ID PP1B_MOUSE Reviewed; 327 AA. AC P62141; P37140; Q3TBE5; Q3TL90; Q542E7; Q8C285; Q9DBY2; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 187. DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit; DE Short=PP-1B; DE EC=3.1.3.16; DE EC=3.1.3.53; GN Name=Ppp1cb; 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]. RC TISSUE=Brain; RX PubMed=2544298; DOI=10.1016/0092-8674(89)90338-3; RA Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.; RT "The fission yeast dis2+ gene required for chromosome disjoining encodes RT one of two putative type 1 protein phosphatases."; RL Cell 57:997-1007(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Dendritic cell, Embryonic head, Embryonic heart, Embryonic RC kidney, Lung, Mammary gland, Morula, and Thymus; 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 STRAIN=C57BL/6J; TISSUE=Brain; 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 26-35; 60-73 AND 150-167, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] 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 [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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 [8] 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 [9] RP FUNCTION IN CIRCADIAN CLOCK. 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). 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 (PP1) is essential CC for cell division, it participates in the regulation of glycogen CC metabolism, muscle contractility and protein synthesis. Involved in CC regulation of ionic conductances and long-term synaptic plasticity. CC Component of the PTW/PP1 phosphatase complex, which plays a role in the CC control of chromatin structure and cell cycle progression during the CC transition from mitosis into interphase. In balance with CSNK1D and CC CSNK1E, determines the circadian period length, through the regulation CC of the speed and rhythmicity of PER1 and PER2 phosphorylation. May CC dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997, CC ECO:0000269|PubMed:21930935}. 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 -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin CC light chain] + phosphate; Xref=Rhea:RHEA:12849, Rhea:RHEA-COMP:13684, CC Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.53; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl- CC [myosin light chain] + phosphate; Xref=Rhea:RHEA:53988, Rhea:RHEA- CC COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.53; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by the toxins okadaic acid, tautomycin CC and microcystin Leu-Arg. The phosphatase activity of the PPP1R15A-PP1 CC complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug CC that protects cells from endoplasmic reticulum stress (By similarity). CC {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. The targeting or regulatory subunits determine the CC substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate CC binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), CC PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. CC Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R12A and NUAK1; CC the interaction is direct. Interacts with TRIM28; the interaction is CC weak (By similarity). Interacts with PPP1R15A; the interaction mediates CC binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1 CC phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA CC or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the CC interaction is weak (By similarity). Part of a complex containing CC PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction CC mediates binding to EIF2S1. Interacts with FOXP3 (By similarity). CC Interacts with RRP1B (By similarity). Interacts with SERPINE1. CC Interacts with LZTR1 (By similarity). {ECO:0000250|UniProtKB:P62140, CC ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be CC relocalized through interaction with targeting subunits. In the CC presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. CC {ECO:0000250|UniProtKB:P62140}. 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; M27073; AAA37527.1; -; mRNA. DR EMBL; AK004686; BAB23473.1; -; mRNA. DR EMBL; AK088893; BAC40636.1; -; mRNA. DR EMBL; AK089067; BAC40733.1; -; mRNA. DR EMBL; AK147112; BAE27684.1; -; mRNA. DR EMBL; AK160743; BAE35984.1; -; mRNA. DR EMBL; AK166168; BAE38608.1; -; mRNA. DR EMBL; AK166623; BAE38902.1; -; mRNA. DR EMBL; AK168141; BAE40108.1; -; mRNA. DR EMBL; AK169379; BAE41126.1; -; mRNA. DR EMBL; AK171283; BAE42366.1; -; mRNA. DR EMBL; BC046832; AAH46832.1; -; mRNA. DR CCDS; CCDS19193.1; -. DR PIR; D32550; D32550. DR RefSeq; NP_766295.2; NM_172707.3. DR AlphaFoldDB; P62141; -. DR SMR; P62141; -. DR BioGRID; 202336; 101. DR IntAct; P62141; 82. DR MINT; P62141; -. DR STRING; 10090.ENSMUSP00000015100; -. DR iPTMnet; P62141; -. DR PhosphoSitePlus; P62141; -. DR SwissPalm; P62141; -. DR EPD; P62141; -. DR jPOST; P62141; -. DR MaxQB; P62141; -. DR PaxDb; 10090-ENSMUSP00000015100; -. DR PeptideAtlas; P62141; -. DR ProteomicsDB; 291641; -. DR Pumba; P62141; -. DR Antibodypedia; 28856; 573 antibodies from 33 providers. DR DNASU; 19046; -. DR Ensembl; ENSMUST00000015100.15; ENSMUSP00000015100.9; ENSMUSG00000014956.16. DR Ensembl; ENSMUST00000201360.4; ENSMUSP00000144047.2; ENSMUSG00000014956.16. DR GeneID; 19046; -. DR KEGG; mmu:19046; -. DR UCSC; uc008wzq.2; mouse. DR AGR; MGI:104871; -. DR CTD; 5500; -. DR MGI; MGI:104871; Ppp1cb. DR VEuPathDB; HostDB:ENSMUSG00000014956; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00940000154644; -. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P62141; -. DR OMA; FGEFDNA; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; P62141; -. DR TreeFam; TF354243; -. DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs. DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs. DR Reactome; R-MMU-5673000; RAF activation. DR BioGRID-ORCS; 19046; 25 hits in 73 CRISPR screens. DR ChiTaRS; Ppp1cb; mouse. DR PRO; PR:P62141; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P62141; Protein. DR Bgee; ENSMUSG00000014956; Expressed in blood and 264 other cell types or tissues. DR ExpressionAtlas; P62141; baseline and differential. 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:0042587; C:glycogen granule; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB. DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB. DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA: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:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; ISS: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 CDD; cd07414; MPP_PP1_PPKL; 1. 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:SF472; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-BETA 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; P62141; MM. PE 1: Evidence at protein level; KW Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle; KW Cell division; Cytoplasm; Direct protein sequencing; Glycogen metabolism; KW Hydrolase; Manganese; Metal-binding; Nucleus; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62140" FT CHAIN 2..327 FT /note="Serine/threonine-protein phosphatase PP1-beta FT catalytic subunit" FT /id="PRO_0000058780" FT REGION 305..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 124 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 123 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 247 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-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P62140" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62140" FT CONFLICT 64 FT /note="I -> N (in Ref. 2; BAC40733)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="W -> R (in Ref. 2; BAE42366)" FT /evidence="ECO:0000305" FT CONFLICT 223 FT /note="S -> F (in Ref. 2; BAE38902)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="V -> E (in Ref. 2; BAB23473)" FT /evidence="ECO:0000305" FT CONFLICT 269 FT /note="P -> S (in Ref. 2; BAE42366)" FT /evidence="ECO:0000305" SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64; MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK KAKYQYGGLN SGRPVTPPRT ANPPKKR //