Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  NEDD8  

UniProtKB / Swiss-Prot ID :  NEDD8_HUMAN

Gene Name (Synonyms) : 
NEDD8  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Note=Mainly nuclear. 

Protein Function :  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. 

Protein Sequence MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLV...
Predicted Secondary Structure CEEEEECCCCCEEEEEECCCCCHHHHHHHHHHHHCCCHHHEEEEECCEEECCCCCHHHCCCCCCCEEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LIKVKTLTG
EEEEECCCC
32.58Phosphositeplus
Link
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TLTGKEIEI
CCCCCEEEE
50.73Phosphositeplus
Link
11NeddyllysineTLTGKEIEI
CCCCCEEEE
50.73Phosphositeplus
Link
20PhosphothreonineDIEPTDKVE
EECCCCCHH
35.34Phosphositeplus
Link
22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EPTDKVERI
CCCCCHHHH
48.77Phosphositeplus
Link
22NeddyllysineEPTDKVERI
CCCCCHHHH
48.77Phosphositeplus
Link
27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VERIKERVE
HHHHHHHHH
45.77Phosphositeplus
Link
33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RVEEKEGIP
HHHHHHCCC
47.97Phosphositeplus
Link
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYSGKQMND
EECCEEECC
40.20Phosphositeplus
Link
48N6-acetyllysineIYSGKQMND
EECCEEECC
40.20HPRD
Link
48N6-acetyllysineIYSGKQMND
EECCEEECC
40.20Phosphositeplus
Link
48N6-acetyllysine.IYSGKQMND
EECCEEECC
40.20UniProtKB
Link
48NeddyllysineIYSGKQMND
EECCEEECC
40.20Phosphositeplus
Link
54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MNDEKTAAD
ECCCCCHHH
46.45Phosphositeplus
Link
59PhosphotyrosineTAADYKILG
CHHHCCCCC
8.66Phosphositeplus
Link
60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AADYKILGG
HHHCCCCCC
31.81Phosphositeplus
Link
60NeddyllysineAADYKILGG
HHHCCCCCC
31.81Phosphositeplus
Link
76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) (interchain with K-? in acceptor proteinsALRGGGGLR
EEECCCCCC
22.14UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CUL1_HUMANphysical interactionMINT-4544716MINT17318178
FBW1A_HUMANphysical interactionMINT-4544692MINT17318178
FBW1A_HUMANphysical interactionMINT-4544702MINT17318178
UB2D2_HUMANdirect interactionDIP:57292EDIP17206147
UCHL1_HUMANphysical interactionEBI-732632
intact16169070
UBA3_HUMANphysical interaction
physical interaction
EBI-1037683
EBI-1037697
intact14690597
14690597
ULA1_HUMANphysical interaction
physical interaction
EBI-1037683
EBI-1037697
intact14690597
14690597
SENP8_HUMANdirect interactionEBI-1041226
intact15567417
UB2R1_HUMANin vitroHPRD:04412HPRD11675391
AHR_HUMANin vitro
in vivo
HPRD:04412HPRD12215427
PSMD4_HUMANin vivoHPRD:04412HPRD11585840
UBC1_HUMANin vitroHPRD:04412HPRD9857030
UCHL3_HUMANin vitro
yeast 2-hybrid
HPRD:04412HPRD9790970
CUL1_HUMANin vitro
in vivo
HPRD:04412HPRD10772955
10713156
16620772
NEDD8_HUMANin vitroHPRD:04412HPRD9857030
ULA1_HUMANin vivoHPRD:04412HPRD16620772
CUL2_HUMANin vivoHPRD:04412HPRD16620772
CUL4B_HUMANin vivoHPRD:04412HPRD16620772
P53_HUMANin vivoHPRD:04412HPRD16620772
PARP1_HUMANin vivoHPRD:04412HPRD16620772
FAK1_HUMANin vivoHPRD:04412HPRD16620772
UCHL1_HUMANyeast 2-hybridHPRD:04412HPRD16169070
UB2R1_HUMANENSP00000250495STRING
RBX1_HUMANENSP00000250495STRING
SKP1_HUMANENSP00000250495STRING
AHR_HUMANENSP00000250495STRING
UBC12_HUMANENSP00000250495STRING
SUMO1_HUMANENSP00000250495STRING
CUL3_HUMANENSP00000250495STRING
P53_HUMANENSP00000250495STRING
ULA1_HUMANENSP00000250495STRING
CUL1_HUMANENSP00000250495STRING
SENP8_HUMANENSP00000250495STRING
CSN8_HUMANENSP00000250495STRING
NUB1_HUMANENSP00000250495STRING
UBA3_HUMANENSP00000250495STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures