Q9WMB4 · PHOSP_MEASC
- ProteinPhosphoprotein
- GeneP/V
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids507 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Essential cofactor of the RNA polymerase L that plays a central role in the transcription and replication by forming the polymerase complex with RNA polymerase L and recruiting L to the genomic N-RNA template for RNA synthesis (By similarity).
Plays also a central role in the encapsidation of nascent RNA chains by forming the encapsidation complex with the nucleocapsid protein N (N-P complex). Acts as a chaperone for newly synthesized free N protein, so-called N0, allowing encapsidation of nascent RNA chains during replication (By similarity).
The nucleoprotein protein N prevents excessive phosphorylation of P, which leads to down-regulation of viral transcription/ replication (By similarity).
Participates, together with N, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (PubMed:32270045).
Plays also a central role in the encapsidation of nascent RNA chains by forming the encapsidation complex with the nucleocapsid protein N (N-P complex). Acts as a chaperone for newly synthesized free N protein, so-called N0, allowing encapsidation of nascent RNA chains during replication (By similarity).
The nucleoprotein protein N prevents excessive phosphorylation of P, which leads to down-regulation of viral transcription/ replication (By similarity).
Participates, together with N, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (PubMed:32270045).
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 | |
---|---|---|
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | DNA-templated transcription | |
Biological Process | viral genome replication |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended namePhosphoprotein
- Short namesProtein P
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Paramyxoviridae > Orthoparamyxovirinae > Morbillivirus > Morbillivirus hominis > Measles morbillivirus
- Virus hosts
Accessions
- Primary accessionQ9WMB4
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000394717 | 1-507 | Phosphoprotein | |||
Sequence: MAEEQARHVKNGLECIRALKAEPIGSLAVEEAMAAWSEISDNPGQDRATCKEEEAGSSGLSKPCLSAIGSTEGGAPRIRGQGSGESDDDAETLGIPSRNLQASSTGLQCYHVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDDESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLKLQSRGNNFPKLGKTLNVPPPPNPSRASTSETPIKKGTDARLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVELNPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKVSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK | ||||||
Modified residue | 86 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 151 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation on serines by host CK2 is necessary for the formation of viral factories.
Keywords
- PTM
Interaction
Subunit
Homotetramer. Interacts (via multimerization domain) with polymerase L; this interaction forms the polymerase L-P complex (By similarity).
Interacts (via N-terminus) with N0 (via Ncore); this interaction allows P to chaperon N0 to avoid N polymerization before encapsidation (By similarity).
Interacts (via C-terminus) with N-RNA template (via C-terminus); this interaction positions the polymerase on the template for both transcription and replication (PubMed:32270045).
Interacts (via N-terminus) with N0 (via Ncore); this interaction allows P to chaperon N0 to avoid N polymerization before encapsidation (By similarity).
Interacts (via C-terminus) with N-RNA template (via C-terminus); this interaction positions the polymerase on the template for both transcription and replication (PubMed:32270045).
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 40-92 | Disordered | ||||
Sequence: SDNPGQDRATCKEEEAGSSGLSKPCLSAIGSTEGGAPRIRGQGSGESDDDAET | ||||||
Region | 133-168 | Disordered | ||||
Sequence: SGLDGDSTLSGGDDESENSDVDIGEPDTEGYAITDR | ||||||
Compositional bias | 142-156 | Acidic residues | ||||
Sequence: SGGDDESENSDVDIG | ||||||
Region | 201-228 | Disordered | ||||
Sequence: NNFPKLGKTLNVPPPPNPSRASTSETPI | ||||||
Region | 252-273 | Disordered | ||||
Sequence: TQCARKSPSEPSGPGAPAGNVP | ||||||
Region | 304-376 | Multimerization | ||||
Sequence: GDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPG | ||||||
Region | 459-507 | Interaction with the nucleocapsid (N-RNA) | ||||
Sequence: ASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK |
Domain
The N-terminus consists of a long intrinsically disordered tail. The central part contains the coiled-coil multimerization domain (PMD) (By similarity).
Forms a four-stranded coiled coil structure (By similarity).
The C-terminus constitutes the alpha-helical domain that binds to the nucleocapsid (N-RNA complex) (By similarity).
Forms a four-stranded coiled coil structure (By similarity).
The C-terminus constitutes the alpha-helical domain that binds to the nucleocapsid (N-RNA complex) (By similarity).
Sequence similarities
Belongs to the morbillivirus P protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length507
- Mass (Da)53,898
- Last updated1999-11-01 v1
- Checksum056474FC4452119A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 142-156 | Acidic residues | ||||
Sequence: SGGDDESENSDVDIG |
RNA Editing
Edited at position 231
Partially edited. RNA editing at this position consists of an insertion of one guanine nucleotide. The sequence displayed here is the P protein, derived from the unedited RNA. The edited RNA gives rise to the V protein (AC P0C774) (By similarity)
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB016162 EMBL· GenBank· DDBJ | BAA34978.1 EMBL· GenBank· DDBJ | Genomic RNA |