NEB2_HUMAN
ID NEB2_HUMAN Reviewed; 817 AA.
AC Q96SB3; D3DTX6; Q8TCR9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Neurabin-2;
DE AltName: Full=Neurabin-II;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 9B;
DE AltName: Full=Spinophilin;
GN Name=PPP1R9B; Synonyms=PPP1R6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CDKN2A.
RX PubMed=11278317; DOI=10.1074/jbc.m006845200;
RA Vivo M., Calogero R.A., Sansone F., Calabro V., Parisi T., Borrelli L.,
RA Saviozzi S., La Mantia G.;
RT "The human tumor suppressor ARF interacts with spinophilin/neurabin II, a
RT type 1 protein-phosphatase-binding protein.";
RL J. Biol. Chem. 276:14161-14169(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 398-817.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPATA13.
RX PubMed=19151759; DOI=10.1038/onc.2008.478;
RA Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.;
RT "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization
RT and are involved in HGF-induced cell migration.";
RL Oncogene 28:1357-1365(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND THR-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INTERACTION WITH ADRA2B.
RX PubMed=24114805; DOI=10.1002/ana.24028;
RA De Fusco M., Vago R., Striano P., Di Bonaventura C., Zara F., Mei D.,
RA Kim M.S., Muallem S., Chen Y., Wang Q., Guerrini R., Casari G.;
RT "The alpha2B-adrenergic receptor is mutant in cortical myoclonus and
RT epilepsy.";
RL Ann. Neurol. 75:77-87(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; SER-438 AND SER-658, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Seems to act as a scaffold protein in multiple signaling
CC pathways. Modulates excitatory synaptic transmission and dendritic
CC spine morphology. Binds to actin filaments (F-actin) and shows cross-
CC linking activity. Binds along the sides of the F-actin. May play an
CC important role in linking the actin cytoskeleton to the plasma membrane
CC at the synaptic junction. Believed to target protein phosphatase 1/PP1
CC to dendritic spines, which are rich in F-actin, and regulates its
CC specificity toward ion channels and other substrates, such as AMPA-type
CC and NMDA-type glutamate receptors. Plays a role in regulation of G-
CC protein coupled receptor signaling, including dopamine D2 receptors and
CC alpha-adrenergic receptors. May establish a signaling complex for
CC dopaminergic neurotransmission through D2 receptors by linking
CC receptors downstream signaling molecules and the actin cytoskeleton.
CC Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling.
CC May confer to Rac signaling specificity by binding to both, RacGEFs and
CC Rac effector proteins. Probably regulates p70 S6 kinase activity by
CC forming a complex with TIAM1 (By similarity). Required for hepatocyte
CC growth factor (HGF)-induced cell migration. {ECO:0000250,
CC ECO:0000269|PubMed:19151759}.
CC -!- SUBUNIT: Interacts with DCLK2 (By similarity). Possibly exists as a
CC homodimer, homotrimer or a homotetramer. Interacts with F-actin,
CC PPP1CA, neurabin-1, TGN38 and D(2) dopamine receptor. Interacts with
CC RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A,
CC PPP1R2, RASGFR1 and TIAM1. Interacts (via C-terminus) with SPATA13 (via
CC C-terminal tail). Interacts with ADRA2B. {ECO:0000250|UniProtKB:Q6R891,
CC ECO:0000269|PubMed:11278317, ECO:0000269|PubMed:19151759,
CC ECO:0000269|PubMed:24114805}.
CC -!- INTERACTION:
CC Q96SB3; P62136: PPP1CA; NbExp=6; IntAct=EBI-351275, EBI-357253;
CC Q96SB3; P62140: PPP1CB; NbExp=2; IntAct=EBI-351275, EBI-352350;
CC Q96SB3; P36873: PPP1CC; NbExp=5; IntAct=EBI-351275, EBI-356283;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:O35274}. Postsynaptic density
CC {ECO:0000250|UniProtKB:O35274}. Synapse. Cell junction, adherens
CC junction {ECO:0000250}. Cytoplasm. Cell membrane. Cell projection,
CC lamellipodium. Cell projection, filopodium. Cell projection, ruffle
CC membrane. Note=Enriched at synapse and cadherin-based cell-cell
CC adhesion sites. In neurons, both cytosolic and membrane-associated, and
CC highly enriched in the postsynaptic density apposed to exitatory
CC synapses. Colocalizes with PPP1R2 at actin-rich adherens junctions in
CC epithelial cells and in dendritic spines (By similarity). Accumulates
CC in the lamellipodium, filopodium and ruffle membrane in response to
CC hepatocyte growth factor (HGF) treatment. {ECO:0000250}.
CC -!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
CC binding, it acquires structure, blocks a substrate-binding site, and
CC restricts PP1 phosphatase specificity to a subset of substrates.
CC {ECO:0000250}.
CC -!- PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94
CC phosphorylation. Dephosphorylation of Ser-94 is mediated mainly by PP1
CC and to a lesser extent by PP2A. Phosphorylation of spinophilin disrupts
CC its association with F-actin, but does not affect its binding to PP1
CC (By similarity). {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PPP1R9BID51558ch17q21.html";
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DR EMBL; AJ401189; CAC37685.1; -; mRNA.
DR EMBL; ABBA01041227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF495721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94638.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94637.1; -; Genomic_DNA.
DR EMBL; AL713642; CAD28455.2; -; mRNA.
DR CCDS; CCDS74102.1; -.
DR RefSeq; NP_115984.3; NM_032595.4.
DR AlphaFoldDB; Q96SB3; -.
DR BMRB; Q96SB3; -.
DR SMR; Q96SB3; -.
DR BioGRID; 124202; 159.
DR IntAct; Q96SB3; 56.
DR MINT; Q96SB3; -.
DR STRING; 9606.ENSP00000478767; -.
DR GlyGen; Q96SB3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96SB3; -.
DR PhosphoSitePlus; Q96SB3; -.
DR BioMuta; PPP1R9B; -.
DR DMDM; 90101416; -.
DR EPD; Q96SB3; -.
DR jPOST; Q96SB3; -.
DR MassIVE; Q96SB3; -.
DR MaxQB; Q96SB3; -.
DR PeptideAtlas; Q96SB3; -.
DR PRIDE; Q96SB3; -.
DR ProteomicsDB; 78097; -.
DR Antibodypedia; 30484; 149 antibodies from 28 providers.
DR DNASU; 84687; -.
DR Ensembl; ENST00000612501.2; ENSP00000478767.1; ENSG00000108819.11.
DR GeneID; 84687; -.
DR KEGG; hsa:84687; -.
DR MANE-Select; ENST00000612501.2; ENSP00000478767.1; NM_032595.5; NP_115984.3.
DR UCSC; uc032fmj.2; human.
DR CTD; 84687; -.
DR DisGeNET; 84687; -.
DR GeneCards; PPP1R9B; -.
DR HGNC; HGNC:9298; PPP1R9B.
DR HPA; ENSG00000108819; Tissue enhanced (brain).
DR MIM; 603325; gene.
DR neXtProt; NX_Q96SB3; -.
DR OpenTargets; ENSG00000108819; -.
DR PharmGKB; PA33662; -.
DR VEuPathDB; HostDB:ENSG00000108819; -.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000158833; -.
DR HOGENOM; CLU_007401_1_0_1; -.
DR InParanoid; Q96SB3; -.
DR OMA; AHKEEVD; -.
DR OrthoDB; 128743at2759; -.
DR PhylomeDB; Q96SB3; -.
DR PathwayCommons; Q96SB3; -.
DR SignaLink; Q96SB3; -.
DR SIGNOR; Q96SB3; -.
DR BioGRID-ORCS; 84687; 17 hits in 250 CRISPR screens.
DR ChiTaRS; PPP1R9B; human.
DR GeneWiki; PPP1R9B; -.
DR GenomeRNAi; 84687; -.
DR Pharos; Q96SB3; Tbio.
DR PRO; PR:Q96SB3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96SB3; protein.
DR Bgee; ENSG00000108819; Expressed in right hemisphere of cerebellum and 161 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990780; C:cytoplasmic side of dendritic spine plasma membrane; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
DR GO; GO:0044326; C:dendritic spine neck; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; TAS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR GO; GO:0008157; F:protein phosphatase 1 binding; NAS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071315; P:cellular response to morphine; ISS:UniProtKB.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; IMP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1904372; P:positive regulation of protein localization to actin cortical patch; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:1903119; P:protein localization to actin cytoskeleton; IEA:Ensembl.
DR GO; GO:1990778; P:protein localization to cell periphery; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:UniProtKB.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; TAS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; NAS:UniProtKB.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0061458; P:reproductive system development; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0097338; P:response to clozapine; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:1904373; P:response to kainic acid; IEA:Ensembl.
DR GO; GO:1904386; P:response to L-phenylalanine derivative; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0034695; P:response to prostaglandin E; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029921; NEB2.
DR InterPro; IPR040645; Neurabin-1/2_PDZ.
DR InterPro; IPR043446; Neurabin-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16154; PTHR16154; 1.
DR PANTHER; PTHR16154:SF24; PTHR16154:SF24; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17817; PDZ_5; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Membrane;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..817
FT /note="Neurabin-2"
FT /id="PRO_0000228614"
FT DOMAIN 496..584
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..154
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 100..371
FT /note="Interaction with D(2) dopamine receptor"
FT /evidence="ECO:0000250"
FT REGION 164..283
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 169..255
FT /note="Interaction with ADRA2A, ADRA2B and ADRA2C"
FT /evidence="ECO:0000250"
FT REGION 216..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..494
FT /note="Interaction with protein phosphatase 1"
FT /evidence="ECO:0000250"
FT REGION 480..525
FT /note="Interaction with RGS2"
FT /evidence="ECO:0000250"
FT REGION 595..816
FT /note="Interaction with TGN38"
FT /evidence="ECO:0000250"
FT COILED 671..788
FT /evidence="ECO:0000255"
FT MOTIF 447..451
FT /note="PP1-binding motif"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R891"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R891"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R891"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 201
FT /note="A -> T (in dbSNP:rs8079707)"
FT /id="VAR_059776"
FT CONFLICT 159
FT /note="A -> G (in Ref. 1; CAC37685)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Missing (in Ref. 1; CAC37685)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="Missing (in Ref. 1; CAC37685)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="V -> VRC (in Ref. 1; CAC37685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 89334 MW; 706A359FE8382DBB CRC64;
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKGAHHKKY GSNVHRIKSM
FLQMGTTAGP SGEAGGGAGL AEAPRASERG VRLSLPRASS LNENVDHSAL LKLGTSVSER
VSRFDSKPAP SAQPAPPPHP PSRLQETRKL FERSAPAAAG GDKEAAARRL LRQERAGLQD
RKLDVVVRFN GSTEALDKLD ADAVSPTVSQ LSAVFEKADS RTGLHRGPGL PRAAGVPQVN
SKLVSKRSRV FQPPPPPPPA PSGDAPAEKE RCPAGQQPPQ HRVAPARPPP KPREVRKIKP
VEVEESGESE AESAPGEVIQ AEVTVHAALE NGSTVATAAS PAPEEPKAQA APEKEAAAVA
PPERGVGNGR APDVAPEEVD ESKKEDFSEA DLVDVSAYSG LGEDSAGSAL EEDDEDDEED
GEPPYEPESG CVEIPGLSEE EDPAPSRKIH FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS
AEYELEKRVE RLELFPVELE KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD
GRIQVNDLLV EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL AENEDALSPV
DMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG RWRVEKAQLE QSVEENKERM
EKLEGYWGEA QSLCQAVDEH LRETQAQYQA LERKYSKAKR LIKDYQQKEI EFLKKETAQR
RVLEESELAR KEEMDKLLDK ISELEGNLQT LRNSNST
