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P03428

- PB2_I34A1

UniProt

P03428 - PB2_I34A1

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Protein

Polymerase basic protein 2

Gene

PB2

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

Functioni

Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Binds the cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with the host mitochondrial antiviral signaling protein MAVS.6 Publications

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. RNA-directed RNA polymerase activity Source: InterPro

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB-KW
  2. cap snatching Source: UniProtKB-KW
  3. fusion of virus membrane with host plasma membrane Source: Reactome
  4. intracellular transport of virus Source: Reactome
  5. receptor-mediated endocytosis of virus by host cell Source: Reactome
  6. suppression by virus of host RNA polymerase II activity Source: UniProtKB-KW
  7. transcription, DNA-templated Source: InterPro
  8. uncoating of virus Source: Reactome
  9. viral entry into host cell Source: Reactome
  10. viral genome maturation Source: Reactome
  11. viral genome packaging Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. viral release from host cell Source: Reactome
  15. viral transcription Source: Reactome
  16. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cap snatching, Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host RNA polymerase II by virus, mRNA capping, mRNA processing, Viral immunoevasion, Viral transcription

Enzyme and pathway databases

ReactomeiREACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
REACT_6212. Budding.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_9434. vRNP Assembly.
REACT_9491. Viral mRNA Translation.
REACT_9497. vRNA Synthesis.
REACT_9527. cRNA Synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Polymerase basic protein 2
Alternative name(s):
RNA-directed RNA polymerase subunit P3
Gene namesi
Name:PB2
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000009255: Genome

Subcellular locationi

Virion. Host nucleus 2 Publications. Host mitochondrion 3 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. host cell mitochondrion Source: UniProtKB-KW
  5. host cell nucleus Source: UniProtKB-KW
  6. nucleoplasm Source: Reactome
  7. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host mitochondrion, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Polymerase basic protein 2PRO_0000078834Add
BLAST

Interactioni

Subunit structurei

Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA. Interacts (via N-terminus) with PB1 (via C-terminus). Interacts with nucleoprotein NP (via N-terminus). Interacts (via N-terminus) with host MAVS (via N-terminus); this interaction inhibits host innate immune response.4 Publications

Protein-protein interaction databases

IntActiP03428. 38 interactions.
MINTiMINT-3375074.

Structurei

Secondary structure

759
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1010Combined sources
Helixi14 – 229Combined sources
Helixi27 – 337Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi328 – 3358Combined sources
Beta strandi338 – 3458Combined sources
Beta strandi351 – 3599Combined sources
Beta strandi361 – 3666Combined sources
Beta strandi368 – 37710Combined sources
Beta strandi380 – 39011Combined sources
Helixi391 – 40515Combined sources
Helixi408 – 4114Combined sources
Helixi430 – 44011Combined sources
Helixi443 – 4497Combined sources
Beta strandi451 – 4533Combined sources
Helixi456 – 4583Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi469 – 4757Combined sources
Beta strandi478 – 4814Combined sources
Helixi536 – 5405Combined sources
Helixi541 – 55515Combined sources
Helixi557 – 56610Combined sources
Helixi568 – 5725Combined sources
Helixi575 – 5773Combined sources
Helixi578 – 5825Combined sources
Turni586 – 5883Combined sources
Helixi589 – 60517Combined sources
Helixi612 – 6187Combined sources
Helixi619 – 6224Combined sources
Beta strandi634 – 6385Combined sources
Beta strandi641 – 6433Combined sources
Beta strandi645 – 6517Combined sources
Beta strandi656 – 6583Combined sources
Beta strandi660 – 6623Combined sources
Beta strandi664 – 67411Combined sources
Beta strandi687 – 6915Combined sources
Beta strandi694 – 6996Combined sources
Helixi702 – 7043Combined sources
Helixi710 – 7145Combined sources
Beta strandi721 – 7277Combined sources
Beta strandi730 – 7367Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP03428.
SMRiP03428. Positions 319-483, 685-759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03428.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi736 – 7394Nuclear localization signalBy similarity

Sequence similaritiesi

Belongs to the influenza viruses PB2 family.Curated

Family and domain databases

InterProiIPR001591. RNA_pol_PB2_orthomyxovir.
[Graphical view]
PfamiPF00604. Flu_PB2. 1 hit.
[Graphical view]
ProDomiPD001667. RNA_pol_PB2_orthomyxovir. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P03428-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM
60 70 80 90 100
MAMKYPITAD KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN
110 120 130 140 150
RNGPITNTVH YPKIYKTYFE RVERLKHGTF GPVHFRNQVK IRRRVDINPG
160 170 180 190 200
HADLSAKEAQ DVIMEVVFPN EVGARILTSE SQLTITKEKK EELQDCKISP
210 220 230 240 250
LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW EQMYTPGGEV
260 270 280 290 300
RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GIRMVDILRQ
310 320 330 340 350
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ
360 370 380 390 400
TLKIRVHEGY EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV
410 420 430 440 450
AMVFSQEDCM IKAVRGDLNF VNRANQRLNP MHQLLRHFQK DAKVLFQNWG
460 470 480 490 500
VEPIDNVMGM IGILPDMTPS IEMSMRGVRI SKMGVDEYSS TERVVVSIDR
510 520 530 540 550
FLRIRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN GPESVLVNTY
560 570 580 590 600
QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
610 620 630 640 650
QQMRDVLGTF DTAQIIKLLP FAAAPPKQSR MQFSSFTVNV RGSGMRILVR
660 670 680 690 700
GNSPVFNYNK ATKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE
710 720 730 740 750
DKRYGPALSI NELSNLAKGE KANVLIGQGD VVLVMKRKRD SSILTDSQTA

TKRIRMAIN
Length:759
Mass (Da):86,095
Last modified:March 6, 2007 - v2
Checksum:i10D2D1608AE536D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051I → M in ABD77685. (PubMed:7060132)Curated
Sequence conflicti251 – 2511R → K in ABD77685. (PubMed:7060132)Curated
Sequence conflicti299 – 2991R → K in ABD77685. (PubMed:7060132)Curated
Sequence conflicti309 – 3091D → G in ABD77685. (PubMed:7060132)Curated
Sequence conflicti504 – 5041I → V in ABD77685. (PubMed:7060132)Curated
Sequence conflicti701 – 7011D → N in ABO21705. (PubMed:11779399)Curated
Sequence conflicti702 – 7021K → R in ABD77685. (PubMed:7060132)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00603 Unassigned RNA. Translation: CAA23855.1.
AF389115 Genomic RNA. Translation: AAM75155.1.
EF467818 Genomic RNA. Translation: ABO21705.1.
CY009451 Genomic RNA. Translation: ABD77685.1.
RefSeqiNP_040987.1. NC_002023.1.

Genome annotation databases

GeneIDi956536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00603 Unassigned RNA. Translation: CAA23855.1 .
AF389115 Genomic RNA. Translation: AAM75155.1 .
EF467818 Genomic RNA. Translation: ABO21705.1 .
CY009451 Genomic RNA. Translation: ABD77685.1 .
RefSeqi NP_040987.1. NC_002023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZTT X-ray 2.10 B/D 1-37 [» ]
3A1G X-ray 1.70 B/D 1-37 [» ]
3CW4 X-ray 2.70 A 535-759 [» ]
3WI0 X-ray 2.00 A 318-484 [» ]
3WI1 X-ray 1.93 A 318-484 [» ]
4ENF X-ray 1.32 A 318-483 [» ]
4J2R X-ray 2.42 A/B 318-484 [» ]
ProteinModelPortali P03428.
SMRi P03428. Positions 319-483, 685-759.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03428. 38 interactions.
MINTi MINT-3375074.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956536.

Enzyme and pathway databases

Reactomei REACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
REACT_6212. Budding.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_9434. vRNP Assembly.
REACT_9491. Viral mRNA Translation.
REACT_9497. vRNA Synthesis.
REACT_9527. cRNA Synthesis.

Miscellaneous databases

EvolutionaryTracei P03428.

Family and domain databases

InterProi IPR001591. RNA_pol_PB2_orthomyxovir.
[Graphical view ]
Pfami PF00604. Flu_PB2. 1 hit.
[Graphical view ]
ProDomi PD001667. RNA_pol_PB2_orthomyxovir. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  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. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  5. "The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex."
    Fodor E., Smith M.
    J. Virol. 78:9144-9153(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: A/WSN/33.
  6. "Characterization of a mitochondrial-targeting signal in the PB2 protein of influenza viruses."
    Carr S.M., Carnero E., Garcia-Sastre A., Brownlee G.G., Fodor E.
    Virology 344:492-508(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: A/WSN/33.
  7. "Role of the influenza virus heterotrimeric RNA polymerase complex in the initiation of replication."
    Deng T., Sharps J.L., Brownlee G.G.
    J. Gen. Virol. 87:3373-3377(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon."
    Graef K.M., Vreede F.T., Lau Y.F., McCall A.W., Carr S.M., Subbarao K., Fodor E.
    J. Virol. 84:8433-8445(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST MAVS, SUBCELLULAR LOCATION.
  9. "Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627."
    Ng A.K., Chan W.H., Choi S.T., Lam M.K., Lau K.F., Chan P.K., Au S.W., Fodor E., Shaw P.C.
    PLoS ONE 7:E36415-E36415(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUCLEOPROTEIN NP.
  10. "Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins."
    Patel D., Schultz L.W., Umland T.C.
    Virus Res. 172:75-80(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST MAVS.
    Strain: A/WSN/33.
  11. "An important amino acid in nucleoprotein contributes to influenza A virus replication by interacting with polymerase PB2."
    Gui X., Li R., Zhang X., Shen C., Yu H., Guo X., Kang Y., Chen J., Chen H., Chen Y., Xia N.
    Virology 464:11-20(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUCLEOPROTEIN NP.
    Strain: A/WSN/193.
  12. "Structural basis of the influenza A virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue."
    Kuzuhara T., Kise D., Yoshida H., Horita T., Murazaki Y., Nishimura A., Echigo N., Utsunomiya H., Tsuge H.
    J. Biol. Chem. 284:6855-6860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 535-759.
  13. "Structural and functional characterization of K339T substitution identified in the PB2 subunit cap-binding pocket of influenza A virus."
    Liu Y., Qin K., Meng G., Zhang J., Zhou J., Zhao G., Luo M., Zheng X.
    J. Biol. Chem. 288:11013-11023(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 318-483.
  14. "Conformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virus."
    Tsurumura T., Qiu H., Yoshida T., Tsumori Y., Hatakeyama D., Kuzuhara T., Tsuge H.
    PLoS ONE 8:E82020-E82020(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 318-484.
  15. "Crystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virus."
    Tsurumura T., Qiu H., Yoshida T., Tsumori Y., Tsuge H.
    Acta Crystallogr. F 70:72-75(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 318-484.

Entry informationi

Entry nameiPB2_I34A1
AccessioniPrimary (citable) accession number: P03428
Secondary accession number(s): A4GXH0, Q20N28, Q8JUU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 98 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

External Data

Dasty 3