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P03428 (PB2_I34A1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polymerase basic protein 2
Alternative name(s):
RNA-directed RNA polymerase subunit P3
Gene names
Name:PB2
OrganismInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1) [Reference proteome]
Taxonomic identifier211044 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. Binds the cap of the target pre-RNA which is subsequently cleaved by PB1. May play a role in genome replication By similarity.

Subunit structure

Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.

Subcellular location

Virion. Host nucleus. Host mitochondrion By similarity.

Sequence similarities

Belongs to the influenza viruses PB2 family.

Ontologies

Keywords
   Biological processCap snatching
Host gene expression shutoff by virus
Host transcription shutoff by virus
Host-virus interaction
Inhibition of host RNA polymerase II by virus
mRNA capping
mRNA processing
   Cellular componentHost mitochondrion
Host nucleus
Virion
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from electronic annotation. Source: UniProtKB-KW

cap snatching

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host plasma membrane

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

receptor-mediated endocytosis of virus by host cell

Traceable author statement. Source: Reactome

suppression by virus of host RNA polymerase II activity

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

uncoating of virus

Traceable author statement. Source: Reactome

viral entry into host cell

Traceable author statement. Source: Reactome

viral genome maturation

Traceable author statement. Source: Reactome

viral genome packaging

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

host cell mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

virion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Polymerase basic protein 2
PRO_0000078834

Regions

Motif736 – 7394Nuclear localization signal By similarity

Experimental info

Sequence conflict1051I → M in ABD77685. Ref.1
Sequence conflict2511R → K in ABD77685. Ref.1
Sequence conflict2991R → K in ABD77685. Ref.1
Sequence conflict3091D → G in ABD77685. Ref.1
Sequence conflict5041I → V in ABD77685. Ref.1
Sequence conflict7011D → N in ABO21705. Ref.3
Sequence conflict7021K → R in ABD77685. Ref.1

Secondary structure

........................................................................... 759
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03428 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 10D2D1608AE536D2

FASTA75986,095
        10         20         30         40         50         60 
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD 

        70         80         90        100        110        120 
KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN RNGPITNTVH YPKIYKTYFE 

       130        140        150        160        170        180 
RVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE 

       190        200        210        220        230        240 
SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW 

       250        260        270        280        290        300 
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GIRMVDILRQ 

       310        320        330        340        350        360 
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIRVHEGY 

       370        380        390        400        410        420 
EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF 

       430        440        450        460        470        480 
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG VEPIDNVMGM IGILPDMTPS IEMSMRGVRI 

       490        500        510        520        530        540 
SKMGVDEYSS TERVVVSIDR FLRIRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN 

       550        560        570        580        590        600 
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF 

       610        620        630        640        650        660 
QQMRDVLGTF DTAQIIKLLP FAAAPPKQSR MQFSSFTVNV RGSGMRILVR GNSPVFNYNK 

       670        680        690        700        710        720 
ATKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE DKRYGPALSI NELSNLAKGE 

       730        740        750 
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN 

« Hide

References

[1]"Nucleotide sequences of influenza virus segments 1 and 3 reveal mosaic structure of a small viral RNA segment."
Fields S., Winter G.
Cell 28:303-313(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Plasmid-only rescue of influenza A virus vaccine candidates."
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L., Garcia-Sastre A., Palese P.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
[4]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00603 Unassigned RNA. Translation: CAA23855.1.
AF389115 Genomic RNA. Translation: AAM75155.1.
EF467818 Genomic RNA. Translation: ABO21705.1.
CY009451 Genomic RNA. Translation: ABD77685.1.
RefSeqNP_040987.1. NC_002023.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZTTX-ray2.10B/D1-37[»]
3A1GX-ray1.70B/D1-37[»]
3CW4X-ray2.70A535-759[»]
3WI0X-ray2.00A318-484[»]
3WI1X-ray1.93A318-484[»]
4ENFX-ray1.32A318-483[»]
4J2RX-ray2.42A/B318-484[»]
ProteinModelPortalP03428.
SMRP03428. Positions 319-483, 685-759.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03428. 38 interactions.
MINTMINT-3375074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956536.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

InterProIPR001591. RNA_pol_PB2_orthomyxovir.
[Graphical view]
PfamPF00604. Flu_PB2. 1 hit.
[Graphical view]
ProDomPD001667. RNA_pol_PB2_orthomyxovir. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP03428.

Entry information

Entry namePB2_I34A1
AccessionPrimary (citable) accession number: P03428
Secondary accession number(s): A4GXH0, Q20N28, Q8JUU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references