PPR1B_MOUSE
ID PPR1B_MOUSE Reviewed; 194 AA.
AC Q60829; A2A564; Q3URF2; Q6DV86; Q91XB5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 1B;
DE AltName: Full=DARPP-32;
DE AltName: Full=Dopamine- and cAMP-regulated neuronal phosphoprotein;
GN Name=Ppp1r1b;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Liu Q.-R., Uhl G.R.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=BALB/cJ;
RX PubMed=7485543; DOI=10.1152/ajprenal.1995.269.4.f564;
RA Blau S., Daly L., Fienberg A., Teitelman G., Ehrlich M.E.;
RT "DARPP-32 promoter directs transgene expression to renal thick ascending
RT limb of loop of Henle.";
RL Am. J. Physiol. 269:F564-F570(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-194.
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-46; THR-75; SER-97
RP AND SER-192, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Pancreas;
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).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60829-1; Sequence=Displayed;
CC Name=2; Synonyms=DARPP-30;
CC IsoId=Q60829-2; Sequence=VSP_025058;
CC -!- PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation of Thr-34 is required for activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC {ECO:0000305}.
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DR EMBL; AY640620; AAT66920.1; -; mRNA.
DR EMBL; AY640621; AAT66921.1; -; mRNA.
DR EMBL; AL591390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011122; AAH11122.1; -; mRNA.
DR EMBL; BC026568; AAH26568.1; -; mRNA.
DR EMBL; BC031129; AAH31129.1; -; mRNA.
DR EMBL; U23160; AAA93223.1; -; Genomic_DNA.
DR EMBL; AK141563; BAE24736.1; -; mRNA.
DR CCDS; CCDS25344.1; -. [Q60829-1]
DR CCDS; CCDS83889.1; -. [Q60829-2]
DR RefSeq; NP_001300899.1; NM_001313970.1. [Q60829-2]
DR RefSeq; NP_659077.1; NM_144828.2. [Q60829-1]
DR AlphaFoldDB; Q60829; -.
DR SMR; Q60829; -.
DR BioGRID; 202338; 3.
DR STRING; 10090.ENSMUSP00000077760; -.
DR iPTMnet; Q60829; -.
DR PhosphoSitePlus; Q60829; -.
DR MaxQB; Q60829; -.
DR PaxDb; Q60829; -.
DR PeptideAtlas; Q60829; -.
DR PRIDE; Q60829; -.
DR ProteomicsDB; 291836; -. [Q60829-1]
DR ProteomicsDB; 291837; -. [Q60829-2]
DR Antibodypedia; 28294; 769 antibodies from 41 providers.
DR DNASU; 19049; -.
DR Ensembl; ENSMUST00000078694; ENSMUSP00000077760; ENSMUSG00000061718. [Q60829-1]
DR Ensembl; ENSMUST00000137634; ENSMUSP00000123528; ENSMUSG00000061718. [Q60829-2]
DR Ensembl; ENSMUST00000150762; ENSMUSP00000121147; ENSMUSG00000061718. [Q60829-2]
DR GeneID; 19049; -.
DR KEGG; mmu:19049; -.
DR UCSC; uc007lfz.1; mouse. [Q60829-1]
DR CTD; 84152; -.
DR MGI; MGI:94860; Ppp1r1b.
DR VEuPathDB; HostDB:ENSMUSG00000061718; -.
DR eggNOG; ENOG502S19Z; Eukaryota.
DR GeneTree; ENSGT00730000111283; -.
DR HOGENOM; CLU_092269_3_0_1; -.
DR InParanoid; Q60829; -.
DR OMA; EDPCEGD; -.
DR OrthoDB; 1412891at2759; -.
DR PhylomeDB; Q60829; -.
DR TreeFam; TF332576; -.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR BioGRID-ORCS; 19049; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ppp1r1b; mouse.
DR PRO; PR:Q60829; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60829; protein.
DR Bgee; ENSMUSG00000061718; Expressed in caudate-putamen and 109 other tissues.
DR Genevisible; Q60829; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031750; F:D3 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031751; F:D4 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031752; F:D5 dopamine receptor binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; TAS:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0071314; P:cellular response to cocaine; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0007621; P:negative regulation of female receptivity; IDA:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR GO; GO:0043278; P:response to morphine; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IGI:MGI.
DR InterPro; IPR015670; DARPP-32.
DR InterPro; IPR008466; PPP1R1A/B/C.
DR PANTHER; PTHR15417; PTHR15417; 1.
DR PANTHER; PTHR15417:SF2; PTHR15417:SF2; 1.
DR Pfam; PF05395; DARPP-32; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..194
FT /note="Protein phosphatase 1 regulatory subunit 1B"
FT /id="PRO_0000071474"
FT REGION 1..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P07516"
FT MOD_RES 34
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P07516"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6J4I0"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025058"
SQ SEQUENCE 194 AA; 21781 MW; E0509291E6615EA3 CRC64;
MDPKDRKKIQ FSVPAPPSQL DPRQVEMIRR RRPTPAMLFR VSEHSSPEEE ASPHQRTSGE
GHHPKSKRPN PCAYTPPSLK AVQHLQTISN LSENQASEEE DELGELRELG YPQEDDEEDE
DEEEDEEEDS QAEVLKGSRG TVGQKPTCGR GLEGPWERPP PLDEPQRDGN SEDQVEGRAT
LSEPGEEPQH PSPP
