Gene Symbol | RAD23B |
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Entrez Gene | 5887 |
Alt Symbol | HHR23B, HR23B, P58 |
Species | Human |
Gene Type | protein-coding |
Description | RAD23 homolog B (S. cerevisiae) |
Other Description | RAD23, yeast homolog of, B|UV excision repair protein RAD23 homolog B|XP-C repair complementing complex 58 kDa|XP-C repair complementing protein|XP-C repair-complementing complex 58 kDa protein |
Swissprots | Q7Z5K8 B3KWK8 G5E9P0 P54727 Q8WUB0 |
Accessions | AAN47194 EAW59016 EAW59017 P54727 AI285544 AI375313 AK125226 BAG54170 AK223479 BAD97199 AK293532 BAG57014 AK297986 BAH12700 AK316189 BAH14560 AL540969 AU125295 AW402384 AY313777 AAP81008 BC015805 BC020973 AAH20973 BE894394 BG678535 BI460482 BQ230600 BQ277025 BQ774932 CA866470 D21090 BAA04652 DC404422 DQ890563 ABM92180 DQ893726 ABM84652 NM_001244713 NP_001231642 NM_001244724 NP_001231653 NM_002874 NP_002865 |
Function | The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn rec |
Subcellular Location | Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S- phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin. |
Top Pathways | Nucleotide excision repair, Protein processing in endoplasmic reticulum |
Human hHR23b full length protein - ab114492 from Abcam
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Human hHR23b protein fragment - ab114493 from Abcam
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RAD23B / HR23B Antibody Blocking Peptide - LS-E3662 from LifeSpan Bioscience
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RAD23B / HR23B Antibody Blocking Peptide - LS-E20523 from LifeSpan Bioscience
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RAD23B / HR23B Antibody Blocking Peptide - LS-E20524 from LifeSpan Bioscience
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Recombinant Human hHR23b Protein - H00005887-P01 from Novus Biologicals
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hHR23b Partial Recombinant Protein - H00005887-Q01 from Novus Biologicals
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hHR23b Peptide - NBP1-96767 from Novus Biologicals
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RAD23B-Antibody-N-term-Blocking-Peptide - BP14862a from Abgent, a WuXi AppTec company
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RAD23B Blocking Peptide - 33R-7736 from Fitzgerald
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RAD23B Blocking Peptide - 33R-7658 from Fitzgerald
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RAD23B Blocking Peptide - abx063176 from Abbexa
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RAD23B - H00005887-P01-10 from Acris Antibodies
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RAD23B - H00005887-P01-25 from Acris Antibodies
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RAD23B - H00005887-Q01-10 from Acris Antibodies
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RAD23B - H00005887-Q01-25 from Acris Antibodies
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RAD23B control peptide - AP09213CP-N from Acris Antibodies
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RAD23B fusion protein - Ag2763 from Proteintech Group
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Recombinant Human RAD23B - RAD23B-27732TH from Creative Biomart
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Recombinant Human RAD23B - RAD23B-29311TH from Creative Biomart
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Recombinant Human RAD23B, GST-tagged - RAD23B-2154H from Creative Biomart
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Recombinant RAD23 Homolog B (RAD23B) - RPP751Hu01 from Uscn Life Science Inc.
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HR23B Peptide - 000-001-391 from Rockland Immunochemicals Inc
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RAD23B Blocking Peptide - CBP1982 from Cohesion Biosciences
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Rad23B (K27) Peptide - BS2424P from Bioworld Technology
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