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UniProtKB - O54943 (PER2_MOUSE)

Protein

Period circadian protein homolog 2

Gene

Per2

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

Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1.17 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

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 processBiological rhythms, Transcription, Transcription regulation

<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:
Period circadian protein homolog 2
Short name:
mPER2
Alternative name(s):
Circadian clock protein PERIOD 2
<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:Per2
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

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

More...MGIi		MGI:1195265 Per2

<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

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Animals show severely disrupted circadian behavior. During myocardial ischemia, they have larger infarct sizes with deficient lactate production. Mice show reduced muscle strength under stress conditions, show endothelial dysfunctions and have a mean arterial pressure significantly lower compared to wild types. They have elevated circulatory insulin levels associated with enhanced glucose-stimulated insulin secretion and impaired insulin clearance. Animals also have increased levels of liver glycogen and impaired hepatic gluconeogenesis. They display altered lipid metabolism with drastic reduction of total triacylglycerides and non-esterified fatty acids. Double knockouts for PER2 and PER1 show an abrupt loss of rhythmicity immediately upon transfer to exposure to constant darkness. Animals have largely affected the water intake (polydipsia) and urine volume (polyuria). Double knocknouts for PER2 and PER3 show the same phenotype as PER2 simple knockouts. Double knockout for NR1D1 and PER2 show a significantly shorter period length compared with wild type or single knockouts for both genes. 50% of double knockouts animals show a stable circadian throughout at least 5 weeks in constant darkness. The other 50% of animals lose their circadian rhythmicity when held in constant darkness for an average of 21 days. Animals have blunted steady-state levels of glycogen in the liver in spite of normal patterns of food consumption.8 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi113 – 116LKEL → AKEA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication4
Mutagenesisi306 – 310LCCLL → ACCAA: Abolishes interaction with PPARA and NR1D1. No effect on interaction with CRY1. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of ARNTL expression; when associated with 1052-E--A-1055. 1 Publication5
Mutagenesisi306 – 310Missing : Abolishes interaction with NR1D1. 1 Publication5
Mutagenesisi415F → E: Abolishes dimerization. 1 Publication1
Mutagenesisi419W → E: Abolishes dimerization. 1 Publication1
Mutagenesisi427I → E: Abolishes dimerization. 1 Publication1
Mutagenesisi464 – 467IHRL → AHRA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 113-A--A-116 and 985-A--A-990. 1 Publication4
Mutagenesisi985 – 990LNLLQL → ANAAQA: Slightly accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication6
Mutagenesisi1052 – 1055NLLL → EAAA: No effect on interaction with PPARA. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of ARNTL expression; when associated with 306-A--A-310. 1 Publication4
Mutagenesisi1052 – 1055Missing : No effect on interaction with NR1D1. 1 Publication4

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001626311 – 1257Period circadian protein homolog 2Add BLAST1257

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 residuei525Phosphoserine1 Publication1
Modified residuei528Phosphoserine1 Publication1
Modified residuei531Phosphoserine1 Publication1
Modified residuei538Phosphoserine1 Publication1
Modified residuei544Phosphoserine1 Publication1
Modified residuei554Phosphothreonine1 Publication1
Modified residuei659PhosphoserineBy similarity1
Modified residuei693PhosphoserineCombined sources1
Modified residuei697PhosphoserineCombined sources1
Modified residuei706Phosphoserine1 Publication1
Modified residuei758Phosphoserine1 Publication1
Modified residuei763Phosphoserine1 Publication1
Modified residuei858Phosphothreonine1 Publication1
Modified residuei939Phosphoserine1 Publication1
Modified residuei964Phosphothreonine1 Publication1
Modified residuei971Phosphoserine1 Publication1
Modified residuei1126Phosphoserine1 Publication1

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

Acetylated. Deacetylated by SIRT1, resulting in decreased protein stability.1 Publication
Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1.5 Publications
Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		O54943

PRoteomics IDEntifications database

More...PRIDEi		O54943

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O54943

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

More...PhosphoSitePlusi		O54943

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In the brain, high expression in SCN during the subjective day. Constitutive expression in the cornu ammonis and in the dentate gyrus of the hyppocampus. Also expressed in the piriform cortex and the glomeruli of the olfactory bulb, and at a lower extent in the cerebral cortex. Not expressed in the pars tuberalis and the Purkinje neurons. Also expressed in adipose tissue (white and brown), heart, kidney, bladder, lumbar spinal cord, skeletal muscle, spleen, lung, pancreas and liver with highest levels in skeletal muscle and liver and lowest levels in spleen.7 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in the SCN during late fetal and early neonatal life. Expression increases during adipogenesis.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Oscillates diurnally in several tissues, mainly in central nervous system and liver (at protein levels) but also in pancreas, bladder and lumbar spinal cord. Rhythmic levels are critical for the generation of circadian rhythms in central as well as peripheral clocks. Targeted degradation of PER and CRY proteins enables the reactivation of CLOCK-ARTNL/BMAL1, thus initiating a new circadian transcriptional cycle with an intrinsic period of 24 hours.7 Publications

Gene expression databases

CleanEx database of gene expression profiles

More...CleanExi		MM_PER2

<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

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts with CLOCK-ARNTL/BMAL1 (off DNA). Interacts with ARNTL2/BMAL2. Interacts directly with PER1 and PER3, and through a C-terminal domain, with CRY1 and CRY2. Interacts, via its second PAS domain, with TIMELESS in vitro. Interacts with NFIL3. Different large complexes have been identified with different repressive functions. The core of PER complexes is composed of at least PER1, PER2, PER3, CRY1, CRY2, CSNK1D and/or CSNK1E. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with SETX; the interaction inhibits termination of circadian target genes. Interacts with the nuclear receptors HNF4A, NR1D1, NR4A2, RORA, PPARA, PPARG and THRA; the interaction with at least PPARG is ligand dependent. Interacts with PML. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and SFPQ. Interacts with SIRT1. Interacts with CAVIN3. Interacts with MAGEL2. Interacts with MAP1LC3B (PubMed:29937374).26 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		202112, 25 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3209 Cry1-Per2 complex
CPX-3210 Cry2-Per2 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O54943

Database of interacting proteins

More...DIPi		DIP-38518N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		O54943

Protein interaction database and analysis system

More...IntActi		O54943, 32 interactors

Molecular INTeraction database

More...MINTi		O54943

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000066620

<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

11257
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
3GDIX-ray2.40A/B170-473[»]
4CT0X-ray2.45B1132-1252[»]
4U8HX-ray2.80B/D1095-1215[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O54943

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

More...SMRi		O54943

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		O54943

<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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini179 – 246PAS 1PROSITE-ProRule annotationAdd BLAST68
Domaini319 – 385PAS 2PROSITE-ProRule annotationAdd BLAST67
Domaini393 – 436PACAdd BLAST44

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>Regioni478 – 482Important for protein stabilityBy similarity5
Regioni510 – 709CSNK1E binding domainAdd BLAST200
Regioni882 – 1067Interaction with PPARG1 PublicationAdd BLAST186
Regioni1157 – 1257CRY binding domainBy similarityAdd BLAST101

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi109 – 118Nuclear export signal 11 Publication10
Motifi306 – 310LXXLL5
Motifi460 – 469Nuclear export signal 21 Publication10
Motifi778 – 794Nuclear localization signal1 PublicationAdd BLAST17
Motifi983 – 990Nuclear export signal 31 Publication8
Motifi1051 – 1055LXXLL5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi831 – 961Pro-richAdd BLAST131
Compositional biasi1061 – 1111Ser-richAdd BLAST51

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3753 Eukaryota
ENOG410Y118 LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008167

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O54943

KEGG Orthology (KO)

More...KOi		K02633

Database of Orthologous Groups

More...OrthoDBi		145617at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O54943

TreeFam database of animal gene trees

More...TreeFami		TF318445

Family and domain databases

Conserved Domains Database

More...CDDi		cd00130 PAS, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013655 PAS_fold_3
IPR022728 Period_circadian-like_C

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08447 PAS_3, 1 hit
PF12114 Period_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55785 SSF55785, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50112 PAS, 1 hit

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O54943-1 [UniParc]FASTAAdd to basket
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MNGYVDFSPS PTSPTKEPGA PQPTQAVLQE DVDMSSGSSG NENCSTGRDS 
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QGSDCDDNGK ELRMLVESSN THPSPDDAFR LMMTEAEHNP STSGCSSEQS 
       110        120        130        140        150
AKADAHKELI RTLKELKVHL PADKKAKGKA STLATLKYAL RSVKQVKANE 
       160        170        180        190        200
EYYQLLMSSE SQPCSVDVPS YSMEQVEGIT SEYIVKNADM FAVAVSLVSG 
       210        220        230        240        250
KILYISNQVA SIFHCKKDAF SDAKFVEFLA PHDVSVFHSY TTPYKLPPWS 
       260        270        280        290        300
VCSGLDSFTQ ECMEEKSFFC RVSVGKHHEN EIRYQPFRMT PYLVKVQEQQ 
       310        320        330        340        350
GAESQLCCLL LAERVHSGYE APRIPPEKRI FTTTHTPNCL FQAVDERAVP 
       360        370        380        390        400
LLGYLPQDLI ETPVLVQLHP SDRPLMLAIH KKILQAGGQP FDYSPIRFRT 
       410        420        430        440        450
RNGEYITLDT SWSSFINPWS RKISFIIGRH KVRVGPLNED VFAAPPCPEE 
       460        470        480        490        500
KTPHPSVQEL TEQIHRLLMQ PVPHSGSSGY GSLGSNGSHE HLMSQTSSSD 
       510        520        530        540        550
SNGQEESHRR RSGIFKTSGK IQTKSHVSHE SGGQKEASVA EMQSSPPAQV 
       560        570        580        590        600
KAVTTIERDS SGASLPKASF PEELAYKNQP PCSYQQISCL DSVIRYLESC 
       610        620        630        640        650
SEAATLKRKC EFPANIPSRK ATVSPGLHSG EAARPSKVTS HTEVSAHLSS 
       660        670        680        690        700
LTLPGKAESV VSLTSQCSYS STIVHVGDKK PQPELETVED MASGPESLDG 
       710        720        730        740        750
AAGGLSQEKG PLQKLGLTKE VLAAHTQKEE QGFLQRFREV SRLSALQAHC 
       760        770        780        790        800
QNYLQERSRA QASDRGLRNT SGLESSWKKT GKNRKLKSKR VKTRDSSEST 
       810        820        830        840        850
GSGGPVSHRP PLMGLNATAW SPSDTSQSSC PSAPFPTAVP AYPLPVFQAP 
       860        870        880        890        900
GIVSTPGTVV APPAATHTGF TMPVVPMGTQ PEFAVQPLPF AAPLAPVMAF 
       910        920        930        940        950
MLPSYPFPPA TPNLPQAFLP SQPHFPAHPT LASEITPASQ AEFPSRTSTL 
       960        970        980        990       1000
RQPCACPVTP PAGTVALGRA SPPLFQSRGS SPLQLNLLQL EEAPEGSTGA 
      1010       1020       1030       1040       1050
AGTLGTTGTA ASGLDCTSGT SRDRQPKAPP TCNEPSDTQN SDAISTSSDL 
      1060       1070       1080       1090       1100
LNLLLGEDLC SATGSALSRS GASATSDSLG SSSLGFGTSQ SGAGSSDTSH 
      1110       1120       1130       1140       1150
TSKYFGSIDS SENNHKAKMI PDTEESEQFI KYVLQDPIWL LMANTDDSIM 
      1160       1170       1180       1190       1200
MTYQLPSRDL QAVLKEDQEK LKLLQRSQPR FTEGQRRELR EVHPWVHTGG 
      1210       1220       1230       1240       1250
LPTAIDVTGC VYCESEEKGN ICLPYEEDSP SPGLCDTSEA KEEEGEQLTG 

PRIEAQT
Length:1,257
Mass (Da):135,881
Last modified:July 15, 1999 - v3
<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:i554B8AFF036CF7FB
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J0U3A0A0R4J0U3_MOUSE
Period circadian protein homolog 2
Per2
1,257Annotation 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 conflicti445P → S in AAC53592 (PubMed:9427249).Curated1
Sequence conflicti728K → R in AAC53592 (PubMed:9427249).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
AF036893 mRNA Translation: AAC39942.1
AF035830 mRNA Translation: AAC53592.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS35663.1

Protein sequence database of the Protein Information Resource

More...PIRi		T09493

NCBI Reference Sequences

More...RefSeqi		NP_035196.2, NM_011066.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.482463

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18627

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18627

<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
AF036893 mRNA Translation: AAC39942.1
AF035830 mRNA Translation: AAC53592.1
CCDSiCCDS35663.1
PIRiT09493
RefSeqiNP_035196.2, NM_011066.3
UniGeneiMm.482463

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GDIX-ray2.40A/B170-473[»]
4CT0X-ray2.45B1132-1252[»]
4U8HX-ray2.80B/D1095-1215[»]
ProteinModelPortaliO54943
SMRiO54943
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202112, 25 interactors
ComplexPortaliCPX-3209 Cry1-Per2 complex
CPX-3210 Cry2-Per2 complex
CORUMiO54943
DIPiDIP-38518N
ELMiO54943
IntActiO54943, 32 interactors
MINTiO54943
STRINGi10090.ENSMUSP00000066620

PTM databases

iPTMnetiO54943
PhosphoSitePlusiO54943

Proteomic databases

PaxDbiO54943
PRIDEiO54943

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		18627
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18627
KEGGimmu:18627

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8864
MGIiMGI:1195265 Per2

Phylogenomic databases

eggNOGiKOG3753 Eukaryota
ENOG410Y118 LUCA
HOVERGENiHBG008167
InParanoidiO54943
KOiK02633
OrthoDBi145617at2759
PhylomeDBiO54943
TreeFamiTF318445

Miscellaneous databases

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

More...ChiTaRSi		Per2 mouse
EvolutionaryTraceiO54943

Protein Ontology

More...PROi		PR:O54943

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

CleanExiMM_PER2

Family and domain databases

CDDicd00130 PAS, 1 hit
InterProiView protein in InterPro
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013655 PAS_fold_3
IPR022728 Period_circadian-like_C
PfamiView protein in Pfam
PF08447 PAS_3, 1 hit
PF12114 Period_C, 1 hit
SMARTiView protein in SMART
SM00091 PAS, 2 hits
SUPFAMiSSF55785 SSF55785, 1 hit
PROSITEiView protein in PROSITE
PS50112 PAS, 1 hit

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 nameiPER2_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: O54943
Secondary accession number(s): O54954
<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: July 15, 1999
Last sequence update: July 15, 1999
Last modified: January 16, 2019
This is version 153 of the entry and version 3 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, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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