ID PP2AB_PIG Reviewed; 293 AA. AC P11493; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 135. DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform; DE Short=PP2A-beta; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P62714}; DE Flags: Fragment; GN Name=PPP2CB; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=2827745; DOI=10.1021/bi00397a003; RA Stone S.R., Hofsteenge J., Hemmings B.A.; RT "Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit RT of protein phosphatase 2A."; RL Biochemistry 26:7215-7220(1987). CC -!- FUNCTION: Catalytic subunit of protein phosphatase 2A (PP2A), a CC serine/threonine phosphatase involved in the regulation of a wide CC variety of enzymes, signal transduction pathways, and cellular events. CC PP2A can modulate the activity of phosphorylase B kinase, casein kinase CC 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. CC {ECO:0000250|UniProtKB:P62714}. 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 Evidence={ECO:0000250|UniProtKB:P62714}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; CC Evidence={ECO:0000250|UniProtKB:P62714}; 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 Evidence={ECO:0000250|UniProtKB:P62714}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; CC Evidence={ECO:0000250|UniProtKB:P62714}; 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: PP2A consists of a common heterodimeric core enzyme, composed CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant CC regulatory subunit (PR65 or subunit A), that associates with a variety CC of regulatory subunits. Proteins that associate with the core dimer CC include three families of regulatory subunits B (the R2/B/PR55/B55, CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable CC regulatory subunit, viral proteins, and cell signaling molecules. Binds CC PPME1. May indirectly interact with SGO1, most probably through CC regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, CC PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD. Interacts with CC CTTNBP2NL. Interacts with PTPA. {ECO:0000250|UniProtKB:P62714, CC ECO:0000250|UniProtKB:Q0P594}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Chromosome, CC centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000250}. Note=In prometaphase cells, but not in anaphase cells, CC localizes at centromeres. During mitosis, also found at spindle poles CC (By similarity). {ECO:0000250}. CC -!- PTM: Reversibly methyl esterified on Leu-293 by leucine carboxyl CC methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 CC (PPME1). Carboxyl methylation influences the affinity of the catalytic CC subunit for the different regulatory subunits, thereby modulating the CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular CC localization (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylation of either threonine (by autophosphorylation- CC activated protein kinase) or tyrosine results in inactivation of the CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism CC for reactivation (By similarity). {ECO:0000250}. CC -!- PTM: May be monoubiquitinated by NOSIP. {ECO:0000250|UniProtKB:P62715}. 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; M20193; AAA30982.1; -; mRNA. DR PIR; B27430; B27430. DR AlphaFoldDB; P11493; -. DR SMR; P11493; -. DR PaxDb; 9823-ENSSSCP00000016788; -. DR PeptideAtlas; P11493; -. DR eggNOG; KOG0371; Eukaryota. DR InParanoid; P11493; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR047129; PPA2-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1. DR PANTHER; PTHR45619:SF44; SERINE_THREONINE-PROTEIN PHOSPHATASE 2A CATALYTIC SUBUNIT BETA ISOFORM; 1. DR Pfam; PF00149; Metallophos; 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 Centromere; Chromosome; Cytoplasm; Cytoskeleton; Hydrolase; Manganese; KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein phosphatase; KW Reference proteome; Ubl conjugation. FT CHAIN <1..293 FT /note="Serine/threonine-protein phosphatase 2A catalytic FT subunit beta isoform" FT /id="PRO_0000058847" FT ACT_SITE 102 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 41 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 43 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 151 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 225 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 291 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62715" FT MOD_RES 293 FT /note="Leucine methyl ester" FT /evidence="ECO:0000250|UniProtKB:P62714" FT NON_TER 1 SQ SEQUENCE 293 AA; 33610 MW; EEFE8E6F0FEF8710 CRC64; LNECKQLNEN QVRTLCEKAK EILTKESNVQ EVRCPVTVCG DVHGQFHDLM ELFRIGGKSP DTNYLFMGDY VDRGYYSVET VTLLVALKVR YPERITILRG NHESRQITQV YGFYDECLRK YGNANVWKYF TDLFDYLPLT ALVDGQIFCL HGGLSPSIDT LDHIRALDRL QEVPHEGPMC DLLWSDPDDR GGWGISPRGA GYTFGQDISE TFNHANGLTL VSRAHQLVME GYNWCHDRNV VTIFSAPNYC YRCGNQAAIM ELDDTLKYSF LQFDPAPRRG EPHVTRRTPD YFL //