P0DXN6 · NCAP_MEASF
- ProteinNucleoprotein
- GeneN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids525 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Forms the helical nucleocapsid (NC) in a ratio of 1 N per 6 ribonucleotides, protecting the genome from nucleases (By similarity).
The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter (By similarity).
The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (By similarity).
Forms the encapsidation complex with the phosphoprotein protein P (PubMed:26719278).
Before encapsidation, the newly synthesized free N protein, so-called N0, is chaperoned by P (By similarity).
Participates, together with P, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (By similarity).
N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response (PubMed:15914856).
The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter (By similarity).
The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (By similarity).
Forms the encapsidation complex with the phosphoprotein protein P (PubMed:26719278).
Before encapsidation, the newly synthesized free N protein, so-called N0, is chaperoned by P (By similarity).
Participates, together with P, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (By similarity).
N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response (PubMed:15914856).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 180 | RNA (UniProtKB | ChEBI) | |||
Binding site | 195 | RNA (UniProtKB | ChEBI) | |||
Binding site | 202 | RNA (UniProtKB | ChEBI) | |||
Binding site | 260 | RNA (UniProtKB | ChEBI) | |||
Binding site | 351 | RNA (UniProtKB | ChEBI) | |||
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNucleoprotein
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Paramyxoviridae > Orthoparamyxovirinae > Morbillivirus > Morbillivirus hominis > Measles morbillivirus
- Virus hosts
Accessions
- Primary accessionP0DXN6
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
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Natural variant | 58 | ||||
Natural variant | 129 | ||||
Natural variant | 137 | ||||
Natural variant | 148 | ||||
Natural variant | 262 | ||||
Natural variant | 405 | ||||
Natural variant | 434 | ||||
Natural variant | 448 | ||||
Natural variant | 465 | ||||
Natural variant | 474 | ||||
Natural variant | 478 | ||||
Natural variant | 479 | ||||
Natural variant | 483 | ||||
Natural variant | 487 | ||||
Natural variant | 493-494 | ||||
Natural variant | 516 | ||||
Natural variant | 521 | ||||
Natural variant | 522 | ||||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000142655 | 1-525 | Nucleoprotein | ||
Modified residue | 279 | Phosphothreonine; by host | |||
Post-translational modification
Phosphorylation at Thr-279 is required for the formation of the nucleocapsid.
Keywords
- PTM
Interaction
Subunit
Homomultimer; forms the nucleocapsid (By similarity).
Binds to viral genomic RNA (By similarity).
N0 interacts (via Ncore) with the phosphoprotein (via N-terminus); this interaction allows P to chaperon N0 to avoid N polymerization and non-specific RNA binding before encapsidation (PubMed:26719278).
Interacts (via the Ntail) as N-RNA template with the phosphoprotein (via C-terminus XD); this interaction maintains the P/L complex anchored to the nucleocapsid template during the sequential transcription (By similarity).
Interacts with the phosphoprotein; this interaction leads to the formation of membraneless organelles that function as viral replication factories (By similarity).
Interacts (via Ncore) with human FCGR2B protein (PubMed:15914856).
Interacts (via Ntail) with a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR); this interaction induces growth arrest (PubMed:15914856, PubMed:14557619).
Interacts with human PPIA/CYPA and PPIB/CYPB (By similarity).
Binds to viral genomic RNA (By similarity).
N0 interacts (via Ncore) with the phosphoprotein (via N-terminus); this interaction allows P to chaperon N0 to avoid N polymerization and non-specific RNA binding before encapsidation (PubMed:26719278).
Interacts (via the Ntail) as N-RNA template with the phosphoprotein (via C-terminus XD); this interaction maintains the P/L complex anchored to the nucleocapsid template during the sequential transcription (By similarity).
Interacts with the phosphoprotein; this interaction leads to the formation of membraneless organelles that function as viral replication factories (By similarity).
Interacts (via Ncore) with human FCGR2B protein (PubMed:15914856).
Interacts (via Ntail) with a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR); this interaction induces growth arrest (PubMed:15914856, PubMed:14557619).
Interacts with human PPIA/CYPA and PPIB/CYPB (By similarity).
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-36 | Homomultimerization | |||
Region | 1-375 | RNA packaging and organization of the helical nucleocapsid | |||
Region | 1-403 | Ncore | |||
Motif | 70-77 | Nuclear localization signal | |||
Region | 373-391 | Homomultimerization | |||
Region | 404-525 | Ntail | |||
Motif | 425-440 | Nuclear export signal | |||
Region | 477-505 | Interaction with the phosphoprotein | |||
Domain
Ncore is globular and carries regions required for N self-assembly and RNA-binding. Ntail is an intrinsically disordered monomeric domain in the C-terminus.
Sequence similarities
Belongs to the paramyxoviruses nucleocapsid family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length525
- Mass (Da)58,131
- Last updated2024-11-27 v1
- Checksum3C35DF4458769BA0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z66517 EMBL· GenBank· DDBJ | CAA91363.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U03650 EMBL· GenBank· DDBJ | AAA56640.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U03653 EMBL· GenBank· DDBJ | AAA56643.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U03656 EMBL· GenBank· DDBJ | AAA56646.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U03658 EMBL· GenBank· DDBJ | AAA56648.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U03661 EMBL· GenBank· DDBJ | AAA56651.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U01987 EMBL· GenBank· DDBJ | AAA18986.1 EMBL· GenBank· DDBJ | mRNA | ||
U01991 EMBL· GenBank· DDBJ | AAA18990.1 EMBL· GenBank· DDBJ | mRNA | ||
U01992 EMBL· GenBank· DDBJ | AAA18991.1 EMBL· GenBank· DDBJ | mRNA | ||
U01993 EMBL· GenBank· DDBJ | AAA18992.1 EMBL· GenBank· DDBJ | mRNA | ||
U01994 EMBL· GenBank· DDBJ | AAA18993.1 EMBL· GenBank· DDBJ | mRNA | ||
U01996 EMBL· GenBank· DDBJ | AAA18995.1 EMBL· GenBank· DDBJ | mRNA | ||
AB052821 EMBL· GenBank· DDBJ | BAB60956.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
AF045218 EMBL· GenBank· DDBJ | AAC03050.1 EMBL· GenBank· DDBJ | Genomic RNA |