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DNA repair protein RAD51 homolog 1

 RAD51_BOVIN             Reviewed;         339 AA.
Q2KJ94;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 1.
27-SEP-2017, entry version 99.
RecName: Full=DNA repair protein RAD51 homolog 1;
Name=RAD51;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays an important role in homologous strand exchange, a
key step in DNA repair through homologous recombination (HR).
Binds to single and double-stranded DNA and exhibits DNA-dependent
ATPase activity. 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. Binds to
single-stranded DNA in an ATP-dependent manner to form
nucleoprotein filaments which are essential for the homology
search and strand exchange. 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. {ECO:0000250|UniProtKB:Q06609}.
-!- 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. 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 FBXO18/FBH1. Interacts with POLN. Interacts with RFWD3.
{ECO:0000250|UniProtKB:Q06609}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}.
Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear
region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix
{ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q06609}. 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.
{ECO:0000250|UniProtKB:Q06609}.
-!- PTM: Ubiquitinated by the SCF(FBXO18) 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.
{ECO:0000250|UniProtKB:Q06609}.
-!- PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may
enhance association with chromatin at sites of DNA damage and
promote DNA repair by homologous recombination. Phosphorylation by
ABL1 inhibits function. {ECO:0000250|UniProtKB:Q06609}.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
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EMBL; BC105458; AAI05459.1; -; mRNA.
RefSeq; NP_001039644.1; NM_001046179.2.
UniGene; Bt.36197; -.
ProteinModelPortal; Q2KJ94; -.
SMR; Q2KJ94; -.
STRING; 9913.ENSBTAP00000003788; -.
PaxDb; Q2KJ94; -.
PRIDE; Q2KJ94; -.
Ensembl; ENSBTAT00000003788; ENSBTAP00000003788; ENSBTAG00000002918.
GeneID; 514749; -.
KEGG; bta:514749; -.
CTD; 5888; -.
eggNOG; KOG1433; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00890000139508; -.
HOGENOM; HOG000227426; -.
HOVERGEN; HBG001504; -.
InParanoid; Q2KJ94; -.
KO; K04482; -.
OMA; VGHTATF; -.
OrthoDB; EOG091G09QY; -.
TreeFam; TF101218; -.
Reactome; R-BTA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-BTA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-BTA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-BTA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-BTA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-BTA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Proteomes; UP000009136; Chromosome 10.
Bgee; ENSBTAG00000002918; -.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000800; C:lateral element; IEA:Ensembl.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; ISS:UniProtKB.
GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; IEA:Ensembl.
GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:Ensembl.
GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
GO; GO:0051106; P:positive regulation of DNA ligation; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:Ensembl.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011941; DNA_recomb/repair_Rad51.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR020588; RecA_ATP-bd.
InterPro; IPR020587; RecA_monomer-monomer_interface.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF47794; SSF47794; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR02239; recomb_RAD51; 1.
PROSITE; PS50162; RECA_2; 1.
PROSITE; PS50163; RECA_3; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; DNA recombination; DNA repair; DNA-binding;
Isopeptide bond; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q06609}.
CHAIN 2 339 DNA repair protein RAD51 homolog 1.
/FTId=PRO_0000253606.
DOMAIN 48 77 HhH.
NP_BIND 127 134 ATP. {ECO:0000250}.
REGION 184 257 Interaction with PALB2. {ECO:0000250}.
MOTIF 245 260 Nuclear export signal; masked by
interaction with BRCA2.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 54 54 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 309 309 Phosphothreonine; by CHEK1.
{ECO:0000250|UniProtKB:Q06609}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q06609}.
CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q06609}.
SEQUENCE 339 AA; 36982 MW; C676352BDD4EDED9 CRC64;
MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL
INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD


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