Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. Additionally we are shipping RFWD2 Antibodies (79) and RFWD2 Kits (4) and many more products for this protein.
Showing 4 out of 5 products:
Data indicate a coordinated regulation of Arabidopsis proteins SHW1, COP1, and HY5 in seedling development.
The COP1 role in CONSTANS protein degradation during photoperiodic flowering
CSU2 interacts with COP1 via the coiled-coil domain association. CSU2 negatively regulates COP1 E3 ubiquitin ligase (show MUL1 Proteins) activity. [COP1]
propose that light perceived by phytochromes causes a switch in the ubiquitination activity of COP1/SPA2 from ubiquitinating downstream substrates to ubiquitinating SPA2, which subsequently causes a repression of COP1/SPA2 function
CUL4(COP1-SPA) E3 ubiquitin ligase is necessary for the light-induced degradation of PIF1 in Arabidopsis.
genetic analyses with transgenes expressing a genomic pmARI12:ARI12-GFP construct confirm the epistatic interaction between COP1 and ARI12 in growth responses to high fluence rate UV-B.
Interaction of phyB with SPA1 promotes COP1-SPA1 dissociation and photomorphogenic development.
AN3 may act with other proteins that bind to COP1 promoter to promote anthocyanin accumulation and inhibit light-induced root elongation.
Two distinct domains of the UVR8 photoreceptor interact with COP1 to initiate UV-B signaling in Arabidopsis
The Transcriptional Regulator BBX19 Promotes Hypocotyl Growth by Facilitating COP1-Mediated EARLY FLOWERING3 Degradation in Arabidopsis
Study shows that post-translational regulation of the transcription factors ETV1 (show ETV1 Proteins), ETV4 (show ETV4 Proteins), and ETV5 (show ETV5 Proteins) by the ubiquitin ligase (show RNF123 Proteins) COP1 (also called RFWD2) in beta cells is critical for insulin (show INS Proteins) secretion. Mice lacking COP1 in beta cells developed diabetes due to insulin (show INS Proteins) granule docking defects that were fully rescued by genetic deletion of Etv1 (show ETV1 Proteins), Etv4 (show ETV4 Proteins), and Etv5 (show ETV5 Proteins).
These results indicate that COP1 and Trib1 (show TRIB1 Proteins) act as an oncoprotein complex functioning upstream of C/EBPalpha (show CEBPA Proteins), and its ligase activity is crucial for leukemogenesis.
COP1 physically interacted with PTP1B (show PTPN1 Proteins) and suppressed PTP1B (show PTPN1 Proteins) phosphatase activity as well as the association of PTP1B (show PTPN1 Proteins) with IRbeta.
Modulation of fatty acid synthase (show FASN Proteins) degradation by concerted action of p38 MAP kinase (show MAPK14 Proteins), E3 ligase COP1, and SH2-tyrosine phosphatase Shp2 (show PTPN11 Proteins).
the ubiquitin ligase (show RNF123 Proteins) COP1 (also known as RFWD2) is a tumour suppressor that negatively regulates ETV1 (show ETV1 Proteins), ETV4 (show ETV4 Proteins) and ETV5 (show ETV5 Proteins); ETV1 (show ETV1 Proteins), which is mutated in prostate cancer more often, was degraded after being ubiquitinated by COP1
Cop1 is a tumor suppressor that functions, at least in part, by antagonizing c-Jun (show JUN Proteins) oncogenic activity.
Rfwd2 is associated with acute lung injury
description of a pathway in which Tribbles 3 (TRB3 (show TRIB3 Proteins)) stimulates lipolysis by triggering the degradation of acetyl-coenzyme A carboxylase (ACC) in adipose tissue; TRB3 (show TRIB3 Proteins) promoted ACC ubiquitination through an association with the E3 ubiquitin ligase (show MUL1 Proteins) COP1
Disruption of the COP1-mediated proteolysis by ionizing radiation leads to MTA1 (show MTA1 Proteins) stabilization.
COP1 (show CARD16 Proteins) expression was an independent predictor of overall survival.
the present study revealed that COP1 (show CARD16 Proteins) plays an important role in CLL cell proliferation and tumorigenicity, and may be a useful indicator of the chronic lymphocytic leukemia processes.
COP1 (show CARD16 Proteins) directly interacts with p27 (show PAK2 Proteins) through a VP motif on p27 (show PAK2 Proteins) and functions as an E3 ligase of p27 (show PAK2 Proteins) to accelerate the ubiquitin-mediated degradation of p27 (show PAK2 Proteins). COP1 (show CARD16 Proteins)-p27 (show PAK2 Proteins) axis deregulation is involved in tumorigenesis.
COP1 (show CARD16 Proteins) overexpression leads to the cytoplasmic distribution of p27 (show PAK2 Proteins), thereby accelerating p27 (show PAK2 Proteins) degradation.
COP1 (show CARD16 Proteins) negatively regulates ETV1 (show ETV1 Proteins) in patients with triple-negative breast cancer.
TRIB2 (show TRIB2 Proteins) associated-ubiquitin E3 ligases beta-transducin repeat-containing E3 ubiquitin protein ligase (beta-TrCP (show BTRC Proteins)), COP1 (show CARD16 Proteins) and Smad ubiquitination regulatory factor 1 (Smurf1 (show SMURF1 Proteins)) reduced TCF4 (show TCF4 Proteins)/beta-Catenin (show CTNNB1 Proteins) expression, and these effects could be enhanced by TRIB2 (show TRIB2 Proteins).
Phosphorylation of the ETS1 (show ETS1 Proteins) and ETS2 (show ETS2 Proteins) transcriptional oncoproteins at specific serine or threonine residues creates binding sites for the COP1 (show CARD16 Proteins) tumor suppressor protein (show TP53 Proteins).
while the role of COP1 (show CARD16 Proteins) in malignancies is controversial, our current data support that COP1 (show CARD16 Proteins) acts as a tumor suppressor in gastric cancer.
co-expressing COP1 and active GSK3beta blocked in vitro cell growth/migration and in vivo metastasis of invasive breast cancer cells.
COP1 (show CARD16 Proteins) physically interacted with PTP1B (show PTPN1 Proteins) and suppressed PTP1B (show PTPN1 Proteins) phosphatase activity as well as the association of PTP1B (show PTPN1 Proteins) with IRbeta.
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1 (By similarity).
E3 ubiquitin-protein ligase RFWD2
, RING finger and WD repeat domain protein 2
, constitutive photomorphogenesis protein 1 homolog
, constitutive photomorphogenic protein 1
, ring finger and WD repeat domain 2-like 1
, ring finger and WD repeat domain 2
, RING finger protein 200
, constitutive photomorphogenic protein (COP1)
, putative ubiquitin ligase COP1