ID   PP2AB_RAT               Reviewed;         309 AA.
AC   P62716; P11082; Q6LDK0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 160.
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};
GN   Name=Ppp2cb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=2554256; DOI=10.1093/nar/17.20.8370;
RA   Posas F., Arino J.;
RT   "Nucleotide sequence of a rat heart cDNA encoding the isotype beta of the
RT   catalytic subunit of protein phosphatase 2A.";
RL   Nucleic Acids Res. 17:8370-8370(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2849437; DOI=10.1016/s0006-291x(88)80323-1;
RA   Kitagawa Y., Sakai R., Tahira T., Tsuda H., Ito N., Sugimura T., Nagao M.;
RT   "Molecular cloning of rat phosphoprotein phosphatase 2A beta cDNA and
RT   increased expressions of phosphatase 2A alpha and 2A beta in rat liver
RT   tumors.";
RL   Biochem. Biophys. Res. Commun. 157:821-827(1988).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 204-260.
RC   TISSUE=Hepatoma, and Pheochromocytoma;
RX   PubMed=2174876; DOI=10.1016/s0021-9258(18)45767-5;
RA   Wadzinski B.E., Heasley L.E., Johnson G.L.;
RT   "Multiplicity of protein serine-threonine phosphatases in PC12
RT   pheochromocytoma and FTO-2B hepatoma cells.";
RL   J. Biol. Chem. 265:21504-21508(1990).
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. Part of the
CC       striatin-interacting phosphatase and kinase (STRIPAK) complexes.
CC       STRIPAK complexes have critical roles in protein (de)phosphorylation
CC       and are regulators of multiple signaling pathways including Hippo,
CC       MAPK, nuclear receptor and cytoskeleton remodeling. Different types of
CC       STRIPAK complexes are involved in a variety of biological processes
CC       such as cell growth, differentiation, apoptosis, metabolism and immune
CC       regulation. {ECO:0000250|UniProtKB:P62714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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) (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. Interacts with CTTNBP2NL. Interacts with PTPA
CC       (By similarity). Found in a complex with at least ARL2, PPP2CB,
CC       PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By
CC       similarity). Part of the core of STRIPAK complexes composed of PP2A
CC       catalytic and scaffolding subunits, the striatins (PP2A regulatory
CC       subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2,
CC       PDCD10 and members of the STE20 kinases, such as STK24 and STK26 (By
CC       similarity). {ECO:0000250|UniProtKB:P62714,
CC       ECO:0000250|UniProtKB:Q0P594}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62714}. Nucleus
CC       {ECO:0000250|UniProtKB:P62714}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:P62714}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:P62714}. Note=In prometaphase cells, but not in
CC       anaphase cells, localizes at centromeres. During mitosis, also found at
CC       spindle poles. {ECO:0000250|UniProtKB:P62714}.
CC   -!- PTM: Reversibly methyl esterified on Leu-309 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}.
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DR   EMBL; M23591; AAA41912.1; -; mRNA.
DR   EMBL; X16044; CAA34167.1; -; mRNA.
DR   EMBL; X14087; CAA32249.1; -; mRNA.
DR   EMBL; M58438; AAA41911.1; -; mRNA.
DR   EMBL; BC085926; AAH85926.1; -; mRNA.
DR   EMBL; M58439; AAA41913.1; -; mRNA.
DR   PIR; S08486; PART2B.
DR   RefSeq; NP_058736.1; NM_017040.3.
DR   AlphaFoldDB; P62716; -.
DR   SMR; P62716; -.
DR   BioGRID; 246805; 2.
DR   FunCoup; P62716; 3608.
DR   IntAct; P62716; 1.
DR   STRING; 10116.ENSRNOP00000020663; -.
DR   iPTMnet; P62716; -.
DR   PhosphoSitePlus; P62716; -.
DR   SwissPalm; P62716; -.
DR   jPOST; P62716; -.
DR   PaxDb; 10116-ENSRNOP00000020663; -.
DR   Ensembl; ENSRNOT00000020663.5; ENSRNOP00000020663.1; ENSRNOG00000015182.8.
DR   Ensembl; ENSRNOT00055020980; ENSRNOP00055016952; ENSRNOG00055012322.
DR   Ensembl; ENSRNOT00060020475; ENSRNOP00060016130; ENSRNOG00060012066.
DR   Ensembl; ENSRNOT00065003519; ENSRNOP00065002433; ENSRNOG00065002633.
DR   GeneID; 24673; -.
DR   KEGG; rno:24673; -.
DR   UCSC; RGD:3381; rat.
DR   AGR; RGD:3381; -.
DR   CTD; 5516; -.
DR   RGD; 3381; Ppp2cb.
DR   eggNOG; KOG0371; Eukaryota.
DR   GeneTree; ENSGT00550000074618; -.
DR   HOGENOM; CLU_004962_0_5_1; -.
DR   InParanoid; P62716; -.
DR   OMA; YRCENQA; -.
DR   OrthoDB; 1930084at2759; -.
DR   PhylomeDB; P62716; -.
DR   Reactome; R-RNO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-180024; DARPP-32 events.
DR   Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-RNO-196299; Beta-catenin phosphorylation cascade.
DR   Reactome; R-RNO-198753; ERK/MAPK targets.
DR   Reactome; R-RNO-202670; ERKs are inactivated.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-389356; Co-stimulation by CD28.
DR   Reactome; R-RNO-389513; Co-inhibition by CTLA4.
DR   Reactome; R-RNO-432142; Platelet sensitization by LDL.
DR   Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-5673000; RAF activation.
DR   Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR   Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-RNO-9833482; PKR-mediated signaling.
DR   PRO; PR:P62716; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000015182; Expressed in cerebellum and 20 other cell types or tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; ISO:RGD.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:RGD.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:RGD.
DR   GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; IMP:ARUK-UCL.
DR   GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR   GO; GO:0010288; P:response to lead ion; IDA:ARUK-UCL.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   FunFam; 3.60.21.10:FF:000003; Serine/threonine-protein phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
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   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..309
FT                   /note="Serine/threonine-protein phosphatase 2A catalytic
FT                   subunit beta isoform"
FT                   /id="PRO_0000058849"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         307
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62715"
FT   MOD_RES         309
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P62714"
SQ   SEQUENCE   309 AA;  35575 MW;  51DA9EB0633FC191 CRC64;
     MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG
     QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES
     RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
     RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
     HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
     TRRTPDYFL
//