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Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed-Annotation score: -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 host 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 that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs 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 unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.UniRule annotation

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • RNA binding Source: UniProtKB-KW
  • structural molecule activity Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding, Viral nucleoprotein
Biological processHost-virus interaction, Viral penetration into host nucleus, Virus entry into host cell

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:
NucleoproteinUniRule annotation
Alternative name(s):
Nucleocapsid proteinUniRule annotation
Short name:
Protein NUniRule annotation
Gene namesi
Name:NPUniRule annotation
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000116373 Componenti: Genome
  • UP000170967 Componenti: Genome
  • UP000009255 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • Host nucleus UniRule annotation2 Publications

GO - Cellular componenti

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.UniRule annotation

Proteomic databases

PRIDEiP03466

Interactioni

Subunit structurei

Homomultimerizes to form the nucleocapsid. May bind host exportin-1/XPO1. 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.UniRule annotation1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-43998N
IntActiP03466, 149 interactors
MINTiP03466

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 signalUniRule annotationAdd BLAST18
Motifi198 – 216Bipartite nuclear localization signalUniRule annotationAdd BLAST19

Sequence similaritiesi

Belongs to the influenza viruses nucleoprotein family.UniRule annotation

Phylogenomic databases

KOiK19391
OrthoDBiVOG0900006S

Family and domain databases

HAMAPiMF_04070 INFV_NCAP, 1 hit
InterProiView protein in InterPro
IPR002141 Flu_NP
PfamiView protein in Pfam
PF00506 Flu_NP, 1 hit

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).1
Sequence conflicti247N → D in CAA24268 (PubMed:7292985).1
Sequence conflicti353L → V in CAA24268 (PubMed:7292985).1
Sequence conflicti425I → V in CAA24268 (PubMed:7292985).1
Sequence conflicti430N → T in CAA24268 (PubMed:7292985).1

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

Similar proteinsi

Entry informationi

Entry nameiNCAP_I34A1
AccessioniPrimary (citable) accession number: P03466
Secondary accession number(s): Q20N34
, Q58NB3, Q67228, Q80AB4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 11, 2007
Last modified: May 23, 2018
This is version 112 of the entry and version 2 of the sequence. See 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

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