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Protein

Non-structural protein 1

Gene

NS

Organism
Influenza B virus (strain B/Lee/1940)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds and inhibits the ubiquitin-like protein G1P2/ISG15, which is an early antiviral protein. Inhibits IRF-3 nuclear translocation and activation. Inhibits IFN-beta promoter activation; this inhibition is not dsRNA-binding dependent Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host ISG15 by virus, Inhibition of host PKR by virus, Viral immunoevasion

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein 1
Short name:
NS1
Alternative name(s):
NS1B
Gene namesi
Name:NS
OrganismiInfluenza B virus (strain B/Lee/1940)
Taxonomic identifieri518987 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008158 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331R → A: Partial loss of dsRNA-binding and no effect on inhibition of IFN-beta promoter; when associated with A-38. 1 Publication
Mutagenesisi38 – 381R → A: Partial loss of dsRNA-binding and no effect on inhibition of IFN-beta promoter; when associated with A-33. 1 Publication
Mutagenesisi47 – 471R → A: Complete loss of dsRNA-binding and 40% loss of inhibition of IFN-beta promoter; when associated with A-50. 1 Publication
Mutagenesisi50 – 501R → A: Complete loss of dsRNA-binding and 40% loss of inhibition of IFN-beta promoter; when associated with A-47. 1 Publication
Mutagenesisi52 – 521K → A: Partial loss of dsRNA-binding and 15% loss of inhibition of IFN-beta promoter; when associated with A-53 and A-54. 1 Publication
Mutagenesisi53 – 531R → A: Partial loss of dsRNA-binding and 15% loss of inhibition of IFN-beta promoter; when associated with A-52 and A-54. 1 Publication
Mutagenesisi54 – 541K → A: Partial loss of dsRNA-binding and 15% loss of inhibition of IFN-beta promoter; when associated with A-52 and A-53. 1 Publication
Mutagenesisi58 – 581R → A: Complete loss of dsRNA-binding and 20% loss of inhibition of IFN-beta promoter; when associated with A-60 and A-64. 1 Publication
Mutagenesisi60 – 601K → A: Complete loss of dsRNA-binding and 20% loss of inhibition of IFN-beta promoter; when associated with A-58 and A-64. 1 Publication
Mutagenesisi64 – 641K → A: Complete loss of dsRNA-binding and 20% loss of inhibition of IFN-beta promoter; when associated with A-58 and A-60. 1 Publication
Mutagenesisi70 – 701K → A: No effect on dsRNA-binding and inhibition of IFN-beta promoter; when associated with A-71. 1 Publication
Mutagenesisi71 – 711R → A: No effect on dsRNA-binding and inhibition of IFN-beta promoter; when associated with A-70. 1 Publication
Mutagenesisi77 – 771R → A: Complete loss of dsRNA-binding and inhibition of IFN-beta promoter; when associated with A-78. 1 Publication
Mutagenesisi78 – 781K → A: Complete loss of dsRNA-binding and inhibition of IFN-beta promoter; when associated with A-77. 1 Publication
Mutagenesisi83 – 831K → A: No effect on dsRNA-binding and 45% loss of inhibition of IFN-beta promoter; when associated with A-86. 1 Publication
Mutagenesisi86 – 861K → A: No effect on dsRNA-binding and 45% loss of inhibition of IFN-beta promoter; when associated with A-83. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Non-structural protein 1PRO_0000078960Add
BLAST

Interactioni

Subunit structurei

Homodimer. Interacts with and inhibits human G1P2 conjugation by UBE1L.1 Publication

Protein-protein interaction databases

DIPiDIP-59701N.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3621Combined sources
Helixi42 – 6322Combined sources
Helixi68 – 703Combined sources
Helixi74 – 9017Combined sources
Helixi93 – 1008Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEQX-ray2.10A/B1-103[»]
3R66X-ray2.30A/B1-103[»]
3RT3X-ray2.01C1-103[»]
3SDLX-ray2.29A/B1-103[»]
ProteinModelPortaliP03502.
SMRiP03502. Positions 15-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03502.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 103103G1P2-bindingAdd
BLAST
Regioni1 – 9393RNA-binding and homodimerizationAdd
BLAST

Domaini

Both N-terminus and C-terminus can inhibit IFN-beta promoter activation and IRF-3 nuclear translocation.

Family and domain databases

InterProiIPR004208. Flu_B_NS1.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF02942. Flu_B_NS1. 1 hit.
[Graphical view]
PIRSFiPIRSF003938. Flu_B_NS1. 1 hit.
SUPFAMiSSF47060. SSF47060. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform NS1 (identifier: P03502-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADNMTTTQI EVGPGATNAT INFEAGILEC YERFSWQRAL DYPGQDRLHR
60 70 80 90 100
LKRKLESRIK THNKSEPENK RMSLEERKAI GVKMMKVLLF MDPSAGIEGF
110 120 130 140 150
EPYCVKNPST SKCPNYDWTD YPPTPGKYLD DIEEEPENVD HPIEVVLRDM
160 170 180 190 200
NNKDARQKIK DEVNTQKEGK FRLTIKRDIR NVLSLRVLVN GTFLKHPNGD
210 220 230 240 250
KSLSTLHRLN AYDQNGGLVA KLVATDDRTV EDEKDGHRIL NSLFERFDEG
260 270 280
HSKPIRAAET AVGVLSQFGQ EHRLSPEEGD N
Length:281
Mass (Da):32,067
Last modified:July 21, 1986 - v1
Checksum:i09C376EA400CA73F
GO
Isoform NEP (identifier: P03511-1) [UniParc]FASTAAdd to basket

Also known as: NS2

The sequence of this isoform can be found in the external entry P03511.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:122
Mass (Da):14,238
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02096 Genomic RNA. Translation: AAA43756.1.
PIRiA04093. MNIVA.
RefSeqiNP_056666.1. NC_002211.1.

Genome annotation databases

GeneIDi26824008.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02096 Genomic RNA. Translation: AAA43756.1.
PIRiA04093. MNIVA.
RefSeqiNP_056666.1. NC_002211.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEQX-ray2.10A/B1-103[»]
3R66X-ray2.30A/B1-103[»]
3RT3X-ray2.01C1-103[»]
3SDLX-ray2.29A/B1-103[»]
ProteinModelPortaliP03502.
SMRiP03502. Positions 15-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59701N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26824008.

Miscellaneous databases

EvolutionaryTraceiP03502.

Family and domain databases

InterProiIPR004208. Flu_B_NS1.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF02942. Flu_B_NS1. 1 hit.
[Graphical view]
PIRSFiPIRSF003938. Flu_B_NS1. 1 hit.
SUPFAMiSSF47060. SSF47060. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Influenza B virus genome: sequences and structural organization of RNA segment 8 and the mRNAs coding for the NS1 and NS2 proteins."
    Briedis D.J., Lamb R.A.
    J. Virol. 42:186-193(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The RNA-binding and effector domains of the viral NS1 protein are conserved to different extents among influenza A and B viruses."
    Wang W., Krug R.M.
    Virology 223:41-50(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  3. "Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein."
    Yuan W., Krug R.M.
    EMBO J. 20:362-371(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN G1P2.
  4. "The N- and C-terminal domains of the NS1 protein of influenza B virus can independently inhibit IRF-3 and beta interferon promoter activation."
    Donelan N.R., Dauber B., Wang X., Basler C.F., Wolff T., Garcia-Sastre A.
    J. Virol. 78:11574-11582(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-33; ARG-38; ARG-47; ARG-50; LYS-52; ARG-53; LYS-54; ARG-58; LYS-60; LYS-64; LYS-70; ARG-71; ARG-77; LYS-78; LYS-83 AND LYS-86.
  5. "Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein."
    Krug R.M., Yuan W., Noah D.L., Latham A.G.
    Virology 309:181-189(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiNS1_INBLE
AccessioniPrimary (citable) accession number: P03502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 78 of the entry and version 1 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

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.