ID Q8BMP0_MOUSE Unreviewed; 447 AA. AC Q8BMP0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 31-JUL-2019, entry version 99. DE SubName: Full=Protein phosphatase 1, regulatory subunit 9A {ECO:0000313|Ensembl:ENSMUSP00000135634}; DE Flags: Fragment; GN Name=Ppp1r9a {ECO:0000313|Ensembl:ENSMUSP00000135634, GN ECO:0000313|MGI:MGI:2442401}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC26944.1}; RN [1] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., RA Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., RA Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T., RA Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S., RA Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M., RA Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y., RA Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., RA Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M., RA Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T., RA Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [7] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAC26944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26944.1}; RC TISSUE=Pituitary gland {ECO:0000313|EMBL:BAC26944.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [9] {ECO:0000213|PubMed:16452087} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [10] {ECO:0000313|Ensembl:ENSMUSP00000135634, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000135634, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [11] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [12] {ECO:0000313|Ensembl:ENSMUSP00000135634} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000135634}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. 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; AC068500; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC074225; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK030399; BAC26944.1; -; mRNA. DR Ensembl; ENSMUST00000177338; ENSMUSP00000135634; ENSMUSG00000032827. DR MGI; MGI:2442401; Ppp1r9a. DR eggNOG; KOG1945; Eukaryota. DR eggNOG; ENOG410Y7F2; LUCA. DR GeneTree; ENSGT00940000155538; -. DR OMA; IKDMFMQ; -. DR ChiTaRS; Ppp1r9a; mouse. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; ENSMUSG00000032827; Expressed in 232 organ(s), highest expression level in caudate-putamen. DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI. DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; IDA:MGI. DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI. DR GO; GO:0030175; C:filopodium; IDA:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:1990761; C:growth cone lamellipodium; ISO:MGI. DR GO; GO:0030027; C:lamellipodium; ISO:MGI. DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI. DR GO; GO:0043005; C:neuron projection; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0051015; F:actin filament binding; ISO:MGI. DR GO; GO:0051020; F:GTPase binding; ISO:MGI. DR GO; GO:0044325; F:ion channel binding; ISO:MGI. DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0007015; P:actin filament organization; IPI:MGI. DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI. DR GO; GO:0097237; P:cellular response to toxic substance; ISO:MGI. DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISO:MGI. DR GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; ISO:MGI. DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI. DR GO; GO:0031175; P:neuron projection development; ISO:MGI. DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI. DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI. DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI. DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISO:MGI. DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI. DR GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI. DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISO:MGI. DR InterPro; IPR029994; Neurabin-1. DR PANTHER; PTHR16154:SF22; PTHR16154:SF22; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Proteomics identification {ECO:0000213|MaxQB:Q8BMP0, KW ECO:0000213|PeptideAtlas:Q8BMP0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT REGION 1 66 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 85 113 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 125 224 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 249 398 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 414 447 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 8 28 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 31 53 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 97 111 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 137 170 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 174 210 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 258 274 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 287 315 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 371 397 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 418 433 Acidic. {ECO:0000256|SAM:MobiDB-lite}. FT NON_TER 447 447 {ECO:0000313|EMBL:BAC26944.1}. SQ SEQUENCE 447 AA; 49118 MW; D2098BFC9AA4DD9C CRC64; MLKAESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKSD GEQKTKEGEG SQQSRGRKYG SNVNRIKNLF MQMGMEPSEN AAIIAKTRGK GRPSSPQRRM KPKEFVEKTD GSVVKLESSV SERISRFDTM HDGPSYAKFT ETRKMFERSV HESGQNHRYS PKKEKGGGTE PQDEWGGSKS NRGSSDSLDS LSPRTEAVSP TVSQLSAVFE NSEPPGALTS GKAESADYSV TGHYPLNLPS VTVTNLDTFG RLKDSNSKPP SNKQDTDTED AQKSDAVPVP EVAQKGTSLA SLPSEESQLS TEAEDVTTAQ PEALDSTDKD SPEEPSAENQ AMPKSHILSP RNEPLEDAEA NVVGSERAQH QKKDLTGGDL TSPDASASSC GREVPEDSNS FESSHVYMHS DYNVYRVRSR YNSDWGETGT EQDEEEDSDE NNYYQPDMEY SEIVGLP //