NEDD8_HUMAN
ID NEDD8_HUMAN Reviewed; 81 AA.
AC Q15843; Q3SXN8; Q6LES6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=NEDD8;
DE AltName: Full=Neddylin;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 8;
DE Short=NEDD-8;
DE AltName: Full=Ubiquitin-like protein Nedd8;
DE Flags: Precursor;
GN Name=NEDD8 {ECO:0000303|PubMed:9694792, ECO:0000312|HGNC:HGNC:7732};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Fibrosarcoma;
RX PubMed=9694792; DOI=10.1101/gad.12.15.2263;
RA Osaka F., Kawasaki H., Aida N., Saeki M., Chiba T., Kawashima S.,
RA Tanaka K., Kato S.;
RT "A new NEDD8-ligating system for cullin-4A.";
RL Genes Dev. 12:2263-2268(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-21, AND FUNCTION.
RX PubMed=10318914; DOI=10.1073/pnas.96.10.5510;
RA Liakopoulos D., Buesgen T., Brychzy A., Jentsch S., Pause A.;
RT "Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to
RT von Hippel-Lindau tumor suppressor function.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5510-5515(1999).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND CLEAVAGE SITE.
RX PubMed=9353319; DOI=10.1074/jbc.272.45.28557;
RA Kamitani T., Kito K., Nguyen H.P., Yeh E.T.H.;
RT "Characterization of NEDD8, a developmentally down-regulated ubiquitin-like
RT protein.";
RL J. Biol. Chem. 272:28557-28562(1997).
RN [6]
RP CLEAVAGE BY UCHL3.
RX PubMed=9790970; DOI=10.1006/bbrc.1998.9532;
RA Wada H., Kito K., Caskey L.S., Yeh E.T.H., Kamitani T.;
RT "Cleavage of the C-terminus of NEDD8 by UCH-L3.";
RL Biochem. Biophys. Res. Commun. 251:688-692(1998).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA Kato S., Tanaka K.;
RT "Covalent modification of all members of human cullin family proteins by
RT NEDD8.";
RL Oncogene 18:6829-6834(1999).
RN [8]
RP INTERACTION WITH NUB1.
RX PubMed=11259415; DOI=10.1074/jbc.m100920200;
RA Kito K., Yeh E.T.H., Kamitani T.;
RT "NUB1, a NEDD8-interacting protein, is induced by interferon and down-
RT regulates the NEDD8 expression.";
RL J. Biol. Chem. 276:20603-20609(2001).
RN [9]
RP FUNCTION.
RX PubMed=11953428; DOI=10.1074/jbc.m200967200;
RA Amir R.E., Iwai K., Ciechanover A.;
RT "The NEDD8 pathway is essential for SCF(beta -TrCP)-mediated ubiquitination
RT and processing of the NF-kappa B precursor p105.";
RL J. Biol. Chem. 277:23253-23259(2002).
RN [10]
RP INTERACTION WITH AHR.
RX PubMed=12215427; DOI=10.1074/jbc.m202413200;
RA Antenos M., Casper R.F., Brown T.J.;
RT "Interaction with Nedd8, a ubiquitin-like protein, enhances the
RT transcriptional activity of the aryl hydrocarbon receptor.";
RL J. Biol. Chem. 277:44028-44034(2002).
RN [11]
RP CLEAVAGE BY SENP8.
RX PubMed=12730221; DOI=10.1074/jbc.m212948200;
RA Mendoza H.M., Shen L.-N., Botting C., Lewis A., Chen J., Ink B., Hay R.T.;
RT "NEDP1, a highly conserved cysteine protease that deneddylates cullins.";
RL J. Biol. Chem. 278:25637-25643(2003).
RN [12]
RP CLEAVAGE BY SENP8.
RX PubMed=12759363; DOI=10.1074/jbc.m302888200;
RA Wu K., Yamoah K., Dolios G., Gan-Erdene T., Tan P., Chen A., Lee C.-G.,
RA Wei N., Wilkinson K.D., Wang R., Pan Z.-Q.;
RT "DEN1 is a dual function protease capable of processing the C-terminus of
RT Nedd8 and deconjugating hyper-neddylated CUL1.";
RL J. Biol. Chem. 278:28882-28891(2003).
RN [13]
RP FUNCTION.
RX PubMed=15242646; DOI=10.1016/j.cell.2004.06.016;
RA Xirodimas D.P., Saville M.K., Bourdon J.-C., Hay R.T., Lane D.P.;
RT "Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional
RT activity.";
RL Cell 118:83-97(2004).
RN [14]
RP DEAMIDATION (MICROBIAL INFECTION).
RX PubMed=20850415; DOI=10.1016/j.bbrc.2010.09.048;
RA Morikawa H., Kim M., Mimuro H., Punginelli C., Koyama T., Nagai S.,
RA Miyawaki A., Iwai K., Sasakawa C.;
RT "The bacterial effector Cif interferes with SCF ubiquitin ligase function
RT by inhibiting deneddylation of Cullin1.";
RL Biochem. Biophys. Res. Commun. 401:268-274(2010).
RN [15]
RP FUNCTION, DEAMIDATION AT GLN-40 (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP GLN-40.
RX PubMed=20688984; DOI=10.1126/science.1193844;
RA Cui J., Yao Q., Li S., Ding X., Lu Q., Mao H., Liu L., Zheng N., Chen S.,
RA Shao F.;
RT "Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a
RT bacterial effector family.";
RL Science 329:1215-1218(2010).
RN [16]
RP DEAMIDATION AT GLN-40 (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-40.
RX PubMed=21903097; DOI=10.1016/j.jmb.2011.08.030;
RA Boh B.K., Ng M.Y., Leck Y.C., Shaw B., Long J., Sun G.W., Gan Y.H.,
RA Searle M.S., Layfield R., Hagen T.;
RT "Inhibition of cullin RING ligases by cycle inhibiting factor: evidence for
RT interference with Nedd8-induced conformational control.";
RL J. Mol. Biol. 413:430-437(2011).
RN [17]
RP DEAMIDATION AT GLN-40 (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-40.
RX PubMed=23589306; DOI=10.1074/jbc.m112.448258;
RA Toro T.B., Toth J.I., Petroski M.D.;
RT "The cyclomodulin cycle inhibiting factor (CIF) alters cullin neddylation
RT dynamics.";
RL J. Biol. Chem. 288:14716-14726(2013).
RN [18]
RP DEAMIDATION AT GLN-40 (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-40.
RX PubMed=26632597; DOI=10.1038/ncomms10053;
RA Yu C., Mao H., Novitsky E.J., Tang X., Rychnovsky S.D., Zheng N., Huang L.;
RT "Gln40 deamidation blocks structural reconfiguration and activation of SCF
RT ubiquitin ligase complex by Nedd8.";
RL Nat. Commun. 6:10053-10053(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=9857030; DOI=10.1074/jbc.273.52.34983;
RA Whitby F.G., Xia G., Pickart C.M., Hill C.P.;
RT "Crystal structure of the human ubiquitin-like protein NEDD8 and
RT interactions with ubiquitin pathway enzymes.";
RL J. Biol. Chem. 273:34983-34991(1998).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-76 IN COMPLEX WITH UBE1C; APPBP1
RP AND ATP, FUNCTION, AND MUTAGENESIS OF ALA-72.
RX PubMed=14690597; DOI=10.1016/s1097-2765(03)00452-0;
RA Walden H., Podgorski M.S., Huang D.T., Miller D.W., Howard R.J.,
RA Minor D.L. Jr., Holton J.M., Schulman B.A.;
RT "The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for
RT selective ubiquitin-like protein activation by an E1.";
RL Mol. Cell 12:1427-1437(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76 IN COMPLEX WITH SENP8.
RX PubMed=15567417; DOI=10.1016/j.jmb.2004.10.022;
RA Reverter D., Wu K., Erdene T.G., Pan Z.-Q., Wilkinson K.D., Lima C.D.;
RT "Structure of a complex between Nedd8 and the Ulp/Senp protease family
RT member Den1.";
RL J. Mol. Biol. 345:141-151(2005).
RN [22] {ECO:0007744|PDB:4F8C, ECO:0007744|PDB:4FBJ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH Y.PSEUDOTUBERCULOSIS
RP PROTEIN CIF, AND DEAMIDATION AT GLN-40 (MICROBIAL INFECTION).
RX PubMed=22691497; DOI=10.1073/pnas.1112107109;
RA Crow A., Hughes R.K., Taieb F., Oswald E., Banfield M.J.;
RT "The molecular basis of ubiquitin-like protein NEDD8 deamidation by the
RT bacterial effector protein Cif.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1830-E1838(2012).
RN [23] {ECO:0007744|PDB:4HCP}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 1-76 IN COMPLEX WITH
RP B.PSEUDOMALLEI PROTEIN CIF, DEAMIDATION AT GLN-40 (MICROBIAL INFECTION),
RP AND MUTAGENESIS OF 7-THR--THR-9; LYS-11; GLU-31 AND HIS-68.
RX PubMed=23175788; DOI=10.1073/pnas.1210831109;
RA Yao Q., Cui J., Wang J., Li T., Wan X., Luo T., Gong Y.N., Xu Y., Huang N.,
RA Shao F.;
RT "Structural mechanism of ubiquitin and NEDD8 deamidation catalyzed by
RT bacterial effectors that induce macrophage-specific apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20395-20400(2012).
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 (PubMed:9694792,
CC PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:15242646,
CC PubMed:14690597). Attachment of NEDD8 to cullins is critical for the
CC recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase
CC complex, thus facilitating polyubiquitination and proteasomal
CC degradation of cyclins and other regulatory proteins (PubMed:9694792,
CC PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:20688984).
CC Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional
CC activity (PubMed:15242646). Covalent attachment to its substrates
CC requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to
CC the E2 enzyme UBE2M (PubMed:14690597). {ECO:0000269|PubMed:10318914,
CC ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:11953428,
CC ECO:0000269|PubMed:14690597, ECO:0000269|PubMed:15242646,
CC ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:9694792}.
CC -!- SUBUNIT: Interacts with AHR; interaction is direct (PubMed:12215427).
CC Interacts with NUB1; interaction is direct (PubMed:11259415).
CC {ECO:0000269|PubMed:11259415, ECO:0000269|PubMed:12215427}.
CC -!- INTERACTION:
CC Q15843; Q9Y297: BTRC; NbExp=2; IntAct=EBI-716247, EBI-307461;
CC Q15843; Q13616: CUL1; NbExp=23; IntAct=EBI-716247, EBI-359390;
CC Q15843; P06396: GSN; NbExp=3; IntAct=EBI-716247, EBI-351506;
CC Q15843; O15037: KHNYN; NbExp=13; IntAct=EBI-716247, EBI-6148525;
CC Q15843; Q9UNA4: POLI; NbExp=2; IntAct=EBI-716247, EBI-741774;
CC Q15843; P63151: PPP2R2A; NbExp=3; IntAct=EBI-716247, EBI-1048931;
CC Q15843; P54725: RAD23A; NbExp=2; IntAct=EBI-716247, EBI-746453;
CC Q15843; P62913: RPL11; NbExp=5; IntAct=EBI-716247, EBI-354380;
CC Q15843; P18124: RPL7; NbExp=2; IntAct=EBI-716247, EBI-350806;
CC Q15843; P60866: RPS20; NbExp=3; IntAct=EBI-716247, EBI-353105;
CC Q15843; P23396: RPS3; NbExp=3; IntAct=EBI-716247, EBI-351193;
CC Q15843; P62081: RPS7; NbExp=2; IntAct=EBI-716247, EBI-354360;
CC Q15843; P04271: S100B; NbExp=3; IntAct=EBI-716247, EBI-458391;
CC Q15843; Q8WXE9: STON2; NbExp=2; IntAct=EBI-716247, EBI-539742;
CC Q15843; P07437: TUBB; NbExp=4; IntAct=EBI-716247, EBI-350864;
CC Q15843; P61086: UBE2K; NbExp=3; IntAct=EBI-716247, EBI-473850;
CC Q15843; P61081: UBE2M; NbExp=8; IntAct=EBI-716247, EBI-1041660;
CC Q15843; O94888: UBXN7; NbExp=2; IntAct=EBI-716247, EBI-1993627;
CC Q15843; P09936: UCHL1; NbExp=4; IntAct=EBI-716247, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9353319}. Note=Mainly
CC nuclear. {ECO:0000269|PubMed:9353319}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, spleen,
CC thymus, prostate, testis, ovary, colon and leukocytes.
CC {ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:9353319}.
CC -!- PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for
CC function. {ECO:0000269|PubMed:12730221, ECO:0000269|PubMed:12759363,
CC ECO:0000269|PubMed:9353319, ECO:0000269|PubMed:9790970}.
CC -!- PTM: (Microbial infection) Deamidated at Gln-40 by bacterial
CC cyclomodulin Cif produced by enteropathogenic E.coli,
CC Y.pseudotuberculosis or B.pseudomallei, leading to impair NEDD8 ability
CC to activate cullin-RING-based E3 ubiquitin-protein ligase complexes
CC (CRL complexes) (PubMed:20688984, PubMed:21903097, PubMed:23589306,
CC PubMed:26632597, PubMed:23175788). Deamidation occurs on NEDD8-modified
CC cullins (PubMed:20850415, PubMed:21903097). NEDD8 deamidation prevents
CC switching from the inactive to active state by maintaining the 'closed'
CC structure of the CRL complexes (PubMed:23589306, PubMed:26632597).
CC Deamidation may also impair its deconjugation by the COP9 signalosome;
CC However this result needs additional evidences (PubMed:20850415,
CC PubMed:21903097). {ECO:0000269|PubMed:20688984,
CC ECO:0000269|PubMed:20850415, ECO:0000269|PubMed:21903097,
CC ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306,
CC ECO:0000269|PubMed:26632597}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; D23662; BAA04889.1; -; mRNA.
DR EMBL; CR407662; CAG28590.1; -; mRNA.
DR EMBL; BC104200; AAI04201.1; -; mRNA.
DR EMBL; BC104201; AAI04202.1; -; mRNA.
DR EMBL; BC104664; AAI04665.1; -; mRNA.
DR CCDS; CCDS9621.1; -.
DR RefSeq; NP_006147.1; NM_006156.2.
DR PDB; 1NDD; X-ray; 1.60 A; A/B/C/D=1-76.
DR PDB; 1R4M; X-ray; 3.00 A; I/J/K/L=1-76.
DR PDB; 1R4N; X-ray; 3.60 A; I/J/K/L=1-76.
DR PDB; 1XT9; X-ray; 2.20 A; B=1-76.
DR PDB; 2BKR; X-ray; 1.90 A; B=1-76.
DR PDB; 2KO3; NMR; -; A=1-76.
DR PDB; 2N7K; NMR; -; A=1-81.
DR PDB; 2NVU; X-ray; 2.80 A; I/J=1-76.
DR PDB; 3DBH; X-ray; 2.85 A; I/J/K/L=1-76.
DR PDB; 3DBL; X-ray; 2.90 A; I/J/K/L=1-76.
DR PDB; 3DBR; X-ray; 3.05 A; I/J/K/L=1-76.
DR PDB; 3DQV; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3GZN; X-ray; 3.00 A; I/J=1-76.
DR PDB; 4F8C; X-ray; 1.95 A; B/D=1-81.
DR PDB; 4FBJ; X-ray; 1.60 A; B=1-81.
DR PDB; 4HCP; X-ray; 2.52 A; B=1-76.
DR PDB; 4P5O; X-ray; 3.11 A; H/K=1-76.
DR PDB; 6R7F; EM; 8.20 A; N=1-76.
DR PDB; 6R7I; EM; 5.90 A; N=1-76.
DR PDB; 6TTU; EM; 3.70 A; N=1-76.
DR PDB; 7B5L; EM; 3.80 A; N=1-76.
DR PDB; 7B5N; EM; 3.60 A; N=1-81.
DR PDB; 7ONI; EM; 3.40 A; N=1-81.
DR PDBsum; 1NDD; -.
DR PDBsum; 1R4M; -.
DR PDBsum; 1R4N; -.
DR PDBsum; 1XT9; -.
DR PDBsum; 2BKR; -.
DR PDBsum; 2KO3; -.
DR PDBsum; 2N7K; -.
DR PDBsum; 2NVU; -.
DR PDBsum; 3DBH; -.
DR PDBsum; 3DBL; -.
DR PDBsum; 3DBR; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 3GZN; -.
DR PDBsum; 4F8C; -.
DR PDBsum; 4FBJ; -.
DR PDBsum; 4HCP; -.
DR PDBsum; 4P5O; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6TTU; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5N; -.
DR PDBsum; 7ONI; -.
DR AlphaFoldDB; Q15843; -.
DR BMRB; Q15843; -.
DR SMR; Q15843; -.
DR BioGRID; 110815; 337.
DR CORUM; Q15843; -.
DR DIP; DIP-29266N; -.
DR IntAct; Q15843; 261.
DR MINT; Q15843; -.
DR STRING; 9606.ENSP00000250495; -.
DR BindingDB; Q15843; -.
DR ChEMBL; CHEMBL4295831; -.
DR MoonDB; Q15843; Predicted.
DR iPTMnet; Q15843; -.
DR PhosphoSitePlus; Q15843; -.
DR BioMuta; NEDD8; -.
DR DMDM; 2833270; -.
DR EPD; Q15843; -.
DR jPOST; Q15843; -.
DR MassIVE; Q15843; -.
DR MaxQB; Q15843; -.
DR PaxDb; Q15843; -.
DR PeptideAtlas; Q15843; -.
DR PRIDE; Q15843; -.
DR ProteomicsDB; 60788; -.
DR TopDownProteomics; Q15843; -.
DR Antibodypedia; 22753; 504 antibodies from 38 providers.
DR DNASU; 4738; -.
DR Ensembl; ENST00000250495.10; ENSP00000250495.5; ENSG00000129559.13.
DR Ensembl; ENST00000643069.2; ENSP00000496420.1; ENSG00000285246.2.
DR GeneID; 4738; -.
DR KEGG; hsa:4738; -.
DR MANE-Select; ENST00000250495.10; ENSP00000250495.5; NM_006156.3; NP_006147.1.
DR UCSC; uc001wnn.3; human.
DR CTD; 4738; -.
DR DisGeNET; 4738; -.
DR GeneCards; NEDD8; -.
DR HGNC; HGNC:7732; NEDD8.
DR HPA; ENSG00000129559; Low tissue specificity.
DR MIM; 603171; gene.
DR neXtProt; NX_Q15843; -.
DR OpenTargets; ENSG00000129559; -.
DR PharmGKB; PA31537; -.
DR VEuPathDB; HostDB:ENSG00000129559; -.
DR eggNOG; KOG0005; Eukaryota.
DR GeneTree; ENSGT00940000155856; -.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q15843; -.
DR OMA; YAGKQMA; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q15843; -.
DR TreeFam; TF300072; -.
DR PathwayCommons; Q15843; -.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SignaLink; Q15843; -.
DR BioGRID-ORCS; 4738; 778 hits in 1008 CRISPR screens.
DR EvolutionaryTrace; Q15843; -.
DR GeneWiki; NEDD8; -.
DR GenomeRNAi; 4738; -.
DR Pharos; Q15843; Tchem.
DR PRO; PR:Q15843; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q15843; protein.
DR Bgee; ENSG00000129559; Expressed in prefrontal cortex and 96 other tissues.
DR ExpressionAtlas; Q15843; baseline and differential.
DR Genevisible; Q15843; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0045116; P:protein neddylation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR CDD; cd01806; Ubl_NEDD8; 1.
DR DisProt; DP02302; -.
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 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8"
FT /id="PRO_0000042767"
FT PROPEP 77..81
FT /evidence="ECO:0000269|PubMed:9353319"
FT /id="PRO_0000042768"
FT REGION 70..72
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000269|PubMed:14690597"
FT SITE 8
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000269|PubMed:14690597"
FT SITE 44
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000269|PubMed:14690597"
FT MOD_RES 40
FT /note="(Microbial infection) Deamidated glutamine"
FT /evidence="ECO:0000269|PubMed:20688984,
FT ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788,
FT ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597"
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 MUTAGEN 7..9
FT /note="TLT->ALA: Decreased interaction with B.pseudomallei
FT Cif protein, leading to decreased deamidation."
FT /evidence="ECO:0000269|PubMed:23175788"
FT MUTAGEN 11
FT /note="K->A: Decreased interaction with B.pseudomallei Cif
FT protein, leading to decreased deamidation."
FT /evidence="ECO:0000269|PubMed:23175788"
FT MUTAGEN 31
FT /note="E->Q: Decreased interaction with B.pseudomallei Cif
FT protein, leading to slightly decreased deamidation."
FT /evidence="ECO:0000269|PubMed:23175788"
FT MUTAGEN 40
FT /note="Q->E: Impaired ability to activate cullin-RING-based
FT E3 ubiquitin-protein ligase complexes."
FT /evidence="ECO:0000269|PubMed:20688984,
FT ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23589306,
FT ECO:0000269|PubMed:26632597"
FT MUTAGEN 68
FT /note="H->A: Decreased interaction with B.pseudomallei Cif
FT protein, leading to slightly decreased deamidation."
FT /evidence="ECO:0000269|PubMed:23175788"
FT MUTAGEN 72
FT /note="A->R: Prevents adenylation by UBE1C."
FT /evidence="ECO:0000269|PubMed:14690597"
FT CONFLICT 15
FT /note="I -> V (in Ref. 2; CAG28590)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1NDD"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:4P5O"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1NDD"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1NDD"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1NDD"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1NDD"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2NVU"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1NDD"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1NDD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1XT9"
SQ SEQUENCE 81 AA; 9072 MW; DC2FE102BE4725D2 CRC64;
MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK
ILGGSVLHLV LALRGGGGLR Q
