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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: 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

GO - Biological processi

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

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-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:
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 virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000009255 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host mitochondrion, Host nucleus, Virion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3317339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000788341 – 759Polymerase basic protein 2Add BLAST759

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

DIPiDIP-43997N.
IntActiP03428. 38 interactors.
MINTiMINT-3375074.

Chemistry databases

BindingDBiP03428.

Structurei

Secondary structure

1759
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 10Combined sources10
Helixi14 – 22Combined sources9
Helixi27 – 33Combined sources7
Beta strandi323 – 325Combined sources3
Beta strandi328 – 335Combined sources8
Beta strandi338 – 345Combined sources8
Beta strandi351 – 359Combined sources9
Beta strandi361 – 366Combined sources6
Beta strandi368 – 377Combined sources10
Beta strandi380 – 390Combined sources11
Helixi391 – 405Combined sources15
Helixi408 – 411Combined sources4
Turni418 – 420Combined sources3
Helixi430 – 440Combined sources11
Helixi443 – 449Combined sources7
Beta strandi451 – 453Combined sources3
Helixi456 – 458Combined sources3
Beta strandi461 – 463Combined sources3
Beta strandi469 – 475Combined sources7
Beta strandi478 – 480Combined sources3
Helixi536 – 540Combined sources5
Helixi541 – 555Combined sources15
Helixi557 – 566Combined sources10
Helixi568 – 572Combined sources5
Helixi575 – 577Combined sources3
Helixi578 – 582Combined sources5
Turni586 – 588Combined sources3
Helixi589 – 605Combined sources17
Helixi612 – 618Combined sources7
Helixi619 – 622Combined sources4
Beta strandi634 – 638Combined sources5
Beta strandi641 – 643Combined sources3
Beta strandi645 – 651Combined sources7
Beta strandi656 – 658Combined sources3
Beta strandi660 – 662Combined sources3
Beta strandi664 – 674Combined sources11
Beta strandi687 – 691Combined sources5
Beta strandi694 – 699Combined sources6
Helixi702 – 704Combined sources3
Helixi710 – 714Combined sources5
Beta strandi721 – 727Combined sources7
Beta strandi730 – 736Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U6OX-ray1.30A/B318-483[»]
ProteinModelPortaliP03428.
SMRiP03428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03428.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi736 – 739Nuclear localization signalBy similarity4

Sequence similaritiesi

Belongs to the influenza viruses PB2 family.Curated

Phylogenomic databases

KOiK19388.

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)DescriptionActionsGraphical viewLength
Sequence conflicti105I → M in ABD77685 (PubMed:7060132).Curated1
Sequence conflicti251R → K in ABD77685 (PubMed:7060132).Curated1
Sequence conflicti299R → K in ABD77685 (PubMed:7060132).Curated1
Sequence conflicti309D → G in ABD77685 (PubMed:7060132).Curated1
Sequence conflicti504I → V in ABD77685 (PubMed:7060132).Curated1
Sequence conflicti701D → N in ABO21705 (PubMed:11779399).Curated1
Sequence conflicti702K → R in ABD77685 (PubMed:7060132).Curated1

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.
KEGGivg:956536.

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.
RefSeqiNP_040987.1. NC_002023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U6OX-ray1.30A/B318-483[»]
ProteinModelPortaliP03428.
SMRiP03428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-43997N.
IntActiP03428. 38 interactors.
MINTiMINT-3375074.

Chemistry databases

BindingDBiP03428.
ChEMBLiCHEMBL3317339.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956536.
KEGGivg:956536.

Phylogenomic databases

KOiK19388.

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-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

EvolutionaryTraceiP03428.

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]
ProtoNetiSearch...

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 2, 2016
This is version 109 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

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.