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UniProtKB - P30153 (2AAA_HUMAN)

Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Gene

PPP2R1A

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

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (PubMed:16580887).2 Publications

<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

  • protein antigen binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase regulator activity Source: GO_Central
  • protein serine/threonine phosphatase activity Source: Ensembl
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

Biological processChromosome partition

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000105568-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...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-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-2995383 Initiation of Nuclear Envelope Reformation
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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-5620912 Anchoring of the basal body to the plasma membrane
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-8854518 AURKA Activation by TPX2
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

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

More...SignaLinki		P30153

SIGNOR Signaling Network Open Resource

More...SIGNORi		P30153

<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 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
Medium tumor antigen-associated 61 kDa protein
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
<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:PPP2R1A
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000105568.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:9302 PPP2R1A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605983 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P30153

<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

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mental retardation, autosomal dominant 36 (MRD36)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:616362
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_073718132V → L in MRD36. 1 Publication1
Natural variantiVAR_074488179P → L in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs786205228EnsemblClinVar.1
Natural variantiVAR_074489182R → W in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs786205227EnsemblClinVar.1
Natural variantiVAR_074490258R → H in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs863225094EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		5518

MalaCards human disease database

More...MalaCardsi		PPP2R1A
MIMi616362 phenotype

Open Targets

More...OpenTargetsi		ENSG00000105568

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		457284 Microcephaly-corpus callosum hypoplasia-intellectual disability-facial dysmorphism syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33666

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PPP2R1A

Domain mapping of disease mutations (DMDM)

More...DMDMi		143811355

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000714002 – 589Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformAdd BLAST588

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 residuei2N-acetylalanineCombined sources1
Modified residuei280N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P30153

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P30153

MaxQB - The MaxQuant DataBase

More...MaxQBi		P30153

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

More...PaxDbi		P30153

PeptideAtlas

More...PeptideAtlasi		P30153

PRoteomics IDEntifications database

More...PRIDEi		P30153

2D gel databases

USC-OGP 2-DE database

More...OGPi		P30153

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00554737

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P30153

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

More...PhosphoSitePlusi		P30153

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P30153

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P30153

<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

More...Bgeei		ENSG00000105568 Expressed in 231 organ(s), highest expression level in anterior cingulate cortex

CleanEx database of gene expression profiles

More...CleanExi		HS_PPP2R1A

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P30153 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P30153 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB018599

<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

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (By similarity). 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 IPO9 (PubMed:12670497). Interacts with TP53 and SGO1 (PubMed:17245430, PubMed:16580887). Interacts with PLA2G16; this interaction might decrease PP2A activity (PubMed:17374643). Interacts with CTTNBP2NL (PubMed:18782753). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (PubMed:15525651). Interacts with CIP2A; this interaction stabilizes CIP2A (PubMed:28174209). Interacts with FAM122A (PubMed:27588481). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (By similarity).By similarity9 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111510, 387 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P30153

Database of interacting proteins

More...DIPi		DIP-29394N

Protein interaction database and analysis system

More...IntActi		P30153, 224 interactors

Molecular INTeraction database

More...MINTi		P30153

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000324804

<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

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B3UX-ray2.30A/B2-589[»]
2IE3X-ray2.80A1-589[»]
2IE4X-ray2.60A1-589[»]
2NPPX-ray3.30A/D1-589[»]
2NYLX-ray3.80A/D8-589[»]
2NYMX-ray3.60A/D8-589[»]
2PKGX-ray3.30A/B10-589[»]
3C5WX-ray2.80A9-46[»]
A400-589[»]
3DW8X-ray2.85A/D9-589[»]
3K7VX-ray2.85A1-589[»]
3K7WX-ray2.96A1-589[»]
4I5LX-ray2.43A/D6-589[»]
4I5NX-ray2.80A/D6-589[»]
4LACX-ray2.82A404-589[»]
5W0WX-ray3.80A/D/G/J9-589[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P30153

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

More...SMRi		P30153

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P30153

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati8 – 46HEAT 1Add BLAST39
Repeati47 – 84HEAT 2Add BLAST38
Repeati85 – 123HEAT 3Add BLAST39
Repeati124 – 161HEAT 4Add BLAST38
Repeati162 – 200HEAT 5Add BLAST39
Repeati201 – 239HEAT 6Add BLAST39
Repeati240 – 278HEAT 7Add BLAST39
Repeati279 – 321HEAT 8Add BLAST43
Repeati322 – 360HEAT 9Add BLAST39
Repeati361 – 399HEAT 10Add BLAST39
Repeati400 – 438HEAT 11Add BLAST39
Repeati439 – 477HEAT 12Add BLAST39
Repeati478 – 516HEAT 13Add BLAST39
Repeati517 – 555HEAT 14Add BLAST39
Repeati556 – 589HEAT 15Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni8 – 399PP2A subunit B bindingAdd BLAST392
Regioni47 – 321Polyoma small and medium T antigens BindingAdd BLAST275
Regioni85 – 239SV40 small T antigen bindingAdd BLAST155
Regioni400 – 589PP2A subunit C bindingAdd BLAST190

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

<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 phosphatase 2A regulatory subunit A family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0211 Eukaryota
ENOG410XQVI LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00730000110944

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000078539

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000011

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30153

KEGG Orthology (KO)

More...KOi		K03456

Identification of Orthologs from Complete Genome Data

More...OMAi		FIPLTIR

Database of Orthologous Groups

More...OrthoDBi		447572at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30153

TreeFam database of animal gene trees

More...TreeFami		TF105552

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000357 HEAT
IPR021133 HEAT_type_2
IPR031090 PP2A_A_meta

The PANTHER Classification System

More...PANTHERi		PTHR10648:SF2 PTHR10648:SF2, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02985 HEAT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371 SSF48371, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50077 HEAT_REPEAT, 11 hits

<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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

P30153-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE 
        60         70         80         90        100
LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE 
       110        120        130        140        150
ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL 
       160        170        180        190        200
FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN 
       210        220        230        240        250
VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ 
       260        270        280        290        300
AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA 
       310        320        330        340        350
AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM 
       360        370        380        390        400
GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL 
       410        420        430        440        450
SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW 
       460        470        480        490        500
LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT 
       510        520        530        540        550
TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI 
       560        570        580 
LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Length:589
Mass (Da):65,309
Last modified:April 3, 2007 - v4
<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:i5174EBE94D537836
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3KQV6B3KQV6_HUMAN
cDNA FLJ33169 fis, clone ADRGL20003...
PPP2R1A
410Annotation score:

Annotation score:1 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>
C9J9C1C9J9C1_HUMAN
Serine/threonine-protein phosphatas...
PPP2R1A
395Annotation score:

Annotation score:1 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>
E9PH38E9PH38_HUMAN
Serine/threonine-protein phosphatas...
PPP2R1A
132Annotation score:

Annotation score:1 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>
M0QXG4M0QXG4_HUMAN
Serine/threonine-protein phosphatas...
PPP2R1A
38Annotation score:

Annotation score:1 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>
M0R0K6M0R0K6_HUMAN
Serine/threonine-protein phosphatas...
PPP2R1A
66Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti130P → A in AAA35531 (PubMed:2554323).Curated1
Sequence conflicti258R → A in AAA36399 (PubMed:2159327).Curated1
Sequence conflicti272K → R AA sequence (PubMed:8694763).Curated1
Sequence conflicti551L → P in CAG29336 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073718132V → L in MRD36. 1 Publication1
Natural variantiVAR_074488179P → L in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs786205228EnsemblClinVar.1
Natural variantiVAR_074489182R → W in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs786205227EnsemblClinVar.1
Natural variantiVAR_074490258R → H in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA. 1 PublicationCorresponds to variant dbSNP:rs863225094EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M31786 mRNA Translation: AAA35531.1
J02902 mRNA Translation: AAA36399.1
CR450340 mRNA Translation: CAG29336.1
BC001537 mRNA Translation: AAH01537.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12849.1

Protein sequence database of the Protein Information Resource

More...PIRi		A34541

NCBI Reference Sequences

More...RefSeqi		NP_055040.2, NM_014225.5

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.467192

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000322088; ENSP00000324804; ENSG00000105568

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5518

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5518

UCSC genome browser

More...UCSCi		uc002pyp.4 human

<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
M31786 mRNA Translation: AAA35531.1
J02902 mRNA Translation: AAA36399.1
CR450340 mRNA Translation: CAG29336.1
BC001537 mRNA Translation: AAH01537.1
CCDSiCCDS12849.1
PIRiA34541
RefSeqiNP_055040.2, NM_014225.5
UniGeneiHs.467192

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B3UX-ray2.30A/B2-589[»]
2IE3X-ray2.80A1-589[»]
2IE4X-ray2.60A1-589[»]
2NPPX-ray3.30A/D1-589[»]
2NYLX-ray3.80A/D8-589[»]
2NYMX-ray3.60A/D8-589[»]
2PKGX-ray3.30A/B10-589[»]
3C5WX-ray2.80A9-46[»]
A400-589[»]
3DW8X-ray2.85A/D9-589[»]
3K7VX-ray2.85A1-589[»]
3K7WX-ray2.96A1-589[»]
4I5LX-ray2.43A/D6-589[»]
4I5NX-ray2.80A/D6-589[»]
4LACX-ray2.82A404-589[»]
5W0WX-ray3.80A/D/G/J9-589[»]
ProteinModelPortaliP30153
SMRiP30153
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111510, 387 interactors
CORUMiP30153
DIPiDIP-29394N
IntActiP30153, 224 interactors
MINTiP30153
STRINGi9606.ENSP00000324804

PTM databases

iPTMnetiP30153
PhosphoSitePlusiP30153
SwissPalmiP30153

Polymorphism and mutation databases

BioMutaiPPP2R1A
DMDMi143811355

2D gel databases

OGPiP30153
REPRODUCTION-2DPAGEiIPI00554737

Proteomic databases

EPDiP30153
jPOSTiP30153
MaxQBiP30153
PaxDbiP30153
PeptideAtlasiP30153
PRIDEiP30153

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5518
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322088; ENSP00000324804; ENSG00000105568
GeneIDi5518
KEGGihsa:5518
UCSCiuc002pyp.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5518
DisGeNETi5518
EuPathDBiHostDB:ENSG00000105568.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		PPP2R1A
HGNCiHGNC:9302 PPP2R1A
HPAiCAB018599
MalaCardsiPPP2R1A
MIMi605983 gene
616362 phenotype
neXtProtiNX_P30153
OpenTargetsiENSG00000105568
Orphaneti457284 Microcephaly-corpus callosum hypoplasia-intellectual disability-facial dysmorphism syndrome
PharmGKBiPA33666

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0211 Eukaryota
ENOG410XQVI LUCA
GeneTreeiENSGT00730000110944
HOGENOMiHOG000078539
HOVERGENiHBG000011
InParanoidiP30153
KOiK03456
OMAiFIPLTIR
OrthoDBi447572at2759
PhylomeDBiP30153
TreeFamiTF105552

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105568-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-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-2995383 Initiation of Nuclear Envelope Reformation
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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-5620912 Anchoring of the basal body to the plasma membrane
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-8854518 AURKA Activation by TPX2
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
SignaLinkiP30153
SIGNORiP30153

Miscellaneous databases

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

More...ChiTaRSi		PPP2R1A human
EvolutionaryTraceiP30153

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PPP2R1A

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

More...GenomeRNAii		5518
PMAP-CutDBiP30153

Protein Ontology

More...PROi		PR:P30153

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000105568 Expressed in 231 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_PPP2R1A
ExpressionAtlasiP30153 baseline and differential
GenevisibleiP30153 HS

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000357 HEAT
IPR021133 HEAT_type_2
IPR031090 PP2A_A_meta
PANTHERiPTHR10648:SF2 PTHR10648:SF2, 1 hit
PfamiView protein in Pfam
PF02985 HEAT, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50077 HEAT_REPEAT, 11 hits

ProtoNet; Automatic hierarchical classification of proteins

More...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 namei2AAA_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: P30153
Secondary accession number(s): Q13773, Q6ICQ3, Q96DH3
<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: April 1, 1993
Last sequence update: April 3, 2007
Last modified: January 16, 2019
This is version 198 of the entry and version 4 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
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