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Protein

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

Gene

PPP2CA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi57Manganese 11 Publication1
Metal bindingi59Manganese 11 Publication1
Metal bindingi85Manganese 11 Publication1
Metal bindingi85Manganese 21 Publication1
Metal bindingi117Manganese 21 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei118Proton donorBy similarity1
Metal bindingi167Manganese 21 Publication1
Metal bindingi241Manganese 21 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • GABA receptor binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: ARUK-UCL
  • protein C-terminus binding Source: Ensembl
  • protein heterodimerization activity Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: ARUK-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processMeiosis
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS03696-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
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-2995383 Initiation of Nuclear Envelope Reformation
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/B2 associated events during G2/M transition
R-HSA-70171 Glycolysis
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P67775

SIGNOR Signaling Network Open Resource

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SIGNORi
P67775

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (EC:3.1.3.16)
Short name:
PP2A-alpha
Alternative name(s):
Replication protein C
Short name:
RP-C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PPP2CA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000113575.9

Human Gene Nomenclature Database

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HGNCi
HGNC:9299 PPP2CA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176915 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P67775

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi309L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5515

Open Targets

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OpenTargetsi
ENSG00000113575

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33663

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4703

Drug and drug target database

More...
DrugBanki
DB00163 Vitamin E

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PPP2CA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
54038809

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588391 – 309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformAdd BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei307PhosphotyrosineBy similarity1
Modified residuei309Leucine methyl ester1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.
Polyubiquitinated, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P67775

MaxQB - The MaxQuant DataBase

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MaxQBi
P67775

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P67775

PeptideAtlas

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PeptideAtlasi
P67775

PRoteomics IDEntifications database

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PRIDEi
P67775

ProteomicsDB human proteome resource

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ProteomicsDBi
57521

PTM databases

DEPOD human dephosphorylation database

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DEPODi
P67775

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P67775

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P67775

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000113575 Expressed in 233 organ(s), highest expression level in adrenal tissue

CleanEx database of gene expression profiles

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CleanExi
HS_PPP2CA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P67775 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P67775 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003848
HPA043236

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 (By similarity). Interacts with KCTD20 (By similarity). Interacts with BTBD10 (By similarity). Interacts with TP53, SGO1 and SGO2. Interacts with AXIN1; the interaction dephosphorylates AXIN1. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3. Interacts with RAF1. Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination. Interacts with GSK3B (via C2 domain). Interacts with MFHAS1; retains PPP2CA into the cytoplasm and excludes it from the nucleus (PubMed:28609714). Interacts with FAM122A (PubMed:27588481). Interacts with ADCY8; interaction is phosphatase activity-dependent; antagonizes interaction between ADCY8 and calmodulin (PubMed:16258073).By similarity16 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111507, 288 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P67775

Database of interacting proteins

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DIPi
DIP-29395N

Protein interaction database and analysis system

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IntActi
P67775, 166 interactors

Molecular INTeraction database

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MINTi
P67775

STRING: functional protein association networks

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STRINGi
9606.ENSP00000418447

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P67775

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P67775

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P67775

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P67775

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0371 Eukaryota
COG0639 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074618

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000172696

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000216

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P67775

KEGG Orthology (KO)

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KOi
K04382

Identification of Orthologs from Complete Genome Data

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OMAi
QILWNDP

Database of Orthologous Groups

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OrthoDBi
EOG091G0B6S

Database for complete collections of gene phylogenies

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PhylomeDBi
P67775

TreeFam database of animal gene trees

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TreeFami
TF105559

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase

Pfam protein domain database

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Pfami
View protein in Pfam
PF00149 Metallophos, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00114 STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00156 PP2Ac, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P67775-1) [UniParc]FASTAAdd to basket
Also known as: PP2Acalpha1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC
60 70 80 90 100
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
110 120 130 140 150
VALKVRYRER 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):35,594
Last modified:October 11, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC602291F78F34555
GO
Isoform 2 (identifier: P67775-2) [UniParc]FASTAAdd to basket
Also known as: PP2Acalpha2

The sequence of this isoform differs from the canonical sequence as follows:
     193-246: Missing.

Note: Catalytically inactive, shows enhanced binding to IGBP1, and does not interact with the scaffolding subunit PPP2R1A.
Show »
Length:255
Mass (Da):29,735
Checksum:iB50450F64CB286AB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ESG8E7ESG8_HUMAN
Serine/threonine-protein phosphatas...
PPP2CA
145Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RHP4E5RHP4_HUMAN
Serine/threonine-protein phosphatas...
PPP2CA
126Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05173552V → A. Corresponds to variant dbSNP:rs11552681Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044320193 – 246Missing in isoform 2. CuratedAdd BLAST54

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X12646 mRNA Translation: CAA31176.1
J03804 mRNA Translation: AAB38019.1
M60483 Genomic DNA Translation: AAA36466.1
BC000400 mRNA Translation: AAH00400.1
BC002657 mRNA Translation: AAH02657.1
BC019275 mRNA Translation: AAH19275.1
BC031696 mRNA Translation: AAH31696.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS4173.1 [P67775-1]

Protein sequence database of the Protein Information Resource

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PIRi
S01986 PAHU2A

NCBI Reference Sequences

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RefSeqi
NP_002706.1, NM_002715.2 [P67775-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.105818

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000481195; ENSP00000418447; ENSG00000113575 [P67775-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5515

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5515

UCSC genome browser

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UCSCi
uc003kze.4 human [P67775-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12646 mRNA Translation: CAA31176.1
J03804 mRNA Translation: AAB38019.1
M60483 Genomic DNA Translation: AAA36466.1
BC000400 mRNA Translation: AAH00400.1
BC002657 mRNA Translation: AAH02657.1
BC019275 mRNA Translation: AAH19275.1
BC031696 mRNA Translation: AAH31696.1
CCDSiCCDS4173.1 [P67775-1]
PIRiS01986 PAHU2A
RefSeqiNP_002706.1, NM_002715.2 [P67775-1]
UniGeneiHs.105818

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50C/F1-309[»]
2IE3X-ray2.80C1-309[»]
2IE4X-ray2.60C1-309[»]
2NPPX-ray3.30C/F1-309[»]
2NYLX-ray3.80C/F2-294[»]
2NYMX-ray3.60C/F2-294[»]
3C5WX-ray2.80C1-309[»]
3DW8X-ray2.85C/F1-309[»]
3FGAX-ray2.70C1-309[»]
3K7VX-ray2.85C1-309[»]
3K7WX-ray2.96C1-309[»]
3P71X-ray2.70C1-309[»]
4I5LX-ray2.43C/F1-309[»]
4I5NX-ray2.80C/F1-309[»]
4IYPX-ray2.80C6-153[»]
4LACX-ray2.82C1-309[»]
5W0WX-ray3.80C/F/I/L1-309[»]
ProteinModelPortaliP67775
SMRiP67775
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111507, 288 interactors
CORUMiP67775
DIPiDIP-29395N
IntActiP67775, 166 interactors
MINTiP67775
STRINGi9606.ENSP00000418447

Chemistry databases

BindingDBiP67775
ChEMBLiCHEMBL4703
DrugBankiDB00163 Vitamin E

PTM databases

DEPODiP67775
iPTMnetiP67775
PhosphoSitePlusiP67775

Polymorphism and mutation databases

BioMutaiPPP2CA
DMDMi54038809

Proteomic databases

EPDiP67775
MaxQBiP67775
PaxDbiP67775
PeptideAtlasiP67775
PRIDEiP67775
ProteomicsDBi57521

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
5515
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000481195; ENSP00000418447; ENSG00000113575 [P67775-1]
GeneIDi5515
KEGGihsa:5515
UCSCiuc003kze.4 human [P67775-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5515
DisGeNETi5515
EuPathDBiHostDB:ENSG00000113575.9

GeneCards: human genes, protein and diseases

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GeneCardsi
PPP2CA
HGNCiHGNC:9299 PPP2CA
HPAiCAB003848
HPA043236
MIMi176915 gene
neXtProtiNX_P67775
OpenTargetsiENSG00000113575
PharmGKBiPA33663

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0371 Eukaryota
COG0639 LUCA
GeneTreeiENSGT00550000074618
HOGENOMiHOG000172696
HOVERGENiHBG000216
InParanoidiP67775
KOiK04382
OMAiQILWNDP
OrthoDBiEOG091G0B6S
PhylomeDBiP67775
TreeFamiTF105559

Enzyme and pathway databases

BioCyciMetaCyc:HS03696-MONOMER
ReactomeiR-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
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-2995383 Initiation of Nuclear Envelope Reformation
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/B2 associated events during G2/M transition
R-HSA-70171 Glycolysis
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
SignaLinkiP67775
SIGNORiP67775

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
PPP2CA human
EvolutionaryTraceiP67775

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PPP2CA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5515

Protein Ontology

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PROi
PR:P67775

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000113575 Expressed in 233 organ(s), highest expression level in adrenal tissue
CleanExiHS_PPP2CA
ExpressionAtlasiP67775 baseline and differential
GenevisibleiP67775 HS

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPP2AA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P67775
Secondary accession number(s): P05323, P13197
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: December 5, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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