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Protein

Neurabin-2

Gene

Ppp1r9b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 similarity2 Publications

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • ion channel binding Source: RGD
  • kinase binding Source: RGD
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein kinase activity Source: RGD
  • protein phosphatase 1 binding Source: RGD
  • protein phosphatase inhibitor activity Source: RGD

GO - Biological processi

  • actin filament depolymerization Source: RGD
  • aging Source: RGD
  • calcium-mediated signaling Source: GO_Central
  • cell migration Source: UniProtKB
  • cellular response to drug Source: RGD
  • cellular response to epidermal growth factor stimulus Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • cellular response to light stimulus Source: RGD
  • cellular response to morphine Source: UniProtKB
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to peptide Source: RGD
  • cerebral cortex development Source: RGD
  • dendrite development Source: Ensembl
  • developmental process involved in reproduction Source: RGD
  • filopodium assembly Source: UniProtKB
  • hippocampus development Source: RGD
  • learning Source: RGD
  • male mating behavior Source: RGD
  • modulation of synaptic transmission Source: InterPro
  • negative regulation of phosphoprotein phosphatase activity Source: RGD
  • neuron projection development Source: GO_Central
  • positive regulation of cellular protein localization Source: RGD
  • positive regulation of establishment of protein localization to plasma membrane Source: RGD
  • positive regulation of protein localization to actin cortical patch Source: RGD
  • protein localization to actin cytoskeleton Source: RGD
  • protein localization to cell periphery Source: RGD
  • regulation of cell proliferation Source: InterPro
  • regulation of opioid receptor signaling pathway Source: UniProtKB
  • regulation of protein phosphorylation Source: Ensembl
  • reproductive system development Source: RGD
  • response to amino acid Source: RGD
  • response to amphetamine Source: RGD
  • response to clozapine Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to immobilization stress Source: RGD
  • response to kainic acid Source: RGD
  • response to L-phenylalanine derivative Source: RGD
  • response to nicotine Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to prostaglandin E Source: RGD
  • response to steroid hormone Source: RGD
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
Neural tissue-specific F-actin-binding protein II
PP1bp134
Protein phosphatase 1 regulatory subunit 9B
Spinophilin
p130
Gene namesi
Name:Ppp1r9b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi632281. Ppp1r9b.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: RGD
  • adherens junction Source: UniProtKB-SubCell
  • cortical actin cytoskeleton Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoplasmic side of dendritic spine plasma membrane Source: RGD
  • dendritic spine Source: RGD
  • dendritic spine head Source: RGD
  • dendritic spine membrane Source: RGD
  • dendritic spine neck Source: RGD
  • filopodium Source: UniProtKB
  • growth cone Source: RGD
  • lamellipodium Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: RGD
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi59S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi87S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi94S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi99S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi100S → A: Diminishes phosphorylation. 2 Publications1
Mutagenesisi116S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi122S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi126S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi177S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi447 – 451Missing : Abolishes protein phosphatase 1 binding. 1 Publication5
Mutagenesisi451F → A: Abolishes protein phosphatase 1 binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715091 – 817Neurabin-2Add BLAST817

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineBy similarity1
Modified residuei17PhosphoserineBy similarity1
Modified residuei94Phosphoserine; by PKA1 Publication1
Modified residuei100Phosphoserine; by CaMK2Combined sources2 Publications1
Modified residuei116Phosphoserine; by CaMK21 Publication1
Modified residuei177Phosphoserine; by PKA1 Publication1
Modified residuei192PhosphoserineBy similarity1
Modified residuei193PhosphothreonineBy similarity1
Modified residuei205PhosphoserineCombined sources1
Modified residuei207PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1

Post-translational modificationi

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 PP1.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35274.
PRIDEiO35274.

PTM databases

iPTMnetiO35274.
PhosphoSitePlusiO35274.

Expressioni

Tissue specificityi

Ubiquitous. Abundantly expressed in the brain. Expressed at highest levels in hippocampus and at lower levels in the cortex, cerebellum and brainstem. Localizes to the dendritic spines of neurons. Also localizes to aspiny neurons, such as GABAergic interneurons.

Developmental stagei

Expression is low during embryogenesis and increases around postnatal day 21.

Gene expression databases

BgeeiENSRNOG00000004052.
GenevisibleiO35274. RN.

Interactioni

Subunit structurei

Interacts with DCLK2 (By similarity). 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 ADRA2B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Drd2P611692EBI-80022,EBI-80012
Ppp1ccP630883EBI-80022,EBI-80049

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • ion channel binding Source: RGD
  • kinase binding Source: RGD
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein phosphatase 1 binding Source: RGD

Protein-protein interaction databases

DIPiDIP-30882N.
IntActiO35274. 4 interactors.
MINTiMINT-8057892.
STRINGi10116.ENSRNOP00000005498.

Structurei

Secondary structure

1817
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi431 – 434Combined sources4
Beta strandi456 – 461Combined sources6
Turni464 – 466Combined sources3
Helixi476 – 489Combined sources14
Beta strandi492 – 500Combined sources9
Beta strandi505 – 513Combined sources9
Beta strandi515 – 518Combined sources4
Beta strandi521 – 531Combined sources11
Helixi536 – 540Combined sources5
Beta strandi548 – 552Combined sources5
Helixi562 – 571Combined sources10
Beta strandi574 – 582Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G5MNMR-B493-602[»]
3EGGX-ray1.85C/D417-583[»]
3EGHX-ray2.00C/D417-583[»]
ProteinModelPortaliO35274.
SMRiO35274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35274.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 154Actin-bindingAdd BLAST154
Regioni100 – 371Interaction with D(2) dopamine receptorAdd BLAST272
Regioni164 – 282Actin-bindingAdd BLAST119
Regioni169 – 255Interaction with ADRA2A, ADRA2B and ADRA2C1 PublicationAdd BLAST87
Regioni417 – 494Interaction with protein phosphatase 1Add BLAST78
Regioni480 – 525Interaction with RGS21 PublicationAdd BLAST46
Regioni595 – 816Interaction with TGN381 PublicationAdd 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 motif1 Publication5

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.

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1945. Eukaryota.
ENOG410Y7F2. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000252962.
HOVERGENiHBG005213.
InParanoidiO35274.
KOiK17551.
OMAiHLNNAAN.
OrthoDBiEOG091G0NSU.
PhylomeDBiO35274.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR029921. NEB2.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR16154:SF24. PTHR16154:SF24. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY
60 70 80 90 100
GSNVHRIKSM FLQMGTTTGP PGEAGGASGM AEAPRASDRG VRLSLPRASS
110 120 130 140 150
LNENVDHSAL LKLGTSVSER VSRFDSKPAP SAQPAPPPHP PSRLQETRKL
160 170 180 190 200
FERSVPAASG GDKEAVARRL LRQERASLQD RKLDVVVRFN GSTEALDKLD
210 220 230 240 250
ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN SKLVTKRSRV
260 270 280 290 300
FQPPPPPPAP SGDAATEKDR GPGGQQPPQH RVAPARPPPK PREVRKIKPV
310 320 330 340 350
EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTTATTASP APEEPKAEAV
360 370 380 390 400
PEEEASSSVA 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):89,646
Last modified:January 1, 1998 - v1
Checksum:iD31D3E94EE2FFB6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016252 mRNA. Translation: AAB72005.1.
AF027181 Genomic DNA. Translation: AAC05183.1.
PIRiT03852.
RefSeqiNP_445926.1. NM_053474.1.
UniGeneiRn.6764.

Genome annotation databases

EnsembliENSRNOT00000089497; ENSRNOP00000074026; ENSRNOG00000052113.
GeneIDi84686.
KEGGirno:84686.
UCSCiRGD:632281. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016252 mRNA. Translation: AAB72005.1.
AF027181 Genomic DNA. Translation: AAC05183.1.
PIRiT03852.
RefSeqiNP_445926.1. NM_053474.1.
UniGeneiRn.6764.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G5MNMR-B493-602[»]
3EGGX-ray1.85C/D417-583[»]
3EGHX-ray2.00C/D417-583[»]
ProteinModelPortaliO35274.
SMRiO35274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-30882N.
IntActiO35274. 4 interactors.
MINTiMINT-8057892.
STRINGi10116.ENSRNOP00000005498.

PTM databases

iPTMnetiO35274.
PhosphoSitePlusiO35274.

Proteomic databases

PaxDbiO35274.
PRIDEiO35274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000089497; ENSRNOP00000074026; ENSRNOG00000052113.
GeneIDi84686.
KEGGirno:84686.
UCSCiRGD:632281. rat.

Organism-specific databases

CTDi84687.
RGDi632281. Ppp1r9b.

Phylogenomic databases

eggNOGiKOG1945. Eukaryota.
ENOG410Y7F2. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000252962.
HOVERGENiHBG005213.
InParanoidiO35274.
KOiK17551.
OMAiHLNNAAN.
OrthoDBiEOG091G0NSU.
PhylomeDBiO35274.

Miscellaneous databases

EvolutionaryTraceiO35274.
PROiO35274.

Gene expression databases

BgeeiENSRNOG00000004052.
GenevisibleiO35274. RN.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR029921. NEB2.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR16154:SF24. PTHR16154:SF24. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEB2_RAT
AccessioniPrimary (citable) accession number: O35274
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 138 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.