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Protein

Neurabin-2

Gene

Ppp1r9b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Developmental protein
Biological processDifferentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Neurabin-2
Alternative name(s):
Neurabin-II
Protein phosphatase 1 regulatory subunit 9B
Spinophilin
Gene namesi
Name:Ppp1r9b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2387581 Ppp1r9b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15S → E: Increases filopodial density. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002286151 – 817Neurabin-2Add BLAST817

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15Phosphoserine; by MAPK11 Publication1
Modified residuei17Phosphoserine; by CDK51 Publication1
Modified residuei94Phosphoserine; by PKA1 Publication1
Modified residuei100PhosphoserineBy similarity1
Modified residuei116PhosphoserineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei193PhosphothreonineBy similarity1
Modified residuei205Phosphoserine; by MAPK11 Publication1
Modified residuei207PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1

Post-translational modificationi

Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 phosphorylation. Dephosphorylation of Ser-94 is mediated mainly by PP1 and to a lesser extent by PP2A. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6R891
PaxDbiQ6R891
PeptideAtlasiQ6R891
PRIDEiQ6R891

PTM databases

iPTMnetiQ6R891
PhosphoSitePlusiQ6R891

Expressioni

Gene expression databases

BgeeiENSMUSG00000038976
CleanExiMM_PPP1R9B
GenevisibleiQ6R891 MM

Interactioni

Subunit structurei

Possibly exists as a homodimer, homotrimer or a homotetramer. Interacts with F-actin, PPP1CA, neurabin-1, TGN38 and D2 dopamine receptor. Interacts with RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and TIAM1. Interacts (via C-terminus) with SPATA13 (via C-terminal tail) (By similarity). Interacts with DCLK2. Interacts with ADRA2B (By similarity).By similarity1 Publication

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: Ensembl
  • protein phosphatase 1 binding Source: Ensembl

Protein-protein interaction databases

BioGridi229847, 8 interactors
IntActiQ6R891, 12 interactors
MINTiQ6R891
STRINGi10090.ENSMUSP00000041732

Structurei

3D structure databases

ProteinModelPortaliQ6R891
SMRiQ6R891
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini496 – 584PDZPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 154Actin-bindingBy similarityAdd BLAST154
Regioni100 – 371Interaction with D(2) dopamine receptorBy similarityAdd BLAST272
Regioni164 – 282Actin-bindingBy similarityAdd BLAST119
Regioni169 – 255Interaction with ADRA2A, ADRA2B and ADRA2CBy similarityAdd BLAST87
Regioni417 – 494Interaction with protein phosphatase 1By similarityAdd BLAST78
Regioni480 – 525Interaction with RGS2By similarityAdd BLAST46
Regioni595 – 816Interaction with TGN38By similarityAdd BLAST222

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili595 – 616Sequence analysisAdd BLAST22
Coiled coili665 – 816Sequence analysisAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi447 – 451PP1-binding motifBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi253 – 260Poly-Pro8

Domaini

The PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1945 Eukaryota
ENOG410Y7F2 LUCA
GeneTreeiENSGT00390000010033
HOGENOMiHOG000252962
HOVERGENiHBG005213
InParanoidiQ6R891
KOiK17551
OMAiFNGSTEA
OrthoDBiEOG091G0NSU
PhylomeDBiQ6R891
TreeFamiTF105540

Family and domain databases

InterProiView protein in InterPro
IPR029921 NEB2
IPR001478 PDZ
IPR036034 PDZ_sf
PANTHERiPTHR16154:SF24 PTHR16154:SF24, 1 hit
PfamiView protein in Pfam
PF00595 PDZ, 1 hit
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
PROSITEiView protein in PROSITE
PS50106 PDZ, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6R891-1) [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
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY
60 70 80 90 100
GSNVHRIKSM FLQMGTTAGP PGEAGGGAGM AEAPRASDRG VRLSLPRASS
110 120 130 140 150
LNENVDHSAL LKLGTSVSER VSRFDSKPAP SAQPAPPPHP PSRLQETRKL
160 170 180 190 200
FERSVPAASG GDKEAVARRL LRQERAGLQD RKLDVVVRFN GSTEALDKLD
210 220 230 240 250
ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN SKLVTKRSRV
260 270 280 290 300
FQPPPPPPAP SGDGATEKER GPGGQQPPQH RVAPARPPPK PREVRKIKPV
310 320 330 340 350
EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTPATTASP APEEPKAEAV
360 370 380 390 400
PEEEAAASVA TLERGVDNGR APDMAPEEVD ESKKEDFSEA DLVDVSAYSG
410 420 430 440 450
LGEDSGGSAL EEDDEEDEED GEPPYEPESG CVEIPGLSEE EDPAPSRKIH
460 470 480 490 500
FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS AEYELEKRVE RLELFPVELE
510 520 530 540 550
KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD GRIQVNDLLV
560 570 580 590 600
EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
610 620 630 640 650
QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL
660 670 680 690 700
AENEDALSPV EMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG
710 720 730 740 750
RWRVEKAQLE QSVEENKERM EKLEGYWGEA QSLCQAVDEH LRETQAQYQA
760 770 780 790 800
LERKYSKAKR LIKDYQQKEI EFLKKETAQR RVLEESELAR KEEMDKLLDK
810
ISELEGNLQT LRNSNST
Length:817
Mass (Da):89,520
Last modified:July 5, 2004 - v1
Checksum:i1654037C196F2F6B
GO
Isoform 2 (identifier: Q6R891-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-424: Missing.
     425-456: YEPESGCVEIPGLSEEEDPAPSRKIHFSTAPI → MDTGLHATQLAQGPSPANVLLPSYGPLRTAPP

Show »
Length:393
Mass (Da):44,846
Checksum:i2CC9E6E92DBC8A80
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0176741 – 424Missing in isoform 2. 1 PublicationAdd BLAST424
Alternative sequenceiVSP_017675425 – 456YEPES…STAPI → MDTGLHATQLAQGPSPANVL LPSYGPLRTAPP in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY508450 mRNA Translation: AAR91608.1
AL606480 Genomic DNA No translation available.
BC029672 mRNA Translation: AAH29672.1
CCDSiCCDS25268.1 [Q6R891-1]
RefSeqiNP_758465.2, NM_172261.3 [Q6R891-1]
UniGeneiMm.229087

Genome annotation databases

EnsembliENSMUST00000038696; ENSMUSP00000041732; ENSMUSG00000038976 [Q6R891-1]
ENSMUST00000107748; ENSMUSP00000103377; ENSMUSG00000038976 [Q6R891-2]
GeneIDi217124
KEGGimmu:217124
UCSCiuc007kzr.2 mouse [Q6R891-1]
uc007kzs.2 mouse [Q6R891-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiNEB2_MOUSE
AccessioniPrimary (citable) accession number: Q6R891
Secondary accession number(s): Q8K0X7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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