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Protein

Period circadian protein homolog 2

Gene

PER2

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

Annotation score:5 out of 5

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

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

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 inhibiting 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.By similarity

<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

GO - Biological processi

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

Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-400253 Circadian Clock

SIGNOR Signaling Network Open Resource

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SIGNORi
O15055

<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:
hPER2
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
Synonyms:KIAA0347
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000132326.11

Human Gene Nomenclature Database

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HGNCi
HGNC:8846 PER2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603426 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O15055

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

Advanced sleep phase syndrome, familial, 1 (FASPS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms.
See also OMIM:604348
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029080662S → G in FASPS1; reduced in vitro phosphorylation by CSNK1E. 1 PublicationCorresponds to variant dbSNP:rs121908635EnsemblClinVar.1

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>Mutagenesisi662S → D: Restores CSNK1E-dependent phosphorylation of variant G-662. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
8864

MalaCards human disease database

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MalaCardsi
PER2
MIMi604348 phenotype

Open Targets

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OpenTargetsi
ENSG00000132326

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

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Orphaneti
164736 Familial advanced sleep-phase syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33185

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3751648

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PER2

<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_00001626301 – 1255Period circadian protein homolog 2Add BLAST1255

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 residuei527PhosphoserineBy similarity1
Modified residuei530PhosphoserineBy similarity1
Modified residuei533PhosphoserineBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei662Phosphoserine1 Publication1
Modified residuei696PhosphoserineBy similarity1
Modified residuei700PhosphoserineBy similarity1
Modified residuei714PhosphoserineBy similarity1
Modified residuei766PhosphoserineBy similarity1
Modified residuei771PhosphoserineBy similarity1
Modified residuei945PhosphoserineBy similarity1
Modified residuei977PhosphoserineBy similarity1
Modified residuei1124PhosphoserineBy similarity1

<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.By similarity
Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1.2 Publications
Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O15055

MaxQB - The MaxQuant DataBase

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MaxQBi
O15055

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

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PaxDbi
O15055

PeptideAtlas

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PeptideAtlasi
O15055

PRoteomics IDEntifications database

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PRIDEi
O15055

ProteomicsDB human proteome resource

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ProteomicsDBi
48405
48406 [O15055-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15055

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

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PhosphoSitePlusi
O15055

<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

Widely expressed. Found in heart, brain, placenta, lung, liver, skeleatal muscle, kidney and pancreas. High levels in skeletal muscle and pancreas. Low levels in lung. Isoform 2 is expressed in keratinocytes (at protein level).1 Publication

<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. 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.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000132326 Expressed in 234 organ(s), highest expression level in oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_PER2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15055 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O15055 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA060510

<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 and CAVIN3 (By similarity). Interacts with MAGEL2 (By similarity). Interacts with MAP1LC3B (By similarity).By similarity2 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114387, 20 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3219 Cry1-Per2 complex
CPX-3220 Cry-Per2 complex

Database of interacting proteins

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DIPi
DIP-38051N

Protein interaction database and analysis system

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IntActi
O15055, 9 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000254657

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O15055

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O15055

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

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SMRi
O15055

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini181 – 248PAS 1PROSITE-ProRule annotationAdd BLAST68
Domaini321 – 387PAS 2PROSITE-ProRule annotationAdd BLAST67
Domaini395 – 438PACAdd 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>Regioni480 – 484Important for protein stabilityBy similarity5
Regioni557 – 771CSNK1E binding domainBy similarityAdd BLAST215
Regioni888 – 1071Interaction with PPARGBy similarityAdd BLAST184
Regioni1155 – 1255CRY 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>Motifi111 – 120Nuclear export signal 1By similarity10
Motifi308 – 312LXXLL5
Motifi462 – 471Nuclear export signal 2By similarity10
Motifi789 – 805Nuclear localization signalBy similarityAdd BLAST17
Motifi989 – 996Nuclear export signal 3By similarity8
Motifi1057 – 1061LXXLL5

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 biasi510 – 513Poly-Arg4
Compositional biasi842 – 979Pro-richAdd BLAST138

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3753 Eukaryota
ENOG410Y118 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156342

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231111

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008167

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O15055

KEGG Orthology (KO)

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KOi
K02633

Identification of Orthologs from Complete Genome Data

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OMAi
ELACKDQ

Database of Orthologous Groups

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OrthoDBi
EOG091G00PA

Database for complete collections of gene phylogenies

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PhylomeDBi
O15055

TreeFam database of animal gene trees

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TreeFami
TF318445

Family and domain databases

Conserved Domains Database

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CDDi
cd00130 PAS, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55785 SSF55785, 1 hit

PROSITE; a protein domain and family database

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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>Sequences (2+)i

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

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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O15055-1) [UniParc]FASTAAdd to basket

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

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MNGYAEFPPS PSNPTKEPVE PQPSQVPLQE DVDMSSGSSG HETNENCSTG
60 70 80 90 100
RDSQGSDCDD SGKELGMLVE PPDARQSPDT FSLMMAKSEH NPSTSGCSSD
110 120 130 140 150
QSSKVDTHKE LIKTLKELKV HLPADKKAKG KASTLATLKY ALRSVKQVKA
160 170 180 190 200
NEEYYQLLMS SEGHPCGADV PSYTVEEMES VTSEHIVKNA DMFAVAVSLV
210 220 230 240 250
SGKILYISDQ VASIFHCKRD AFSDAKFVEF LAPHDVGVFH SFTSPYKLPL
260 270 280 290 300
WSMCSGADSF TQECMEEKSF FCRVSVRKSH ENEIRYHPFR MTPYLVKVRD
310 320 330 340 350
QQGAESQLCC LLLAERVHSG YEAPRIPPEK RIFTTTHTPN CLFQDVDERA
360 370 380 390 400
VPLLGYLPQD LIETPVLVQL HPSDRPLMLA IHKKILQSGG QPFDYSPIRF
410 420 430 440 450
RARNGEYITL DTSWSSFINP WSRKISFIIG RHKVRVGPLN EDVFAAHPCT
460 470 480 490 500
EEKALHPSIQ ELTEQIHRLL LQPVPHSGSS GYGSLGSNGS HEHLMSQTSS
510 520 530 540 550
SDSNGHEDSR RRRAEICKNG NKTKNRSHYS HESGEQKKKS VTEMQTNPPA
560 570 580 590 600
EKKAVPAMEK DSLGVSFPEE LACKNQPTCS YQQISCLDSV IRYLESCNEA
610 620 630 640 650
ATLKRKCEFP ANVPALRSSD KRKATVSPGP HAGEAEPPSR VNSRTGVGTH
660 670 680 690 700
LTSLALPGKA ESVASLTSQC SYSSTIVHVG DKKPQPELEM VEDAASGPES
710 720 730 740 750
LDCLAGPALA CGLSQEKEPF KKLGLTKEVL AAHTQKEEQS FLQKFKEIRK
760 770 780 790 800
LSIFQSHCHY YLQERSKGQP SERTAPGLRN TSGIDSPWKK TGKNRKLKSK
810 820 830 840 850
RVKPRDSSES TGSGGPVSAR PPLVGLNATA WSPSDTSQSS CPAVPFPAPV
860 870 880 890 900
PAAYSLPVFP APGTVAAPPA PPHASFTVPA VPVDLQHQFA VQPPPFPAPL
910 920 930 940 950
APVMAFMLPS YSFPSGTPNL PQAFFPSQPQ FPSHPTLTSE MASASQPEFP
960 970 980 990 1000
SRTSIPRQPC ACPATRATPP SAMGRASPPL FQSRSSSPLQ LNLLQLEEAP
1010 1020 1030 1040 1050
EGGTGAMGTT GATETAAVGA DCKPGTSRDQ QPKAPLTRDE PSDTQNSDAL
1060 1070 1080 1090 1100
STSSGLLNLL LNEDLCSASG SAASESLGSG SLGCDASPSG AGSSDTSHTS
1110 1120 1130 1140 1150
KYFGSIDSSE NNHKAKMNTG MEESEHFIKC VLQDPIWLLM ADADSSVMMT
1160 1170 1180 1190 1200
YQLPSRNLEA VLKEDREKLK LLQKLQPRFT ESQKQELREV HQWMQTGGLP
1210 1220 1230 1240 1250
AAIDVAECVY CENKEKGNIC IPYEEDIPSL GLSEVSDTKE DENGSPLNHR

IEEQT
Length:1,255
Mass (Da):136,579
Last modified:July 11, 2001 - v2
<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:i2AEF2C6BD4B6CBB0
GO
Isoform 2 (identifier: O15055-2) [UniParc]FASTAAdd to basket
Also known as: PER2S

The sequence of this isoform differs from the canonical sequence as follows:
     349-404: RAVPLLGYLP...YSPIRFRARN → SPAVRRAAFR...EAQSQGGPFE
     405-1255: Missing.

Show »
Length:404
Mass (Da):45,175
Checksum:iB6DED6DD2AC3F971
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
E9PD89E9PD89_HUMAN
Period circadian protein homolog 2
PER2
109Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA20804 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0515755A → S. Corresponds to variant dbSNP:rs35572922Ensembl.1
Natural variantiVAR_029080662S → G in FASPS1; reduced in vitro phosphorylation by CSNK1E. 1 PublicationCorresponds to variant dbSNP:rs121908635EnsemblClinVar.1
Natural variantiVAR_051576729V → I. Corresponds to variant dbSNP:rs4429421Ensembl.1
Natural variantiVAR_036041823L → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_051577903V → I. Corresponds to variant dbSNP:rs35333999Ensembl.1
Natural variantiVAR_051578949F → Y. Corresponds to variant dbSNP:rs35998480Ensembl.1
Natural variantiVAR_0245581244G → E. Corresponds to variant dbSNP:rs934945Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_021653349 – 404RAVPL…FRARN → SPAVRRAAFRLFSHSVSRPE RRVHHVGHQLVQLHQPMEQE NLLHHWEAQSQGGPFE in isoform 2. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_021654405 – 1255Missing in isoform 2. 1 PublicationAdd BLAST851

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB012614 mRNA Translation: BAA83709.1
EF015905 Genomic DNA Translation: ABM64216.1
AB002345 mRNA Translation: BAA20804.2 Different initiation.
AC012485 Genomic DNA Translation: AAX88976.1
CH471063 Genomic DNA Translation: EAW71155.1
AY647991 Genomic DNA Translation: AAT68170.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2528.1 [O15055-1]

NCBI Reference Sequences

More...
RefSeqi
NP_073728.1, NM_022817.2 [O15055-1]
XP_005246168.1, XM_005246111.4 [O15055-1]
XP_006712887.1, XM_006712824.3 [O15055-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.58756

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000254657; ENSP00000254657; ENSG00000132326 [O15055-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8864

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8864

UCSC genome browser

More...
UCSCi
uc002vyc.4 human [O15055-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012614 mRNA Translation: BAA83709.1
EF015905 Genomic DNA Translation: ABM64216.1
AB002345 mRNA Translation: BAA20804.2 Different initiation.
AC012485 Genomic DNA Translation: AAX88976.1
CH471063 Genomic DNA Translation: EAW71155.1
AY647991 Genomic DNA Translation: AAT68170.1
CCDSiCCDS2528.1 [O15055-1]
RefSeqiNP_073728.1, NM_022817.2 [O15055-1]
XP_005246168.1, XM_005246111.4 [O15055-1]
XP_006712887.1, XM_006712824.3 [O15055-1]
UniGeneiHs.58756

3D structure databases

ProteinModelPortaliO15055
SMRiO15055
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114387, 20 interactors
ComplexPortaliCPX-3219 Cry1-Per2 complex
CPX-3220 Cry-Per2 complex
DIPiDIP-38051N
IntActiO15055, 9 interactors
STRINGi9606.ENSP00000254657

Chemistry databases

BindingDBiO15055
ChEMBLiCHEMBL3751648

PTM databases

iPTMnetiO15055
PhosphoSitePlusiO15055

Polymorphism and mutation databases

BioMutaiPER2

Proteomic databases

EPDiO15055
MaxQBiO15055
PaxDbiO15055
PeptideAtlasiO15055
PRIDEiO15055
ProteomicsDBi48405
48406 [O15055-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
8864
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254657; ENSP00000254657; ENSG00000132326 [O15055-1]
GeneIDi8864
KEGGihsa:8864
UCSCiuc002vyc.4 human [O15055-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8864
DisGeNETi8864
EuPathDBiHostDB:ENSG00000132326.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PER2

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0030280
HGNCiHGNC:8846 PER2
HPAiHPA060510
MalaCardsiPER2
MIMi603426 gene
604348 phenotype
neXtProtiNX_O15055
OpenTargetsiENSG00000132326
Orphaneti164736 Familial advanced sleep-phase syndrome
PharmGKBiPA33185

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3753 Eukaryota
ENOG410Y118 LUCA
GeneTreeiENSGT00940000156342
HOGENOMiHOG000231111
HOVERGENiHBG008167
InParanoidiO15055
KOiK02633
OMAiELACKDQ
OrthoDBiEOG091G00PA
PhylomeDBiO15055
TreeFamiTF318445

Enzyme and pathway databases

ReactomeiR-HSA-400253 Circadian Clock
SIGNORiO15055

Miscellaneous databases

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

More...
ChiTaRSi
PER2 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PER2

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

More...
GenomeRNAii
8864

Protein Ontology

More...
PROi
PR:O15055

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000132326 Expressed in 234 organ(s), highest expression level in oocyte
CleanExiHS_PER2
ExpressionAtlasiO15055 baseline and differential
GenevisibleiO15055 HS

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_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O15055
Secondary accession number(s): A2I2P7
, Q4ZG49, Q6DT41, Q9UQ45
<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 11, 2001
Last modified: December 5, 2018
This is version 178 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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