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Protein

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

Gene

Ppp2cb

Organism
Rattus norvegicus (Rat)
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

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB
  3. protein C-terminus binding Source: RGD
  4. protein heterodimerization activity Source: UniProtKB
  5. protein serine/threonine phosphatase activity Source: RGD

GO - Biological processi

  1. apoptotic mitochondrial changes Source: Ensembl
  2. negative regulation of Ras protein signal transduction Source: RGD
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  4. protein dephosphorylation Source: RGD
  5. regulation of gene expression Source: Ensembl
  6. response to antibiotic Source: Ensembl
  7. response to endoplasmic reticulum stress Source: Ensembl
  8. response to hydrogen peroxide Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_194781. Separation of Sister Chromatids.
REACT_198611. Resolution of Sister Chromatid Cohesion.
REACT_198842. MASTL Facilitates Mitotic Progression.
REACT_199007. Spry regulation of FGF signaling.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_225694. Glycolysis.
REACT_232045. truncations of AMER1 destabilize the destruction complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_235914. Cyclin A/B1 associated events during G2/M transition.
REACT_237042. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_242934. DARPP-32 events.
REACT_243245. Integration of energy metabolism.
REACT_244383. CTLA4 inhibitory signaling.
REACT_245819. Mitotic Prometaphase.
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249104. APC truncation mutants have impaired AXIN binding.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_252890. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_253353. Cyclin D associated events in G1.
REACT_253470. ERKs are inactivated.
REACT_254856. ERK/MAPK targets.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_260559. AXIN missense mutants destabilize the destruction complex.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3381. Ppp2cb.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle pole By similarity
Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles (By similarity).By similarity

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: UniProtKB-SubCell
  5. protein phosphatase type 2A complex Source: Ensembl
  6. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformPRO_0000058849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071PhosphotyrosineBy similarity
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

PaxDbiP62716.
PRIDEiP62716.

2D gel databases

World-2DPAGE0004:P62716.

PTM databases

PhosphoSiteiP62716.

Expressioni

Gene expression databases

GenevestigatoriP62716.

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

BioGridi246805. 1 interaction.
IntActiP62716. 1 interaction.
STRINGi10116.ENSRNOP00000020663.

Structurei

3D structure databases

ProteinModelPortaliP62716.
SMRiP62716. 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.
InParanoidiP62716.
KOiK04382.
OMAiEGFNWCH.
OrthoDBiEOG74N5H2.
PhylomeDBiP62716.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP62716.
SMRiP62716. Positions 6-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246805. 1 interaction.
IntActiP62716. 1 interaction.
STRINGi10116.ENSRNOP00000020663.

PTM databases

PhosphoSiteiP62716.

2D gel databases

World-2DPAGE0004:P62716.

Proteomic databases

PaxDbiP62716.
PRIDEiP62716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5516.
RGDi3381. Ppp2cb.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62716.
KOiK04382.
OMAiEGFNWCH.
OrthoDBiEOG74N5H2.
PhylomeDBiP62716.
TreeFamiTF105559.

Enzyme and pathway databases

ReactomeiREACT_194781. Separation of Sister Chromatids.
REACT_198611. Resolution of Sister Chromatid Cohesion.
REACT_198842. MASTL Facilitates Mitotic Progression.
REACT_199007. Spry regulation of FGF signaling.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_225694. Glycolysis.
REACT_232045. truncations of AMER1 destabilize the destruction complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_235914. Cyclin A/B1 associated events during G2/M transition.
REACT_237042. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_242934. DARPP-32 events.
REACT_243245. Integration of energy metabolism.
REACT_244383. CTLA4 inhibitory signaling.
REACT_245819. Mitotic Prometaphase.
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249104. APC truncation mutants have impaired AXIN binding.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_252890. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_253353. Cyclin D associated events in G1.
REACT_253470. ERKs are inactivated.
REACT_254856. ERK/MAPK targets.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_260559. AXIN missense mutants destabilize the destruction complex.

Miscellaneous databases

NextBioi604049.
PROiP62716.

Gene expression databases

GenevestigatoriP62716.

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. "Nucleotide sequence of a rat heart cDNA encoding the isotype beta of the catalytic subunit of protein phosphatase 2A."
    Posas F., Arino J.
    Nucleic Acids Res. 17:8370-8370(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Molecular cloning of rat phosphoprotein phosphatase 2A beta cDNA and increased expressions of phosphatase 2A alpha and 2A beta in rat liver tumors."
    Kitagawa Y., Sakai R., Tahira T., Tsuda H., Ito N., Sugimura T., Nagao M.
    Biochem. Biophys. Res. Commun. 157:821-827(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "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].
    Tissue: Kidney.
  4. "Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells."
    Wadzinski B.E., Heasley L.E., Johnson G.L.
    J. Biol. Chem. 265:21504-21508(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 204-260.
    Tissue: Hepatoma and Pheochromocytoma.

Entry informationi

Entry nameiPP2AB_RAT
AccessioniPrimary (citable) accession number: P62716
Secondary accession number(s): P11082, Q6LDK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: January 7, 2015
This is version 93 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, Reference proteome

Documents

  1. 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.