 278:456-466(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC       cycle control and embryogenesis via its conjugation to a limited number
CC       of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8
CC       to cullins is critical for the recruitment of E2 to the cullin-RING-
CC       based E3 ubiquitin-protein ligase complex, thus facilitating
CC       polyubiquitination and proteasomal degradation of cyclins and other
CC       regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53
CC       transcriptional activity. Covalent attachment to its substrates
CC       requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to
CC       the E2 enzyme UBE2M. {ECO:0000250|UniProtKB:Q15843}.
CC   -!- SUBUNIT: Interacts with AHR; interaction is direct. Interacts with
CC       NUB1; interaction is direct. {ECO:0000250|UniProtKB:Q15843}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15843}.
CC       Note=Mainly nuclear. {ECO:0000250|UniProtKB:Q15843}.
CC   -!- PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for
CC       function. {ECO:0000250|UniProtKB:Q15843}.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; AF227256; AAF73911.1; -; mRNA.
DR   EMBL; BC102306; AAI02307.1; -; mRNA.
DR   RefSeq; NP_777189.1; NM_174764.3.
DR   AlphaFoldDB; P61282; -.
DR   BMRB; P61282; -.
DR   SMR; P61282; -.
DR   STRING; 9913.ENSBTAP00000003514; -.
DR   PaxDb; P61282; -.
DR   PeptideAtlas; P61282; -.
DR   PRIDE; P61282; -.
DR   Ensembl; ENSBTAT00000003514; ENSBTAP00000003514; ENSBTAG00000038842.
DR   GeneID; 286796; -.
DR   KEGG; bta:286796; -.
DR   CTD; 4738; -.
DR   VEuPathDB; HostDB:ENSBTAG00000038842; -.
DR   eggNOG; KOG0005; Eukaryota.
DR   GeneTree; ENSGT00940000155856; -.
DR   InParanoid; P61282; -.
DR   OMA; YAGKQMA; -.
DR   OrthoDB; 1536766at2759; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000038842; Expressed in oocyte and 103 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; ISS:AgBase.
DR   GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR   GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:AgBase.
DR   CDD; cd01806; Ubl_NEDD8; 1.
DR   InterPro; IPR038738; Nedd8-like.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Isopeptide bond; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..76
FT                   /note="NEDD8"
FT                   /id="PRO_0000042765"
FT   PROPEP          77..81
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT                   /id="PRO_0000042766"
FT   REGION          70..72
FT                   /note="Interaction with UBE1C"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   SITE            8
FT                   /note="Interaction with UBE1C"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   SITE            44
FT                   /note="Interaction with UBE1C"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P29595"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   81 AA;  9072 MW;  DC2FE102BE4725D2 CRC64;
     MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK
     ILGGSVLHLV LALRGGGGLR Q