ID   PP2AB_BOVIN             Reviewed;         309 AA.
AC   Q0P594;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 123.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH TBCD, IDENTIFICATION IN A COMPLEX WITH ARL2; PPP2R1A;
RP   PPP2R2A; PPP2R5E AND TBCD, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12912990; DOI=10.1074/jbc.m308678200;
RA   Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S.,
RA   Pohl J., Kahn R.A.;
RT   "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A.";
RL   J. Biol. Chem. 278:40829-40836(2003).
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) (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 (By similarity). Found in a complex with at
CC       least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with
CC       TBCD. Interacts with CTTNBP2NL (PubMed:12912990). Interacts with PTPA
CC       (By similarity). {ECO:0000250|UniProtKB:P62714,
CC       ECO:0000269|PubMed:12912990}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Chromosome, centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC       pole {ECO:0000250}. Note=In prometaphase cells, but not in anaphase
CC       cells, localizes at centromeres. During mitosis, also found at spindle
CC       poles (By similarity). {ECO:0000250}.
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; BC120332; AAI20333.1; -; mRNA.
DR   RefSeq; NP_001069325.1; NM_001075857.1.
DR   AlphaFoldDB; Q0P594; -.
DR   SMR; Q0P594; -.
DR   STRING; 9913.ENSBTAP00000012182; -.
DR   PaxDb; 9913-ENSBTAP00000012182; -.
DR   PeptideAtlas; Q0P594; -.
DR   Ensembl; ENSBTAT00000012182.5; ENSBTAP00000012182.4; ENSBTAG00000009245.5.
DR   GeneID; 524361; -.
DR   KEGG; bta:524361; -.
DR   CTD; 5516; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009245; -.
DR   VGNC; VGNC:33252; PPP2CB.
DR   eggNOG; KOG0371; Eukaryota.
DR   GeneTree; ENSGT00550000074618; -.
DR   HOGENOM; CLU_004962_0_5_1; -.
DR   InParanoid; Q0P594; -.
DR   OMA; GENMDQS; -.
DR   OrthoDB; 19833at2759; -.
DR   TreeFam; TF105559; -.
DR   Reactome; R-BTA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-BTA-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-BTA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-BTA-180024; DARPP-32 events.
DR   Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-BTA-196299; Beta-catenin phosphorylation cascade.
DR   Reactome; R-BTA-198753; ERK/MAPK targets.
DR   Reactome; R-BTA-202670; ERKs are inactivated.
DR   Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-BTA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-BTA-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-BTA-432142; Platelet sensitization by LDL.
DR   Reactome; R-BTA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-BTA-5673000; RAF activation.
DR   Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-BTA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-BTA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-BTA-68877; Mitotic Prometaphase.
DR   Reactome; R-BTA-69231; Cyclin D associated events in G1.
DR   Reactome; R-BTA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-BTA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-BTA-9833482; PKR-mediated signaling.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000009245; Expressed in occipital lobe and 104 other cell types or tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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   1: Evidence at protein 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_0000283053"
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;  35561 MW;  50AD45DD126F8485 CRC64;
     MDDKAFTKDL 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
//