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Protein

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

Gene

PPP2CB

Organism
Homo sapiens (Human)
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.1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS02605-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
SIGNORiP62714.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:9300. PPP2CB.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5516.
OpenTargetsiENSG00000104695.
PharmGKBiPA33664.

Chemistry databases

DrugBankiDB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiPPP2CB.
DMDMi50402236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000588451 – 309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformAdd BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei307PhosphotyrosineBy similarity1
Modified residuei309Leucine methyl ester1 Publication1

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.1 Publication
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.
May be monoubiquitinated by NOSIP.By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62714.
MaxQBiP62714.
PaxDbiP62714.
PeptideAtlasiP62714.
PRIDEiP62714.

2D gel databases

OGPiP62714.
REPRODUCTION-2DPAGEIPI00429689.

PTM databases

DEPODiP62714.
iPTMnetiP62714.
PhosphoSitePlusiP62714.
SwissPalmiP62714.

Expressioni

Gene expression databases

BgeeiENSG00000104695.
CleanExiHS_PPP2CB.
ExpressionAtlasiP62714. baseline and differential.
GenevisibleiP62714. HS.

Organism-specific databases

HPAiCAB018600.
HPA043236.

Interactioni

Subunit structurei

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By similarity). 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. Interacts with CTTNBP2NL.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q13642-23EBI-1044367,EBI-8477209
AXIN2Q9Y2T14EBI-1044367,EBI-4400025
IGBP1P783185EBI-1044367,EBI-1055954

Protein-protein interaction databases

BioGridi111508. 141 interactors.
DIPiDIP-42325N.
IntActiP62714. 130 interactors.
MINTiMINT-1348293.
STRINGi9606.ENSP00000221138.

Structurei

3D structure databases

ProteinModelPortaliP62714.
SMRiP62714.
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.
InParanoidiP62714.
KOiK04382.
OMAiMDDKTFT.
OrthoDBiEOG091G0B6S.
PhylomeDBiP62714.
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.

P62714-1 [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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19E → D in AAB38020 (PubMed:2837763).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12656 mRNA. Translation: CAA31183.1.
CR541747 mRNA. Translation: CAG46547.1.
J03805 mRNA. Translation: AAB38020.1.
CH471080 Genomic DNA. Translation: EAW63434.1.
CH471080 Genomic DNA. Translation: EAW63435.1.
CH471080 Genomic DNA. Translation: EAW63436.1.
BC012022 mRNA. Translation: AAH12022.1.
M60484 Genomic DNA. Translation: AAA36467.1.
CCDSiCCDS6079.1.
PIRiB37135. PAHU2B.
RefSeqiNP_001009552.1. NM_001009552.1.
UniGeneiHs.491440.

Genome annotation databases

EnsembliENST00000221138; ENSP00000221138; ENSG00000104695.
GeneIDi5516.
KEGGihsa:5516.
UCSCiuc003xik.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12656 mRNA. Translation: CAA31183.1.
CR541747 mRNA. Translation: CAG46547.1.
J03805 mRNA. Translation: AAB38020.1.
CH471080 Genomic DNA. Translation: EAW63434.1.
CH471080 Genomic DNA. Translation: EAW63435.1.
CH471080 Genomic DNA. Translation: EAW63436.1.
BC012022 mRNA. Translation: AAH12022.1.
M60484 Genomic DNA. Translation: AAA36467.1.
CCDSiCCDS6079.1.
PIRiB37135. PAHU2B.
RefSeqiNP_001009552.1. NM_001009552.1.
UniGeneiHs.491440.

3D structure databases

ProteinModelPortaliP62714.
SMRiP62714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111508. 141 interactors.
DIPiDIP-42325N.
IntActiP62714. 130 interactors.
MINTiMINT-1348293.
STRINGi9606.ENSP00000221138.

Chemistry databases

DrugBankiDB00163. Vitamin E.

PTM databases

DEPODiP62714.
iPTMnetiP62714.
PhosphoSitePlusiP62714.
SwissPalmiP62714.

Polymorphism and mutation databases

BioMutaiPPP2CB.
DMDMi50402236.

2D gel databases

OGPiP62714.
REPRODUCTION-2DPAGEIPI00429689.

Proteomic databases

EPDiP62714.
MaxQBiP62714.
PaxDbiP62714.
PeptideAtlasiP62714.
PRIDEiP62714.

Protocols and materials databases

DNASUi5516.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221138; ENSP00000221138; ENSG00000104695.
GeneIDi5516.
KEGGihsa:5516.
UCSCiuc003xik.4. human.

Organism-specific databases

CTDi5516.
DisGeNETi5516.
GeneCardsiPPP2CB.
HGNCiHGNC:9300. PPP2CB.
HPAiCAB018600.
HPA043236.
MIMi176916. gene.
neXtProtiNX_P62714.
OpenTargetsiENSG00000104695.
PharmGKBiPA33664.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0371. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62714.
KOiK04382.
OMAiMDDKTFT.
OrthoDBiEOG091G0B6S.
PhylomeDBiP62714.
TreeFamiTF105559.

Enzyme and pathway databases

BioCyciZFISH:HS02605-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
SIGNORiP62714.

Miscellaneous databases

ChiTaRSiPPP2CB. human.
GeneWikiiPPP2CB.
GenomeRNAii5516.
PROiP62714.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104695.
CleanExiHS_PPP2CB.
ExpressionAtlasiP62714. baseline and differential.
GenevisibleiP62714. HS.

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...

Entry informationi

Entry nameiPP2AB_HUMAN
AccessioniPrimary (citable) accession number: P62714
Secondary accession number(s): D3DSV4, P11082, Q6FHK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.