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Q96SB3

- NEB2_HUMAN

UniProt

Q96SB3 - NEB2_HUMAN

Protein

Neurabin-2

Gene

PPP1R9B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      Previous versions | rss
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    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

    1. protein binding Source: UniProtKB
    2. protein phosphatase 1 binding Source: UniProtKB
    3. protein phosphatase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. calcium-mediated signaling Source: Ensembl
    3. cell cycle arrest Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. cellular response to morphine Source: UniProtKB
    6. dendrite development Source: Ensembl
    7. filopodium assembly Source: UniProtKB
    8. negative regulation of catalytic activity Source: GOC
    9. negative regulation of cell growth Source: UniProtKB
    10. regulation of cell growth by extracellular stimulus Source: UniProtKB
    11. regulation of cell proliferation Source: UniProtKB
    12. regulation of exit from mitosis Source: UniProtKB
    13. regulation of opioid receptor signaling pathway Source: UniProtKB
    14. regulation of protein phosphorylation Source: Ensembl
    15. RNA splicing Source: UniProtKB

    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: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9298. PPP1R9B.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapse. Cell junctionadherens junction By similarity. Cytoplasm. Cell membrane. Cell projectionlamellipodium. Cell projectionfilopodium. Cell projectionruffle membrane
    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 By similarity. Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment.By similarity

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. cortical actin cytoskeleton Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. dendritic spine Source: UniProtKB-SubCell
    5. filopodium Source: UniProtKB
    6. lamellipodium Source: UniProtKB
    7. nucleoplasm Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. protein phosphatase type 1 complex Source: UniProtKB
    10. ruffle membrane Source: UniProtKB
    11. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33662.

    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

    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.
    GenevestigatoriQ96SB3.

    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. 21 interactions.
    IntActiQ96SB3. 17 interactions.
    MINTiMINT-193423.
    STRINGi9606.ENSP00000320510.

    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.
    OMAiPKAAHHK.
    PhylomeDBiQ96SB3.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q96SB3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKGAHHKKY    50
    GSNVHRIKSM FLQMGTTAGP SGEAGGGAGL AEAPRASERG VRLSLPRASS 100
    LNENVDHSAL LKLGTSVSER VSRFDSKPAP SAQPAPPPHP PSRLQETRKL 150
    FERSAPAAGG DKEAARRLLR QERAGLQDRK LDVVVRFNGS TEALDKLDAD 200
    AVSPTVSQLS AVFEKADSRT GLHRGPGLPR AAGVPQVNSK LVSKRSRVFQ 250
    PPPPPPPAPS GDAPAEKERC PAGQQPPQHR VAPARPPPKP REVRKIKPVE 300
    VEESGESEAE SAPGEVIQAE VTVHAALENG STVATAASPA PEEPKAQAAP 350
    EKEAAAVAPP ERGVGNGRAP DVAPEEVDES KKEDFSEADL VDVSAYSGLG 400
    EDSAGSALEE DDEDDEEDGE PPYEPESGCV EIPGLSEEED PAPSRKIHFS 450
    TAPIQVFSTY SNEDYDRRNE DVDPMAASAE YELEKRVERL ELFPVELEKD 500
    SEGLGISIIG MGAGADMGLE KLGIFVKTVT EGGAAHRDGR IQVNDLLVEV 550
    DGTSLVGVTQ SFAASVLRNT KGRVRFMIGR ERPGEQSEVA QLIQQTLEQE 600
    RWQREMMEQR YAQYGEDDEE TGEYATDEDE ELSPTFPGGE MAIEVFELAE 650
    NEDALSPVDM EPEKLVHKFK ELQIKHAVTE AEIQQLKRKL QSLEQEKGRW 700
    RVEKAQLEQS VEENKERMEK LEGYWGEAQS LCQAVDEHLR ETQAQYQALE 750
    RKYSKAKRLI KDYQQKEIEF LKKETAQRRV LEESELARKE EMDKLLDKIS 800
    ELEGNLQTLR NSNST 815
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi90101416.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ401189 mRNA. Translation: CAC37685.1 .
    AL713642 mRNA. Translation: CAD28455.2 .
    RefSeqi NP_115984.3. NM_032595.4.
    UniGenei Hs.514323.

    3D structure databases

    ProteinModelPortali Q96SB3.
    SMRi Q96SB3. Positions 422-581.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124202. 21 interactions.
    IntActi Q96SB3. 17 interactions.
    MINTi MINT-193423.
    STRINGi 9606.ENSP00000320510.

    PTM databases

    PhosphoSitei Q96SB3.

    Polymorphism databases

    DMDMi 90101416.

    Proteomic databases

    MaxQBi Q96SB3.
    PaxDbi Q96SB3.
    PRIDEi Q96SB3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316878 ; ENSP00000475417 ; ENSG00000108819 .
    GeneIDi 84687.
    KEGGi hsa:84687.

    Organism-specific databases

    CTDi 84687.
    GeneCardsi GC17M048211.
    H-InvDB HIX0202435.
    HGNCi HGNC:9298. PPP1R9B.
    MIMi 603325. gene.
    neXtProti NX_Q96SB3.
    PharmGKBi PA33662.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314102.
    HOVERGENi HBG005213.
    InParanoidi Q96SB3.
    KOi K17551.
    OMAi PKAAHHK.
    PhylomeDBi Q96SB3.

    Enzyme and pathway databases

    SignaLinki Q96SB3.

    Miscellaneous databases

    ChiTaRSi PPP1R9B. human.
    GeneWikii PPP1R9B.
    GenomeRNAii 84687.
    NextBioi 74732.
    PROi Q96SB3.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_PPP1R9B.
    Genevestigatori Q96SB3.

    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

    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].

    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: October 1, 2014
    This is version 106 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