Sequence Browser (P46934-4)

Available Structures (Graph-View Mode)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
1319

Isoforms (From UniProt)

Isoform
Remark
Ref
P46934-1
No experimental confirmation available.
P46934-2
No experimental confirmation available.
VSP_038259
P46934-3
No experimental confirmation available.
VSP_038258
P46934-4  
Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.
VSP_038256 VSP_038257
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Protein Information (From UniProt)

Protein:
E3 ubiquitin-protein ligase NEDD4
Other Names:
Cell proliferation-inducing gene 53 protein, HECT-type E3 ubiquitin transferase NEDD4, Neural precursor cell expressed developmentally down-regulated protein 4
Primary Accession:
P46934
Other Accessions:
A1KY35, A6ND72, A7MD29, B4E2R7, B7ZM59, B7ZM60, B9EGN5, D6RF89
Gene :
NEDD4*, synonyms (KIAA0093, NEDD4-1)
Organism :
Human
Entry Name :
NEDD4_HUMAN
Length :
1,319
Mass (Da) :
149,114
Last modified :
30-Jan-2010
Version :
v4
Isoforms :
4 
Structures :
Experimental 0 | Phyre prediction 8
Function : Show Hide

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046).

(Microbial infection) Involved in the ubiquitination of Ebola virus protein VP40 which plays a role in viral budding.