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Protein

Phosphoprotein

Gene

P

Organism
Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N0. Plays a role in virion assembly (By similarity).By similarity

GO - Molecular functioni

Keywordsi

Molecular functionChaperone
Biological processViral RNA replication

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoprotein
Short name:
Protein P
Alternative name(s):
Protein M1
Gene namesi
Name:P
OrganismiVesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV)
Taxonomic identifieri11279 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesRhabdoviridaeVesiculovirus
Virus hostiAedes [TaxID: 7158]
Bos taurus (Bovine) [TaxID: 9913]
Culicoides [TaxID: 58271]
Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Lutzomyia [TaxID: 252607]
Musca domestica (House fly) [TaxID: 7370]
Simuliidae (black flies) [TaxID: 7190]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002228371 – 265PhosphoproteinAdd BLAST265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60Phosphoserine; by host CK2By similarity1
Modified residuei62Phosphothreonine; by host CK2By similarity1
Modified residuei64Phosphoserine; by host CK2By similarity1
Modified residuei226Phosphoserine; by hostBy similarity1
Modified residuei227Phosphoserine; by hostBy similarity1

Post-translational modificationi

Domain I is phosphorylated by host CK2. Domain II is phosphorylated by other unknown kinases. Phosphorylation play an important role in facilitating trimerization and possibly P-L complex formation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotrimer when phosphorylated in domain I. This trimer is stabilized by binding to the L protein. Binds N0, and N in ribonucleocapsid.

Structurei

Secondary structure

1265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP04880
SMRiP04880
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04880

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 137Domain IBy similarityAdd BLAST137
Regioni150 – 210HingeBy similarityAdd BLAST61
Regioni211 – 244Domain IIBy similarityAdd BLAST34
Regioni245 – 265Domain III:By similarityAdd BLAST21

Domaini

Sequences comparison studies have defined several domains. Domain I binds the protein L, contains phosphorylation sites required for trimerization and is involved in transcription. Hinge region is highly variable and may act as a spacer between domain I and II. Domain II is also phosphorylated, binds protein L, and plays a role in replication. Domain III is basic and essential for binding the N-RNA template (By similarity).By similarity

Sequence similaritiesi

Belongs to the vesiculovirus protein P family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR037263 Phosphoprotein_central
IPR000224 Phosphoprotein_vesiculovirus
PfamiView protein in Pfam
PF00922 Phosphoprotein, 1 hit
SUPFAMiSSF160892 SSF160892, 1 hit

Sequencei

Sequence statusi: Complete.

P04880-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNLTKVREY LKSYSRLDQA VGEIDEIEAQ RAEKSNYELF QEDGVEEHTR
60 70 80 90 100
PSYFQAADDS DTESEPEIED NQGLYVPDPE AEQVEGFIQG PLDDYADEDV
110 120 130 140 150
DVVFTSDWKQ PELESDEHGK TLRLTLPEGL SGEQKSQWLL TIKAVVQSAK
160 170 180 190 200
HWNLAECTFE ASGEGVIIKK RQITPDVYKV TPVMNTHPYQ SEAVSDVWSL
210 220 230 240 250
SKTSMTFQPK KASLQPLTIS LDELFSSRGE FISVGGNGRM SHKEAILLGL
260
RYKKLYNQAR VKYSL
Length:265
Mass (Da):30,035
Last modified:August 13, 1987 - v1
Checksum:i49E9C49627191803
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04196 Genomic RNA Translation: CAA27788.1
PIRiA29144 MNVNIM

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04196 Genomic RNA Translation: CAA27788.1
PIRiA29144 MNVNIM

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FQMX-ray2.30A/B/C/D/E/F107-177[»]
3HHWX-ray2.70A/B/C/D/E183-265[»]
3HHZX-ray3.50A/B/C/D/E183-265[»]
ProteinModelPortaliP04880
SMRiP04880
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04880

Family and domain databases

InterProiView protein in InterPro
IPR037263 Phosphoprotein_central
IPR000224 Phosphoprotein_vesiculovirus
PfamiView protein in Pfam
PF00922 Phosphoprotein, 1 hit
SUPFAMiSSF160892 SSF160892, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPHOSP_VSIVM
AccessioniPrimary (citable) accession number: P04880
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 22, 2017
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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