PP1A_MOUSE
ID PP1A_MOUSE Reviewed; 330 AA.
AC P62137; P08129; P20653; P22802; Q3U7G7; Q9Z1G2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
DE Short=PP-1A;
DE EC=3.1.3.16;
GN Name=Ppp1ca; Synonyms=Ppp1a;
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].
RA Ortiz J.M., Lorenzo M.L., Eguiraun A., Andres I., Sangrador A.,
RA Allshire R., Hastie N.D.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Extraembryonic tissue, Liver, Pancreas, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PROTEIN SEQUENCE OF 44-74; 114-122 AND 247-260, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
RX PubMed=8077208; DOI=10.1016/s0021-9258(17)31686-1;
RA Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
RT "Molecular cloning of a protein serine/threonine phosphatase containing a
RT putative regulatory tetratricopeptide repeat domain.";
RL J. Biol. Chem. 269:22586-22592(1994).
RN [6]
RP INTERACTION WITH PPP1R15B.
RX PubMed=14638860; DOI=10.1083/jcb.200308075;
RA Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.;
RT "Inhibition of a constitutive translation initiation factor 2alpha
RT phosphatase, CReP, promotes survival of stressed cells.";
RL J. Cell Biol. 163:767-775(2003).
RN [7]
RP IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
RX PubMed=16835242; DOI=10.1074/jbc.m513556200;
RA Latreille M., Larose L.;
RT "Nck in a complex containing the catalytic subunit of protein phosphatase 1
RT regulates eukaryotic initiation factor 2alpha signaling and cell survival
RT to endoplasmic reticulum stress.";
RL J. Biol. Chem. 281:26633-26644(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH PHACTR4.
RX PubMed=17609112; DOI=10.1016/j.devcel.2007.04.018;
RA Kim T.H., Goodman J., Anderson K.V., Niswander L.;
RT "Phactr4 regulates neural tube and optic fissure closure by controlling
RT PP1-, Rb-, and E2F1-regulated cell-cycle progression.";
RL Dev. Cell 13:87-102(2007).
RN [9]
RP INTERACTION WITH BTBD10.
RX PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004;
RA Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.;
RT "A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits
RT familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal
RT death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB.";
RL Cell. Signal. 20:493-505(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
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]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21712997; DOI=10.1371/journal.pone.0021325;
RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the
RT mammalian circadian clock.";
RL PLoS ONE 6:E21325-E21325(2011).
RN [13]
RP FUNCTION IN CIRCADIAN CLOCK, AND MUTAGENESIS OF ASP-64 AND ASP-95.
RX PubMed=21930935; DOI=10.1073/pnas.1107178108;
RA Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
RT "The period of the circadian oscillator is primarily determined by the
RT balance between casein kinase 1 and protein phosphatase 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
RN [14]
RP FUNCTION.
RX PubMed=22215812; DOI=10.1101/gad.179283.111;
RA Zhang Y., Kim T.H., Niswander L.;
RT "Phactr4 regulates directional migration of enteric neural crest through
RT PP1, integrin signaling, and cofilin activity.";
RL Genes Dev. 26:69-81(2012).
RN [15]
RP INTERACTION WITH KCTD20.
RX PubMed=24156551; DOI=10.1186/1471-2091-14-27;
RA Nawa M., Matsuoka M.;
RT "KCTD20, a relative of BTBD10, is a positive regulator of Akt.";
RL BMC Biochem. 14:27-27(2013).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC proteins to form highly specific holoenzymes which dephosphorylate
CC hundreds of biological targets. Protein phosphatase 1 (PP1) is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis.
CC Involved in regulation of ionic conductances and long-term synaptic
CC plasticity. May play an important role in dephosphorylating substrates
CC such as the postsynaptic density-associated Ca(2+)/calmodulin dependent
CC protein kinase II. Component of the PTW/PP1 phosphatase complex, which
CC plays a role in the control of chromatin structure and cell cycle
CC progression during the transition from mitosis into interphase.
CC Regulates NEK2 function in terms of kinase activity and centrosome
CC number and splitting, both in the presence and absence of radiation-
CC induced DNA damage. Regulator of neural tube and optic fissure closure,
CC and enteric neural crest cell (ENCCs) migration during development. In
CC balance with CSNK1D and CSNK1E, determines the circadian period length,
CC through the regulation of the speed and rhythmicity of PER1 and PER2
CC phosphorylation. May dephosphorylate CSNK1D and CSNK1E.
CC Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139'
CC residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex,
CC thereby inhibiting autophagy (By similarity).
CC {ECO:0000250|UniProtKB:P62136, ECO:0000269|PubMed:17609112,
CC ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:21930935,
CC ECO:0000269|PubMed:22215812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then complexed to one or several targeting or
CC regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to
CC myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C,
CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts
CC with PPP1R9A, PPP1R9B and PPP1R7. Interacts with PPP1R15A; the
CC interaction mediates binding to EIF2S1. Interacts with YLPM1. Forms a
CC complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with
CC NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts. with RPSA only in
CC the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex,
CC composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
CC Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the
CC presence of PPP1R10/PNUTS. Interacts with PPP1R39. Interacts with
CC TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms
CC a complex at the p21 promoter site (By similarity). Interacts with
CC PPP1R15B; the interaction mediates binding to EIF2S1. Part of a complex
CC containing PPP1R15B, PP1 and NCK1/2. Interacts with NEK2. Interacts
CC with FER; this promotes phosphorylation at Thr-320 (By similarity).
CC Interacts with PHACTR4; which acts as an activator of PP1 activity.
CC Interacts with BTBD10 (PubMed:18160256). Interacts with KCTD20
CC (PubMed:24156551). Interacts with FOXP3 (By similarity). Interacts with
CC CENPA (By similarity). Interacts with ATG16L1 (By similarity). Found in
CC a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity).
CC {ECO:0000250|UniProtKB:P62136, ECO:0000250|UniProtKB:P62139,
CC ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242,
CC ECO:0000269|PubMed:17609112, ECO:0000269|PubMed:18160256,
CC ECO:0000269|PubMed:24156551}.
CC -!- INTERACTION:
CC P62137; Q9WTL8: Arntl; NbExp=2; IntAct=EBI-357187, EBI-644534;
CC P62137; O35625: Axin1; NbExp=2; IntAct=EBI-357187, EBI-2365912;
CC P62137; P41136: Id2; NbExp=2; IntAct=EBI-357187, EBI-309167;
CC P62137; P17918: Pcna; NbExp=2; IntAct=EBI-357187, EBI-1173716;
CC P62137; Q3UM45: Ppp1r7; NbExp=3; IntAct=EBI-357187, EBI-8318179;
CC P62137; Q9WTX5: Skp1; NbExp=2; IntAct=EBI-357187, EBI-1202363;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
CC Note=Primarily nuclear and largely excluded from the nucleolus. Highly
CC mobile in cells and can be relocalized through interaction with
CC targeting subunits. NOM1 plays a role in targeting this protein to the
CC nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to
CC nuclear speckles (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence of
CC ionizing radiation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; U25809; AAC99814.1; -; mRNA.
DR EMBL; AK007932; BAB25358.1; -; mRNA.
DR EMBL; AK028392; BAC25928.1; -; mRNA.
DR EMBL; AK090070; BAC41078.1; -; mRNA.
DR EMBL; AK151582; BAE30522.1; -; mRNA.
DR EMBL; AK152667; BAE31402.1; -; mRNA.
DR EMBL; AK153517; BAE32060.1; -; mRNA.
DR EMBL; AK159575; BAE35196.1; -; mRNA.
DR EMBL; AK167244; BAE39365.1; -; mRNA.
DR EMBL; AK167538; BAE39605.1; -; mRNA.
DR EMBL; AK167880; BAE39893.1; -; mRNA.
DR EMBL; AK167981; BAE39973.1; -; mRNA.
DR EMBL; BC014828; AAH14828.1; -; mRNA.
DR CCDS; CCDS29421.1; -.
DR RefSeq; NP_114074.1; NM_031868.2.
DR PDB; 5ZQV; X-ray; 2.95 A; A/B/C/D=1-330.
DR PDB; 5ZT0; X-ray; 3.32 A; A/B/C/D/E/F=7-300.
DR PDBsum; 5ZQV; -.
DR PDBsum; 5ZT0; -.
DR AlphaFoldDB; P62137; -.
DR SMR; P62137; -.
DR BioGRID; 202335; 172.
DR IntAct; P62137; 168.
DR MINT; P62137; -.
DR STRING; 10090.ENSMUSP00000039109; -.
DR iPTMnet; P62137; -.
DR PhosphoSitePlus; P62137; -.
DR SwissPalm; P62137; -.
DR EPD; P62137; -.
DR jPOST; P62137; -.
DR MaxQB; P62137; -.
DR PaxDb; P62137; -.
DR PeptideAtlas; P62137; -.
DR PRIDE; P62137; -.
DR ProteomicsDB; 291640; -.
DR Antibodypedia; 3872; 625 antibodies from 40 providers.
DR DNASU; 19045; -.
DR Ensembl; ENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385.
DR GeneID; 19045; -.
DR KEGG; mmu:19045; -.
DR UCSC; uc008fzg.1; mouse.
DR CTD; 5499; -.
DR MGI; MGI:103016; Ppp1ca.
DR VEuPathDB; HostDB:ENSMUSG00000040385; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000153472; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P62137; -.
DR OMA; YLVMESR; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P62137; -.
DR TreeFam; TF354243; -.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR BioGRID-ORCS; 19045; 20 hits in 76 CRISPR screens.
DR ChiTaRS; Ppp1ca; mouse.
DR PRO; PR:P62137; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P62137; protein.
DR Bgee; ENSMUSG00000040385; Expressed in embryonic brain and 61 other tissues.
DR Genevisible; P62137; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0042587; C:glycogen granule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; TAS:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; TAS:MGI.
DR GO; GO:0010288; P:response to lead ion; ISO:MGI.
DR DisProt; DP03014; -.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037979; PPP1CA.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Biological rhythms; Carbohydrate metabolism;
KW Cell cycle; Cell division; Cytoplasm; Direct protein sequencing;
KW Glycogen metabolism; Hydrolase; Manganese; Metal-binding; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT CHAIN 2..330
FT /note="Serine/threonine-protein phosphatase PP1-alpha
FT catalytic subunit"
FT /id="PRO_0000058775"
FT REGION 306..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 306
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MUTAGEN 64
FT /note="D->N: Dominant negative, severely disrupts circadian
FT rhythmicity of transcription."
FT /evidence="ECO:0000269|PubMed:21930935"
FT MUTAGEN 95
FT /note="D->N: Dominant negative, severely disrupts circadian
FT rhythmicity of transcription."
FT /evidence="ECO:0000269|PubMed:21930935"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5ZQV"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:5ZT0"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5ZQV"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5ZQV"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:5ZQV"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:5ZQV"
SQ SEQUENCE 330 AA; 37540 MW; 8FBFD158A52282E0 CRC64;
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIRYPENFFL
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
