ID   Q8BMP0_MOUSE            Unreviewed;       447 AA.
AC   Q8BMP0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 101.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 prepare
RT   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., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   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., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   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., 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., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   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 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.
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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; TSKLAHK; -.
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:0042802; F:identical protein 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: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   Proteomics identification {ECO:0000213|MaxQB:Q8BMP0,
KW   ECO:0000213|PeptideAtlas:Q8BMP0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..53
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..170
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..210
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..274
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..315
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..397
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..433
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         447
FT                   /evidence="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
//