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RAD9-, RAD1-, AND HUS1-INTERACTING NUCLEAR ORPHAN 1; RHNO1

RAD9-, RAD1-, AND HUS1-INTERACTING NUCLEAR ORPHAN 1; RHNO1

Alternative titles; symbolsRHINOCHROMOSOME 12 OPEN READING FRAME 32; C12ORF32HGNC Approved Gene Symbol: RHNO1Cytogenetic location: 12p13.33 Genomic coordinat...

Alternative titles; symbols

  • RHINO
  • CHROMOSOME 12 OPEN READING FRAME 32; C12ORF32

HGNC Approved Gene Symbol: RHNO1

Cytogenetic location: 12p13.33 Genomic coordinates (GRCh38): 12:2,876,264-2,889,523 (from NCBI)

▼ Cloning and Expression

Using expression profiling to identify genes upregulated in mammary carcinogenesis, followed by PCR of breast cancer cells, Kim et al. (2010) cloned C12ORF32. Database analysis revealed a C12ORF32 splice variant lacking exon 2, which contains the start codon in the full-length transcript. This short transcript lacks a long ORF. Northern blot analysis detected robust expression of 1.9- and 1.6-kb C12ORF32 transcripts in breast cancer cells, with much lower expression in normal tissues, predominantly testis, prostate, ovary, thymus, and small intestine. Western blot analysis of breast cancer cell lines revealed a 16-kD C12ORF32 protein instead of the predicted 35-kD full-length protein. This 16-kD protein appeared to be a processed form of full-length C12ORF32 containing only N-terminal amino acids 1 through 144. C12ORF23 protein localized to nuclei of interphase cells and was more diffusely dispersed at mitosis.

Using a small interfering RNA (siRNA) screen to identify components of the DNA damage response in U2OS osteosarcoma cells, Cotta-Ramusino et al. (2011) identified C12ORF32, which they called RHINO. The deduced 238-amino acid protein has a putative N-terminal DNA-binding domain and 3 potential ATM (607585)/ATR (601215) phosphorylation sites.

▼ Gene Function

Kim et al. (2010) found that depletion of C12ORF32 in breast cancer cells via RNA interference suppressed cell growth, possibly due to inhibition of G1/S transition and subsequent cell death.

Cotta-Ramusino et al. (2011) found that RHINO was phosphorylated on thr33 and localized to nuclear foci upon DNA damage in U2OS cells. Knockdown of RHINO via siRNA led to checkpoint bypass and sensitivity to ionizing radiation, mitomycin C, and camptothecin. The extent of RHINO depletion correlated with both checkpoint and homologous recombination defects. Mass spectrometry and Western blot analysis of proteins immunoprecipitated with epitope-tagged RHINO identified RAD9 (RAD9A; 603761), RAD1 (603153), and HUS1 (603760), the 3 subunits of the 9-1-1 complex. The 9-1-1 complex acts as a DNA damage-specific clamp that binds the ATR activator TOPBP1 (607760), the E3 ubiquitin ligase RAD18 (605256), and the E2 conjugating enzyme UBC13 (UBE2N; 603679). Mutation of a 7-amino acid motif within the putative N-terminal DNA-binding domain of RHINO blocked interaction of RHINO with the 9-1-1 complex, but not interaction of RHINO with TOPBP1, and interfered with localization of RHINO to sites of DNA damage. Cotta-Ramusino et al. (2011) concluded that the RHINO/9-1-1/TOPBP1 axis promotes the DNA damage response to lesions occurring during S phase.

▼ Gene Structure

Kim et al. (2010) determined that the C12ORF32 gene contains 3 exons, the first of which is noncoding.

▼ Mapping

Hartz (2011) mapped the RHNO1 gene to chromosome 12p13.33 based on an alignment of the RHNO1 sequence (GenBank BC005106) with the genomic sequence (GRCh37).

Tags: 12p13.33

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