P70099 · RAD51_CRIGR
- ProteinDNA repair protein RAD51 homolog 1
- GeneRAD51
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids339 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
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.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameDNA repair protein RAD51 homolog 1
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionP70099
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Recruited at sites of DNA damage following interaction with TOPBP1 in S-phase. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000122931 | 2-339 | DNA repair protein RAD51 homolog 1 | |||
Sequence: AMQMQLEANADTSVEEESFGPQPISRLEQCGISANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFTADPKKPIGGNIIAHASTTRLYLRKGRGETRICKVYDSPCLPEAEAMFAINADGVGDAKD | ||||||
Modified residue | 13 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 14 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 54 | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | ||||||
Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 64 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 309 | Phosphothreonine; by CHEK1 | ||||
Sequence: T |
Post-translational modification
Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA. Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination.
Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. Phosphorylated at Ser-14 by PLK1, triggering phosphorylation at Thr-13 by CK2, thereby promoting interaction with TOPBP1 and recruitment to DNA damage sites during S-phase. Phosphorylation by ABL1 inhibits function.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Component of the homologous recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal region); the interaction is direct. Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Interacts with POLQ; POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends. Interacts with FBH1. Interacts with POLN. Interacts with RFWD3. Interacts with the MCM8-MCM9 complex; the interaction recruits RAD51 to DNA damage sites (By similarity).
Component of a multiprotein complex with MEIOB and SPATA22. Interacts with the complex BRME1:HSF2BP:BRCA2 (By similarity).
Interacts with HELQ; stimulating HELQ DNA helicase activity and ability to unwing DNA. Interacts with MMS22L; the interaction is direct and promotes recruitment of RAD51 to sites of DNA damage. Interacts with the ATAD5 RFC-like complex. Within the ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the interaction is direct and enhanced under replication stress. Interacts with WDR48; the interaction is enhanced under replication stress (By similarity).
Interacts with DNA helicase ZGRF1; the interaction promotes RAD51 strand exchange activity (By similarity).
Interacts (when phosphorylated) with TOPBP1; interaction takes place following phosphorylation by CK2 and PLK1 and promotes recruitment to DNA damage sites (By similarity).
Interacts with GRB2; this interaction inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (By similarity).
Component of a multiprotein complex with MEIOB and SPATA22. Interacts with the complex BRME1:HSF2BP:BRCA2 (By similarity).
Interacts with HELQ; stimulating HELQ DNA helicase activity and ability to unwing DNA. Interacts with MMS22L; the interaction is direct and promotes recruitment of RAD51 to sites of DNA damage. Interacts with the ATAD5 RFC-like complex. Within the ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the interaction is direct and enhanced under replication stress. Interacts with WDR48; the interaction is enhanced under replication stress (By similarity).
Interacts with DNA helicase ZGRF1; the interaction promotes RAD51 strand exchange activity (By similarity).
Interacts (when phosphorylated) with TOPBP1; interaction takes place following phosphorylation by CK2 and PLK1 and promotes recruitment to DNA damage sites (By similarity).
Interacts with GRB2; this interaction inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (By similarity).
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 48-77 | HhH | ||||
Sequence: TVEAVAYAPKKELINIKGISEAKADKILAE | ||||||
Region | 184-257 | Interaction with PALB2 | ||||
Sequence: DVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLAD | ||||||
Motif | 245-260 | Nuclear export signal; masked by the interaction with BRCA2 | ||||
Sequence: LARFLRMLLRLADEFG |
Sequence similarities
Belongs to the RecA family. RAD51 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,941
- Last updated1997-02-01 v1
- ChecksumDAD453F1A026A010
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y08202 EMBL· GenBank· DDBJ | CAA69384.1 EMBL· GenBank· DDBJ | mRNA |