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Human RAD23B Protein expressed in Wheat germ - ABIN1317279
Chen, Lin, Chow, Lee: Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells. in Proteomics 2011
Data show that nucleotide excision repair factor XPC (show XPC Proteins)-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1 (show PARP1 Proteins)).
RAD23B has a potential role in breast cancer progression and a tumor suppressor role of nuclear RAD23B in breast cancer.
It is unlikely that the RAD23B 249Val/Val polymorphism may contribute to the individual susceptibility to cancer risk.
Results define a regulatory mechanism that involves the interplay between HR23B and HDAC6 (show HDAC6 Proteins) that influences the biological outcome of HDAC (show HDAC3 Proteins) inhibitor treatment.
Polymorphism in RAD23B gene is associated with breast cancer.
HR23B expression was associated with disease stabilization for patients with unresectable hepatocellular carcinoma treated with epigenetic therapy using belinostat, a histone deacetylase (show HDAC1 Proteins) inhibitor.
Single nucleotide polymorphisms of CCND2 (show CCND2 Proteins), RAD23B, GRP78 (show HSPA5 Proteins), CEP164, MDM2 (show MDM2 Proteins), and ALDH2 (show ALDH2 Proteins) genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
PNGase (show NGLY1 Proteins)-PUB serves not only as p97 (show EIF4G2 Proteins)-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
26S proteasomes and p97/VCP (show vcp Proteins) complexes bind to the ubiquitin-like domain of HHR23B.
Gene expression of RAD23B was down-regulated during early apoptosis in human hepatoma cells exposed to Paeoniae Radix extract in vitro.
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC (show XPC Proteins) to DNA damage in living cells in addition to stabilizing XPC (show XPC Proteins). RAD23 proteins rapidly dissociated from XPC (show XPC Proteins) upon binding to damaged DNA.
analysis of mHR23A (show RAD23A Proteins)/B double-mutant cells showed that HR23 proteins function in nucleotide excision repair by governing xeroderma pigmentosum group C protein (show HNRNPC Proteins) stability via partial protection against proteasomal degradation
The crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B is described; the results suggest a co-evolution of ER-associated degradation and DNA repair pathways.
This illustrates that impairment of the ubiquitin-proteasome system (UPS) by expanded glutamine (show GFPT1 Proteins) repeats, including the sequestration of HR23B, is not affecting NER (show NR1H2 Proteins).
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER). This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
UV excision repair protein RAD23 homolog B
, RAD23 homolog B (S. cerevisiae)
, RAD23 homolog B
, RAD23, yeast homolog of, B
, XP-C repair complementing complex 58 kDa
, XP-C repair complementing protein
, XP-C repair-complementing complex 58 kDa protein
, RAD23b homolog