Ppp1r9b
entrez
84686
canonical
uniprot
O35274
canonical
ensembl
ENSRNOG00000052113
resolver
ensembl
ENSRNOG00055032697
resolver
ensembl
ENSRNOG00060021417
resolver
ensembl
ENSRNOG00065017558
resolver
ensp
ENSRNOP00000074026
resolver
ensp
ENSRNOP00055046615
resolver
ensp
ENSRNOP00060030707
resolver
ensp
ENSRNOP00065023321
resolver
enst
ENSRNOT00000089497
resolver
enst
ENSRNOT00055056509
resolver
enst
ENSRNOT00060037218
resolver
enst
ENSRNOT00065029375
resolver
genesymbol
Ppp1r9b
resolver
genesymbol_syn
Spino
resolver
uniprot_entry
NEB2_RAT
resolver
amino_acid_sequence
MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTTGPPGEAGGASGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERASLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDAATEKDRGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTTATTASPAPEEPKAEAVPEEEASSSVATLERGVDNGRAPDMAPEEVDESKKEDFSEADLVDVSAYSGLGEDSGGSALEEDDEEDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVEMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250, ECO:0000269|PubMed:15743906, ECO:0000269|PubMed:15793568}.
uniprot
proteins
mass_dalton
89646
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 59; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 87; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 94; /note="S->A: Diminishes phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 99; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 100; /note="S->A: Diminishes phosphorylation."; /evidence="ECO:0000269|PubMed:12417592, ECO:0000269|PubMed:15228588"; MUTAGEN 116; /note="S->A: Diminishes phosphorylation."; /evidence="ECO:0000269|PubMed:15228588"; MUTAGEN 122; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 126; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 177; /note="S->A: Diminishes phosphorylation."; /evidence="ECO:0000269|PubMed:12417592"; MUTAGEN 447..451; /note="Missing: Abolishes protein phosphatase 1 binding."; /evidence="ECO:0000269|PubMed:10194355"; MUTAGEN 451; /note="F->A: Abolishes protein phosphatase 1 binding."; /evidence="ECO:0000269|PubMed:10194355
uniprot
proteins
post_translational_modification
PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 and Ser-177 phosphorylation. Dephosphorylation of these residues is mediated by PP1 and possibly PP2A. Spinophilin unphosphorylated or phosphorylated at Ser-94 is concentrated in the postsynaptic density, whereas spinophilin phosphorylated at Ser-177 is absent from the postsynaptic density and enriched in the cytosol. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1. {ECO:0000269|PubMed:12417592, ECO:0000269|PubMed:15228588}.
uniprot
proteins
pubmed
10194355
uniprot
proteins
pubmed
10391935
uniprot
proteins
pubmed
10514494
uniprot
proteins
pubmed
10585469
uniprot
proteins
pubmed
11154706
uniprot
proteins
pubmed
12417592
uniprot
proteins
pubmed
12531897
uniprot
proteins
pubmed
15135218
uniprot
proteins
pubmed
15228588
uniprot
proteins
pubmed
15514983
uniprot
proteins
pubmed
15743906
uniprot
proteins
pubmed
15793568
uniprot
proteins
pubmed
20305656
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9275233
uniprot
proteins
pubmed
9452470
uniprot
proteins
sequence_length
817
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:15514983}. Cell junction, adherens junction. Cell projection, dendritic spine {ECO:0000269|PubMed:15514983}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Enriched at synapse and cadherin-based cell-cell adhesion sites. In neurons, both cytosolic and membrane-associated, and highly enriched in the postsynaptic density apposed to exitatory synapses (PubMed:15514983). Colocalizes with PPP1R2 at actin-rich adherens junctions in epithelial cells and in dendritic spines. Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment (By similarity). {ECO:0000250, ECO:0000269|PubMed:15514983}.
uniprot
proteins