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UniProtKB - Q96SB3 (NEB2_HUMAN)

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Protein

Neurabin-2

Gene

PPP1R9B

Organism
Homo sapiens (Human)
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 (By similarity). Required for hepatocyte growth factor (HGF)-induced cell migration.By similarity1 Publication

GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • protein phosphatase 1 binding Source: UniProtKB
  • protein phosphatase inhibitor activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell cycle arrest Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • cell migration Source: UniProtKB
  • cellular response to morphine Source: UniProtKB
  • filopodium assembly Source: UniProtKB
  • modulation of chemical synaptic transmission Source: InterPro
  • negative regulation of cell growth Source: UniProtKB
  • nervous system development Source: UniProtKB-KW
  • regulation of cell growth by extracellular stimulus Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of exit from mitosis Source: UniProtKB
  • regulation of opioid receptor signaling pathway Source: UniProtKB
  • RNA splicing Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin-binding, Developmental protein
Biological processDifferentiation, Neurogenesis

Enzyme and pathway databases

SignaLinkiQ96SB3
SIGNORiQ96SB3

Names & Taxonomyi

Protein namesi
Recommended name:
Neurabin-2
Alternative name(s):
Neurabin-II
Protein phosphatase 1 regulatory subunit 9B
Spinophilin
Gene namesi
Name:PPP1R9B
Synonyms:PPP1R6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9298 PPP1R9B
MIMi603325 gene
neXtProtiNX_Q96SB3

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

Organism-specific databases

DisGeNETi84687
PharmGKBiPA33662

Polymorphism and mutation databases

BioMutaiPPP1R9B
DMDMi90101416

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002286141 – 815Neurabin-2Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineBy similarity1
Modified residuei17PhosphoserineBy similarity1
Modified residuei94PhosphoserineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei116PhosphoserineBy similarity1
Modified residuei190PhosphoserineCombined sources1
Modified residuei191PhosphothreonineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei205PhosphothreonineCombined sources1
Modified residuei436PhosphoserineCombined sources1
Modified residuei656PhosphoserineCombined sources1

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

EPDiQ96SB3
MaxQBiQ96SB3
PeptideAtlasiQ96SB3
PRIDEiQ96SB3
ProteomicsDBi78097

PTM databases

iPTMnetiQ96SB3
PhosphoSitePlusiQ96SB3

Expressioni

Gene expression databases

CleanExiHS_PPP1R9B

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). Interacts with ADRA2B.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621364EBI-351275,EBI-357253

GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • protein phosphatase 1 binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi124202, 48 interactors
IntActiQ96SB3, 36 interactors
MINTiQ96SB3

Structurei

3D structure databases

ProteinModelPortaliQ96SB3
SMRiQ96SB3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini494 – 582PDZPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 154Actin-bindingBy similarityAdd BLAST154
Regioni100 – 369Interaction with D(2) dopamine receptorBy similarityAdd BLAST270
Regioni163 – 281Actin-bindingBy similarityAdd BLAST119
Regioni167 – 253Interaction with ADRA2A, ADRA2B and ADRA2CBy similarityAdd BLAST87
Regioni415 – 492Interaction with protein phosphatase 1By similarityAdd BLAST78
Regioni478 – 523Interaction with RGS2By similarityAdd BLAST46
Regioni593 – 814Interaction with TGN38By similarityAdd BLAST222

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili593 – 614Sequence analysisAdd BLAST22
Coiled coili663 – 814Sequence analysisAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi445 – 449PP1-binding motifBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi251 – 259Poly-Pro9

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

HOVERGENiHBG005213
InParanoidiQ96SB3
KOiK17551
PhylomeDBiQ96SB3

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

Sequencei

Sequence statusi: Complete.

Q96SB3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKGAHHKKY 
        60         70         80         90        100
GSNVHRIKSM FLQMGTTAGP SGEAGGGAGL AEAPRASERG VRLSLPRASS 
       110        120        130        140        150
LNENVDHSAL LKLGTSVSER VSRFDSKPAP SAQPAPPPHP PSRLQETRKL 
       160        170        180        190        200
FERSAPAAGG DKEAARRLLR QERAGLQDRK LDVVVRFNGS TEALDKLDAD 
       210        220        230        240        250
AVSPTVSQLS AVFEKADSRT GLHRGPGLPR AAGVPQVNSK LVSKRSRVFQ 
       260        270        280        290        300
PPPPPPPAPS GDAPAEKERC PAGQQPPQHR VAPARPPPKP REVRKIKPVE 
       310        320        330        340        350
VEESGESEAE SAPGEVIQAE VTVHAALENG STVATAASPA PEEPKAQAAP 
       360        370        380        390        400
EKEAAAVAPP ERGVGNGRAP DVAPEEVDES KKEDFSEADL VDVSAYSGLG 
       410        420        430        440        450
EDSAGSALEE DDEDDEEDGE PPYEPESGCV EIPGLSEEED PAPSRKIHFS 
       460        470        480        490        500
TAPIQVFSTY SNEDYDRRNE DVDPMAASAE YELEKRVERL ELFPVELEKD 
       510        520        530        540        550
SEGLGISIIG MGAGADMGLE KLGIFVKTVT EGGAAHRDGR IQVNDLLVEV 
       560        570        580        590        600
DGTSLVGVTQ SFAASVLRNT KGRVRFMIGR ERPGEQSEVA QLIQQTLEQE 
       610        620        630        640        650
RWQREMMEQR YAQYGEDDEE TGEYATDEDE ELSPTFPGGE MAIEVFELAE 
       660        670        680        690        700
NEDALSPVDM EPEKLVHKFK ELQIKHAVTE AEIQQLKRKL QSLEQEKGRW 
       710        720        730        740        750
RVEKAQLEQS VEENKERMEK LEGYWGEAQS LCQAVDEHLR ETQAQYQALE 
       760        770        780        790        800
RKYSKAKRLI KDYQQKEIEF LKKETAQRRV LEESELARKE EMDKLLDKIS 
       810 
ELEGNLQTLR NSNST
Length:815
Mass (Da):89,192
Last modified:March 21, 2006 - v2
Checksum:iD004CAA7030D3267
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti574V → VRC in CAC37685 (PubMed:11278317).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_059776199A → T. Corresponds to variant dbSNP:rs8079707Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ401189 mRNA Translation: CAC37685.1
AL713642 mRNA Translation: CAD28455.2
RefSeqiNP_115984.3, NM_032595.4
UniGeneiHs.514323

Genome annotation databases

EnsembliENST00000316878; ENSP00000475417; ENSG00000108819
GeneIDi84687
KEGGihsa:84687

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNEB2_HUMAN
AccessioniPrimary (citable) accession number: Q96SB3
Secondary accession number(s): Q8TCR9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 18, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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