Details for: RNF8

Gene ID: 9025

Gene Type:  Protein-coding  - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.

Symbol: RNF8

Ensembl ID: ENSG00000112130

Description: ring finger protein 8

Selected Context(s):  Overall

Cell Significance Landscape

Contexts:

Associated with

Significant Cells

Cell Significance Index (CSI) scores for the chosen context(s)

  • neural progenitor cell CL0011020
    CSI 7.55
    rCSI 33.2%
    PRS 53.08
  • hematopoietic multipotent progenitor cell CL0000837
    CSI 5.14
    rCSI 12.36%
    PRS 80.56
  • myoepithelial cell CL0000185
    CSI 4
    rCSI 10.12%
    PRS 70.87
  • pancreatic A cell CL0000171
    CSI 3.78
    rCSI 3.96%
    PRS 66.55
  • retina horizontal cell CL0000745
    CSI 3.58
    rCSI 5.46%
    PRS 59.25
  • rod bipolar cell CL0000751
    CSI 3.53
    rCSI 6.35%
    PRS 56.05
  • common myeloid progenitor CL0000049
    CSI 3.45
    rCSI 2.79%
    PRS 64.35
  • pancreatic D cell CL0000173
    CSI 3.39
    rCSI 3.33%
    PRS 65.64
  • duct epithelial cell CL0000068
    CSI 3.29
    rCSI 4.81%
    PRS 67.85
  • T-helper 17 cell CL0000899
    CSI 3.22
    rCSI 2.56%
    PRS 83.79
  • cerebral cortex endothelial cell CL1001602
    CSI 3.16
    rCSI 5.47%
    PRS 52.97
  • pro-B cell CL0000826
    CSI 3.11
    rCSI 2.58%
    PRS 65.19
  • enteric smooth muscle cell CL0002504
    CSI 2.99
    rCSI 4.27%
    PRS 65.13
  • melanocyte CL0000148
    CSI 2.98
    rCSI 2.21%
    PRS 55.4
  • enteroendocrine cell CL0000164
    CSI 2.89
    rCSI 3.95%
    PRS 64.59
  • interneuron CL0000099
    CSI 2.83
    rCSI 5.67%
    PRS 51.92
  • ciliated epithelial cell CL0000067
    CSI 2.68
    rCSI 2.36%
    PRS 50.82
  • early lymphoid progenitor CL0000936
    CSI 2.67
    rCSI 2.35%
    PRS 68.47
  • chondrocyte CL0000138
    CSI 2.51
    rCSI 3.99%
    PRS 55.27
  • interstitial cell of Cajal CL0002088
    CSI 2.48
    rCSI 3.15%
    PRS 69.36
  • bronchus fibroblast of lung CL2000093
    CSI 2.4
    rCSI 1.95%
    PRS 63.42
  • kidney loop of Henle thin descending limb epithelial cell CL1001111
    CSI 2.39
    rCSI 3.38%
    PRS 59.2
  • hematopoietic stem cell CL0000037
    CSI 2.38
    rCSI 1.58%
    PRS 65.98
  • choroid plexus epithelial cell CL0000706
    CSI 2.38
    rCSI 3.9%
    PRS 52.03
  • cerebral cortex GABAergic interneuron CL0010011
    CSI 2.37
    rCSI 6.99%
    PRS 65.94
  • ON-bipolar cell CL0000749
    CSI 2.34
    rCSI 3.48%
    PRS 64.36
  • renal alpha-intercalated cell CL0005011
    CSI 2.33
    rCSI 3.12%
    PRS 71.91
  • neural crest cell CL0011012
    CSI 2.26
    rCSI 1.79%
    PRS 49.76
  • epithelial cell of lung CL0000082
    CSI 2.22
    rCSI 1.84%
    PRS 62.26
  • ionocyte CL0005006
    CSI 2.21
    rCSI 2.37%
    PRS 62.57
  • retinal blood vessel endothelial cell CL0002585
    CSI 2.16
    rCSI 3.45%
    PRS 67.15
  • erythrocyte CL0000232
    CSI 2.09
    rCSI 4.74%
    PRS 66.58
  • vascular leptomeningeal cell CL4023051
    CSI 2.09
    rCSI 3.66%
    PRS 54.76
  • alveolar adventitial fibroblast CL4028006
    CSI 2.08
    rCSI 3.28%
    PRS 65.31
  • progenitor cell CL0011026
    CSI 2.05
    rCSI 4.37%
    PRS 62.11
  • respiratory basal cell CL0002633
    CSI 2.05
    rCSI 2.13%
    PRS 68.71
  • mesodermal cell CL0000222
    CSI 2.04
    rCSI 2.45%
    PRS 61.01
  • hematopoietic precursor cell CL0008001
    CSI 2
    rCSI 2.05%
    PRS 79.25
  • squamous epithelial cell CL0000076
    CSI 1.98
    rCSI 4.7%
    PRS 66.5
  • colon epithelial cell CL0011108
    CSI 1.96
    rCSI 2.06%
    PRS 59.35
  • stem cell CL0000034
    CSI 1.95
    rCSI 1.88%
    PRS 53.62
  • type B pancreatic cell CL0000169
    CSI 1.91
    rCSI 4.22%
    PRS 60.94
  • sst GABAergic cortical interneuron CL4023017
    CSI 1.9
    rCSI 2.45%
    PRS 45.79
  • ependymal cell CL0000065
    CSI 1.88
    rCSI 3.82%
    PRS 42.1
  • VIP GABAergic cortical interneuron CL4023016
    CSI 1.87
    rCSI 2.23%
    PRS 44.23
  • megakaryocyte CL0000556
    CSI 1.85
    rCSI 8.01%
    PRS 74.99
  • fallopian tube secretory epithelial cell CL4030006
    CSI 1.83
    rCSI 1.76%
    PRS 62.86
  • multi-ciliated epithelial cell CL0005012
    CSI 1.79
    rCSI 1.79%
    PRS 56.24
  • astrocyte of the cerebral cortex CL0002605
    CSI 1.74
    rCSI 3.89%
    PRS 45.21
  • neuroblast (sensu Nematoda and Protostomia) CL0000338
    CSI 1.73
    rCSI 2%
    PRS 56.01
  • glioblast CL0000030
    CSI 1.73
    rCSI 2.76%
    PRS 55.4
  • transit amplifying cell of colon CL0009011
    CSI 1.72
    rCSI 2.02%
    PRS 65.18
  • retinal bipolar neuron CL0000748
    CSI 1.72
    rCSI 3.21%
    PRS 51.13
  • colonocyte CL1000347
    CSI 1.7
    rCSI 2.44%
    PRS 66.39
  • neuroblast (sensu Vertebrata) CL0000031
    CSI 1.69
    rCSI 2.17%
    PRS 60.08
  • caudal ganglionic eminence derived cortical interneuron CL4023064
    CSI 1.66
    rCSI 2.93%
    PRS 43.57
  • pvalb GABAergic cortical interneuron CL4023018
    CSI 1.66
    rCSI 2.06%
    PRS 42.6
  • BEST4+ enteroycte CL4030026
    CSI 1.62
    rCSI 2.02%
    PRS 64.65
  • granulocyte monocyte progenitor cell CL0000557
    CSI 1.62
    rCSI 1.4%
    PRS 67.89
  • lung ciliated cell CL1000271
    CSI 1.56
    rCSI 1.81%
    PRS 53.1
  • placental villous trophoblast CL2000060
    CSI 1.5
    rCSI 2.32%
    PRS 61.24
  • kidney loop of Henle thin ascending limb epithelial cell CL1001107
    CSI 1.43
    rCSI 3.69%
    PRS 57.89
  • lamp5 GABAergic cortical interneuron CL4023011
    CSI 1.38
    rCSI 2.32%
    PRS 44.47
  • megakaryocyte-erythroid progenitor cell CL0000050
    CSI 1.27
    rCSI 1.14%
    PRS 59.86
  • near-projecting glutamatergic cortical neuron CL4023012
    CSI 1.2
    rCSI 4.55%
    PRS 45.22
  • melanocyte of skin CL1000458
    CSI 1.19
    rCSI 1.63%
    PRS 33.02
  • sncg GABAergic cortical interneuron CL4023015
    CSI 1.17
    rCSI 1.88%
    PRS 46.49
  • retinal cone cell CL0000573
    CSI 1.16
    rCSI 1.87%
    PRS 52.44
  • helper T cell CL0000912
    CSI 1.15
    rCSI 1.62%
    PRS 67.72
  • forebrain radial glial cell CL0013000
    CSI 1.13
    rCSI 3.64%
    PRS 67.81
  • amacrine cell CL0000561
    CSI 1.09
    rCSI 3.15%
    PRS 52.49
  • basal cell of epidermis CL0002187
    CSI 1.08
    rCSI 1.92%
    PRS 36.97
  • cardiac muscle cell CL0000746
    CSI 1.05
    rCSI 1.51%
    PRS 52.38
  • CD8-positive, alpha-beta memory T cell, CD45RO-positive CL0001203
    CSI 1
    rCSI 1.21%
    PRS 49.54
  • platelet CL0000233
    CSI 0.99
    rCSI 4.11%
    PRS 65.94
  • suprabasal keratinocyte CL4033013
    CSI 0.86
    rCSI 1.4%
    PRS 32.95
  • corticothalamic-projecting glutamatergic cortical neuron CL4023013
    CSI 0.81
    rCSI 4.8%
    PRS 45.7
  • L2/3-6 intratelencephalic projecting glutamatergic neuron CL4023040
    CSI 0.77
    rCSI 1.87%
    PRS 43.04
  • retinal ganglion cell CL0000740
    CSI 0.7
    rCSI 1.55%
    PRS 48.94
  • L6b glutamatergic cortical neuron CL4023038
    CSI 0.66
    rCSI 2.06%
    PRS 46.14
  • ON parasol ganglion cell CL4033052
    CSI 0.62
    rCSI 8.84%
    PRS 53.78
  • L5 extratelencephalic projecting glutamatergic cortical neuron CL4023041
    CSI 0.58
    rCSI 2.09%
    PRS 42.85
  • kidney connecting tubule epithelial cell CL1000768
    CSI 0.5
    rCSI 1.27%
    PRS 52.35
  • central nervous system neuron CL2000029
    CSI 0.36
    rCSI 2.66%
    PRS 49.37
  • effector memory CD8-positive, alpha-beta T cell, terminally differentiated CL0001062
    CSI 0.34
    rCSI 1.69%
    PRS 75.48
  • direct pathway medium spiny neuron CL4023026
    CSI 0.27
    rCSI 6.53%
    PRS 43.52
  • indirect pathway medium spiny neuron CL4023029
    CSI 0.24
    rCSI 5.85%
    PRS 44.35

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

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Legend:
  • Query Gene
  • Node Color (Target Cell CSI, relative to current network):
    • Very High
    • High
    • Medium
    • Low
    • Very Low
    • CSI N/A
  • Node Size: Proportional to Target Cell CSI magnitude
  • STRING PPI Edge
  • Shared Pathway Edge (ONTOLOGY)

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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

## Summary [RNF8](/details-gene/9025) (Ring Finger Protein 8) is a protein-coding gene located on chromosome 6 that encodes a critical E3 ubiquitin ligase. This enzyme is a central player in the cellular DNA damage response (DDR), particularly in the signaling and repair of DNA double-strand breaks ([Link](https://doi.org/10.1126/science.1150034)). By catalyzing the ubiquitination of histones and other proteins at sites of damage, it orchestrates the recruitment of downstream repair factors, thereby maintaining genomic stability. Its expression is particularly significant in highly proliferative cell populations, such as [neural progenitor cells](/details-cell/CL0011020) and [hematopoietic multipotent progenitor cells](/details-cell/CL0000837), underscoring its essential role in safeguarding the genomes of developing and renewing tissues. ## Cellular Roles and Expression Landscape **Overall**, the expression profile of [RNF8](/details-gene/9025) suggests a fundamental role in maintaining genomic integrity across a range of cell types, with a notable emphasis on progenitor and developmentally active lineages. The highest significance of [RNF8](/details-gene/9025) is observed in [neural progenitor cells](/details-cell/CL0011020) (CSI: 7.55) and various hematopoietic progenitors, including [hematopoietic multipotent progenitor cells](/details-cell/CL0000837) (CSI: 5.14), [common myeloid progenitors](/details-cell/CL0000049) (CSI: 3.45), and [pro-B cells](/details-cell/CL0000826) (CSI: 3.11). This pattern is consistent with its crucial function in DNA repair, a process that is highly active in cells undergoing frequent division where the risk of DNA damage is elevated. Furthermore, its significant expression in specialized, terminally differentiated cells such as [pancreatic A cells](/details-cell/CL0000171) and [retina horizontal cells](/details-cell/CL0000745) suggests that its role in DNA damage surveillance and repair is also vital for the long-term maintenance and function of post-mitotic cells. Expression in [myoepithelial cells](/details-cell/CL0000185) and [duct epithelial cells](/details-cell/CL0000068) further points to a broad requirement for [RNF8](/details-gene/9025)-mediated pathways in maintaining tissue homeostasis. ## Pathways and Molecular Function Functionally, [RNF8](/details-gene/9025) is an E3 ubiquitin ligase ([GO:0061630](https://www.ebi.ac.uk/QuickGO/term/GO:0061630)) that acts as a master regulator of the [DNA damage response](/details-go/GO0006974) ([GO:0006974](https://www.ebi.ac.uk/QuickGO/term/GO:0006974)). Its activity is central to multiple repair pathways, including [DNA double-strand break repair](/details-reactome/R-HSA-5693532) ([R-HSA-5693532](https://reactome.org/content/detail/R-HSA-5693532)) via both [homology directed repair](/details-reactome/R-HSA-5693538) ([R-HSA-5693538](https://reactome.org/content/detail/R-HSA-5693538)) and [nonhomologous end-joining](/details-reactome/R-HSA-5693571) ([R-HSA-5693571](https://reactome.org/content/detail/R-HSA-5693571)). Upon detection of a DNA double-strand break, [RNF8](/details-gene/9025) is recruited to the damaged chromatin. There, it catalyzes K63-linked polyubiquitin chains ([GO:0070534](https://www.ebi.ac.uk/QuickGO/term/GO:0070534)) on histone H2A and H2AX, a key step that serves as a docking platform for downstream signaling and repair proteins like 53BP1 and BRCA1 complex components ([Link](https://doi.org/10.1016/j.cell.2007.09.040), [Link](https://doi.org/10.1073/pnas.0710061104)). This function is integral to the [recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks](/details-reactome/R-HSA-5693565) ([R-HSA-5693565](https://reactome.org/content/detail/R-HSA-5693565)). Beyond its core role in DNA repair, [RNF8](/details-gene/9025) is also implicated in broader cellular processes including the regulation of the [cell cycle](/details-reactome/R-HSA-1640170) ([R-HSA-1640170](https://reactome.org/content/detail/R-HSA-1640170)), particularly at [G2/M DNA damage checkpoints](/details-reactome/R-HSA-69473) ([R-HSA-69473](https://reactome.org/content/detail/R-HSA-69473)), and has been shown to regulate mitotic exit ([Link](https://doi.org/10.1038/sj.onc.1210782)). ## Research Directions The central role of [RNF8](/details-gene/9025) in DNA repair and its high expression in progenitor cells suggest critical functions in development, tissue maintenance, and cancer prevention. Future research could investigate several testable hypotheses: 1. Given its high significance in [neural progenitor cells](/details-cell/CL0011020), germline mutations or somatic dysfunction of [RNF8](/details-gene/9025) may contribute to neurodevelopmental disorders by causing an accumulation of DNA damage that impairs progenitor cell proliferation and differentiation. 2. The high expression of [RNF8](/details-gene/9025) in hematopoietic progenitors suggests it is a critical gatekeeper against hematopoietic malignancies. Loss of [RNF8](/details-gene/9025) function in this compartment could lead to genomic instability, predisposing these cells to leukemic transformation. 3. Based on its role in [isotype switching](/details-go/GO0045190) ([GO:0045190](https://www.ebi.ac.uk/QuickGO/term/GO:0045190)), a process involving programmed DNA breaks, [RNF8](/details-gene/9025) may be essential for generating antibody diversity, and its deficiency could result in specific immunodeficiencies. A compelling experimental approach to test the first hypothesis would involve generating a conditional knockout mouse model where [RNF8](/details-gene/9025) is specifically deleted in neural stem cells (e.g., via a Sox2-Cre or Nestin-Cre driver). The resulting animals could be analyzed for defects in brain architecture, increased apoptosis in neurogenic regions, and elevated levels of DNA damage markers (e.g., γH2AX foci) in neural progenitors. Long-term monitoring of these mice would also reveal if loss of [RNF8](/details-gene/9025) increases susceptibility to brain tumors. From a therapeutic perspective, [RNF8](/details-gene/9025) is a promising target for cancer therapy. As its function is essential for repairing DNA damage, its inhibition could sensitize cancer cells to genotoxic agents like chemotherapy and radiation. A small molecule inhibitor targeting the E3 ligase activity of [RNF8](/details-gene/9025) could act as a potent chemo- or radio-sensitizer, particularly in tumors that rely heavily on specific DNA repair pathways. Therefore, inhibition of [RNF8](/details-gene/9025) represents a viable strategy to enhance the efficacy of existing cancer treatments.

Genular Protein ID: 3951299770

Symbol: RNF8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9852682

Title: Isolation, tissue expression, and chromosomal assignment of a novel human gene which encodes a protein with RING finger motif.

PubMed ID: 9852682

DOI: 10.1007/s100380050088

PubMed ID: 16215985

Title: The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation.

PubMed ID: 16215985

DOI: 10.1002/jcb.20587

PubMed ID: 9734811

Title: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.

PubMed ID: 9734811

DOI: 10.1093/dnares/5.3.169

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 14574404

Title: The DNA sequence and analysis of human chromosome 6.

PubMed ID: 14574404

DOI: 10.1038/nature02055

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 23233665

Title: Identification of RNF8 as a ubiquitin ligase involved in targeting the p12 subunit of DNA polymerase delta for degradation in response to DNA damage.

PubMed ID: 23233665

DOI: 10.1074/jbc.m112.423392

PubMed ID: 11322894

Title: N-terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8.

PubMed ID: 11322894

DOI: 10.1046/j.1432-1327.2001.02169.x

PubMed ID: 14981089

Title: The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity.

PubMed ID: 14981089

DOI: 10.1074/jbc.m309148200

PubMed ID: 18001824

Title: RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins.

PubMed ID: 18001824

DOI: 10.1016/j.cell.2007.09.040

PubMed ID: 18077395

Title: Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage.

PubMed ID: 18077395

DOI: 10.1073/pnas.0710061104

PubMed ID: 18006705

Title: Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase.

PubMed ID: 18006705

DOI: 10.1126/science.1150034

PubMed ID: 17724460

Title: Regulation of mitotic exit by the RNF8 ubiquitin ligase.

PubMed ID: 17724460

DOI: 10.1038/sj.onc.1210782

PubMed ID: 18948756

Title: PCNA is ubiquitinated by RNF8.

PubMed ID: 18948756

DOI: 10.4161/cc.7.21.6949

PubMed ID: 18337245

Title: RNF8-dependent and RNF8-independent regulation of 53BP1 in response to DNA damage.

PubMed ID: 18337245

DOI: 10.1074/jbc.m710197200

PubMed ID: 18678647

Title: Noncanonical E2 variant-independent function of UBC13 in promoting checkpoint protein assembly.

PubMed ID: 18678647

DOI: 10.1128/mcb.00987-08

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20023648

Title: HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.

PubMed ID: 20023648

DOI: 10.1038/ncb2008

PubMed ID: 19203578

Title: The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage.

PubMed ID: 19203578

DOI: 10.1016/j.cell.2008.12.042

PubMed ID: 19203579

Title: RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins.

PubMed ID: 19203579

DOI: 10.1016/j.cell.2008.12.041

PubMed ID: 19124460

Title: Accumulation of Pax2 transactivation domain interaction protein (PTIP) at sites of DNA breaks via RNF8-dependent pathway is required for cell survival after DNA damage.

PubMed ID: 19124460

DOI: 10.1074/jbc.m809158200

PubMed ID: 19015238

Title: Histone ubiquitination associates with BRCA1-dependent DNA damage response.

PubMed ID: 19015238

DOI: 10.1128/mcb.01302-08

PubMed ID: 19202061

Title: The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks.

PubMed ID: 19202061

DOI: 10.1073/pnas.0807485106

PubMed ID: 20550933

Title: ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks.

PubMed ID: 20550933

DOI: 10.1016/j.cell.2010.04.038

PubMed ID: 21558560

Title: Critical roles of ring finger protein RNF8 in replication stress responses.

PubMed ID: 21558560

DOI: 10.1074/jbc.m111.232041

PubMed ID: 21857671

Title: DNA-damage response and repair activities at uncapped telomeres depend on RNF8.

PubMed ID: 21857671

DOI: 10.1038/ncb2326

PubMed ID: 22865450

Title: RNF8 regulates assembly of RAD51 at DNA double-strand breaks in the absence of BRCA1 and 53BP1.

PubMed ID: 22865450

DOI: 10.1158/0008-5472.can-12-1057

PubMed ID: 22373579

Title: RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites.

PubMed ID: 22373579

DOI: 10.1038/emboj.2012.47

PubMed ID: 22531782

Title: A new non-catalytic role for ubiquitin ligase RNF8 in unfolding higher-order chromatin structure.

PubMed ID: 22531782

DOI: 10.1038/emboj.2012.104

PubMed ID: 23115235

Title: The RING finger protein RNF8 ubiquitinates Nbs1 to promote DNA double-strand break repair by homologous recombination.

PubMed ID: 23115235

DOI: 10.1074/jbc.m112.421545

PubMed ID: 22405594

Title: Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain.

PubMed ID: 22405594

DOI: 10.1016/j.molcel.2012.02.004

PubMed ID: 22705371

Title: A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network.

PubMed ID: 22705371

DOI: 10.1016/j.molcel.2012.05.026

PubMed ID: 22266820

Title: The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.

PubMed ID: 22266820

DOI: 10.1038/nsmb.2211

PubMed ID: 21911360

Title: Differential regulation of RNF8-mediated Lys48- and Lys63-based poly-ubiquitylation.

PubMed ID: 21911360

DOI: 10.1093/nar/gkr655

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25512560

Title: The scaffold protein WRAP53beta orchestrates the ubiquitin response critical for DNA double-strand break repair.

PubMed ID: 25512560

DOI: 10.1101/gad.246546.114

PubMed ID: 18001825

Title: RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly.

PubMed ID: 18001825

DOI: 10.1016/j.cell.2007.09.041

PubMed ID: 22980979

Title: RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling.

PubMed ID: 22980979

DOI: 10.1016/j.cell.2012.08.005

PubMed ID: 22589545

Title: Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.

PubMed ID: 22589545

DOI: 10.1074/jbc.m112.359653

Sequence Information:

  • Length: 485
  • Mass: 55518
  • Checksum: 54650B2FFC9948B1
  • Sequence:
  • MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGCEVTV GRGFGVTYQL VSKICPLMIS 
    RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI HQGDYIQLGV PLENKENAEY 
    EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL RTKRKFSLDE LAGPGAEGPS NLKSKINKVS 
    CESGQPVKSQ GKGEVASTPS DNLDPKLTAL EPSKTTGAPI YPGFPKVTEV HHEQKASNSS 
    ASQRSLQMFK VTMSRILRLK IQMQEKHEAV MNVKKQTQKG NSKKVVQMEQ ELQDLQSQLC 
    AEQAQQQARV EQLEKTFQEE EQHLQGLEIA QGEKDLKQQL AQALQEHWAL MEELNRSKKD 
    FEAIIQAKNK ELEQTKEEKE KMQAQKEEVL SHMNDVLENE LQCIICSEYF IEAVTLNCAH 
    SFCSYCINEW MKRKIECPIC RKDIKSKTYS LVLDNCINKM VNNLSSEVKE RRIVLIRERK 
    AKRLF