ID PP1B_PONAB Reviewed; 327 AA. AC Q5R740; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 127. 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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). {ECO:0000250}. 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 PPP1R3D (in brain) mediate binding to glycogen. CC PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex CC containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R7 and CC PPP1R12C. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase CC complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB CC or PPP1CC. Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1; CC the interaction is direct. Interacts with TRIM28; the interaction CC dephosphorylates TRIM28 on 'Ser-824'. Interacts with FOXP3. Interacts CC with RRP1B. Interacts with SERPINE1. Interacts with LZTR1 (By CC similarity). {ECO:0000250|UniProtKB:P62140, CC ECO:0000250|UniProtKB:P62141}. 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 --------------------------------------------------------------------------- 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; CR860278; CAH92420.1; -; mRNA. DR RefSeq; NP_001126427.1; NM_001132955.1. DR RefSeq; XP_009235693.1; XM_009237418.1. DR RefSeq; XP_009235694.1; XM_009237419.1. DR AlphaFoldDB; Q5R740; -. DR SMR; Q5R740; -. DR STRING; 9601.ENSPPYP00000013994; -. DR Ensembl; ENSPPYT00000052215.1; ENSPPYP00000029764.1; ENSPPYG00000033907.1. DR GeneID; 100173410; -. DR KEGG; pon:100173410; -. DR CTD; 5500; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00940000154644; -. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; Q5R740; -. DR OrthoDB; 19833at2759; -. DR TreeFam; TF354243; -. DR Proteomes; UP000001595; Chromosome 2A. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. 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; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. 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. PE 2: Evidence at transcript level; KW Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle; KW Cell division; Cytoplasm; Glycogen metabolism; Hydrolase; Manganese; KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; KW 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_0000293479" 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" 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 //