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 27-MAR-2024, entry version 185. 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 Interacts with tensin TNS1 (By similarity). Interacts with SAXO4, CC PPP1R21, PPP1R26, PPP1R27, PPP1R35, PPP1R36, PPP1R37, SH3RF2, ELFN1 and CC ELFN2 (By similarity). {ECO:0000250|UniProtKB:P62136, CC ECO:0000250|UniProtKB:P62139, ECO:0000269|PubMed:14638860, CC ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17609112, CC ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551}. CC -!- INTERACTION: CC P62137; O35625: Axin1; NbExp=2; IntAct=EBI-357187, EBI-2365912; CC P62137; Q9WTL8: Bmal1; NbExp=2; IntAct=EBI-357187, EBI-644534; 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"; 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; 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; 179. DR IntAct; P62137; 170. DR MINT; P62137; -. DR STRING; 10090.ENSMUSP00000039109; -. DR GlyGen; P62137; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62137; -. DR PhosphoSitePlus; P62137; -. DR SwissPalm; P62137; -. DR EPD; P62137; -. DR jPOST; P62137; -. DR MaxQB; P62137; -. DR PaxDb; 10090-ENSMUSP00000039109; -. DR PeptideAtlas; P62137; -. DR ProteomicsDB; 291640; -. DR Pumba; P62137; -. DR Antibodypedia; 3872; 682 antibodies from 40 providers. DR DNASU; 19045; -. DR Ensembl; ENSMUST00000046094.6; ENSMUSP00000039109.5; ENSMUSG00000040385.8. DR GeneID; 19045; -. DR KEGG; mmu:19045; -. DR UCSC; uc008fzg.1; mouse. DR AGR; MGI:103016; -. 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; KQSVECI; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; P62137; -. DR TreeFam; TF354243; -. DR Reactome; R-MMU-180024; DARPP-32 events. DR BioGRID-ORCS; 19045; 20 hits in 81 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 64 other cell types or tissues. DR GO; GO:0005912; C:adherens junction; ISO:MGI. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. 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: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 CDD; cd07414; MPP_PP1_PPKL; 1. 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; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF377; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR Genevisible; P62137; MM. 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 //