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Protein

Phosphoprotein

Gene

P

Organism
Rabies virus (strain CVS-11) (RABV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cytoplasmic inwards viral transport, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, Interferon antiviral system evasion, Microtubular inwards viral transport, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoprotein
Short name:
Protein P
Alternative name(s):
Protein M1
Gene namesi
Name:P
OrganismiRabies virus (strain CVS-11) (RABV)
Taxonomic identifieri11294 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesRhabdoviridaeLyssavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mammalia [TaxID: 40674]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297PhosphoproteinPRO_0000222828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631Phosphoserine; by host1 Publication
Modified residuei64 – 641Phosphoserine; by host1 Publication
Modified residuei162 – 1621Phosphoserine; by host PKC1 Publication
Modified residuei210 – 2101Phosphoserine; by host PKC1 Publication
Modified residuei271 – 2711Phosphoserine; by host PKC1 Publication

Post-translational modificationi

Phosphorylated by host PKC and by an unknown kinase.By similarity

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP22363.

Interactioni

Subunit structurei

Homotrimer when phosphorylated. This trimer is stabilized by binding to the L protein. Binds soluble protein N, and ribonucleocapsid. Interacts with host DYNLL1 and DYNLL2; this interaction may play a role in intracellular microtubule-dependent virus transport of incoming virus. Interacts with host STAT1, STAT2 and PML. Isoform P3 binds host PML.5 Publications

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi190 – 20718Combined sources
Turni208 – 2103Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi222 – 2254Combined sources
Helixi227 – 2304Combined sources
Helixi234 – 2418Combined sources
Helixi247 – 2526Combined sources
Helixi259 – 27012Combined sources
Helixi272 – 2776Combined sources
Helixi280 – 29213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYIX-ray1.50A186-297[»]
ProteinModelPortaliP22363.
SMRiP22363. Positions 186-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22363.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 17235DYNLL1 and DYNLL2 bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 5810Nuclear export signal
Motifi211 – 2144Nuclear localization signal

Sequence similaritiesi

Belongs to the lyssavirus protein P family.Curated

Family and domain databases

InterProiIPR004259. PP_M1.
[Graphical view]
PfamiPF03012. PP_M1. 1 hit.
[Graphical view]
ProDomiPD004155. PP_M1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform P (identifier: P22363-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSKIFVNPSA IRAGLADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDNLP
60 70 80 90 100
EDMKRLHLDD EKSSNLGEMV RVGEGKYRED FQMDEGEDPN LLFQSYLDNV
110 120 130 140 150
GVQIVRQMRS GERFLKIWSQ TVEEIVSYVT VNFPNPPRRS SEDKSTQTTG
160 170 180 190 200
RELKKETTSA FSQRESQPSK ARMVAQVAPG PPALEWSATN EEDDLSVEAE
210 220 230 240 250
IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVKE AKNVPGVTRL
260 270 280 290
AHDGSKIPLR CVLGWVALAN SKKFQLLVEA DKLSKIMQDD LNRYTSC
Length:297
Mass (Da):33,616
Last modified:August 1, 1991 - v1
Checksum:iE93EDE6BFFA4AAB6
GO
Isoform P2 (identifier: P22363-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Show »
Length:278
Mass (Da):31,601
Checksum:i4CA9833BA65120AC
GO
Isoform P3 (identifier: P22363-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:245
Mass (Da):27,857
Checksum:iC43E30CC191C3F10
GO
Isoform P4 (identifier: P22363-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Show »
Length:229
Mass (Da):26,003
Checksum:i25D7A21F4A4DB726
GO
Isoform P5 (identifier: P22363-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Show »
Length:215
Mass (Da):24,307
Checksum:i48C26245875004D2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221V → I in strain: CVS.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8282Missing in isoform P5. CuratedVSP_026783Add
BLAST
Alternative sequencei1 – 6868Missing in isoform P4. CuratedVSP_026784Add
BLAST
Alternative sequencei1 – 5252Missing in isoform P3. CuratedVSP_026785Add
BLAST
Alternative sequencei1 – 1919Missing in isoform P2. CuratedVSP_026786Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55727 Genomic RNA. Translation: CAA39258.1.
X57783 Genomic RNA. Translation: CAA40929.1.
PIRiS13706.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55727 Genomic RNA. Translation: CAA39258.1.
X57783 Genomic RNA. Translation: CAA40929.1.
PIRiS13706.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYIX-ray1.50A186-297[»]
ProteinModelPortaliP22363.
SMRiP22363. Positions 186-296.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP22363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22363.

Family and domain databases

InterProiIPR004259. PP_M1.
[Graphical view]
PfamiPF03012. PP_M1. 1 hit.
[Graphical view]
ProDomiPD004155. PP_M1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide and deduced amino acid sequences of the nominal nonstructural phosphoprotein of the ERA, PM and CVS-11 strains of rabies virus."
    Larson J.K., Wunner W.H.
    Nucleic Acids Res. 18:7172-7172(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Nucleotide sequence of the NS gene of rabies virus CVS strain."
    Mannen K., Takita Y., Hiramatsu K., Mifune K.
    Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: CVS.
  3. "Mapping the interacting domains between the rabies virus polymerase and phosphoprotein."
    Chenik M., Schnell M., Conzelmann K.K., Blondel D.
    J. Virol. 72:1925-1930(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN L.
  4. "Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways."
    Vidy A., Chelbi-Alix M., Blondel D.
    J. Virol. 79:14411-14420(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST STAT1.
  5. "Translation initiation at alternate in-frame AUG codons in the rabies virus phosphoprotein mRNA is mediated by a ribosomal leaky scanning mechanism."
    Chenik M., Chebli K., Blondel D.
    J. Virol. 69:707-712(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.
  6. "The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C."
    Gupta A.K., Blondel D., Choudhary S., Banerjee A.K.
    J. Virol. 74:91-98(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-63; SER-64; SER-162; SER-210 AND SER-271.
  7. "Interaction of the rabies virus P protein with the LC8 dynein light chain."
    Raux H., Flamand A., Blondel D.
    J. Virol. 74:10212-10216(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAT DYNLL1 AND DYNLL2.
  8. "Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P."
    Poisson N., Real E., Gaudin Y., Vaney M.C., King S., Jacob Y., Tordo N., Blondel D.
    J. Gen. Virol. 82:2691-2696(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAT DYNLL1 AND DYNLL2.
  9. "Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies."
    Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P., De The H., Chelbi-Alix M.K.
    Oncogene 21:7957-7970(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HAMSTER PML.
  10. "Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal."
    Pasdeloup D., Poisson N., Raux H., Gaudin Y., Ruigrok R.W., Blondel D.
    Virology 334:284-293(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1."
    Vidy A., El Bougrini J., Chelbi-Alix M.K., Blondel D.
    J. Virol. 81:4255-4263(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERFERON ANTIVIRAL SYSTEM EVASION.
  12. "Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus."
    Mavrakis M., McCarthy A.A., Roche S., Blondel D., Ruigrok R.W.
    J. Mol. Biol. 343:819-831(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-297.

Entry informationi

Entry nameiPHOSP_RABVC
AccessioniPrimary (citable) accession number: P22363
Secondary accession number(s): Q85414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.