Protein: DNA repair protein RAD51 homolog 1 (HsRAD51) (hRAD51) (RAD51 homolog A) (Q06609)
Organism: Homo sapiens (Human)
Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:9192668}. Cytoplasm {ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:26681308}. Cytoplasm, perinuclear region. Mitochondrion matrix {ECO:0000269|PubMed:20413593}. Chromosome {ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21276791}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage (PubMed:20154705). DNA damage induces an increase in nuclear levels (PubMed:20154705). Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR-dependent manner (PubMed:23509288). Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner (PubMed:23401855). Recruited at sites of DNA damage following interaction with TOPBP1 in S-phase (PubMed:26811421). Colocalizes with ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner (PubMed:27797818, PubMed:31844045). {ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}.
Interaction partners:
- DNA repair protein RAD52 homolog
- Breast cancer type 2 susceptibility protein
- Partner and localizer of BRCA2
- Cellular tumor antigen p53
- BRCA1-associated RING domain protein 1
- Breast cancer type 1 susceptibility protein
- Transcriptional regulator ATRX
- RecQ-like DNA helicase BLM
- Fanconi anemia group D2 protein
- DNA repair protein XRCC3
Sequence:
MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD