PP2AB_BOVIN
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 03-AUG-2022, entry version 115.
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; Q0P594; -.
DR PeptideAtlas; Q0P594; -.
DR PRIDE; Q0P594; -.
DR Ensembl; ENSBTAT00000012182; ENSBTAP00000012182; ENSBTAG00000009245.
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; DHINYAF; -.
DR OrthoDB; 808922at2759; -.
DR TreeFam; TF105559; -.
DR Reactome; R-BTA-1295596; Spry regulation of FGF signaling.
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-389513; CTLA4 inhibitory signaling.
DR Reactome; R-BTA-432142; Platelet sensitization by LDL.
DR Reactome; R-BTA-5673000; RAF activation.
DR Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000009245; Expressed in occipital lobe and 104 other 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:0000159; C:protein phosphatase type 2A complex; IEA:Ensembl.
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:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
