NEDD8_DICDI
ID NEDD8_DICDI Reviewed; 77 AA.
AC Q54XV3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=NEDD8;
DE AltName: Full=Neddylin;
DE AltName: Full=Ubiquitin-like protein NEDD8;
DE Flags: Precursor;
GN Name=nedd8; ORFNames=DDB_G0278711;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC cycle control. Attachment of nedd8 to cullins activates their
CC associated E3 ubiquitin ligase activity, and thus promotes
CC polyubiquitination and proteasomal degradation of cyclins and other
CC regulatory proteins (By similarity). {ECO:0000250|UniProtKB:Q15843}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15843}.
CC -!- PTM: Cleavage of precursor form is necessary for function.
CC {ECO:0000250|UniProtKB:Q15843}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68528.2; -; Genomic_DNA.
DR RefSeq; XP_642449.2; XM_637357.2.
DR AlphaFoldDB; Q54XV3; -.
DR SMR; Q54XV3; -.
DR STRING; 44689.DDB0238041; -.
DR PaxDb; Q54XV3; -.
DR EnsemblProtists; EAL68528; EAL68528; DDB_G0278711.
DR GeneID; 8621655; -.
DR KEGG; ddi:DDB_G0278711; -.
DR dictyBase; DDB_G0278711; nedd8.
DR eggNOG; KOG0005; Eukaryota.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q54XV3; -.
DR OMA; ASDYKIQ; -.
DR PhylomeDB; Q54XV3; -.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-917937; Iron uptake and transport.
DR PRO; PR:Q54XV3; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:dictyBase.
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:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; ISS:dictyBase.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
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 Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8"
FT /id="PRO_0000328672"
FT PROPEP 77
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT /id="PRO_0000328673"
FT REGION 30..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 77 AA; 8515 MW; A4BCB5528B179C22 CRC64;
MLIKVKTLTG KEIEIDIDPT DKIQRIKERV EEKEGIPPSQ QRLIFGGKQM GDDKPASEYS
IEGGSVLHLV LALRGGL
