P03428 · PB2_I34A1
- ProteinPolymerase basic protein 2
- GenePB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids759 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein 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 and inhibition of the host mitochondrial antiviral signaling protein MAVS.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 627 | Mammalian adaptation | ||||
Sequence: K |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | host cell mitochondrion | |
Cellular Component | host cell nucleus | |
Cellular Component | virion component | |
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | 7-methylguanosine mRNA capping | |
Biological Process | cap snatching | |
Biological Process | DNA-templated transcription | |
Biological Process | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity | |
Biological Process | symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity | |
Biological Process | viral RNA genome replication | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolymerase basic protein 2
- Alternative names
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Insthoviricetes > Articulavirales > Orthomyxoviridae > Alphainfluenzavirus > Alphainfluenzavirus influenzae > Influenza A virus
- Virus hosts
Accessions
- Primary accessionP03428
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000078834 | 1-759 | Polymerase basic protein 2 | |||
Sequence: MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPITNTVHYPKIYKTYFERVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGVEPIDNVMGMIGILPDMTPSIEMSMRGVRISKMGVDEYSSTERVVVSIDRFLRIRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTAQIIKLLPFAAAPPKQSRMQFSSFTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGTLTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN |
Interaction
Subunit
Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA. Interacts (via N-terminus) with PB1 (via C-terminus) (PubMed:28169297).
Interacts with nucleoprotein NP (via N-terminus) (PubMed:22570712, PubMed:25043584).
Interacts (via N-terminus) with host MAVS (via N-terminus); this interaction inhibits host innate immune response (PubMed:20538852, PubMed:23246644).
Interacts with nucleoprotein NP (via N-terminus) (PubMed:22570712, PubMed:25043584).
Interacts (via N-terminus) with host MAVS (via N-terminus); this interaction inhibits host innate immune response (PubMed:20538852, PubMed:23246644).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P03428 | NP P03466 | 3 | EBI-2547475, EBI-2547640 | |
BINARY | P03428 | PB1 P03431 | 3 | EBI-2547475, EBI-2547514 |
Protein-protein interaction databases
Chemistry
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P03428-1
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.
- NamePolymerase basic protein 2
- Length759
- Mass (Da)86,095
- Last updated2007-03-06 v2
- Checksum10D2D1608AE536D2
P0DOG6-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NamePB2-S1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 105 | in Ref. 1; ABD77685 | ||||
Sequence: I → M | ||||||
Sequence conflict | 251 | in Ref. 1; ABD77685 | ||||
Sequence: R → K | ||||||
Sequence conflict | 299 | in Ref. 1; ABD77685 | ||||
Sequence: R → K | ||||||
Sequence conflict | 309 | in Ref. 1; ABD77685 | ||||
Sequence: D → G | ||||||
Sequence conflict | 504 | in Ref. 1; ABD77685 | ||||
Sequence: I → V | ||||||
Sequence conflict | 701 | in Ref. 2; ABO21705 | ||||
Sequence: D → N | ||||||
Sequence conflict | 702 | in Ref. 1; ABD77685 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00603 EMBL· GenBank· DDBJ | CAA23855.1 EMBL· GenBank· DDBJ | Unassigned RNA | ||
AF389115 EMBL· GenBank· DDBJ | AAM75155.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EF467818 EMBL· GenBank· DDBJ | ABO21705.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
CY009451 EMBL· GenBank· DDBJ | ABD77685.1 EMBL· GenBank· DDBJ | Genomic RNA |