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UniProtKB - P63330 (PP2AA_MOUSE)

Entry version 153 (10 Feb 2021)
Sequence version 1 (11 Oct 2004)
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Protein

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

Gene

Ppp2ca

Organism
Mus musculus (Mouse)
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. Activates RAF1 by dephosphorylating it at 'Ser-259' (By similarity). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (By similarity).By similarity1 Publication

Miscellaneous

Double mutation Phe-307 and Gln-309 results in association of the PP2A C subunit with alpha-4 protein.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 1By similarity1
Metal bindingi59Manganese 1By similarity1
Metal bindingi85Manganese 1By similarity1
Metal bindingi85Manganese 2By similarity1
Metal bindingi117Manganese 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 2By similarity1
Metal bindingi241Manganese 2By similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-1295596, Spry regulation of FGF signaling
R-MMU-141444, Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-180024, DARPP-32 events
R-MMU-195253, Degradation of beta-catenin by the destruction complex
R-MMU-196299, Beta-catenin phosphorylation cascade
R-MMU-198753, ERK/MAPK targets
R-MMU-202670, ERKs are inactivated
R-MMU-2467813, Separation of Sister Chromatids
R-MMU-2500257, Resolution of Sister Chromatid Cohesion
R-MMU-2995383, Initiation of Nuclear Envelope (NE) Reformation
R-MMU-389513, CTLA4 inhibitory signaling
R-MMU-432142, Platelet sensitization by LDL
R-MMU-4641262, Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5663220, RHO GTPases Activate Formins
R-MMU-5673000, RAF activation
R-MMU-5675221, Negative regulation of MAPK pathway
R-MMU-6804757, Regulation of TP53 Degradation
R-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-68877, Mitotic Prometaphase
R-MMU-69231, Cyclin D associated events in G1
R-MMU-69273, Cyclin A/B1/B2 associated events during G2/M transition
R-MMU-9648025, EML4 and NUDC in mitotic spindle formation
R-MMU-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<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%5Fand%5Ftaxonomy%5Fsection">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:3.1.3.16By similarity)
Short name:
PP2A-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1321159, Ppp2ca

<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 & Seán O’Donoghue; 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi307Y → Q: Loss of trimeric subunit ABC assembly. 1 Publication1
Mutagenesisi309L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588401 – 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 residuei307Phosphotyrosine1 Publication1
Modified residuei309Leucine methyl ester1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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.1 Publication
Polyubiquitinated, leading to its degradation by the proteasome (By similarity). May be monoubiquitinated by NOSIP.By similarity1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P63330

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63330

MaxQB - The MaxQuant DataBase

More...MaxQBi		P63330

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

More...PaxDbi		P63330

PeptideAtlas

More...PeptideAtlasi		P63330

PRoteomics IDEntifications database

More...PRIDEi		P63330

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63330

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

More...PhosphoSitePlusi		P63330

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P63330

<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		ENSMUSG00000020349, Expressed in cerebellum and 320 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63330, MM

<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%5Fsection">'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%5Fsection">'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.

Interacts with TP53, SGO1 and SGO2.

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).

Interacts with KCTD20 (PubMed:24156551).

Interacts with BTBD10 (PubMed:18160256).

Interacts with MFHAS1; retains PPP2CA into the cytoplasm and excludes it from the nucleus (By similarity).

Interacts with PABIR1/FAM122A (By similarity).

Interacts with ADCY8; interaction is phosphatase activity-dependent; antagonizes interaction between ADCY8 and calmodulin (PubMed:16258073).

Interacts with CRTC3 (when phosphorylated at 'Ser-391') (PubMed:30611118).

Interacts with SPRY2; the interaction is inhibited by TESK1 interaction with SPRY2, possibly by vesicular sequestration of SPRY2 (By similarity).

Interacts with TRAF3IP3 (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202341, 104 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P63330

Protein interaction database and analysis system

More...IntActi		P63330, 67 interactors

Molecular INTeraction database

More...MINTi		P63330

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000020608

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P63330, protein

<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

3D structure databases

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

More...SMRi		P63330

Database of comparative protein structure models

More...ModBasei		Search...

<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

More...eggNOGi		KOG0371, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074618

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004962_0_5_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63330

Identification of Orthologs from Complete Genome Data

More...OMAi		MKVRYPN

Database of Orthologous Groups

More...OrthoDBi		808922at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63330

TreeFam database of animal gene trees

More...TreeFami		TF105559

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...Pfami		View protein in Pfam
PF00149, Metallophos, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00114, STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00156, PP2Ac, 1 hit

PROSITE; a protein domain and family database

More...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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P63330-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDEKLFTKEL 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):35,608
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:i8DC11276E6DF9E33
GO

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 conflicti31L → P in AAD12587 (PubMed:9920888).Curated1
Sequence conflicti73G → V in AAD12587 (PubMed:9920888).Curated1

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
AF076192 mRNA Translation: AAD12587.1
Z67745 mRNA Translation: CAA91558.1
AK076110 mRNA Translation: BAC36190.1
AK172644 mRNA Translation: BAE43111.1
AL935177 Genomic DNA No translation available.
BC003856 mRNA Translation: AAH03856.1
BC054458 mRNA Translation: AAH54458.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS24666.1

NCBI Reference Sequences

More...RefSeqi		NP_062284.1, NM_019411.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000020608; ENSMUSP00000020608; ENSMUSG00000020349

Database of genes from NCBI RefSeq genomes

More...GeneIDi		19052

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:19052

UCSC genome browser

More...UCSCi		uc007ivb.1, mouse

<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
AF076192 mRNA Translation: AAD12587.1
Z67745 mRNA Translation: CAA91558.1
AK076110 mRNA Translation: BAC36190.1
AK172644 mRNA Translation: BAE43111.1
AL935177 Genomic DNA No translation available.
BC003856 mRNA Translation: AAH03856.1
BC054458 mRNA Translation: AAH54458.1
CCDSiCCDS24666.1
RefSeqiNP_062284.1, NM_019411.4

3D structure databases

SMRiP63330
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202341, 104 interactors
CORUMiP63330
IntActiP63330, 67 interactors
MINTiP63330
STRINGi10090.ENSMUSP00000020608

PTM databases

iPTMnetiP63330
PhosphoSitePlusiP63330
SwissPalmiP63330

Proteomic databases

EPDiP63330
jPOSTiP63330
MaxQBiP63330
PaxDbiP63330
PeptideAtlasiP63330
PRIDEiP63330

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3550, 634 antibodies

Genome annotation databases

EnsembliENSMUST00000020608; ENSMUSP00000020608; ENSMUSG00000020349
GeneIDi19052
KEGGimmu:19052
UCSCiuc007ivb.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5515
MGIiMGI:1321159, Ppp2ca

Phylogenomic databases

eggNOGiKOG0371, Eukaryota
GeneTreeiENSGT00550000074618
HOGENOMiCLU_004962_0_5_1
InParanoidiP63330
OMAiMKVRYPN
OrthoDBi808922at2759
PhylomeDBiP63330
TreeFamiTF105559

Enzyme and pathway databases

ReactomeiR-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-1295596, Spry regulation of FGF signaling
R-MMU-141444, Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-180024, DARPP-32 events
R-MMU-195253, Degradation of beta-catenin by the destruction complex
R-MMU-196299, Beta-catenin phosphorylation cascade
R-MMU-198753, ERK/MAPK targets
R-MMU-202670, ERKs are inactivated
R-MMU-2467813, Separation of Sister Chromatids
R-MMU-2500257, Resolution of Sister Chromatid Cohesion
R-MMU-2995383, Initiation of Nuclear Envelope (NE) Reformation
R-MMU-389513, CTLA4 inhibitory signaling
R-MMU-432142, Platelet sensitization by LDL
R-MMU-4641262, Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5663220, RHO GTPases Activate Formins
R-MMU-5673000, RAF activation
R-MMU-5675221, Negative regulation of MAPK pathway
R-MMU-6804757, Regulation of TP53 Degradation
R-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-68877, Mitotic Prometaphase
R-MMU-69231, Cyclin D associated events in G1
R-MMU-69273, Cyclin A/B1/B2 associated events during G2/M transition
R-MMU-9648025, EML4 and NUDC in mitotic spindle formation
R-MMU-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		19052, 7 hits in 16 CRISPR screens

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

More...ChiTaRSi		Ppp2ca, mouse

Protein Ontology

More...PROi		PR:P63330
RNActiP63330, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000020349, Expressed in cerebellum and 320 other tissues
GenevisibleiP63330, MM

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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_MOUSE
<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: P63330
Secondary accession number(s): O88591, P13353, Q5SNY5
<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%5Fand%5Fisoforms">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: February 10, 2021
This is version 153 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

<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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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