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Details on Person UniProt:P03421 P

Class:Id	ReferenceGeneProduct:9825431
_chainChangeLog	chain:1-241 for 9825431 added on Fri February 24 2023
_displayName	UniProt:P03421 P
_timestamp	2024-11-03 20:20:45
chain	chain:1-241
checksum	21A9E45CA2DFD50C
comment	FUNCTION Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (PubMed:25568210, PubMed:26474524). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (PubMed:26474524). Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA (PubMed:26474524). Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs (PubMed:25568210). Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (PubMed:29489893). Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (By similarity).SUBUNIT Homotetramer (PubMed:15166449, PubMed:22978633). Interacts with protein M2-1; the interaction between the two tetramers is required for the anti-termination and elongation transcriptional activities of protein M2-1 (PubMed:12970453, PubMed:17098979, PubMed:22978633, PubMed:26474524, PubMed:29489893). Interacts with host phosphatase PP1; this interaction recruits PP1 to the inclusion bodies (PubMed:29489893). Formation of a complex PP1/M2-1/P allows P to target host PP1 phosphatase to the M2-1 substrate (PubMed:29489893). Interacts (via C-terminus) with the nucleoprotein N (via N-terminus); the phosphorylated phosphoprotein P binds to N-RNA complex (PubMed:11861854, PubMed:12368320, PubMed:17170452, PubMed:22623798, PubMed:25407889, PubMed:26474524). Interacts (via N-terminus) with the monomeric RNA-free nucleoprotein N (PubMed:25568210, PubMed:28031463, PubMed:30626736). Interacts (via C-terminus) with RNA-directed RNA polymerase L; the association of P and L forms the polymerase complex (PubMed:25653447, PubMed:26474524, PubMed:31953395).SUBCELLULAR LOCATION Localizes in cytoplasmic inclusion bodies.DOMAIN The N-terminus is important for viral particle assembly (PubMed:31009855). The oligomerization region is central (PubMed:15166449). The C-terminus part contains binding regions for the RNA-directed RNA polymerase L and the nucleoprotein (PubMed:26474524).PTM Constitutively phosphorylated by host (PubMed:17098979). Phosphorylation at S-116, S-117, S-119, S-232 and S-237 is required for transcription inhibition by M2-2 and viral particle egress (PubMed:26474524). Phosphorylation at S-232 and S-237 increases the affinity of the binding to the nucleoprotein (PubMed:25407889).SIMILARITY Belongs to the pneumoviridae phosphoprotein P family.
created	[InstanceEdit:9825429] Orlic-Milacic, Marija, 2023-01-26
description	recommendedName: Phosphoprotein shortName: Protein P
geneName	P
identifier	P03421
isSequenceChanged	FALSE
keyword	3D-structure Host cytoplasm Host-virus interaction Inhibition of host NF-kappa-B by virus Phosphoprotein Viral RNA replication Virion
modified	[InstanceEdit:9829221] Weiser, Joel [InstanceEdit:9834092] Weiser, Joel [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03
name	P
referenceDatabase	[ReferenceDatabase:2] UniProt
secondaryIdentifier	PHOSP_HRSVA P90196
sequenceLength	241
species	[Species:9717528] Human respiratory syncytial virus A
(referenceEntity)	[EntityWithAccessionedSequence:9825432] p-P [cytosol] [Human respiratory syncytial virus A] [EntityWithAccessionedSequence:9831695] Nascent P [cytosol] [Human respiratory syncytial virus A] [EntityWithAccessionedSequence:9832783] p-S232,S237-P [cytosol] [Human respiratory syncytial virus A]
(referenceSequence)	[ModifiedResidue:9831524] O-phospho-L-serine at 117 [ModifiedResidue:9831526] O-phospho-L-serine at 119 [ModifiedResidue:9831530] O-phospho-L-serine at 232 [ModifiedResidue:9831539] O-phospho-L-serine at 156 [ModifiedResidue:9831545] O-phospho-L-threonine at 108 [ModifiedResidue:9831551] O-phospho-L-serine at 116 [ModifiedResidue:9831553] O-phospho-L-serine at 237 [ModifiedResidue:9831558] O-phospho-L-serine at 54
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No pathways have been reviewed or authored by UniProt:P03421 P (9825431)