PP2AB_RABIT
ID PP2AB_RABIT Reviewed; 309 AA.
AC P11611;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=2826253; DOI=10.1016/0014-5793(87)80574-4;
RA da Cruz e Silva O.B., Cohen P.T.W.;
RT "A second catalytic subunit of type-2A protein phosphatase from rabbit
RT skeletal muscle.";
RL FEBS Lett. 226:176-178(1987).
RN [2]
RP PHOSPHORYLATION AT TYR-307.
RX PubMed=1325671; DOI=10.1126/science.1325671;
RA Chen J., Martin B.L., Brautigan D.L.;
RT "Regulation of protein serine-threonine phosphatase type-2A by tyrosine
RT phosphorylation.";
RL Science 257:1261-1264(1992).
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-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; Y00763; CAA68732.1; -; mRNA.
DR PIR; S00220; PARB2B.
DR RefSeq; NP_001095177.1; NM_001101707.1.
DR AlphaFoldDB; P11611; -.
DR SMR; P11611; -.
DR STRING; 9986.ENSOCUP00000004530; -.
DR iPTMnet; P11611; -.
DR PRIDE; P11611; -.
DR Ensembl; ENSOCUT00000045283; ENSOCUP00000045823; ENSOCUG00000005230.
DR GeneID; 100009300; -.
DR KEGG; ocu:100009300; -.
DR CTD; 5516; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00550000074618; -.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; P11611; -.
DR OMA; DHINYAF; -.
DR OrthoDB; 808922at2759; -.
DR TreeFam; TF105559; -.
DR Proteomes; UP000001811; Chromosome 2.
DR Bgee; ENSOCUG00000005230; Expressed in aorta and 15 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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_0000058848"
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:0000269|PubMed:1325671"
FT MOD_RES 309
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62714"
SQ SEQUENCE 309 AA; 35605 MW; BE76EEB6B0EAC19E CRC64;
MDDKTFTKEL 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
