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- Data Summary
Gene Report
Approved Symbol | RAD23B |
---|---|
Symbol Alias | HHR23B, P58, HR23B |
Approved Name | RAD23 homolog B (S. cerevisiae) |
Previous Name | RAD23 (S. cerevisiae) homolog B |
Name Alias | XP-C repair complementing protein, "XP-C repair complementing complex 58 kDa" |
Location | 9q31.2 |
Position | chr9:110045418-110094475, + |
External Links |
HGNC: 9813 Entrez Gene: 5887 Ensembl: ENSG00000119318 UCSC: uc004bde.2 |
No. of Studies | 0 (significant: 0; non-significant: 0; trend: 0) |
Source | Mapped by significant region |
Region Name | Position | No. of Studies (significant/non-significant/trend) |
---|---|---|
9q31.1-33.1 | chr9:102600000-122500000 | 1 (1/0/0) |
GO terms by PBA (with statistical significance of FDR<0.05) (count: 0)
GO terms by database search (count: 17)
ID | Name | No. of Genes in ADHDgene | Brief Description |
---|---|---|---|
hsa03420 | Nucleotide excision repair | 9 | Nucleotide excision repair (NER) is a mechanism to recognize...... Nucleotide excision repair (NER) is a mechanism to recognize and repair bulky DNA damage caused by compounds, environmental carcinogens, and exposure to UV-light. In humans hereditary defects in the NER pathway are linked to at least three diseases: xeroderma pigmentosum (XP), Cockayne syndrome (CS), and trichothiodystrophy (TTD). The repair of damaged DNA involves at least 30 polypeptides within two different sub-pathways of NER known as transcription-coupled repair (TCR-NER) and global genome repair (GGR-NER). TCR refers to the expedited repair of lesions located in the actively transcribed strand of genes by RNA polymerase II (RNAP II). In GGR-NER the first step of damage recognition involves XPC-hHR23B complex together with XPE complex (in prokaryotes, uvrAB complex). The following steps of GGR-NER and TCR-NER are similar. More... |
hsa04141 | Protein processing in endoplasmic reticulum | 26 | The endoplasmic reticulum (ER) is a subcellular organelle wh...... The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis. More... |
Region: chr9:110045418..110094475 View in gBrowse
Copyright: Bioinformatics Lab, Institute of Psychology, Chinese Academy of Sciences Feedback
Last update: Feb 26, 2014