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Protein

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

Gene

Ppp2cb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Manganese 1By similarity
Metal bindingi59 – 591Manganese 1By similarity
Metal bindingi85 – 851Manganese 1By similarity
Metal bindingi85 – 851Manganese 2By similarity
Metal bindingi117 – 1171Manganese 2By similarity
Active sitei118 – 1181Proton donorBy similarity
Metal bindingi167 – 1671Manganese 2By similarity
Metal bindingi241 – 2411Manganese 2By similarity

GO - Molecular functioni

GO - Biological processi

  • apoptotic mitochondrial changes Source: MGI
  • negative regulation of Ras protein signal transduction Source: Ensembl
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  • protein dephosphorylation Source: Ensembl
  • regulation of gene expression Source: MGI
  • response to antibiotic Source: MGI
  • response to endoplasmic reticulum stress Source: MGI
  • response to hydrogen peroxide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_279737. Integration of energy metabolism.
REACT_289448. Cyclin D associated events in G1.
REACT_298419. Spry regulation of FGF signaling.
REACT_299247. ERKs are inactivated.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_306375. Mitotic Prometaphase.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314687. Glycolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321346. Separation of Sister Chromatids.
REACT_323000. ERK/MAPK targets.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325290. DARPP-32 events.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342444. MASTL Facilitates Mitotic Progression.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_358264. RHO GTPases Activate Formins.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1321161. Ppp2cb.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • protein phosphatase type 2A complex Source: MGI
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071Y → Q: Loss of trimeric subunit ABC assembly. 1 Publication
Mutagenesisi309 – 3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication
Mutagenesisi309 – 3091L → Q: Loss of trimeric subunit ABC assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformPRO_0000058846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071Phosphotyrosine1 Publication
Modified residuei309 – 3091Leucine methyl esterBy similarity

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

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP62715.
PaxDbiP62715.
PRIDEiP62715.

PTM databases

PhosphoSiteiP62715.

Expressioni

Gene expression databases

BgeeiP62715.
GenevestigatoriP62715.

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 (By similarity). May indirectly interact with SGOL1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By similarity). Interacts with CTTNBP2NL (By similarity).By similarity

Protein-protein interaction databases

BioGridi202342. 11 interactions.
IntActiP62715. 2 interactions.
STRINGi10090.ENSMUSP00000009774.

Structurei

3D structure databases

ProteinModelPortaliP62715.
SMRiP62715. Positions 6-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62715.
KOiK04382.
OMAiEGFNWCH.
OrthoDBiEOG74N5H2.
PhylomeDBiP62715.
TreeFamiTF105559.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62715-1 [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
Z67746 mRNA. Translation: CAA91559.1.
BC058582 mRNA. Translation: AAH58582.1.
CCDSiCCDS22233.1.
RefSeqiNP_059070.1. NM_017374.3.
UniGeneiMm.288765.
Mm.29301.

Genome annotation databases

EnsembliENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
GeneIDi19053.
KEGGimmu:19053.
UCSCiuc009lkd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67746 mRNA. Translation: CAA91559.1.
BC058582 mRNA. Translation: AAH58582.1.
CCDSiCCDS22233.1.
RefSeqiNP_059070.1. NM_017374.3.
UniGeneiMm.288765.
Mm.29301.

3D structure databases

ProteinModelPortaliP62715.
SMRiP62715. Positions 6-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202342. 11 interactions.
IntActiP62715. 2 interactions.
STRINGi10090.ENSMUSP00000009774.

PTM databases

PhosphoSiteiP62715.

Proteomic databases

MaxQBiP62715.
PaxDbiP62715.
PRIDEiP62715.

Protocols and materials databases

DNASUi19053.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
GeneIDi19053.
KEGGimmu:19053.
UCSCiuc009lkd.1. mouse.

Organism-specific databases

CTDi5516.
MGIiMGI:1321161. Ppp2cb.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62715.
KOiK04382.
OMAiEGFNWCH.
OrthoDBiEOG74N5H2.
PhylomeDBiP62715.
TreeFamiTF105559.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_279737. Integration of energy metabolism.
REACT_289448. Cyclin D associated events in G1.
REACT_298419. Spry regulation of FGF signaling.
REACT_299247. ERKs are inactivated.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_306375. Mitotic Prometaphase.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314687. Glycolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321346. Separation of Sister Chromatids.
REACT_323000. ERK/MAPK targets.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325290. DARPP-32 events.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342444. MASTL Facilitates Mitotic Progression.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiPpp2cb. mouse.
NextBioi21334.
PROiP62715.
SOURCEiSearch...

Gene expression databases

BgeeiP62715.
GenevestigatoriP62715.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Goetz J.M., Kues W.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X DBA/2.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  3. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
    Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
    J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-83.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 284-294, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. "Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts."
    Chen J., Parsons S., Brautigan D.L.
    J. Biol. Chem. 269:7957-7962(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-307.
  6. "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2."
    Chung H., Nairn A.C., Murata K., Brautigan D.L.
    Biochemistry 38:10371-10376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-307 AND LEU-309.

Entry informationi

Entry nameiPP2AB_MOUSE
AccessioniPrimary (citable) accession number: P62715
Secondary accession number(s): P11082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: May 27, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.