Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P62137 (PP1A_MOUSE)

Entry version 167 (17 Jun 2020)
Sequence version 1 (21 Jun 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

Ppp1ca

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

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity).By similarity4 Publications

<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

Protein has several cofactor binding sites:

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 bindingi64Manganese 1By similarity1
Metal bindingi66Manganese 1By similarity1
Metal bindingi92Manganese 1By similarity1
Metal bindingi92Manganese 2By similarity1
Metal bindingi124Manganese 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 sitei125Proton donorBy similarity1
Metal bindingi173Manganese 2By similarity1
Metal bindingi248Manganese 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 processBiological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism
LigandManganese, Metal-binding

<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 PP1-alpha catalytic subunit (EC:3.1.3.16)
Short name:
PP-1A
<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:Ppp1ca
Synonyms:Ppp1a
<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 19

Organism-specific databases

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

More...MGIi		MGI:103016 Ppp1ca

<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

Cytoplasm, 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>Mutagenesisi64D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. 1 Publication1
Mutagenesisi95D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 methionineiRemovedBy similarity
<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_00000587752 – 330Serine/threonine-protein phosphatase PP1-alpha catalytic subunitAdd BLAST329

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-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei305N6-acetyllysineCombined sources1
Modified residuei306PhosphotyrosineCombined sources1
Modified residuei320PhosphothreonineCombined sources1
Modified residuei325PhosphoserineBy similarity1

<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

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P62137

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P62137

MaxQB - The MaxQuant DataBase

More...MaxQBi		P62137

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

More...PaxDbi		P62137

PeptideAtlas

More...PeptideAtlasi		P62137

PRoteomics IDEntifications database

More...PRIDEi		P62137

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P62137

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

More...PhosphoSitePlusi		P62137

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P62137

<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		ENSMUSG00000040385 Expressed in thymus and 270 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P62137 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

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen.

Interacts with PPP1R9A, PPP1R9B and PPP1R7.

Interacts with PPP1R15A; the interaction mediates binding to EIF2S1.

Interacts with YLPM1.

Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5.

Interacts with NOM1 and PPP1R8.

Interacts with PPP1R16B. Interacts. with RPSA only in the presence of PPP1R16B.

Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.

Interacts with PPP1R10/PNUTS and PPP1R8.

Interacts with WDR82 in the presence of PPP1R10/PNUTS.

Interacts with PPP1R39.

Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site (By similarity).

Interacts with PPP1R15B; the interaction mediates binding to EIF2S1.

Part of a complex containing PPP1R15B, PP1 and NCK1/2.

Interacts with NEK2.

Interacts with FER; this promotes phosphorylation at Thr-320 (By similarity).

Interacts with PHACTR4; which acts as an activator of PP1 activity.

Interacts with BTBD10 (PubMed:18160256).

Interacts with KCTD20 (PubMed:24156551).

Interacts with FOXP3 (By similarity).

Interacts with CENPA (By similarity).

Interacts with ATG16L1 (By similarity).

Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="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		202335, 46 interactors

Protein interaction database and analysis system

More...IntActi		P62137, 169 interactors

Molecular INTeraction database

More...MINTi		P62137

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000039109

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P62137 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

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P62137

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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		ENOG410IN85 Eukaryota
ENOG410XPVF LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153472

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004962_8_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P62137

KEGG Orthology (KO)

More...KOi		K06269

Identification of Orthologs from Complete Genome Data

More...OMAi		YLVMESR

Database of Orthologous Groups

More...OrthoDBi		766640at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P62137

TreeFam database of animal gene trees

More...TreeFami		TF354243

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
IPR031675 STPPase_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00149 Metallophos, 1 hit
PF16891 STPPase_N, 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.

<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 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.

P62137-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP 
        60         70         80         90        100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 
       110        120        130        140        150
LETICLLLAY KIRYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 
       160        170        180        190        200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 
       210        220        230        240        250
LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 
       260        270        280        290        300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 
       310        320        330
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
Length:330
Mass (Da):37,540
Last modified:June 21, 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:i8FBFD158A52282E0
GO

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
U25809 mRNA Translation: AAC99814.1
AK007932 mRNA Translation: BAB25358.1
AK028392 mRNA Translation: BAC25928.1
AK090070 mRNA Translation: BAC41078.1
AK151582 mRNA Translation: BAE30522.1
AK152667 mRNA Translation: BAE31402.1
AK153517 mRNA Translation: BAE32060.1
AK159575 mRNA Translation: BAE35196.1
AK167244 mRNA Translation: BAE39365.1
AK167538 mRNA Translation: BAE39605.1
AK167880 mRNA Translation: BAE39893.1
AK167981 mRNA Translation: BAE39973.1
BC014828 mRNA Translation: AAH14828.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS29421.1

NCBI Reference Sequences

More...RefSeqi		NP_114074.1, NM_031868.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385
ENSMUST00000180575; ENSMUSP00000137997; ENSMUSG00000096994

Database of genes from NCBI RefSeq genomes

More...GeneIDi		19045

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:19045

UCSC genome browser

More...UCSCi		uc008fzg.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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25809 mRNA Translation: AAC99814.1
AK007932 mRNA Translation: BAB25358.1
AK028392 mRNA Translation: BAC25928.1
AK090070 mRNA Translation: BAC41078.1
AK151582 mRNA Translation: BAE30522.1
AK152667 mRNA Translation: BAE31402.1
AK153517 mRNA Translation: BAE32060.1
AK159575 mRNA Translation: BAE35196.1
AK167244 mRNA Translation: BAE39365.1
AK167538 mRNA Translation: BAE39605.1
AK167880 mRNA Translation: BAE39893.1
AK167981 mRNA Translation: BAE39973.1
BC014828 mRNA Translation: AAH14828.1
CCDSiCCDS29421.1
RefSeqiNP_114074.1, NM_031868.2

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
5ZQVX-ray2.95A/B/C/D1-330[»]
5ZT0X-ray3.32A/B/C/D/E/F7-300[»]
SMRiP62137
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi202335, 46 interactors
IntActiP62137, 169 interactors
MINTiP62137
STRINGi10090.ENSMUSP00000039109

PTM databases

iPTMnetiP62137
PhosphoSitePlusiP62137
SwissPalmiP62137

Proteomic databases

EPDiP62137
jPOSTiP62137
MaxQBiP62137
PaxDbiP62137
PeptideAtlasiP62137
PRIDEiP62137

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3872 575 antibodies

Genome annotation databases

EnsembliENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385
ENSMUST00000180575; ENSMUSP00000137997; ENSMUSG00000096994
GeneIDi19045
KEGGimmu:19045
UCSCiuc008fzg.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5499
MGIiMGI:103016 Ppp1ca

Phylogenomic databases

eggNOGiENOG410IN85 Eukaryota
ENOG410XPVF LUCA
GeneTreeiENSGT00940000153472
HOGENOMiCLU_004962_8_1_1
InParanoidiP62137
KOiK06269
OMAiYLVMESR
OrthoDBi766640at2759
PhylomeDBiP62137
TreeFamiTF354243

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		19045 4 hits in 12 CRISPR screens

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

More...ChiTaRSi		Ppp1ca mouse

Protein Ontology

More...PROi		PR:P62137
RNActiP62137 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000040385 Expressed in thymus and 270 other tissues
GenevisibleiP62137 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
IPR031675 STPPase_N
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PF16891 STPPase_N, 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 nameiPP1A_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: P62137
Secondary accession number(s): P08129
, P20653, P22802, Q3U7G7, Q9Z1G2
<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: August 1, 1988
Last sequence update: June 21, 2004
Last modified: June 17, 2020
This is version 167 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

3D-structure, 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again