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UBR5 encodes a progestin-induced protein, which belongs to the HECT (homology to E6-AP carboxyl terminus) family. Additionally we are shipping UBR5 Kits (3) and and many more products for this protein.
Showing 10 out of 79 products:
Human Polyclonal UBR5 Primary Antibody for IHC, ELISA - ABIN184976
Henderson, Russell, Hird, Muñoz, Clancy, Lehrbach, Calanni, Jans, Sutherland, Watts: EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response. in The Journal of biological chemistry 2002
Cow (Bovine) Polyclonal UBR5 Primary Antibody for EIA, IHC (p) - ABIN1109445
Hay-Koren, Caspi, Zilberberg, Rosin-Arbesfeld: The EDD E3 ubiquitin ligase ubiquitinates and up-regulates beta-catenin. in Molecular biology of the cell 2011
Study highlights many functional biological role of UBR5 especially in cancer where it seems to be a key regulator of cell signaling. [review]
Colony-formation assays and soft agar assays show that gain of function of TIP60 or depletion of EDD1 in HPV-positive cervical cancer cells significantly inhibits cell growth in vitro
Human herpesvirus-6 U14 induces cell cycle arrest in G2/M phase by associating with a cellular protein, EDD.
Elevated metaphase RanGTP levels use Ubr5 to couple overall chromosome congression to SAC (show ADCY10 Antibodies) silencing.
results confirm the role of the MLLE domain of UBR5 in substrate recruitment and suggest a potential role in regulating UBR5 ligase activity.
these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis.
Utilizing a high throughput RNAi screening approach author identified UBR5, a protein commonly amplified in breast cancer, as a novel regulator of ERalpha (show ESR1 Antibodies) protein levels and transcriptional activity.
the alpha4 N-terminus binding to endogenous PP2Ac (show PPP2CA Antibodies) and PABP (show PABPC1 Antibodies), and the C-terminus to EDD, is reported.
These results identify EDD as a dual regulator of cell survival and cisplatin resistance and suggest that EDD is a therapeutic target for ovarian cancer.
Determined is the three-dimensional solution structure of the catalytic RING2 (show RNF2 Antibodies) domain from HHARI (show ARIH1 Antibodies). It shows glimpses of a HECT E3 ligase.
UBR5-mediated ATMIN (show ATMIN Antibodies) ubiquitination is a vital event for ATM (show ATM Antibodies) pathway selection and activation in response to DNA damage
a novel function of RIP1 (show RALBP1 Antibodies) kinase involving its interaction with EDD to regulate JNK (show MAPK8 Antibodies) activation and TNFalpha (show TNF Antibodies) production.
Silencing Edd1 with shRNA in mouse embryonic stem cells significantly suppressed their growth.
The SCF (show KITLG Antibodies) E3 ligase complex containing Fbxo40 (show FBXO40 Antibodies) directly ubiquitinates IRS1 (show IRS1 Antibodies), and this activity is enhanced by increased tyrosine phosphorylation of IRS1 (show IRS1 Antibodies).
Through the PABC domain, EDD participates in miRNA silencing by recruiting downstream effectors.
UBR5 can attenuate myocardin (show MYOCD Antibodies) protein degradation resulting in increased myocardin (show MYOCD Antibodies) protein expression without affecting myocardin (show MYOCD Antibodies) mRNA expression.
Results suggest that Edd has an essential role in extraembryonic development.
This gene encodes a progestin-induced protein, which belongs to the HECT (homology to E6-AP carboxyl terminus) family. The HECT family proteins function as E3 ubiquitin-protein ligases, targeting specific proteins for ubiquitin-mediated proteolysis. This gene is localized to chromosome 8q22 which is disrupted in a variety of cancers. This gene potentially has a role in regulation of cell proliferation or differentiation.
E3 identified by differential display
, E3 ubiquitin protein ligase, HECT domain containing, 1
, E3 ubiquitin-protein ligase UBR5
, E3 ubiquitin-protein ligase, HECT domain-containing 1
, hyperplastic discs protein homolog
, progestin induced protein
, progestin-induced protein
, ubiquitin-protein ligase
, extraembryonic development