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Q15843

- NEDD8_HUMAN

UniProt

Q15843 - NEDD8_HUMAN

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Protein
NEDD8
Gene
NEDD8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei8 – 81Interaction with UBE1C
Sitei44 – 441Interaction with UBE1C

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. cellular protein modification process Source: ProtInc
  3. protein localization Source: Ensembl
  4. protein neddylation Source: MGI
  5. proteolysis Source: ProtInc
  6. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. response to organic cyclic compound Source: Ensembl
  8. transforming growth factor beta receptor signaling pathway Source: Reactome
  9. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_120850. TGF-beta receptor signaling activates SMADs.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8
Alternative name(s):
Neddylin
Neural precursor cell expressed developmentally down-regulated protein 8
Short name:
NEDD-8
Ubiquitin-like protein Nedd8
Gene namesi
Name:NEDD8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7732. NEDD8.

Subcellular locationi

Nucleus
Note: Mainly nuclear.1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721A → R: Prevents adenylation by UBE1C. 1 Publication

Organism-specific databases

PharmGKBiPA31537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676NEDD8
PRO_0000042767Add
BLAST
Propeptidei77 – 815
PRO_0000042768

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysine By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

Cleavage of precursor form by UCHL3 or SENP8 is necessary for function.

Keywords - PTMi

Acetylation, Isopeptide bond

Proteomic databases

MaxQBiQ15843.
PaxDbiQ15843.
PeptideAtlasiQ15843.
PRIDEiQ15843.

PTM databases

PhosphoSiteiQ15843.

Miscellaneous databases

PMAP-CutDBQ15843.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, spleen, thymus, prostate, testis, ovary, colon and leukocytes.2 Publications

Gene expression databases

ArrayExpressiQ15843.
BgeeiQ15843.
CleanExiHS_NEDD8.
GenevestigatoriQ15843.

Organism-specific databases

HPAiCAB004082.

Interactioni

Subunit structurei

Directly interacts with NUB1 and AHR. Covalently attached to cullins and p53.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTRCQ9Y2972EBI-716247,EBI-307461
CUL1Q136165EBI-716247,EBI-359390
RPL11P629134EBI-716247,EBI-354380
RPL7P181242EBI-716247,EBI-350806
RPS20P608662EBI-716247,EBI-353105
RPS3P233962EBI-716247,EBI-351193
RPS7P620812EBI-716247,EBI-354360
UBE2MP610812EBI-716247,EBI-1041660

Protein-protein interaction databases

BioGridi110815. 748 interactions.
DIPiDIP-29266N.
IntActiQ15843. 88 interactions.
MINTiMINT-268324.
STRINGi9606.ENSP00000250495.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Beta strandi12 – 165
Helixi23 – 3412
Helixi38 – 403
Beta strandi41 – 455
Beta strandi52 – 554
Helixi56 – 594
Beta strandi66 – 716
Beta strandi73 – 753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDDX-ray1.60A/B/C/D1-76[»]
1R4MX-ray3.00I/J/K/L1-76[»]
1R4NX-ray3.60I/J/K/L1-76[»]
1XT9X-ray2.20B1-76[»]
2BKRX-ray1.90B1-76[»]
2KO3NMR-A1-76[»]
2NVUX-ray2.80I/J1-76[»]
3DBHX-ray2.85I/J/K/L1-76[»]
3DBLX-ray2.90I/J/K/L1-76[»]
3DBRX-ray3.05I/J/K/L1-76[»]
3DQVX-ray3.00A/B1-76[»]
3GZNX-ray3.00I/J1-76[»]
4F8CX-ray1.95B/D1-81[»]
4FBJX-ray1.60B1-81[»]
4HCPX-ray2.52B1-76[»]
ProteinModelPortaliQ15843.
SMRiQ15843. Positions 1-76.

Miscellaneous databases

EvolutionaryTraceiQ15843.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 723Interaction with UBE1C

Sequence similaritiesi

Belongs to the ubiquitin family.

Phylogenomic databases

eggNOGiCOG5272.
HOGENOMiHOG000233942.
HOVERGENiHBG000057.
InParanoidiQ15843.
KOiK12158.
OMAiHPAINSR.
OrthoDBiEOG7JDR1W.
PhylomeDBiQ15843.
TreeFamiTF300072.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15843-1 [UniParc]FASTAAdd to Basket

« Hide

MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM   50
NDEKTAADYK ILGGSVLHLV LALRGGGGLR Q 81
Length:81
Mass (Da):9,072
Last modified:November 1, 1996 - v1
Checksum:iDC2FE102BE4725D2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151I → V in CAG28590. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D23662 mRNA. Translation: BAA04889.1.
CR407662 mRNA. Translation: CAG28590.1.
BC104200 mRNA. Translation: AAI04201.1.
BC104201 mRNA. Translation: AAI04202.1.
BC104664 mRNA. Translation: AAI04665.1.
CCDSiCCDS9621.1.
RefSeqiNP_006147.1. NM_006156.2.
UniGeneiHs.531064.

Genome annotation databases

EnsembliENST00000250495; ENSP00000250495; ENSG00000129559.
GeneIDi4738.
KEGGihsa:4738.
UCSCiuc001wnn.2. human.

Polymorphism databases

DMDMi2833270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D23662 mRNA. Translation: BAA04889.1 .
CR407662 mRNA. Translation: CAG28590.1 .
BC104200 mRNA. Translation: AAI04201.1 .
BC104201 mRNA. Translation: AAI04202.1 .
BC104664 mRNA. Translation: AAI04665.1 .
CCDSi CCDS9621.1.
RefSeqi NP_006147.1. NM_006156.2.
UniGenei Hs.531064.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NDD X-ray 1.60 A/B/C/D 1-76 [» ]
1R4M X-ray 3.00 I/J/K/L 1-76 [» ]
1R4N X-ray 3.60 I/J/K/L 1-76 [» ]
1XT9 X-ray 2.20 B 1-76 [» ]
2BKR X-ray 1.90 B 1-76 [» ]
2KO3 NMR - A 1-76 [» ]
2NVU X-ray 2.80 I/J 1-76 [» ]
3DBH X-ray 2.85 I/J/K/L 1-76 [» ]
3DBL X-ray 2.90 I/J/K/L 1-76 [» ]
3DBR X-ray 3.05 I/J/K/L 1-76 [» ]
3DQV X-ray 3.00 A/B 1-76 [» ]
3GZN X-ray 3.00 I/J 1-76 [» ]
4F8C X-ray 1.95 B/D 1-81 [» ]
4FBJ X-ray 1.60 B 1-81 [» ]
4HCP X-ray 2.52 B 1-76 [» ]
ProteinModelPortali Q15843.
SMRi Q15843. Positions 1-76.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110815. 748 interactions.
DIPi DIP-29266N.
IntActi Q15843. 88 interactions.
MINTi MINT-268324.
STRINGi 9606.ENSP00000250495.

PTM databases

PhosphoSitei Q15843.

Polymorphism databases

DMDMi 2833270.

Proteomic databases

MaxQBi Q15843.
PaxDbi Q15843.
PeptideAtlasi Q15843.
PRIDEi Q15843.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000250495 ; ENSP00000250495 ; ENSG00000129559 .
GeneIDi 4738.
KEGGi hsa:4738.
UCSCi uc001wnn.2. human.

Organism-specific databases

CTDi 4738.
GeneCardsi GC14M024686.
HGNCi HGNC:7732. NEDD8.
HPAi CAB004082.
MIMi 603171. gene.
neXtProti NX_Q15843.
PharmGKBi PA31537.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5272.
HOGENOMi HOG000233942.
HOVERGENi HBG000057.
InParanoidi Q15843.
KOi K12158.
OMAi HPAINSR.
OrthoDBi EOG7JDR1W.
PhylomeDBi Q15843.
TreeFami TF300072.

Enzyme and pathway databases

Reactomei REACT_120850. TGF-beta receptor signaling activates SMADs.

Miscellaneous databases

EvolutionaryTracei Q15843.
GeneWikii NEDD8.
GenomeRNAii 4738.
NextBioi 18272.
PMAP-CutDB Q15843.
PROi Q15843.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15843.
Bgeei Q15843.
CleanExi HS_NEDD8.
Genevestigatori Q15843.

Family and domain databases

InterProi IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view ]
Pfami PF00240. ubiquitin. 1 hit.
[Graphical view ]
PRINTSi PR00348. UBIQUITIN.
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    Tissue: Fibrosarcoma.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function."
    Liakopoulos D., Buesgen T., Brychzy A., Jentsch S., Pause A.
    Proc. Natl. Acad. Sci. U.S.A. 96:5510-5515(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21, FUNCTION, SUBUNIT.
  5. "Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein."
    Kamitani T., Kito K., Nguyen H.P., Yeh E.T.H.
    J. Biol. Chem. 272:28557-28562(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CLEAVAGE SITE.
  6. Cited for: CLEAVAGE BY UCHL3.
  7. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
  8. "NUB1, a NEDD8-interacting protein, is induced by interferon and down-regulates the NEDD8 expression."
    Kito K., Yeh E.T.H., Kamitani T.
    J. Biol. Chem. 276:20603-20609(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUB1.
  9. "The NEDD8 pathway is essential for SCF(beta -TrCP)-mediated ubiquitination and processing of the NF-kappa B precursor p105."
    Amir R.E., Iwai K., Ciechanover A.
    J. Biol. Chem. 277:23253-23259(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Interaction with Nedd8, a ubiquitin-like protein, enhances the transcriptional activity of the aryl hydrocarbon receptor."
    Antenos M., Casper R.F., Brown T.J.
    J. Biol. Chem. 277:44028-44034(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHR.
  11. "NEDP1, a highly conserved cysteine protease that deneddylates cullins."
    Mendoza H.M., Shen L.-N., Botting C., Lewis A., Chen J., Ink B., Hay R.T.
    J. Biol. Chem. 278:25637-25643(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY SENP8.
  12. "DEN1 is a dual function protease capable of processing the C-terminus of Nedd8 and deconjugating hyper-neddylated CUL1."
    Wu K., Yamoah K., Dolios G., Gan-Erdene T., Tan P., Chen A., Lee C.-G., Wei N., Wilkinson K.D., Wang R., Pan Z.-Q.
    J. Biol. Chem. 278:28882-28891(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY SENP8.
  13. "Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity."
    Xirodimas D.P., Saville M.K., Bourdon J.-C., Hay R.T., Lane D.P.
    Cell 118:83-97(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  14. "Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes."
    Whitby F.G., Xia G., Pickart C.M., Hill C.P.
    J. Biol. Chem. 273:34983-34991(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  15. "The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1."
    Walden H., Podgorski M.S., Huang D.T., Miller D.W., Howard R.J., Minor D.L. Jr., Holton J.M., Schulman B.A.
    Mol. Cell 12:1427-1437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-76 IN COMPLEX WITH UBE1C; APPBP1 AND ATP, MUTAGENESIS OF ALA-72.
  16. "Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1."
    Reverter D., Wu K., Erdene T.G., Pan Z.-Q., Wilkinson K.D., Lima C.D.
    J. Mol. Biol. 345:141-151(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76 IN COMPLEX WITH SENP8.

Entry informationi

Entry nameiNEDD8_HUMAN
AccessioniPrimary (citable) accession number: Q15843
Secondary accession number(s): Q3SXN8, Q6LES6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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