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P67774 (PP2AA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 alpha isoform

Short name=PP2A-alpha
EC=3.1.3.16
Gene names
Name:PPP2CA
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

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

General annotation (Comments)

Function

PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Activates RAF1 by dephosphorylating it at 'Ser-259' By similarity.

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 PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or 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. Interacts with NXN; the interaction is direct. Interacts with TP53, SGOL1 and SGOL2. Interacts with AXIN1; the interaction dephosphorylates AXIN1 By similarity. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3 By similarity. Interacts with RAF1. Interacts with GSK3B (via C2 domain) By similarity. Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination 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. Centromeric localization requires the presence of SGOL2 By similarity.

Post-translational modification

Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly, enhancing the affinity of the PP2A core enzyme for some, but not all, regulatory subunits. It varies during the cell cycle.

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.

The N-terminus is blocked.

Sequence similarities

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

Sequence caution

The sequence AAA30695.1 differs from that shown. Reason: Frameshift at position 294.

Ontologies

Keywords
   Biological processMeiosis
   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_processmeiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mesoderm development

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein phosphatase type 2A complex

Inferred from electronic annotation. Source: Ensembl

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
PRO_0000058838

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
Modified residue3091Leucine methyl ester Ref.5

Sequences

Sequence LengthMass (Da)Tools
P67774 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C602291F78F34555

FASTA30935,594
        10         20         30         40         50         60 
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER 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]Tang P.M., de Paoli-Roach A.A.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aortic smooth muscle.
[2]"Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase."
Green D.D., Yang S.-I., Mumby M.C.
Proc. Natl. Acad. Sci. U.S.A. 84:4880-4884(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Chen S., Boynton A.
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.
[5]"Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase."
Lee J., Stock J.
J. Biol. Chem. 268:19192-19195(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 42-48 AND 284-308, METHYLATION AT LEU-309.
Tissue: Brain.
[6]"Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A."
Guo H., Damuni Z.
Proc. Natl. Acad. Sci. U.S.A. 90:2500-2504(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52554 mRNA. Translation: CAA36789.1.
M16968 mRNA. Translation: AAA30695.1. Frameshift.
X72858 mRNA. Translation: CAA51381.1.
BC147979 mRNA. Translation: AAI47980.1.
PIRA28029.
S10371.
RefSeqNP_851374.1. NM_181031.2.
UniGeneBt.34380.

3D structure databases

ProteinModelPortalP67774.
SMRP67774. Positions 2-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid159582. 1 interaction.
IntActP67774. 4 interactions.
MINTMINT-203725.

Chemistry

BindingDBP67774.
ChEMBLCHEMBL3862.

Proteomic databases

PaxDbP67774.
PRIDEP67774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000596; ENSBTAP00000000596; ENSBTAG00000000469.
GeneID282320.
KEGGbta:282320.

Organism-specific databases

CTD5515.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
HOGENOMHOG000172696.
HOVERGENHBG000216.
InParanoidP67774.
KOK04382.
OMALMACKQL.
OrthoDBEOG74N5H2.
TreeFamTF105559.

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

NextBio20806117.

Entry information

Entry namePP2AA_BOVIN
AccessionPrimary (citable) accession number: P67774
Secondary accession number(s): A6QLI7, P05323, P13197
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 81 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