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P62715 (PP2AB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform

Short name=PP2A-beta
EC=3.1.3.16
Gene names
Name:Ppp2cb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subunit structure

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.

Subcellular location

Cytoplasm. 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.

Post-translational modification

Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly. It varies during the cell cycle. Demethylated by PME1 (in vitro) 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.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMMethylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic mitochondrial changes

Inferred from mutant phenotype PubMed 16717086. Source: MGI

negative regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 16717086. Source: MGI

protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from mutant phenotype PubMed 16717086. Source: MGI

response to antibiotic

Inferred from mutant phenotype PubMed 16717086. Source: MGI

response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 16717086. Source: MGI

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 16717086. Source: MGI

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 10781942. Source: MGI

nucleus

Traceable author statement PubMed 10781942. Source: MGI

protein phosphatase type 2A complex

Inferred from direct assay PubMed 16717086. Source: MGI

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
PRO_0000058846

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Amino acid modifications

Modified residue3071Phosphotyrosine Ref.5
Modified residue3091Leucine methyl ester By similarity

Experimental info

Mutagenesis3071Y → Q: Loss of trimeric subunit ABC assembly. Ref.6
Mutagenesis3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. Ref.6
Mutagenesis3091L → Q: Loss of trimeric subunit ABC assembly. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P62715 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 51DA9EB0633FC191

FASTA30935,575
        10         20         30         40         50         60 
MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI 

       190        200        210        220        230        240 
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA 

       250        260        270        280        290        300 
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 


TRRTPDYFL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67746 mRNA. Translation: CAA91559.1.
BC058582 mRNA. Translation: AAH58582.1.
RefSeqNP_059070.1. NM_017374.3.
UniGeneMm.288765.
Mm.29301.

3D structure databases

ProteinModelPortalP62715.
SMRP62715. Positions 6-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202342. 8 interactions.
IntActP62715. 2 interactions.
STRING10090.ENSMUSP00000009774.

Chemistry

BindingDBP62715.

PTM databases

PhosphoSiteP62715.

Proteomic databases

PaxDbP62715.
PRIDEP62715.

Protocols and materials databases

DNASU19053.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
GeneID19053.
KEGGmmu:19053.
UCSCuc009lkd.1. mouse.

Organism-specific databases

CTD5516.
MGIMGI:1321161. Ppp2cb.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
HOGENOMHOG000172696.
HOVERGENHBG000216.
InParanoidP62715.
KOK04382.
OMAVENDIFC.
OrthoDBEOG74N5H2.
PhylomeDBP62715.
TreeFamTF105559.

Gene expression databases

BgeeP62715.
GenevestigatorP62715.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP2CB. mouse.
NextBio21334.
PROP62715.
SOURCESearch...

Entry information

Entry namePP2AB_MOUSE
AccessionPrimary (citable) accession number: P62715
Secondary accession number(s): P11082
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot