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RAD23 homolog B

hHR23B, HR23B, RAD23B
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. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: XPC, XPA, CAN, XPG, ERCC1
Papers using hHR23B antibodies
Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses
Zhang Jian-Ting et al., In Oncogene, 2005
... Rabbit polyclonal IgGs against XPA, XPC, RPA32, RAD23B, as well as eIF3a siRNA were purchased from Santa Cruz Biotechnology, Inc ...
Papers on hHR23B
Base and Nucleotide Excision Repair of Oxidatively Generated Guanine Lesions in DNA.
Geacintov et al., New York City, United States. In J Biol Chem, Feb 2016
However, normal NER activity appeared when the XPC(-/-) cell extracts were complemented with XPC-RAD23B proteins.
Pediatric targeted therapy: Clinical feasibility of personalized diagnostics in children with relapsed and progressive tumors.
Milde et al., Heidelberg, Germany. In Brain Pathol, Nov 2015
10 markers (HDAC2, HR23B, p-AKT, p-ERK, p-S6, p-EGFR, PDGFR-alpha/beta, p53, and BRAFV600E) were analyzed by immunohistochemistry. Pediatric patients with tumors independent of the histological diagnosis, with relapse or progression after treatment according to standard protocols were included.
Poly(ADP-ribose) Polymerase 1 Modulates Interaction of the Nucleotide Excision Repair Factor XPC-RAD23B with DNA via Poly(ADP-ribosyl)ation.
Lavrik et al., Novosibirsk, Russia. In J Biol Chem, Oct 2015
The XPC-RAD23B complex is one of the key factors of nucleotide excision repair participating in the primary DNA damage recognition.
Functional and mechanistic studies of XPC DNA-repair complex as transcriptional coactivator in embryonic stem cells.
Tjian et al., Cambridge, United States. In Proc Natl Acad Sci U S A, Jun 2015
We recently identified the DNA-repair complex xeroderma pigmentosum C (XPC)-RAD23B-CETN2 as a stem cell coactivator (SCC) required for OCT4/SOX2 transcriptional activation.
A functional screen identifies miRNAs that inhibit DNA repair and sensitize prostate cancer cells to ionizing radiation.
Lupold et al., Baltimore, United States. In Nucleic Acids Res, May 2015
miR-890 directly targeted MAD2L2, as well as WEE1 and XPC, where miR-744-3p directly targeted RAD23B.
Y-box binding protein 1 (YB-1) promotes detection of DNA bulky lesions by XPC-HR23B factor.
Lavrik et al., Novosibirsk, Russia. In Biochemistry (mosc), Feb 2015
One of the major NER components is XPC-HR23B, the key factor during the damage recognition step of repair.
Epigenetic therapy using belinostat for patients with unresectable hepatocellular carcinoma: a multicenter phase I/II study with biomarker and pharmacokinetic analysis of tumors from patients in the Mayo Phase II Consortium and the Cancer Therapeutics Research Group.
Goh et al., Hong Kong, Hong Kong. In J Clin Oncol, 2012
Exploratory analysis was conducted on pretreatment tumor tissues to determine whether HR23B expression is a potential biomarker for response.
NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23.
Kato et al., Okazaki, Japan. In Febs Lett, 2012
PNGase-PUB serves not only as p97-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
Genetic risk of hepatocellular carcinoma in patients with hepatitis C virus: a case control study.
Shimizu et al., Okayama, Japan. In J Gastroenterol Hepatol, 2012
Single nucleotide polymorphisms of CCND2, RAD23B, GRP78, CEP164, MDM2, and ALDH2 genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
eNERgizing pluripotent gene transcription.
Mostoslavsky et al., Boston, United States. In Cell Stem Cell, 2011
(2011) in the most recent issue of Cell demonstrates that the XPC/RAD23B/CETN2 nucleotide excision repair complex additionally functions as a transcriptional coactivator of Oct4/Sox2, critically regulating maintenance and reestablishment of stem cell pluripotency.
XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase.
Tainer et al., Berkeley, United States. In Dna Repair (amst), 2011
NER is initiated by arrested RNA polymerase or damage recognition by XPC-RAD23B with or without DDB1/DDB2.
Open, repair and close again: chromatin dynamics and the response to UV-induced DNA damage.
Zurita et al., Ecatepec, Mexico. In Dna Repair (amst), 2011
The ubiquitinated nucleosome facilitates the recruitment of ATP-dependent chromatin-remodeling factors and the XPC-HR23B-Centrin 2 complex to the target region.
Dynamic two-stage mechanism of versatile DNA damage recognition by xeroderma pigmentosum group C protein.
Naegeli et al., Z├╝rich, Switzerland. In Mutat Res, 2010
It remains to be elucidated how accessory factors like Rad23B, centrin-2 or the UV-damaged DNA-binding complex contribute to this dynamic two-stage quality control process.
Modulation of nucleotide excision repair by mammalian SWI/SNF chromatin-remodeling complex.
Wani et al., Columbus, United States. In J Biol Chem, 2009
BRG1 stimulates the recruitment of XPG and PCNA to successfully culminate the nucleotide excision repair.
Laryngeal cancer risk associated with smoking and alcohol consumption is modified by genetic polymorphisms in ERCC5, ERCC6 and RAD23B but not by polymorphisms in five other nucleotide excision repair genes.
Popanda et al., Heidelberg, Germany. In Int J Cancer, 2009
Genetic polymorphisms in RAD23B is associated with Laryngeal cancer risk associated with smoking and alcohol consumption.
Photoactivated DNA analogs of substrates of the nucleotide excision repair system and their interaction with proteins of NER-competent HeLa cell extract.
Lavrik et al., Novosibirsk, Russia. In Biochemistry (mosc), 2009
XPC subunit interaction with DNA is stimulated by endogenous HR23B.
The ubiquitin receptor Rad23: at the crossroads of nucleotide excision repair and proteasomal degradation.
Hoogstraten et al., Stockholm, Sweden. In Dna Repair (amst), 2009
A protein that exemplifies the intimate link between the ubiquitin/proteasome system (UPS) and DNA repair is the yeast nucleotide excision repair (NER) protein Rad23 and its human orthologs hHR23A and hHR23B.
Genome-wide loss-of-function screen reveals an important role for the proteasome in HDAC inhibitor-induced apoptosis.
La Thangue et al., Oxford, United Kingdom. In Cancer Cell, 2009
A genome-wide loss-of-function screen identified HR23B, which shuttles ubiquitinated cargo proteins to the proteasome, as a sensitivity determinant for HDAC inhibitor-induced apoptosis.
Transcription-coupled nucleotide excision repair in mammalian cells: molecular mechanisms and biological effects.
Mullenders et al., Leiden, Netherlands. In Cell Res, 2008
The emerging picture of TC-NER is complex: repair of transcription-blocking lesions occurs without displacement of the DNA damage-stalled RNAPIIo, and requires at least two essential assembly factors (CSA and CSB), the core NER factors (except for XPC-RAD23B), and TC-NER specific factors.
Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors.
Rando et al., Stanford, United States. In Cell, 2007
Monoubiquitinated Pax3 was shuttled to the intrinsic proteasomal protein S5a by interacting specifically with the ubiquitin-binding protein Rad23B.
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