O15049 · N4BP3_HUMAN
- ProteinNEDD4-binding protein 3
- GeneN4BP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids544 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a positive role in the antiviral innate immune signaling pathway. Mechanistically, interacts with MAVS and functions as a positive regulator to promote 'Lys-63'-linked polyubiquitination of MAVS and thus strengthens the interaction between MAVS and TRAF2 (PubMed:34880843).
Also plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (By similarity).
Also plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | dendrite | |
Biological Process | innate immune response | |
Biological Process | nervous system development |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNEDD4-binding protein 3
- Short namesN4BP3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15049
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 725 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000096682 | 1-544 | UniProt | NEDD4-binding protein 3 | |||
Sequence: MATAPGPAGIAMGSVGSLLERQDFSPEELRAALAGSRGSRQPDGLLRKGLGQREFLSYLHLPKKDSKSTKNTKRAPRNEPADYATLYYREHSRAGDFSKTSLPERGRFDKCRIRPSVFKPTAGNGKGFLSMQSLASHKGQKLWRSNGSLHTLACHPPLSPGPRASQARAQLLHALSLDEGGPEPEPSLSDSSSGGSFGRSPGTGPSPFSSSLGHLNHLGGSLDRASQGPKEAGPPAVLSCLPEPPPPYEFSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALREPPTPWSPRLESSKI | |||||||
Modified residue (large scale data) | 83 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 100 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 176 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 536 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binds NEDD4 (PubMed:11717310).
Interacts with 14-3-3 proteins (PubMed:15324660).
Interacts with MAVS (PubMed:34880843).
Interacts with 14-3-3 proteins (PubMed:15324660).
Interacts with MAVS (PubMed:34880843).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15049 | CCDC146 Q8IYE0 | 5 | EBI-2512055, EBI-10749669 | |
BINARY | O15049 | CCDC17 Q96LX7-5 | 3 | EBI-2512055, EBI-12165781 | |
BINARY | O15049 | CNKSR3 Q6P9H4 | 3 | EBI-2512055, EBI-10253274 | |
BINARY | O15049 | CTDSP2 O14595 | 3 | EBI-2512055, EBI-2802973 | |
BINARY | O15049 | ENKD1 Q9H0I2 | 3 | EBI-2512055, EBI-744099 | |
BINARY | O15049 | LMO4 P61968 | 3 | EBI-2512055, EBI-2798728 | |
BINARY | O15049 | NTAQ1 Q96HA8 | 3 | EBI-2512055, EBI-741158 | |
BINARY | O15049 | PRR35 P0CG20 | 3 | EBI-2512055, EBI-11986293 | |
BINARY | O15049 | RFC5 P40937 | 5 | EBI-2512055, EBI-712376 | |
BINARY | O15049 | RNF41 Q9H4P4 | 6 | EBI-2512055, EBI-2130266 | |
BINARY | O15049 | RUSC1 Q9BVN2 | 3 | EBI-2512055, EBI-6257312 | |
BINARY | O15049 | SDCBP O00560 | 3 | EBI-2512055, EBI-727004 | |
BINARY | O15049 | SPG21 Q9NZD8 | 3 | EBI-2512055, EBI-742688 | |
BINARY | O15049 | UBASH3A P57075-2 | 3 | EBI-2512055, EBI-7353612 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 61-77 | Basic and acidic residues | ||||
Sequence: LPKKDSKSTKNTKRAPR | ||||||
Region | 61-84 | Disordered | ||||
Sequence: LPKKDSKSTKNTKRAPRNEPADYA | ||||||
Region | 116-252 | Disordered | ||||
Sequence: SVFKPTAGNGKGFLSMQSLASHKGQKLWRSNGSLHTLACHPPLSPGPRASQARAQLLHALSLDEGGPEPEPSLSDSSSGGSFGRSPGTGPSPFSSSLGHLNHLGGSLDRASQGPKEAGPPAVLSCLPEPPPPYEFSC | ||||||
Compositional bias | 126-147 | Polar residues | ||||
Sequence: KGFLSMQSLASHKGQKLWRSNG | ||||||
Compositional bias | 186-216 | Polar residues | ||||
Sequence: PSLSDSSSGGSFGRSPGTGPSPFSSSLGHLN | ||||||
Coiled coil | 294-530 | |||||
Sequence: LAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALRE | ||||||
Region | 335-365 | Disordered | ||||
Sequence: KELRAQQGLAPEPRAPGTLPEADPSARPEEE | ||||||
Region | 430-465 | Disordered | ||||
Sequence: QEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSA |
Sequence similarities
Belongs to the N4BP3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length544
- Mass (Da)60,470
- Last updated2007-04-17 v3
- Checksum40F2652D0848C27C
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 29 | in Ref. 1; BAA20799 | ||||
Sequence: L → P | ||||||
Compositional bias | 61-77 | Basic and acidic residues | ||||
Sequence: LPKKDSKSTKNTKRAPR | ||||||
Compositional bias | 126-147 | Polar residues | ||||
Sequence: KGFLSMQSLASHKGQKLWRSNG | ||||||
Sequence conflict | 163 | in Ref. 3; AAH53323 | ||||
Sequence: R → Q | ||||||
Compositional bias | 186-216 | Polar residues | ||||
Sequence: PSLSDSSSGGSFGRSPGTGPSPFSSSLGHLN | ||||||
Sequence conflict | 317 | in Ref. 4; BAC86891 | ||||
Sequence: R → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB002339 EMBL· GenBank· DDBJ | BAA20799.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471165 EMBL· GenBank· DDBJ | EAW53851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53852.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53854.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC053323 EMBL· GenBank· DDBJ | AAH53323.2 EMBL· GenBank· DDBJ | mRNA | ||
AK127224 EMBL· GenBank· DDBJ | BAC86891.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK295663 EMBL· GenBank· DDBJ | BAG58525.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |