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Protein

Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform

Gene

Ppp2cb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Manganese 1By similarity1
Metal bindingi59Manganese 1By similarity1
Metal bindingi85Manganese 1By similarity1
Metal bindingi85Manganese 2By similarity1
Metal bindingi117Manganese 2By similarity1
Active sitei118Proton donorBy similarity1
Metal bindingi167Manganese 2By similarity1
Metal bindingi241Manganese 2By similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: RGD

GO - Biological processi

  • apoptotic mitochondrial changes Source: Ensembl
  • negative regulation of Ras protein signal transduction Source: RGD
  • positive regulation of microtubule binding Source: ARUK-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  • protein dephosphorylation Source: RGD
  • regulation of gene expression Source: Ensembl
  • response to endoplasmic reticulum stress Source: Ensembl
  • response to hydrogen peroxide Source: Ensembl
  • response to lead ion Source: ARUK-UCL

Keywordsi

Molecular functionHydrolase, Protein phosphatase
LigandManganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-RNO-1295596 Spry regulation of FGF signaling
R-RNO-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-RNO-180024 DARPP-32 events
R-RNO-195253 Degradation of beta-catenin by the destruction complex
R-RNO-196299 Beta-catenin phosphorylation cascade
R-RNO-198753 ERK/MAPK targets
R-RNO-202670 ERKs are inactivated
R-RNO-2467813 Separation of Sister Chromatids
R-RNO-2500257 Resolution of Sister Chromatid Cohesion
R-RNO-389513 CTLA4 inhibitory signaling
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-5673000 RAF activation
R-RNO-5675221 Negative regulation of MAPK pathway
R-RNO-6804757 Regulation of TP53 Degradation
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-68877 Mitotic Prometaphase
R-RNO-69231 Cyclin D associated events in G1
R-RNO-69273 Cyclin A/B1/B2 associated events during G2/M transition

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (EC:3.1.3.16)
Short name:
PP2A-beta
Gene namesi
Name:Ppp2cb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi3381 Ppp2cb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000588491 – 309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformAdd BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei307PhosphotyrosineBy similarity1
Modified residuei309Leucine methyl esterBy similarity1

Post-translational modificationi

Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 (Ppme1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization (By similarity).By similarity
Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation (By similarity).By similarity
May be monoubiquitinated by NOSIP.By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62716
PRIDEiP62716

2D gel databases

World-2DPAGEi0004:P62716

PTM databases

iPTMnetiP62716
PhosphoSitePlusiP62716
SwissPalmiP62716

Expressioni

Gene expression databases

BgeeiENSRNOG00000015182
GenevisibleiP62716 RN

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme (composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65) (subunit A)) that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Binds PPME1. May indirectly interact with SGO1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD. Interacts with CTTNBP2NL. Interacts with PTPA.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246805, 1 interactor
IntActiP62716, 1 interactor
STRINGi10116.ENSRNOP00000020663

Structurei

3D structure databases

ProteinModelPortaliP62716
SMRiP62716
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiKOG0371 Eukaryota
COG0639 LUCA
GeneTreeiENSGT00550000074618
HOGENOMiHOG000172696
HOVERGENiHBG000216
InParanoidiP62716
KOiK04382
OMAiNWGHDKN
OrthoDBiEOG091G0B6S
PhylomeDBiP62716
TreeFamiTF105559

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

Sequencei

Sequence statusi: Complete.

P62716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC
60 70 80 90 100
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
110 120 130 140 150
VALKVRYPER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF
160 170 180 190 200
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW
210 220 230 240 250
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW
260 270 280 290 300
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV

TRRTPDYFL
Length:309
Mass (Da):35,575
Last modified:July 19, 2004 - v1
Checksum:i51DA9EB0633FC191
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23591 mRNA Translation: AAA41912.1
X16044 mRNA Translation: CAA34167.1
X14087 mRNA Translation: CAA32249.1
M58438 mRNA Translation: AAA41911.1
BC085926 mRNA Translation: AAH85926.1
M58439 mRNA Translation: AAA41913.1
PIRiS08486 PART2B
RefSeqiNP_058736.1, NM_017040.1
UniGeneiRn.1271
Rn.977

Genome annotation databases

EnsembliENSRNOT00000020663; ENSRNOP00000020663; ENSRNOG00000015182
GeneIDi24673
KEGGirno:24673
UCSCiRGD:3381 rat

Entry informationi

Entry nameiPP2AB_RAT
AccessioniPrimary (citable) accession number: P62716
Secondary accession number(s): P11082, Q6LDK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: May 23, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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