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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
NucleoproteinUniRule annotation
Alternative name(s):
Nucleocapsid proteinUniRule annotation
Short name:
Protein NUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NPUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri211044 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000116373 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000170967 Componenti: Genome
  • UP000009255 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Host nucleus, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000790921 – 498NucleoproteinAdd BLAST498

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PRoteomics IDEntifications database

More...
PRIDEi
P03466

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-43998N

Protein interaction database and analysis system

More...
IntActi
P03466, 149 interactors

Molecular INTeraction database

More...
MINTi
P03466

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5NPZX-ray1.43C252-260[»]
5NQ3X-ray1.57C/F252-260[»]
5V5OX-ray2.24A/B198-216[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P03466

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P03466

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03466

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1 – 18Unconventional nuclear localization signalUniRule annotationAdd BLAST18
Motifi198 – 216Bipartite nuclear localization signalUniRule annotationAdd BLAST19

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the influenza viruses nucleoprotein family.UniRule annotation

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K19391

Database of Orthologous Groups

More...
OrthoDBi
1638at10239

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_04070 INFV_NCAP, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002141 Flu_NP

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00506 Flu_NP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F750FEF05D6E668
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

NCBI Reference Sequences

More...
RefSeqi
NP_040982.1, NC_002019.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
956531

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:956531

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
5NPZX-ray1.43C252-260[»]
5NQ3X-ray1.57C/F252-260[»]
5V5OX-ray2.24A/B198-216[»]
ProteinModelPortaliP03466
SMRiP03466
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-43998N
IntActiP03466, 149 interactors
MINTiP03466

Proteomic databases

PRIDEiP03466

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956531
KEGGivg:956531

Phylogenomic databases

KOiK19391
OrthoDBi1638at10239

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

Protein Ontology

More...
PROi
PR:P03466

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNCAP_I34A1
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03466
Secondary accession number(s): Q20N34
, Q58NB3, Q67228, Q80AB4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 11, 2007
Last modified: January 16, 2019
This is version 114 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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