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NEDD8_DROME
ID   NEDD8_DROME             Reviewed;          84 AA.
AC   Q9VJ33; Q29QE5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=NEDD8;
DE   AltName: Full=Neddylin;
DE   AltName: Full=Ubiquitin-like protein Nedd8;
DE   Flags: Precursor;
GN   Name=Nedd8; ORFNames=CG10679;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=12231629; DOI=10.1101/gad.1011402;
RA   Ou C.-Y., Lin Y.-F., Chen Y.-J., Chien C.-T.;
RT   "Distinct protein degradation mechanisms mediated by Cul1 and Cul3
RT   controlling Ci stability in Drosophila eye development.";
RL   Genes Dev. 16:2403-2414(2002).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15843622; DOI=10.1523/jneurosci.0149-05.2005;
RA   Zhu S., Perez R., Pan M., Lee T.;
RT   "Requirement of Cul3 for axonal arborization and dendritic elaboration in
RT   Drosophila mushroom body neurons.";
RL   J. Neurosci. 25:4189-4197(2005).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=16127432; DOI=10.1038/ncb1301;
RA   Wu J.-T., Lin H.-C., Hu Y.-C., Chien C.-T.;
RT   "Neddylation and deneddylation regulate Cul1 and Cul3 protein
RT   accumulation.";
RL   Nat. Cell Biol. 7:1014-1020(2005).
CC   -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC       cycle control, embryogenesis and neurogenesis. Covalent attachment to
CC       its substrates requires prior activation by the E1 complex Uba3-Ula1
CC       and linkage to the E2 enzyme UbcE2M. Attachment of Nedd8 to cullins
CC       activates their associated E3 ubiquitin ligase activity, and thus
CC       promotes polyubiquitination and proteasomal degradation of cyclins and
CC       other regulatory proteins. {ECO:0000269|PubMed:12231629,
CC       ECO:0000269|PubMed:15843622, ECO:0000269|PubMed:16127432}.
CC   -!- SUBUNIT: Covalently attached to cullins. {ECO:0000269|PubMed:12231629,
CC       ECO:0000269|PubMed:15843622, ECO:0000269|PubMed:16127432}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15843}.
CC   -!- PTM: Cleavage of precursor form is necessary for function.
CC       {ECO:0000250|UniProtKB:Q15843}.
CC   -!- DISRUPTION PHENOTYPE: Flies die from growth arrest in the first-instar
CC       larval stage. {ECO:0000269|PubMed:12231629}.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF53724.1; -; Genomic_DNA.
DR   EMBL; BT024445; ABC86507.1; -; mRNA.
DR   RefSeq; NP_001286070.1; NM_001299141.1.
DR   RefSeq; NP_609919.1; NM_136075.3.
DR   AlphaFoldDB; Q9VJ33; -.
DR   SMR; Q9VJ33; -.
DR   BioGRID; 61142; 9.
DR   IntAct; Q9VJ33; 8.
DR   STRING; 7227.FBpp0080733; -.
DR   PaxDb; Q9VJ33; -.
DR   PRIDE; Q9VJ33; -.
DR   DNASU; 35151; -.
DR   EnsemblMetazoa; FBtr0081192; FBpp0080733; FBgn0032725.
DR   EnsemblMetazoa; FBtr0342928; FBpp0309711; FBgn0032725.
DR   GeneID; 35151; -.
DR   KEGG; dme:Dmel_CG10679; -.
DR   CTD; 4738; -.
DR   FlyBase; FBgn0032725; Nedd8.
DR   VEuPathDB; VectorBase:FBgn0032725; -.
DR   eggNOG; KOG0005; Eukaryota.
DR   HOGENOM; CLU_010412_6_4_1; -.
DR   InParanoid; Q9VJ33; -.
DR   OMA; YAGKQMA; -.
DR   OrthoDB; 1536766at2759; -.
DR   PhylomeDB; Q9VJ33; -.
DR   Reactome; R-DME-5689603; UCH proteinases.
DR   Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-917937; Iron uptake and transport.
DR   SignaLink; Q9VJ33; -.
DR   BioGRID-ORCS; 35151; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35151; -.
DR   PRO; PR:Q9VJ33; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032725; Expressed in secondary oocyte and 26 other tissues.
DR   ExpressionAtlas; Q9VJ33; baseline and differential.
DR   Genevisible; Q9VJ33; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031386; F:protein tag; IDA:FlyBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0045116; P:protein neddylation; IMP:FlyBase.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR   GO; GO:0030162; P:regulation of proteolysis; IMP:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
DR   GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
DR   GO; GO:0030431; P:sleep; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Developmental protein; Isopeptide bond; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..76
FT                   /note="NEDD8"
FT                   /id="PRO_0000042775"
FT   PROPEP          77..84
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT                   /id="PRO_0000042776"
FT   REGION          70..72
FT                   /note="Interaction with Uba3"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   SITE            8
FT                   /note="Interaction with Uba3"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   SITE            44
FT                   /note="Interaction with Uba3"
FT                   /evidence="ECO:0000250|UniProtKB:Q15843"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
SQ   SEQUENCE   84 AA;  9346 MW;  2B0858BB4DC77AA3 CRC64;
     MLIKVKTLTG KEIEIDIEPT DKVDRIKERV EEKEGIPPQQ QRLIFSGKQM NDDKTAADYK
     VQGGSVLHLV LALRGGDSIL TPCV
 
 
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