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Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Host-virus interaction, Viral penetration into host nucleus, Virus entry into host cell

Keywords - Ligandi

RNA-binding, Viral nucleoprotein

Enzyme and pathway databases

ReactomeiR-HSA-168255. Influenza Life Cycle.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168275. Entry of Influenza Virion into Host Cell via Endocytosis.
R-HSA-168288. Fusion of the Influenza Virion to the Host Cell Endosome.
R-HSA-168298. Release.
R-HSA-168302. Budding.
R-HSA-168303. Packaging of Eight RNA Segments.
R-HSA-168316. Assembly of Viral Components at the Budding Site.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168330. Viral RNP Complexes in the Host Cell Nucleus.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-168336. Uncoating of the Influenza Virion.
R-HSA-192814. vRNA Synthesis.
R-HSA-192823. Viral mRNA Translation.
R-HSA-192869. cRNA Synthesis.
R-HSA-192905. vRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoprotein
Alternative name(s):
Nucleocapsid protein
Short name:
Protein N
Gene namesi
Name:NP
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000009255 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi8R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi104W → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi120W → A: Partial loss of RNA-binding activity. 1 Publication1
Mutagenesisi139W → A: Partial loss of RNA-binding activity. 1 Publication1
Mutagenesisi148Y → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi150R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi156R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi175R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi199R → A: 60% loss of Homomultimerization affinity. No effect on RNA-binding activity. 2 Publications1
Mutagenesisi204R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi207W → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi208R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi213R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi267R → A: Complete loss of RNA-binding activity. 1 Publication1
Mutagenesisi330W → A: Complete loss of RNA-binding activity. 1 Publication1
Mutagenesisi386W → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi391R → A: No effect on RNA-binding activity. 1 Publication1
Mutagenesisi412F → A: Complete loss of RNA-binding activity. 1 Publication1
Mutagenesisi416R → A: Complete loss of Homomultimerization. Complete loss of RNA-binding activity. 2 Publications1
Mutagenesisi479F → A: 2-fold increase of self association. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000790921 – 498NucleoproteinAdd BLAST498

Post-translational modificationi

Late in virus-infected cells, may be cleaved from a 56-kDa protein to a 53-kDa protein by a cellular caspase. This cleavage might be a marker for the onset of apoptosis in infected cells or have a specific function in virus host interaction (By similarity).By similarity

Interactioni

Subunit structurei

Homomultimerizes to form the nucleocapsid. May bind human exportin-1. Binds to viral genomic RNA. Protein-RNA contacts are mediated by a combination of electrostatic interactions between positively charged residues and the phosphate backbone and planar interactions between aromatic side chains and bases.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN4O437072EBI-2547640,EBI-351526From a different organism.
MP034852EBI-2547640,EBI-2547543

Protein-protein interaction databases

DIPiDIP-43998N.
IntActiP03466. 21 interactors.
MINTiMINT-3375097.

Structurei

Secondary structure

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 13Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BSTX-ray2.10C383-391[»]
2WFSelectron microscopy12.00A/B/C/D/E/F/G/H/I8-498[»]
4NQVX-ray2.39M/N/O/P/Q/R44-52[»]
4ZDUX-ray2.30B2-15[»]
ProteinModelPortaliP03466.
SMRiP03466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03466.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1 – 18Unconventional nuclear localization signalAdd BLAST18
Motifi198 – 216Bipartite nuclear localization signalAdd BLAST19

Sequence similaritiesi

Phylogenomic databases

KOiK19391.

Family and domain databases

InterProiIPR002141. Flu_NP.
[Graphical view]
PfamiPF00506. Flu_NP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS
60 70 80 90 100
DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV
110 120 130 140 150
NGKWMRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR
160 170 180 190 200
TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELVRMIKRG
210 220 230 240 250
INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD QVRESRNPGN
260 270 280 290 300
AEFEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
310 320 330 340 350
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT
360 370 380 390 400
KVLPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR
410 420 430 440 450
ASAGQISIQP TFSVQRNLPF DRTTIMAAFN GNTEGRTSDM RTEIIRMMES
460 470 480 490
ARPEDVSFQG RGVFELSDEK AASPIVPSFD MSNEGSYFFG DNAEEYDN
Length:498
Mass (Da):56,210
Last modified:September 11, 2007 - v2
Checksum:i4F750FEF05D6E668
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135H → N in CAA24268 (PubMed:7292985).Curated1
Sequence conflicti247N → D in CAA24268 (PubMed:7292985).Curated1
Sequence conflicti353L → V in CAA24268 (PubMed:7292985).Curated1
Sequence conflicti425I → V in CAA24268 (PubMed:7292985).Curated1
Sequence conflicti430N → T in CAA24268 (PubMed:7292985).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01084 Genomic RNA. Translation: CAA24268.1.
J02147 Genomic RNA. Translation: AAA43467.1.
AF389119 Genomic RNA. Translation: AAM75159.1.
EF467822 Genomic RNA. Translation: ABO21710.1.
AY936882 Genomic RNA. Translation: AAX39501.1.
CY009447 Genomic RNA. Translation: ABD77679.1.
RefSeqiNP_040982.1. NC_002019.1.

Genome annotation databases

GeneIDi956531.
KEGGivg:956531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01084 Genomic RNA. Translation: CAA24268.1.
J02147 Genomic RNA. Translation: AAA43467.1.
AF389119 Genomic RNA. Translation: AAM75159.1.
EF467822 Genomic RNA. Translation: ABO21710.1.
AY936882 Genomic RNA. Translation: AAX39501.1.
CY009447 Genomic RNA. Translation: ABD77679.1.
RefSeqiNP_040982.1. NC_002019.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BSTX-ray2.10C383-391[»]
2WFSelectron microscopy12.00A/B/C/D/E/F/G/H/I8-498[»]
4NQVX-ray2.39M/N/O/P/Q/R44-52[»]
4ZDUX-ray2.30B2-15[»]
ProteinModelPortaliP03466.
SMRiP03466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-43998N.
IntActiP03466. 21 interactors.
MINTiMINT-3375097.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956531.
KEGGivg:956531.

Phylogenomic databases

KOiK19391.

Enzyme and pathway databases

ReactomeiR-HSA-168255. Influenza Life Cycle.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168275. Entry of Influenza Virion into Host Cell via Endocytosis.
R-HSA-168288. Fusion of the Influenza Virion to the Host Cell Endosome.
R-HSA-168298. Release.
R-HSA-168302. Budding.
R-HSA-168303. Packaging of Eight RNA Segments.
R-HSA-168316. Assembly of Viral Components at the Budding Site.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168330. Viral RNP Complexes in the Host Cell Nucleus.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-168336. Uncoating of the Influenza Virion.
R-HSA-192814. vRNA Synthesis.
R-HSA-192823. Viral mRNA Translation.
R-HSA-192869. cRNA Synthesis.
R-HSA-192905. vRNP Assembly.

Miscellaneous databases

EvolutionaryTraceiP03466.

Family and domain databases

InterProiIPR002141. Flu_NP.
[Graphical view]
PfamiPF00506. Flu_NP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCAP_I34A1
AccessioniPrimary (citable) accession number: P03466
Secondary accession number(s): Q20N34
, Q58NB3, Q67228, Q80AB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 11, 2007
Last modified: November 30, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.