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IID50058
UniprotO35274
ProteinNeurabin-2
GenePpp1r9b
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
817
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 417-494
 Evidence NMR Reference
       Region 417-494 disorder
Seq 417-583 Hetero trimer : IID00311Complex
 Evidence X-RAY 3egh D Reference
       Region 3egh D 417-423 disorder
       Region 3egh D 424-489 order
       Region 3egh D 490-583 disorder
 Evidence X-RAY 3egh C Reference
       Region 3egh C 417-423 disorder
       Region 3egh C 424-583 order
Seq 417-583 Hetero dimer : IID00311Complex
 Evidence X-RAY 3egh D Reference
       Region 3egh D 417-423 disorder
       Region 3egh D 424-489 order
       Region 3egh D 490-583 disorder
 Evidence X-RAY 3egg D Reference
       Region 3egg D 417-423 disorder
       Region 3egg D 424-489 order
       Region 3egg D 490-583 disorder
Seq 417-583 Hetero dimer : IID00311Complex
 Evidence X-RAY 3egh C Reference
       Region 3egh C 417-423 disorder
       Region 3egh C 424-583 order
 Evidence X-RAY 3egg C Reference
       Region 3egg C 417-423 disorder
       Region 3egg C 424-583 order
Seq 493-602 Monomer :
 Evidence NMR 2g5m B Reference
       Region 2g5m B 493-583 order
       Region 2g5m B 517-520 high_rmsd
       Region 2g5m B 584-602 disorder
       Region 2g5m B 585-602 high_rmsd
SeqProS verified 424-489 Hetero dimer : IID00311Complex
       Region 3egg C 424-583 order
       Region 3egh C 424-583 order
       Region 417-494 disorder
SeqProS verified 424-489 Hetero trimer : IID00311Complex
       Region 3egh C 424-583 order
       Region 3egh D 424-489 order
       Region 417-494 disorder
SeqProS verified 424-489 Hetero dimer : IID00311Complex
       Region 3egg D 424-489 order
       Region 3egh D 424-489 order
       Region 417-494 disorder
Seqphosphorylation
    15-15 Phosphoserine
    17-17 Phosphoserine
    438-438 Phosphoserine
    658-658 Phosphoserine
    207-207 Phosphothreonine
    205-205 Phosphoserine
    193-193 Phosphothreonine
    192-192 Phosphoserine
    177-177 Phosphoserine; by PKA
    116-116 Phosphoserine; by CaMK2
    100-100 Phosphoserine; by CaMK2
    94-94 Phosphoserine; by PKA
 
Prediction
NeProc
Disorder 1-482,595-670,727-733,815-817
Order 483-594,671-726,734-814
ProS 16-37,48-61,120-126,179-187,378-440,450-470,621-627,652-659,665-670,727-733
AlphaFold
Disorder 1-53,63-423,515-521,586-586,588-588,613-662,815-817
Order 54-62,424-514,522-585,587-587,589-612,663-814
Pfam Hmmer
PF00595 496-581 1.3e-14
SEG 64-84 ,126-142 ,226-237 ,253-260 ,281-317 ,332-361 ,399-430 ,600-612
Function
Function in SwissProt
Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity).