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STK40 (zeige STK40 Proteine) binds the COP1 (zeige CARD16 Proteine) WD40 domain (zeige DCAF12L2 Proteine) using a VPD/E motif in its C-terminal tail.
In conclusion, miR (zeige MLXIP Proteine)-214 functions as a tumor suppressor by regulating the RFWD2-p53 (zeige TP53 Proteine) cascade, thus delivery of miR (zeige MLXIP Proteine)-214 analogs could be a potential adjunct therapy in breast cancer harboring wild type p53 (zeige TP53 Proteine).
the reduced expression of COP1 (zeige CARD16 Proteine) and the upregulated expression of ETV1 (zeige ETV1 Proteine) in RCC (zeige XRCC1 Proteine) tissue samples, which was associated with a high tumor-node-metastasis stage of RCC (zeige XRCC1 Proteine). Furthermore, the overexpression of COP1 (zeige CARD16 Proteine) in the RCC (zeige XRCC1 Proteine) ACHN (zeige LARP6 Proteine) cells inhibited the migration and invasion of ACHN (zeige LARP6 Proteine) cells, and downregulated ETV1 (zeige ETV1 Proteine) and MMP7 (zeige MMP7 Proteine) expression levels.
COP1 (zeige CARD16 Proteine) expression was an independent predictor of overall survival.
the present study revealed that COP1 (zeige CARD16 Proteine) plays an important role in CLL cell proliferation and tumorigenicity, and may be a useful indicator of the chronic lymphocytic leukemia processes.
COP1 (zeige CARD16 Proteine) directly interacts with p27 (zeige PAK2 Proteine) through a VP motif on p27 (zeige PAK2 Proteine) and functions as an E3 ligase of p27 (zeige PAK2 Proteine) to accelerate the ubiquitin-mediated degradation of p27 (zeige PAK2 Proteine). COP1 (zeige CARD16 Proteine)-p27 (zeige PAK2 Proteine) axis deregulation is involved in tumorigenesis.
COP1 (zeige CARD16 Proteine) overexpression leads to the cytoplasmic distribution of p27 (zeige PAK2 Proteine), thereby accelerating p27 (zeige PAK2 Proteine) degradation.
COP1 (zeige CARD16 Proteine) negatively regulates ETV1 (zeige ETV1 Proteine) in patients with triple-negative breast cancer.
TRIB2 (zeige TRIB2 Proteine) associated-ubiquitin E3 ligases beta-transducin repeat-containing E3 ubiquitin protein ligase (beta-TrCP (zeige BTRC Proteine)), COP1 (zeige CARD16 Proteine) and Smad ubiquitination regulatory factor 1 (Smurf1 (zeige SMURF1 Proteine)) reduced TCF4 (zeige TCF4 Proteine)/beta-Catenin (zeige CTNNB1 Proteine) expression, and these effects could be enhanced by TRIB2 (zeige TRIB2 Proteine).
Phosphorylation of the ETS1 (zeige ETS1 Proteine) and ETS2 (zeige ETS2 Proteine) transcriptional oncoproteins at specific serine or threonine residues creates binding sites for the COP1 (zeige CARD16 Proteine) tumor suppressor protein (zeige TP53 Proteine).
Prenatal inactivation of Rfwd2 gene in the lung epithelium led to a striking halt in branching morphogenesis shortly after secondary branch formation.
Study shows that post-translational regulation of the transcription factors ETV1 (zeige ETV1 Proteine), ETV4 (zeige ETV4 Proteine), and ETV5 (zeige ETV5 Proteine) by the ubiquitin ligase (zeige RNF123 Proteine) COP1 (also called RFWD2) in beta cells is critical for insulin (zeige INS Proteine) secretion. Mice lacking COP1 in beta cells developed diabetes due to insulin (zeige INS Proteine) granule docking defects that were fully rescued by genetic deletion of Etv1 (zeige ETV1 Proteine), Etv4 (zeige ETV4 Proteine), and Etv5 (zeige ETV5 Proteine).
These results indicate that COP1 and Trib1 (zeige TRIB1 Proteine) act as an oncoprotein complex functioning upstream of C/EBPalpha (zeige CEBPA Proteine), and its ligase activity is crucial for leukemogenesis.
COP1 physically interacted with PTP1B (zeige PTPN1 Proteine) and suppressed PTP1B (zeige PTPN1 Proteine) phosphatase activity as well as the association of PTP1B (zeige PTPN1 Proteine) with IRbeta.
Modulation of fatty acid synthase (zeige FASN Proteine) degradation by concerted action of p38 MAP kinase (zeige MAPK14 Proteine), E3 ligase COP1, and SH2-tyrosine phosphatase Shp2 (zeige PTPN11 Proteine).
the ubiquitin ligase (zeige RNF123 Proteine) COP1 (also known as RFWD2) is a tumour suppressor that negatively regulates ETV1 (zeige ETV1 Proteine), ETV4 (zeige ETV4 Proteine) and ETV5 (zeige ETV5 Proteine); ETV1 (zeige ETV1 Proteine), 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 (zeige JUN Proteine) oncogenic activity.
Rfwd2 is associated with acute lung injury
description of a pathway in which Tribbles 3 (TRB3 (zeige TRIB3 Proteine)) stimulates lipolysis by triggering the degradation of acetyl-coenzyme A carboxylase (ACC) in adipose tissue; TRB3 (zeige TRIB3 Proteine) promoted ACC ubiquitination through an association with the E3 ubiquitin ligase (zeige MUL1 Proteine) COP1
Disruption of the COP1-mediated proteolysis by ionizing radiation leads to MTA1 (zeige MTA1 Proteine) stabilization.
Exposure to blue light is required for an in vivo-association of CRY1 (zeige CRY1 Proteine) and CRY2 (zeige CRY2 Proteine) with COP1.
DHU1 negatively regulates UV-B signaling via its direct interaction with COP1 and RUP1 (zeige SCGB1A1 Proteine) (At5g52250).
BBX21 is a pivotal component involved in the COP1-HY5 regulatory hub.
Meanwhile, transcript levels of ABA biosynthesis genes are higher in cip1 (zeige CDKN1A Proteine)-1 than in the wild-type. These results suggested that CIP1 (zeige CDKN1A Proteine) is positively involved in ABA response.
salt stress and ethylene antagonistically regulate nucleocytoplasmic partitioning of COP1.
Our genetic and biochemical studies identify a function for SIZ1 in photomorphogenesis and reveal a novel SUMO-regulated ubiquitin ligase, COP1, in plants.
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 (zeige MUL1 Proteine) 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
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
, RING finger protein 200
, constitutive photomorphogenesis protein 1 homolog
, constitutive photomorphogenic protein (COP1)
, putative ubiquitin ligase COP1
, constitutive photomorphogenic protein 1
, ring finger and WD repeat domain 2
, ring finger and WD repeat domain 2-like 1