Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping.
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
The role of COP1 in repression of Arabidopsis photomorphogenic development.
A novel motif mediates the targeting of the Arabidopsis COP1 protein to subnuclear foci.
The RING finger motif of photomorphogenic repressor COP1 specifically interacts with the RING-H2 motif of a novel Arabidopsis protein.
Targeted destabilization of HY5 during light-regulated development of Arabidopsis.
HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain.
Modular domain structure of Arabidopsis COP1. Reconstitution of activity by fragment complementation and mutational analysis of a nuclear localization signal in planta.
Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1.
The phytochrome A-specific signaling intermediate SPA1 interacts directly with COP1, a constitutive repressor of light signaling in Arabidopsis.
Direct interaction of Arabidopsis cryptochromes with COP1 in light control development.
The signaling mechanism of Arabidopsis CRY1 involves direct interaction with COP1.
Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis.
Two interacting bZIP proteins are direct targets of COP1-mediated control of light-dependent gene expression in Arabidopsis.
Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8).
LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated by SPA1.
The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the light.
The COP1-SPA1 interaction defines a critical step in phytochrome A-mediated regulation of HY5 activity.
Light regulates COP1-mediated degradation of HFR1, a transcription factor essential for light signaling in Arabidopsis.
HFR1 is targeted by COP1 E3 ligase for post-translational proteolysis during phytochrome A signaling.
From The Cover: A role for Arabidopsis cryptochromes and COP1 in the regulation of stomatal opening.
Arabidopsis CONSTANS-LIKE3 is a positive regulator of red light signaling and root growth.
CONSTITUTIVELY PHOTOMORPHOGENIC1 is required for the UV-B response in Arabidopsis.
Arabidopsis CULLIN4 Forms an E3 Ubiquitin Ligase with RBX1 and the CDD Complex in Mediating Light Control of Development.
HY5 is a point of convergence between cryptochrome and cytokinin signalling pathways in Arabidopsis thaliana.
Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues.
Independent and interdependent functions of LAF1 and HFR1 in phytochrome A signaling.
Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases.
COP1-mediated ubiquitination of CONSTANS is implicated in cryptochrome regulation of flowering in Arabidopsis.
Arabidopsis COP1 shapes the temporal pattern of CO accumulation conferring a photoperiodic flowering response.
CRY1 inhibits COP1-mediated degradation of BIT1, a MYB transcription factor, to activate blue light-dependent gene expression in Arabidopsis.
The Arabidopsis COP9 signalosome is essential for G2 phase progression and genomic stability.
Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin ligase with DDB1 and CUL4 that is involved in multiple plant developmental processes.
Biochemical characterization of Arabidopsis complexes containing CONSTITUTIVELY PHOTOMORPHOGENIC1 and SUPPRESSOR OF PHYA proteins in light control of plant development.
COP1 and ELF3 control circadian function and photoperiodic flowering by regulating GI stability.
Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis.
Arabidopsis CULLIN4-damaged DNA binding protein 1 interacts with CONSTITUTIVELY PHOTOMORPHOGENIC1-SUPPRESSOR OF PHYA complexes to regulate photomorphogenesis and flowering time.
Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated viral defense by negatively regulating an E3 ubiquitin ligase.
Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis.
Functional interaction of the circadian clock and UV RESISTANCE LOCUS 8-controlled UV-B signaling pathways in Arabidopsis thaliana.
Evidence for network evolution in an Arabidopsis interactome map.
BZS1, a B-box protein, promotes photomorphogenesis downstream of both brassinosteroid and light signaling pathways.
C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein.
COP1 re-accumulates in the nucleus under shade.
Short Hypocotyl in White Light1 Interacts with Elongated Hypocotyl5 (HY5) and Constitutive Photomorphogenic1 (COP1) and Promotes COP1-Mediated Degradation of HY5 during Arabidopsis Seedling Development.
DHU1 negatively regulates UV-B signaling via its direct interaction with COP1 and RUP1.
COP1 mediates dark-specific degradation of microtubule-associated protein WDL3 in regulating Arabidopsis hypocotyl elongation.
PHYTOCHROME INTERACTING FACTOR8 Inhibits Phytochrome A-Mediated Far-Red Light Responses in Arabidopsis.
PCH1 and PCHL Directly Interact with PIF1, Promote Its Degradation, and Inhibit Its Transcriptional Function during Photomorphogenesis.
Arabidopsis COP1 protein specifically interacts in vitro with a cytoskeleton-associated protein, CIP1.
Genetic and molecular analysis of an allelic series of cop1 mutants suggests functional roles for the multiple protein domains.
Molecular interaction between COP1 and HY5 defines a regulatory switch for light control of Arabidopsis development.
Role of a COP1 interactive protein in mediating light-regulated gene expression in arabidopsis.
Functional dissection of Arabidopsis COP1 reveals specific roles of its three structural modules in light control of seedling development.
Deep research on COP1 function
Falcon (Edison Scientific) deep research report: Arabidopsis thaliana COP1 (UniProt P43254; At2g32950)
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COP1 is a RING-finger E3 ubiquitin ligase that, via E2-dependent ubiquitin transfer, polyubiquitinates substrates for 26S proteasome-dependent degradation to repress light-induced developmental programs in darkness.
"COP1 is a **RING-finger E3 ubiquitin ligase** that catalyzes E2-dependent ubiquitin transfer to substrates, leading commonly to **polyubiquitination** and **26S proteasome-dependent degradation** as a mechanism to repress light-induced developmental programs in darkness."
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COP1 is the central switch repressing photomorphogenesis by promoting turnover of positive regulators, including the direct substrate HY5.
"COP1 is a “central switch” of global light-responsive gene expression by promoting the turnover of multiple nuclear positive regulators of photomorphogenesis, including the bZIP transcription factor **HY5** (direct COP1 substrate)."
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COP1 acts predominantly in the nucleus in darkness and carries a bipartite NLS plus an N-terminal cytoplasmic localization signal enabling light-regulated nucleocytoplasmic partitioning.
"COP1 functions prominently in the **nucleus** in darkness, where it targets nuclear substrates for ubiquitination. COP1 contains a **bipartite nuclear localization signal (NLS)** and an **N-terminal cytoplasmic localization signal**, enabling **light-regulated nucleocytoplasmic partitioning**."
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Substrate specificity is largely conferred by the WD40 domain, with VP-motif-based recognition used by many substrates and photoreceptors.
"Specificity is largely mediated by the **WD40 domain**, including **VP-motif-based recognition** used by many substrates/photoreceptors."
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COP1 associates with SPA proteins and connects to a CUL4-DDB1-RBX1 scaffold, forming a multimeric E3 ligase module.
"COP1 associates with **SPA proteins** to form COP1/SPA complexes and connects to a **CUL4–DDB1–RBX1** scaffold, creating a multimeric E3 ligase module that supports substrate ubiquitylation in light signaling."
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Nuclear COP1 forms punctate speckles/bodies where interaction partners colocalize.
"Nuclear COP1 can appear in **punctate nuclear speckles/bodies** where interaction partners can colocalize, consistent with subnuclear organization of light signaling."
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COP1 integrates photoreceptor inputs: it interacts with UVR8 in UV-B signaling (supporting HY5 stabilization) and cooperates with phytochromes/SPA to regulate PIF stability.
"UV-B involves COP1 interaction with UVR8 in a pathway that supports HY5 stabilization, and COP1/SPA can cooperate with phytochromes in regulating PIF stability in light signaling."