Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6R891

- NEB2_MOUSE

UniProt

Q6R891 - NEB2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Neurabin-2

Gene

Ppp1r9b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- 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

  1. actin binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. actin filament organization Source: MGI
  3. calcium-mediated signaling Source: MGI
  4. cell migration Source: UniProtKB
  5. cellular response to morphine Source: UniProtKB
  6. dendrite development Source: MGI
  7. filopodium assembly Source: UniProtKB
  8. negative regulation of cell growth Source: Ensembl
  9. regulation of opioid receptor signaling pathway Source: UniProtKB
  10. regulation of protein phosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2387581. Ppp1r9b.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapse. Cell junctionadherens junction By similarity. Cytoplasm By similarity. Cell membrane By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle membrane By similarity
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. 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).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cortical actin cytoskeleton Source: MGI
  3. cytoplasm Source: UniProtKB
  4. filopodium Source: MGI
  5. lamellipodium Source: UniProtKB
  6. nucleoplasm Source: Ensembl
  7. plasma membrane Source: UniProtKB
  8. ruffle membrane Source: UniProtKB
  9. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151S → E: Increases filopodial density. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 817817Neurabin-2PRO_0000228615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine; by MAPK11 Publication
Modified residuei17 – 171Phosphoserine; by CDK51 Publication
Modified residuei94 – 941Phosphoserine; by PKA1 Publication
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei205 – 2051Phosphoserine; by MAPK11 Publication

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

MaxQBiQ6R891.
PaxDbiQ6R891.
PRIDEiQ6R891.

PTM databases

PhosphoSiteiQ6R891.

Expressioni

Gene expression databases

BgeeiQ6R891.
CleanExiMM_PPP1R9B.
ExpressionAtlasiQ6R891. baseline and differential.
GenevestigatoriQ6R891.

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi229847. 5 interactions.
IntActiQ6R891. 7 interactions.
MINTiMINT-275541.

Structurei

3D structure databases

ProteinModelPortaliQ6R891.
SMRiQ6R891. Positions 424-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 58489PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 154154Actin-bindingBy similarityAdd
BLAST
Regioni100 – 371272Interacts with D(2) dopamine receptorBy similarityAdd
BLAST
Regioni164 – 282119Actin-bindingBy similarityAdd
BLAST
Regioni169 – 25587Interacts with ADRA2A, ADRA2B and ADRA2CBy similarityAdd
BLAST
Regioni417 – 49478Interacts with protein phosphatase 1By similarityAdd
BLAST
Regioni480 – 52546Interacts with RGS2By similarityAdd
BLAST
Regioni595 – 816222Interacts with TGN38By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili595 – 61622Sequence AnalysisAdd
BLAST
Coiled coili665 – 816152Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi575 – 5784PP1-binding motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi253 – 2608Poly-Pro

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

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG314102.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000252962.
HOVERGENiHBG005213.
InParanoidiQ6R891.
KOiK17551.
OMAiPKAAHHK.
OrthoDBiEOG7XM2WV.
PhylomeDBiQ6R891.
TreeFamiTF105540.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6R891) [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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 424424Missing in isoform 2. 1 PublicationVSP_017674Add
BLAST
Alternative sequencei425 – 45632YEPES…STAPI → MDTGLHATQLAQGPSPANVL LPSYGPLRTAPP in isoform 2. 1 PublicationVSP_017675Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY508450 mRNA. Translation: AAR91608.1.
AL606480 Genomic DNA. Translation: CAI23964.1.
AL606480 Genomic DNA. Translation: CAI23965.1.
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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY508450 mRNA. Translation: AAR91608.1 .
AL606480 Genomic DNA. Translation: CAI23964.1 .
AL606480 Genomic DNA. Translation: CAI23965.1 .
BC029672 mRNA. Translation: AAH29672.1 .
CCDSi CCDS25268.1. [Q6R891-1 ]
RefSeqi NP_758465.2. NM_172261.3. [Q6R891-1 ]
UniGenei Mm.229087.

3D structure databases

ProteinModelPortali Q6R891.
SMRi Q6R891. Positions 424-583.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229847. 5 interactions.
IntActi Q6R891. 7 interactions.
MINTi MINT-275541.

PTM databases

PhosphoSitei Q6R891.

Proteomic databases

MaxQBi Q6R891.
PaxDbi Q6R891.
PRIDEi Q6R891.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038696 ; ENSMUSP00000041732 ; ENSMUSG00000038976 . [Q6R891-1 ]
ENSMUST00000107748 ; ENSMUSP00000103377 ; ENSMUSG00000038976 . [Q6R891-2 ]
GeneIDi 217124.
KEGGi mmu:217124.
UCSCi uc007kzr.2. mouse. [Q6R891-1 ]
uc007kzs.2. mouse. [Q6R891-2 ]

Organism-specific databases

CTDi 84687.
MGIi MGI:2387581. Ppp1r9b.

Phylogenomic databases

eggNOGi NOG314102.
GeneTreei ENSGT00390000010033.
HOGENOMi HOG000252962.
HOVERGENi HBG005213.
InParanoidi Q6R891.
KOi K17551.
OMAi PKAAHHK.
OrthoDBi EOG7XM2WV.
PhylomeDBi Q6R891.
TreeFami TF105540.

Miscellaneous databases

ChiTaRSi PPP1R9B. mouse.
NextBioi 375573.
PROi Q6R891.
SOURCEi Search...

Gene expression databases

Bgeei Q6R891.
CleanExi MM_PPP1R9B.
ExpressionAtlasi Q6R891. baseline and differential.
Genevestigatori Q6R891.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
InterProi IPR001478. PDZ.
[Graphical view ]
Pfami PF00595. PDZ. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
PROSITEi PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse spinophilin cDNA."
    Allen P.B.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Eye.
  4. "Regulation of spinophilin Ser94 phosphorylation in neostriatal neurons involves both DARPP-32-dependent and independent pathways."
    Uematsu K., Futter M., Hsieh-Wilson L.C., Higashi H., Maeda H., Nairn A.C., Greengard P., Nishi A.
    J. Neurochem. 95:1642-1652(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKA, PHOSPHORYLATION AT SER-94, DEPHOSPHORYLATION BY PP1 AND PP2A.
  5. Cited for: PHOSPHORYLATION BY MAPK1 AND CDK5, PHOSPHORYLATION AT SER-15; SER-17 AND SER-205, MUTAGENESIS OF SER-15.
  6. "Common and divergent roles for members of the mouse DCX superfamily."
    Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T., Brody Y., Orr I., Barkai N., Eichele G., Reiner O.
    Cell Cycle 5:976-983(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLK2.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNEB2_MOUSE
AccessioniPrimary (citable) accession number: Q6R891
Secondary accession number(s): Q8K0X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3