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Entry version 167 (22 Apr 2020)
Sequence version 2 (15 Dec 1998)
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Protein

Cryptochrome-2

Gene

CRY2

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation, and regulates other light responses, including circadian rhythms, tropic growth, stomata opening, guard cell development, root development, bacterial and viral pathogen responses, abiotic stress responses, cell cycles, programmed cell death, apical dominance, fruit and ovule development, seed dormancy, and magnetoreception. Photoexcited cryptochromes interact with signaling partner proteins to alter gene expression at both transcriptional and post-translational levels and, consequently, regulate the corresponding metabolic and developmental programs (PubMed:21841916). Blue-light absorbing flavoprotein that activates reversible flavin photoreduction via an electron transport chain comprising a tryptophan triad (W-321, W-374 and W-397), or via an alternative electron transport that involves small metabolites, including NADPH, NADH, and ATP. The half-life of the activated signaling state is about 16 minutes (PubMed:25428980, PubMed:23398192). Perceives low blue light (LBL) and responds by directly contacting two bHLH transcription factors, PIF4 and PIF5, at chromatin on E-box variant 5'-CA[CT]GTG-3' to promote their activity and stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation and hyponastic growth in low blue light) (PubMed:26724867, PubMed:19558423). In response to blue light, binds to CIB proteins (e.g. BHLH63/CIB1 and BHLH76/CIB5) to activates transcription and floral initiation (PubMed:24130508). Mediates blue light-induced gene expression, floral initiation and hypocotyl elongation through the interaction with SPA1 that prevents formation of SPA1/COP1 complex but stimulates COP1 binding, and thus inhibits COP1-mediated degradation of transcription factors (e.g. CO and HY5) (PubMed:21514160, PubMed:21511872, PubMed:16093319). Promotes flowering time in continuous light (LL) (PubMed:21296763). Involved in shortening the circadian clock period, especially at 27 degrees Celsius, in blue light (BL). Required to maintain clock genes expression rhythm (PubMed:23511208). Triggers nuclear accumulation of ROS in response to blue light illumination (PubMed:26179959). Involved in blue light-dependent stomatal opening, transpiration and inhibition of stem and root growth, probably by regulating abscisic acid (ABA) (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:9482948, PubMed:9565033). Regulates the timing of flowering by promoting the expression of 'FLOWERING LOCUS T' (FT) in vascular bundles. Negatively regulated by 'FLOWERING LOCUS C' (FLC) (PubMed:14605222, PubMed:17259260). General positive regulator of reversible low light-induced chromatin decompaction (PubMed:20935177). Involved in triggering chromatin decondensation during floral transition (PubMed:17470059). Together with phototropins, involved in phototropism regulation by various blue light fluence; blue light attenuates phototropism in high fluence rates (100 µmol.m-2.s-1) but enhances phototropism in low fluence rates (<1.0 µmol.m-2.s-1) (PubMed:12857830). The effect of near-null magnetic field on flowering is altered by changes of blue light cycle and intensity in a CRY1/CRY2-dependent manner (PubMed:26095447). Involved in the strigolactone signaling that regulates hypocotyl growth in response to blue light (PubMed:24126495).1 Publication22 Publications
Confers resistance to turnip crinkle virus (TCV) by preventing COP1-mediated proteasome-mediated degradation of RPP8/HRT, thus promoting its stability in light. Exposure to darkness or blue-light induces degradation of CRY2, and in turn of RPP8/HRT, resulting in susceptibility to TCV.1 Publication

Miscellaneous

Phosphorylation of the C-terminal tail and resulting derepression of NC80 domain may both depend on homodimerization.

Caution

Was originally thought to be a DNA photolyase.1 Publication

<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 describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei232FADBy similarity1
<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 bindingi235Magnesium 1; via carbonyl oxygenBy similarity1
Metal bindingi243Magnesium 1By similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei321Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1
Metal bindingi355Magnesium 1; via tele nitrogenBy similarity1
Binding sitei356FADBy similarity1
Sitei374Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1
Sitei397Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1
Binding sitei406ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi244 – 248FADBy similarity5
Nucleotide bindingi356 – 357ATPBy similarity2
Nucleotide bindingi387 – 389FADBy similarity3

<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

Molecular functionChromatin regulator, Photoreceptor protein, Receptor
Biological processPlant defense, Sensory transduction
LigandATP-binding, Chromophore, FAD, Flavoprotein, Magnesium, Metal-binding, Nucleotide-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:
Cryptochrome-21 Publication
Short name:
Atcry21 Publication
Alternative name(s):
Blue light photoreceptor1 Publication
Protein PHR homolog 11 Publication
Short name:
AtPHH11 Publication
Protein SUPPRESSOR OF elf3 201 Publication
<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:CRY21 Publication
Synonyms:PHH11 Publication, SEL201 Publication
Ordered Locus Names:At1g04400Imported
ORF Names:F19P19.14Imported
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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
  • UP000006548 <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 1

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT1G04400

The Arabidopsis Information Resource

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TAIRi
locus:2018254 AT1G04400

<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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics 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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

The rapid blue light-mediated reversible interaction between CRY2 and BHLH63/CIB1 is used to design an optogenetic control of target proteins or organelles.5 Publications

<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

Plants show increased root elongation in blue light (PubMed:16703358, PubMed:21511872). Reduced attenuating effect of high fluence rates of blue light in the cry1 cry2 double mutant. Slow rate of curvature at low fluence rates of blue light in cry1 cry2 (PubMed:12857830). The double mutant cry1 cry2 exhibits a reduced impact of near-null magnetic field on flowering in lower blue light intensity and short days (PubMed:26095447). Little detectable phenotype on circadian clock in blue light (BL). The double mutant cry1 cry2 is impaired in blue light signaling, resulting in long-period, lower-amplitude oscillations at 12 and 17 degrees Celsius and completely abolishing rhythms at 27 degrees Celsius (PubMed:23511208). Reduced hyponastic growth (differential growth-driven upward leaf movement) in low blue light fluence (PubMed:19558423). The double mutant cry1 cry2 is hyposensitive to the strigolactone analog GR24 (PubMed:24126495). The mutant cry2 exposed to a background of red light show severely impaired stomatal opening responses to blue light. The double mutant cry1 cry2 has reduced stomatal conductance, transpiration, and photosynthesis, particularly under the high irradiance of full sunlight at midday, associated with elevated abscisic acid levels (PubMed:22147516). Mutation sel20 suppresses the inhibitory effect of continuous light (LL) on the hypocotyl elongation of elf3-1. The double mutant elf3 sel20 exhibits a late-flowering phenotype (PubMed:21296763). Impaired chromatin decondensation during the floral transition and in low light conditions (PubMed:20935177). Increased sensitivity to turnip crinkle virus (TCV) and associated with reduced HRT levels and stability, and characterized by hypersensitive response (HR) symptoms (PubMed:20624951).11 Publications

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>Mutagenesisi321W → A or F: Photochemically inactive in vitro. Undergo robust light-dependent photoreduction in an in vivo context via an alternative electron transport involving small molecule activators including ATP, NADH, and NADPH. 2 Publications1
Mutagenesisi331W → A: Decreased light sensitivity. Enhanced photoreduction in the presence of added ATP. 1 Publication1
Mutagenesisi337G → E: Loss of activity. 1 Publication1
Mutagenesisi374W → A: Photochemically inactive in vitro. Undergo robust light-dependent photoreduction in an in vivo context via an alternative electron transport involving small molecule activators including ATP, NADH, and NADPH. Enhanced photoreduction in the presence of added ATP. Constitutive interaction with SPA1 and BHLH63/CIB1. 2 Publications1
Mutagenesisi374W → F: Photochemically inactive in vitro. Undergo robust light-dependent photoreduction in an in vivo context via an alternative electron transport involving small molecule activators including ATP, NADH, and NADPH. Enhanced photoreduction in the presence of added ATP. 2 Publications1
Mutagenesisi376W → A: Decreased light sensitivity. Enhanced photoreduction in the presence of added ATP. 1 Publication1
Mutagenesisi377G → R: Constitutive light response. 1 Publication1
Mutagenesisi387D → A: Impaired FAD-binding leading to impaired blue light-mediated inhibition of hypocotyl elongation and loss of blue light-induced degradation. Disturbed BHLH63/CIB1 and SPA1 interactions. 2 Publications1
Mutagenesisi397W → A: Photochemically inactive in vitro. Undergo robust light-dependent photoreduction in an in vivo context via an alternative electron transport involving small molecule activators including ATP, NADH, and NADPH. 2 Publications1
Mutagenesisi397W → F: Photochemically inactive both in vitro and in vivo. 2 Publications1
Mutagenesisi399Y → A or F: Impaired ATP-mediated enhanced photoreduction and decreased affinity for ATP. 1 Publication1
Mutagenesisi541K → R: Impaired nuclear importation leading to reduced phosphorylation, physiological activities, and degradation in response to blue light. Forms protein bodies (photobodies) in both the nucleus and cytosol in response to blue light. 1 Publication1
Mutagenesisi554 – 555KK → RR: Impaired nuclear importation leading to reduced phosphorylation, physiological activities, and degradation in response to blue light. Forms protein bodies (photobodies) in both the nucleus and cytosol in response to blue light. 1 Publication2
Mutagenesisi570 – 575SSSSSS → AAAAAA: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with A-580, A-582, A-584, A-587, 598-A-A-599 and A-605. 1 Publication6
Mutagenesisi570 – 575SSSSSS → DDDDDD: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with D-580, D-582, D-584, D-587, 598-D-D-599 and D-605. 1 Publication6
Mutagenesisi580S → A: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-582, A-584, A-587, 598-A-A-599 and A-605. 1 Publication1
Mutagenesisi580S → D: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-582, D-584, D-587, 598-D-D-599 and D-605. 1 Publication1
Mutagenesisi582S → A: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-580, A-584, A-587, 598-A-A-599 and A-605. 1 Publication1
Mutagenesisi582S → D: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-580, D-584, D-587, 598-D-D-599 and D-605. 1 Publication1
Mutagenesisi584S → A: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-580, A-582, A-587, 598-A-A-599 and A-605. 1 Publication1
Mutagenesisi584S → D: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-580, D-582, D-587, 598-D-D-599 and D-605. 1 Publication1
Mutagenesisi587S → A: Impaired regulation of hypocotyl growth in blue light. Phosphorylated by CK1 proteins CK1.3 and CK1.4. Reduced phosphorylation by CK1 proteins CK1.3 and CK1.4; when associated with A-603. Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-580, A-582, A-584, 598-A-A-599 and A-605. 2 Publications1
Mutagenesisi587S → D: Constitutive regulation of hypocotyl growth in blue light. Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-580, D-582, D-584, 598-D-D-599 and D-605. 2 Publications1
Mutagenesisi598 – 599SS → AA: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-580, A-582, A-584, A-587 and A-605. 1 Publication2
Mutagenesisi598 – 599SS → DD: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-580, D-582, D-584, D-587 and D-605. 1 Publication2
Mutagenesisi603T → A: Impaired regulation of hypocotyl growth in blue light. Phosphorylated by CK1 proteins CK1.3 and CK1.4. Reduced phosphorylation by CK1 proteins CK1.3 and CK1.4; when associated with A-587. 1 Publication1
Mutagenesisi603T → D: Constitutive regulation of hypocotyl growth in blue light. 1 Publication1
Mutagenesisi605S → A: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-A--A-573, A-580, A-582, A-584, A-587 and 598-A-A-599. 1 Publication1
Mutagenesisi605S → D: Reduced blue light-mediated phosphorylation and impaired blue light-dependent proteolysis and hypocotyl inhibition response; when associated with 570-D--D-573, D-580, D-582, D-584, D-587 and 598-D-D-599. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000851221 – 612Cryptochrome-2Add BLAST612

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 residuei587Phosphoserine; by CK11 Publication1
Modified residuei598Phosphoserine1 Publication1
Modified residuei599Phosphoserine1 Publication1
Modified residuei603Phosphothreonine; by CK11 Publication1
Modified residuei605Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by CK1.3 and CK1.4; in response to blue light. Required for degradation (PubMed:12066190, PubMed:17438275, PubMed:17965271, PubMed:9651577, PubMed:25792146, PubMed:23897926). Adopts an open conformation when phosphorylated upon photoexcitation and thus interacts with signaling partner proteins (PubMed:21841916). Not autophosphorylated, even in complex with FAD cofactor (PubMed:17073458).1 Publication7 Publications
Ubiquitinated; in response to blue light.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

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

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PaxDbi
Q96524

PRoteomics IDEntifications database

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PRIDEi
Q96524

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q96524

<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

Mostly expressed in the shoot meristems and root tips, and, to a lower extent, in the cotyledons, hypocotyls, and roots.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

Daily oscillation of protein abundance in plants grown in short days (SD) but not in long days (LD) (PubMed:12578985). Expression levels display circadian oscillations under constant conditions, with a low amplitude and a late phase, with maximal expression around the end of the light phase. Repressed by light (PubMed:11743105). In response to blue light and darkness, phosphorylated, ubiquitinated, and subsequently degraded (at protein level) in a SPA proteins-dependent manner (PubMed:20624951, PubMed:25792146, PubMed:22739826, PubMed:22311776). Transcripts levels oscillate weakly and proportionally to temperature, but protein levels are stable (PubMed:23511208). Accumulates in response to low blue light (LBL) and in low light (PubMed:26724867, PubMed:20935177).9 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q96524 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96524 AT

<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

Homodimer (PubMed:11089975, PubMed:11509693, PubMed:17438275, PubMed:27846570). Blue-light dependent dimerization (PubMed:27846570).

Interacts with COP1 and PHYB in the nucleus (PubMed:11089975, PubMed:11509693, PubMed:17438275, PubMed:20624951). Binds reversibly to CIBs proteins such as BHLH63/CIB1, BHLH78/CIB2, BHLH74/CIB4 and BHLH76/CIB5 after blue light illumination to stimulate their transcription factor activities (PubMed:18988809, PubMed:22139370, PubMed:24130508, PubMed:24780222).

Interacts with PIF4 and PIF5 in the nucleus in response to low blue light (LBL) (PubMed:26724867). Binds to SPA1 in response to blue light, this interaction prevents SPA1/COP1 complex formation but stimulates interaction with COP1, and thus avoid COP1-dependent degradation of the transcription factors CO and HY5 by the proteasome and promotes hypocotyl elongation and floral initiation (PubMed:21514160, PubMed:22139370, PubMed:21511872, PubMed:22739826). Binding to ATP mediates conformational changes which facilitate flavin binding (PubMed:17073458).

Interacts with BIC1 in both darkness and light (PubMed:27846570).

14 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

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
24764, 11 interactors

Database of interacting proteins

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DIPi
DIP-33589N

Protein interaction database and analysis system

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IntActi
Q96524, 4 interactors

STRING: functional protein association networks

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STRINGi
3702.AT1G04400.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

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SMRi
Q96524

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini5 – 134Photolyase/cryptochrome alpha/betaSequence analysisAdd BLAST130

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>Regioni1 – 485CNT2, binds chromophores to sense blue light and mediate CRY dimerization1 PublicationAdd BLAST485
Regioni486 – 612CCT2/CCE2, mediates blue light signaling1 Publication1 PublicationAdd BLAST127

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>Motifi541 – 555Nuclear localization signalPROSITE-ProRule annotationAdd BLAST15

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 biasi22 – 27Poly-AlaSequence analysis6
Compositional biasi546 – 550Poly-GluSequence analysis5
Compositional biasi566 – 587Ser-richPROSITE-ProRule annotationAdd BLAST22

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

The NC80 domain (486-565) contains a major active site responsible for the signal transduction processes regulating both hypocotyl inhibition and floral promotion. The C-terminal tail (564-612) is not required for physiological activity of the protein.

<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 DNA photolyase class-1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0133 Eukaryota
COG0415 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_010348_5_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96524

KEGG Orthology (KO)

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KOi
K12119

Identification of Orthologs from Complete Genome Data

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OMAi
NTQGWEP

Database of Orthologous Groups

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OrthoDBi
378952at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q96524

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR014134 Cryptochrome_pln
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

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Pfami
View protein in Pfam
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00147 DNAPHOTLYASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR02766 crypt_chrom_pln, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 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.

Q96524-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKMDKKTIVW FRRDLRIEDN PALAAAAHEG SVFPVFIWCP EEEGQFYPGR
60 70 80 90 100
ASRWWMKQSL AHLSQSLKAL GSDLTLIKTH NTISAILDCI RVTGATKVVF
110 120 130 140 150
NHLYDPVSLV RDHTVKEKLV ERGISVQSYN GDLLYEPWEI YCEKGKPFTS
160 170 180 190 200
FNSYWKKCLD MSIESVMLPP PWRLMPITAA AEAIWACSIE ELGLENEAEK
210 220 230 240 250
PSNALLTRAW SPGWSNADKL LNEFIEKQLI DYAKNSKKVV GNSTSLLSPY
260 270 280 290 300
LHFGEISVRH VFQCARMKQI IWARDKNSEG EESADLFLRG IGLREYSRYI
310 320 330 340 350
CFNFPFTHEQ SLLSHLRFFP WDADVDKFKA WRQGRTGYPL VDAGMRELWA
360 370 380 390 400
TGWMHNRIRV IVSSFAVKFL LLPWKWGMKY FWDTLLDADL ECDILGWQYI
410 420 430 440 450
SGSIPDGHEL DRLDNPALQG AKYDPEGEYI RQWLPELARL PTEWIHHPWD
460 470 480 490 500
APLTVLKASG VELGTNYAKP IVDIDTAREL LAKAISRTRE AQIMIGAAPD
510 520 530 540 550
EIVADSFEAL GANTIKEPGL CPSVSSNDQQ VPSAVRYNGS KRVKPEEEEE
560 570 580 590 600
RDMKKSRGFD ERELFSTAES SSSSSVFFVS QSCSLASEGK NLEGIQDSSD
610
QITTSLGKNG CK
Length:612
Mass (Da):69,457
Last modified:December 15, 1998 - 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:i082E311301465904
GO

<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 AAT80593 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80594 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80595 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80596 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80597 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80598 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80599 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80600 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80601 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80602 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80603 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80604 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80605 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80606 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80607 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80608 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80609 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80610 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80611 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80612 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80613 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80614 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80615 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80616 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80617 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80618 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80619 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80620 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80621 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80622 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT80623 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAD94467 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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 conflicti78K → Q in AAB04996 (PubMed:9003312).Curated1
Sequence conflicti78K → Q in AAB04997 (PubMed:9003312).Curated1
Sequence conflicti95A → P in AAB04996 (PubMed:9003312).Curated1
Sequence conflicti95A → P in AAB04997 (PubMed:9003312).Curated1
Sequence conflicti188S → L in AAL16379 (PubMed:11726930).Curated1
Sequence conflicti366A → G in AAB04996 (PubMed:9003312).Curated1
Sequence conflicti534A → V in AAB04996 (PubMed:9003312).Curated1
Sequence conflicti534A → V in AAB04997 (PubMed:9003312).Curated1
Sequence conflicti590K → E in CAA67508 (PubMed:9003312).Curated1
Sequence conflicti612K → Q in CAA67508 (PubMed:9003312).Curated1

Natural variant

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 varianti83I → V in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti127Q → S in strain: cv. Bu-0, cv. Da(1)-12, cv. Di-G, cv. Landsberg erecta, cv. Le-0, cv. Lip-0, cv. Mrk-0, cv. Stw-0 and cv. Ta-0. 1 Publication1
Natural varianti326D → E in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti367V → M in strain: cv. Cvi-0. 1 Publication1
Natural varianti476T → I in strain: cv. Cvi-0. 1 Publication1
Natural varianti482A → G in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti498A → S in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti507F → L in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti511G → E in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti543V → L in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1
Natural varianti611C → Y in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha. 1 Publication1

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
U62549 mRNA Translation: AAB04996.1
U62550 mRNA Translation: AAB04997.1
X99061 Genomic DNA Translation: CAA67508.1
U43397 mRNA Translation: AAD09837.1
AY057440 mRNA Translation: AAL16377.1
AY057441 Genomic DNA Translation: AAL16378.1
AY057442 Genomic DNA Translation: AAL16379.1
EU351967 Genomic DNA Translation: ABY77601.1
EU351968 Genomic DNA Translation: ABY77602.1
EU351969 Genomic DNA Translation: ABY77603.1
EU351970 Genomic DNA Translation: ABY77604.1
EU351971 Genomic DNA Translation: ABY77605.1
EU351972 Genomic DNA Translation: ABY77606.1
EU351973 Genomic DNA Translation: ABY77607.1
EU351974 Genomic DNA Translation: ABY77608.1
EU351975 Genomic DNA Translation: ABY77609.1
EU351976 Genomic DNA Translation: ABY77610.1
EU351977 Genomic DNA Translation: ABY77611.1
EU351978 Genomic DNA Translation: ABY77612.1
EU351979 Genomic DNA Translation: ABY77613.1
EU351980 Genomic DNA Translation: ABY77614.1
EU351981 Genomic DNA Translation: ABY77615.1
EU351982 Genomic DNA Translation: ABY77616.1
EU351983 Genomic DNA Translation: ABY77617.1
EU351984 Genomic DNA Translation: ABY77618.1
EU351985 Genomic DNA Translation: ABY77619.1
EU351986 Genomic DNA Translation: ABY77620.1
EU351987 Genomic DNA Translation: ABY77621.1
EU351988 Genomic DNA Translation: ABY77622.1
EU351989 Genomic DNA Translation: ABY77623.1
EU351990 Genomic DNA Translation: ABY77624.1
EU351991 Genomic DNA Translation: ABY77625.1
EU351993 Genomic DNA Translation: ABY77627.1
EU351992 Genomic DNA Translation: ABY77626.1
EU351994 Genomic DNA Translation: ABY77628.1
EU351995 Genomic DNA Translation: ABY77629.1
EU351996 Genomic DNA Translation: ABY77630.1
EU351997 Genomic DNA Translation: ABY77631.1
EU351998 Genomic DNA Translation: ABY77632.1
AC000104 Genomic DNA Translation: AAB70435.1
CP002684 Genomic DNA Translation: AEE27692.1
CP002684 Genomic DNA Translation: AEE27693.1
BT008576 mRNA Translation: AAP40403.1
BT008648 mRNA Translation: AAP40463.1
AY576241 Genomic DNA Translation: AAT80593.1 Different initiation.
AY576242 Genomic DNA Translation: AAT80594.1 Different initiation.
AY576243 Genomic DNA Translation: AAT80595.1 Different initiation.
AY576244 Genomic DNA Translation: AAT80596.1 Different initiation.
AY576245 Genomic DNA Translation: AAT80597.1 Different initiation.
AY576246 Genomic DNA Translation: AAT80598.1 Different initiation.
AY576247 Genomic DNA Translation: AAT80599.1 Different initiation.
AY576248 Genomic DNA Translation: AAT80600.1 Different initiation.
AY576249 Genomic DNA Translation: AAT80601.1 Different initiation.
AY576250 Genomic DNA Translation: AAT80602.1 Different initiation.
AY576251 Genomic DNA Translation: AAT80603.1 Different initiation.
AY576252 Genomic DNA Translation: AAT80604.1 Different initiation.
AY576253 Genomic DNA Translation: AAT80605.1 Different initiation.
AY576254 Genomic DNA Translation: AAT80606.1 Different initiation.
AY576255 Genomic DNA Translation: AAT80607.1 Different initiation.
AY576256 Genomic DNA Translation: AAT80608.1 Different initiation.
AY576257 Genomic DNA Translation: AAT80609.1 Different initiation.
AY576258 Genomic DNA Translation: AAT80610.1 Different initiation.
AY576259 Genomic DNA Translation: AAT80611.1 Different initiation.
AY576260 Genomic DNA Translation: AAT80612.1 Different initiation.
AY576261 Genomic DNA Translation: AAT80613.1 Different initiation.
AY576262 Genomic DNA Translation: AAT80614.1 Different initiation.
AY576263 Genomic DNA Translation: AAT80615.1 Different initiation.
AY576264 Genomic DNA Translation: AAT80616.1 Different initiation.
AY576265 Genomic DNA Translation: AAT80617.1 Different initiation.
AY576266 Genomic DNA Translation: AAT80618.1 Different initiation.
AY576267 Genomic DNA Translation: AAT80619.1 Different initiation.
AY576268 Genomic DNA Translation: AAT80620.1 Different initiation.
AY576269 Genomic DNA Translation: AAT80621.1 Different initiation.
AY576270 Genomic DNA Translation: AAT80622.1 Different initiation.
AY576271 Genomic DNA Translation: AAT80623.1 Different initiation.
AK220946 mRNA Translation: BAD94467.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
A86176
S71221

NCBI Reference Sequences

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RefSeqi
NP_171935.1, NM_100320.4
NP_849588.1, NM_179257.2

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT1G04400.1; AT1G04400.1; AT1G04400
AT1G04400.2; AT1G04400.2; AT1G04400

Database of genes from NCBI RefSeq genomes

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GeneIDi
839529

Gramene; a comparative resource for plants

More...
Gramenei
AT1G04400.1; AT1G04400.1; AT1G04400
AT1G04400.2; AT1G04400.2; AT1G04400

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G04400

<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
U62549 mRNA Translation: AAB04996.1
U62550 mRNA Translation: AAB04997.1
X99061 Genomic DNA Translation: CAA67508.1
U43397 mRNA Translation: AAD09837.1
AY057440 mRNA Translation: AAL16377.1
AY057441 Genomic DNA Translation: AAL16378.1
AY057442 Genomic DNA Translation: AAL16379.1
EU351967 Genomic DNA Translation: ABY77601.1
EU351968 Genomic DNA Translation: ABY77602.1
EU351969 Genomic DNA Translation: ABY77603.1
EU351970 Genomic DNA Translation: ABY77604.1
EU351971 Genomic DNA Translation: ABY77605.1
EU351972 Genomic DNA Translation: ABY77606.1
EU351973 Genomic DNA Translation: ABY77607.1
EU351974 Genomic DNA Translation: ABY77608.1
EU351975 Genomic DNA Translation: ABY77609.1
EU351976 Genomic DNA Translation: ABY77610.1
EU351977 Genomic DNA Translation: ABY77611.1
EU351978 Genomic DNA Translation: ABY77612.1
EU351979 Genomic DNA Translation: ABY77613.1
EU351980 Genomic DNA Translation: ABY77614.1
EU351981 Genomic DNA Translation: ABY77615.1
EU351982 Genomic DNA Translation: ABY77616.1
EU351983 Genomic DNA Translation: ABY77617.1
EU351984 Genomic DNA Translation: ABY77618.1
EU351985 Genomic DNA Translation: ABY77619.1
EU351986 Genomic DNA Translation: ABY77620.1
EU351987 Genomic DNA Translation: ABY77621.1
EU351988 Genomic DNA Translation: ABY77622.1
EU351989 Genomic DNA Translation: ABY77623.1
EU351990 Genomic DNA Translation: ABY77624.1
EU351991 Genomic DNA Translation: ABY77625.1
EU351993 Genomic DNA Translation: ABY77627.1
EU351992 Genomic DNA Translation: ABY77626.1
EU351994 Genomic DNA Translation: ABY77628.1
EU351995 Genomic DNA Translation: ABY77629.1
EU351996 Genomic DNA Translation: ABY77630.1
EU351997 Genomic DNA Translation: ABY77631.1
EU351998 Genomic DNA Translation: ABY77632.1
AC000104 Genomic DNA Translation: AAB70435.1
CP002684 Genomic DNA Translation: AEE27692.1
CP002684 Genomic DNA Translation: AEE27693.1
BT008576 mRNA Translation: AAP40403.1
BT008648 mRNA Translation: AAP40463.1
AY576241 Genomic DNA Translation: AAT80593.1 Different initiation.
AY576242 Genomic DNA Translation: AAT80594.1 Different initiation.
AY576243 Genomic DNA Translation: AAT80595.1 Different initiation.
AY576244 Genomic DNA Translation: AAT80596.1 Different initiation.
AY576245 Genomic DNA Translation: AAT80597.1 Different initiation.
AY576246 Genomic DNA Translation: AAT80598.1 Different initiation.
AY576247 Genomic DNA Translation: AAT80599.1 Different initiation.
AY576248 Genomic DNA Translation: AAT80600.1 Different initiation.
AY576249 Genomic DNA Translation: AAT80601.1 Different initiation.
AY576250 Genomic DNA Translation: AAT80602.1 Different initiation.
AY576251 Genomic DNA Translation: AAT80603.1 Different initiation.
AY576252 Genomic DNA Translation: AAT80604.1 Different initiation.
AY576253 Genomic DNA Translation: AAT80605.1 Different initiation.
AY576254 Genomic DNA Translation: AAT80606.1 Different initiation.
AY576255 Genomic DNA Translation: AAT80607.1 Different initiation.
AY576256 Genomic DNA Translation: AAT80608.1 Different initiation.
AY576257 Genomic DNA Translation: AAT80609.1 Different initiation.
AY576258 Genomic DNA Translation: AAT80610.1 Different initiation.
AY576259 Genomic DNA Translation: AAT80611.1 Different initiation.
AY576260 Genomic DNA Translation: AAT80612.1 Different initiation.
AY576261 Genomic DNA Translation: AAT80613.1 Different initiation.
AY576262 Genomic DNA Translation: AAT80614.1 Different initiation.
AY576263 Genomic DNA Translation: AAT80615.1 Different initiation.
AY576264 Genomic DNA Translation: AAT80616.1 Different initiation.
AY576265 Genomic DNA Translation: AAT80617.1 Different initiation.
AY576266 Genomic DNA Translation: AAT80618.1 Different initiation.
AY576267 Genomic DNA Translation: AAT80619.1 Different initiation.
AY576268 Genomic DNA Translation: AAT80620.1 Different initiation.
AY576269 Genomic DNA Translation: AAT80621.1 Different initiation.
AY576270 Genomic DNA Translation: AAT80622.1 Different initiation.
AY576271 Genomic DNA Translation: AAT80623.1 Different initiation.
AK220946 mRNA Translation: BAD94467.1 Different initiation.
PIRiA86176
S71221
RefSeqiNP_171935.1, NM_100320.4
NP_849588.1, NM_179257.2

3D structure databases

SMRiQ96524
ModBaseiSearch...

Protein-protein interaction databases

BioGridi24764, 11 interactors
DIPiDIP-33589N
IntActiQ96524, 4 interactors
STRINGi3702.AT1G04400.1

PTM databases

iPTMnetiQ96524

Proteomic databases

PaxDbiQ96524
PRIDEiQ96524

Genome annotation databases

EnsemblPlantsiAT1G04400.1; AT1G04400.1; AT1G04400
AT1G04400.2; AT1G04400.2; AT1G04400
GeneIDi839529
GrameneiAT1G04400.1; AT1G04400.1; AT1G04400
AT1G04400.2; AT1G04400.2; AT1G04400
KEGGiath:AT1G04400

Organism-specific databases

AraportiAT1G04400
TAIRilocus:2018254 AT1G04400

Phylogenomic databases

eggNOGiKOG0133 Eukaryota
COG0415 LUCA
HOGENOMiCLU_010348_5_0_1
InParanoidiQ96524
KOiK12119
OMAiNTQGWEP
OrthoDBi378952at2759
PhylomeDBiQ96524

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q96524

Gene expression databases

ExpressionAtlasiQ96524 baseline and differential
GenevisibleiQ96524 AT

Family and domain databases

Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR014134 Cryptochrome_pln
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit
PRINTSiPR00147 DNAPHOTLYASE
SUPFAMiSSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit
TIGRFAMsiTIGR02766 crypt_chrom_pln, 1 hit
PROSITEiView protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiCRY2_ARATH
<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: Q96524
Secondary accession number(s): B0LQ23
, B0LQ24, B0LQ25, B0LQ29, Q42549, Q42603, Q42604, Q56ZL8, Q696X6, Q696X8, Q696Z7, Q697A2, Q8VWL9, Q8VZY9
<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: December 15, 1998
Last sequence update: December 15, 1998
Last modified: April 22, 2020
This is version 167 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 programPlant Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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