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 24-JAN-2024, entry version 174. 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; P38398: BRCA1; NbExp=4; IntAct=EBI-351275, EBI-349905; 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="https://atlasgeneticsoncology.org/gene/51558/PPP1R9B"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 208. DR IntAct; Q96SB3; 64. 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 PaxDb; 9606-ENSP00000478767; -. DR PeptideAtlas; Q96SB3; -. DR ProteomicsDB; 78097; -. DR Pumba; Q96SB3; -. DR Antibodypedia; 30484; 171 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 AGR; HGNC:9298; -. 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; APKVPHH; -. DR OrthoDB; 2911512at2759; -. DR PhylomeDB; Q96SB3; -. DR PathwayCommons; Q96SB3; -. DR SignaLink; Q96SB3; -. DR SIGNOR; Q96SB3; -. DR BioGRID-ORCS; 84687; 17 hits in 307 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 163 other cell types or 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: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: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:0030308; P:negative regulation of cell growth; IDA:UniProtKB. 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: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 CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR040645; Neurabin-1/2_PDZ. DR InterPro; IPR043446; Neurabin-like. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR16154; NEURABIN; 1. DR PANTHER; PTHR16154:SF24; NEURABIN-2; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF17817; PDZ_5; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 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 //