Xrcc4 Gene Summary [Rat]
Predicted to enable several functions, including FHA domain binding activity; enzyme binding activity; and identical protein binding activity. Predicted to contribute to 3' overhang single-stranded DNA endodeoxyribonuclease activity. Involved in cellular response to lithium ion. Predicted to be located in chromosome, telomeric region; cytosol; and nucleoplasm. Predicted to be part of DNA ligase IV complex; DNA-dependent protein kinase-DNA ligase 4 complex; and ERCC4-ERCC1 complex. Predicted to be active in cytoplasm; nucleus; and site of double-strand break. Human ortholog(s) of this gene implicated in multiple myeloma; salivary gland adenoid cystic carcinoma; and salivary gland carcinoma. Orthologous to human XRCC4 (X-ray repair cross complementing 4). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Xrcc4 |
| Official Name | X-ray repair cross complementing 4 [Source:RGD Symbol;Acc:1359573] |
| Ensembl ID | ENSRNOG00000029966 |
| Bio databases IDs | |
| Aliases | X-ray repair cross complementing 4 |
| Synonyms | 2310057B22Rik, hXRCC4, LOC100044170, SSMED, X-ray repair complementing defective repair in Chinese hamster cells 4, X-ray repair cross complementing 4 |
| Species | Rat, Rattus norvegicus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Xrcc4 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- DNA-ligase IV Xrcc4-interacting region
- homodimerization domain
- enzyme binding
- DNA double-strand break repair and V(D)J recombination protein XRCC4
- protein domain specific binding
- enzyme
- protein binding
- N-terminal head domain found in the XRCC4 superfamily of proteins
- identical protein binding
- single-stranded DNA specific endodeoxyribonuclease
- DNA binding
Pathways
Biological processes and signaling networks where the Xrcc4 gene in rat plays a role, providing insight into its function and relevance in health or disease.
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- chronic pain
- epithelial neoplasia
- epithelial cancer
- cancer
- lymphomagenesis
- hematologic cancer
- lymphoid cancer
- hematological neoplasia
- lymphatic neoplasia
- liver cancer
regulated by
- staurosporine
- etoposide
- fenofibrate
- PRKDC
- bleomycin
- lactic acid
- RIGI
- 5-azacytidine
- calicheamicin gamma(1)I
- ZNF281
role in cell
- expression in
- cell death
- apoptosis
- proliferation
- differentiation
- survival
- radiosensitivity
- cell division
- function
- class switching
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Nucleus
- interchromatin granule cluster fractions
- nuclear fraction
- soluble fraction
- Cytoplasm
- cytosol
- nucleoplasm
- telomeres
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Xrcc4 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- DNA ligation involved in DNA repair
- cellular response to lithium ion
- response to X-ray
- immunoglobulin V(D)J recombination
- positive regulation of ligase activity
- double-strand break repair via nonhomologous end joining
- double-strand break repair
Cellular Component
Where in the cell the gene product is active
- condensed chromosome
- nucleus
- site of double-strand break
- nonhomologous end joining complex
- DNA-dependent protein kinase-DNA ligase 4 complex
- DNA ligase IV complex
- cytosol
- nucleoplasm
Molecular Function
What the gene product does at the molecular level
- DNA binding
- identical protein binding
- protein binding
- ligase activity
- FHA domain binding