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Protein

Neurabin-2

Gene

PPP1R9B

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

GO - Molecular functioni

  • protein phosphatase 1 binding Source: UniProtKB
  • protein phosphatase inhibitor activity Source: UniProtKB

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
  • negative regulation of catalytic activity Source: GOC
  • 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
  • regulation of synaptic transmission Source: InterPro
  • RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ96SB3.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9298. PPP1R9B.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • dendritic spine Source: UniProtKB-SubCell
  • filopodium Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein phosphatase type 1 complex Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33662.

Polymorphism and mutation databases

BioMutaiPPP1R9B.
DMDMi90101416.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 815815Neurabin-2PRO_0000228614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei203 – 2031Phosphoserine3 Publications
Modified residuei205 – 2051Phosphothreonine1 Publication
Modified residuei436 – 4361Phosphoserine1 Publication
Modified residuei656 – 6561Phosphoserine1 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

MaxQBiQ96SB3.
PaxDbiQ96SB3.
PRIDEiQ96SB3.

PTM databases

PhosphoSiteiQ96SB3.

Expressioni

Gene expression databases

CleanExiHS_PPP1R9B.
GenevisibleiQ96SB3. HS.

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 similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621365EBI-351275,EBI-357253

Protein-protein interaction databases

BioGridi124202. 22 interactions.
IntActiQ96SB3. 17 interactions.
MINTiMINT-193423.

Structurei

3D structure databases

ProteinModelPortaliQ96SB3.
SMRiQ96SB3. Positions 422-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 58289PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 154154Actin-bindingBy similarityAdd
BLAST
Regioni100 – 369270Interacts with D(2) dopamine receptorBy similarityAdd
BLAST
Regioni163 – 281119Actin-bindingBy similarityAdd
BLAST
Regioni167 – 25387Interacts with ADRA2A, ADRA2B and ADRA2CBy similarityAdd
BLAST
Regioni415 – 49278Interacts with protein phosphatase 1By similarityAdd
BLAST
Regioni478 – 52346Interacts with RGS2By similarityAdd
BLAST
Regioni593 – 814222Interacts with TGN38By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili593 – 61422Sequence AnalysisAdd
BLAST
Coiled coili663 – 814152Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi573 – 5764PP1-binding motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 2599Poly-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.
HOVERGENiHBG005213.
InParanoidiQ96SB3.
KOiK17551.
OMAiHLNNAAN.
PhylomeDBiQ96SB3.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti574 – 5741V → VRC in CAC37685 (PubMed:11278317).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991A → T.
Corresponds to variant rs8079707 [ dbSNP | Ensembl ].
VAR_059776

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

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

3D structure databases

ProteinModelPortaliQ96SB3.
SMRiQ96SB3. Positions 422-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124202. 22 interactions.
IntActiQ96SB3. 17 interactions.
MINTiMINT-193423.

PTM databases

PhosphoSiteiQ96SB3.

Polymorphism and mutation databases

BioMutaiPPP1R9B.
DMDMi90101416.

Proteomic databases

MaxQBiQ96SB3.
PaxDbiQ96SB3.
PRIDEiQ96SB3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316878; ENSP00000475417; ENSG00000108819.
GeneIDi84687.
KEGGihsa:84687.

Organism-specific databases

CTDi84687.
GeneCardsiGC17M048211.
H-InvDBHIX0202435.
HGNCiHGNC:9298. PPP1R9B.
MIMi603325. gene.
neXtProtiNX_Q96SB3.
PharmGKBiPA33662.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314102.
HOVERGENiHBG005213.
InParanoidiQ96SB3.
KOiK17551.
OMAiHLNNAAN.
PhylomeDBiQ96SB3.

Enzyme and pathway databases

SignaLinkiQ96SB3.

Miscellaneous databases

ChiTaRSiPPP1R9B. human.
GeneWikiiPPP1R9B.
GenomeRNAii84687.
NextBioi74732.
PROiQ96SB3.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PPP1R9B.
GenevisibleiQ96SB3. HS.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The human tumor suppressor ARF interacts with spinophilin/neurabin II, a type 1 protein-phosphatase-binding protein."
    Vivo M., Calogero R.A., Sansone F., Calabro V., Parisi T., Borrelli L., Saviozzi S., La Mantia G.
    J. Biol. Chem. 276:14161-14169(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-815.
    Tissue: Amygdala.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization and are involved in HGF-induced cell migration."
    Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.
    Oncogene 28:1357-1365(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPATA13.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-436 AND SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNEB2_HUMAN
AccessioniPrimary (citable) accession number: Q96SB3
Secondary accession number(s): Q8TCR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: June 24, 2015
This is version 112 of the entry and version 2 of the sequence. [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
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.