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Protein

DNA repair protein RAD51 homolog 1

Gene

RAD51

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments. 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 XRCC3.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1348ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: MGI
  • damaged DNA binding Source: InterPro
  • DNA polymerase binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded DNA-dependent ATPase activity Source: UniProtKB

GO - Biological processi

  • cellular response to camptothecin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • DNA recombinase assembly Source: Reactome
  • DNA recombination Source: UniProtKB
  • DNA repair Source: Reactome
  • DNA unwinding involved in DNA replication Source: UniProtKB
  • double-strand break repair Source: Reactome
  • double-strand break repair via homologous recombination Source: UniProtKB
  • meiotic nuclear division Source: UniProtKB
  • mitotic recombination Source: ProtInc
  • positive regulation of DNA ligation Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • reciprocal meiotic recombination Source: ProtInc
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_27271. Meiotic recombination.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
SignaLinkiQ06609.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD51 homolog 1
Short name:
HsRAD51
Short name:
hRAD51
Alternative name(s):
RAD51 homolog A
Gene namesi
Name:RAD51
Synonyms:RAD51A, RECA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9817. RAD51.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: UniProtKB
  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • lateral element Source: Ensembl
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Breast cancer (BC)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.

See also OMIM:114480
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501R → Q in BC; familial. 1 Publication
Corresponds to variant rs121917739 [ dbSNP | Ensembl ].
VAR_010899
Mirror movements 2 (MRMV2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.

See also OMIM:614508

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861F → A: Loss of homooligomerization. 1 Publication
Mutagenesisi89 – 891A → E: Loss of homooligomerization. 1 Publication
Mutagenesisi309 – 3091T → A: Confers hypersensitivity to hydroxyurea. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi114480. phenotype.
614508. phenotype.
Orphaneti238722. Familial congenital mirror movements.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA34176.

Polymorphism and mutation databases

BioMutaiRAD51.
DMDMi548663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 339338DNA repair protein RAD51 homolog 1PRO_0000122932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei54 – 541Phosphotyrosine; by ABL11 Publication
Modified residuei309 – 3091Phosphothreonine; by CHEK11 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ06609.
PaxDbiQ06609.
PRIDEiQ06609.

PTM databases

PhosphoSiteiQ06609.

Miscellaneous databases

PMAP-CutDBQ06609.

Expressioni

Tissue specificityi

Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.

Inductioni

Stress-induced increase in the mitochondrial levels is seen.1 Publication

Gene expression databases

BgeeiQ06609.
CleanExiHS_RAD51.
ExpressionAtlasiQ06609. baseline and differential.
GenevisibleiQ06609. HS.

Organism-specific databases

HPAiCAB010381.
HPA039310.

Interactioni

Subunit structurei

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 (PubMed:25642963).23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-297202,EBI-297202
BRCA2P5158736EBI-297202,EBI-79792
CHEK1O147573EBI-297202,EBI-974488
FAM84BQ96KN14EBI-297202,EBI-9057780
IL24Q130072EBI-297202,EBI-3915542
NAT2P112454EBI-297202,EBI-9057228
PALB2Q86YC25EBI-297202,EBI-1222653
RAD51AP1Q96B01-24EBI-297202,EBI-1178743
RAD51AP1Q96B01-35EBI-297202,EBI-1178748
RAD51CO435026EBI-297202,EBI-2267048
RAD52P433513EBI-297202,EBI-706448
SWSAP1Q6NVH72EBI-297202,EBI-5281637
TP53P046372EBI-297202,EBI-366083
WHSC1L1Q9BZ954EBI-297202,EBI-3390132
XRCC3O435423EBI-297202,EBI-2849976

Protein-protein interaction databases

BioGridi111825. 66 interactions.
DIPiDIP-462N.
IntActiQ06609. 54 interactions.
MINTiMINT-1374477.
STRINGi9606.ENSP00000372088.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 306Combined sources
Helixi35 – 428Combined sources
Helixi49 – 513Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 615Combined sources
Turni62 – 654Combined sources
Helixi70 – 8112Combined sources
Helixi107 – 1126Combined sources
Turni113 – 1153Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1266Combined sources
Helixi133 – 14311Combined sources
Helixi148 – 1503Combined sources
Beta strandi154 – 16411Combined sources
Helixi168 – 17710Combined sources
Helixi182 – 1876Combined sources
Beta strandi189 – 1935Combined sources
Helixi197 – 21317Combined sources
Beta strandi216 – 2227Combined sources
Helixi226 – 2283Combined sources
Helixi238 – 25922Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi323 – 3308Combined sources
Beta strandi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
ProteinModelPortaliQ06609.
SMRiQ06609. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 7730HhHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 25774Interaction with PALB2Add
BLAST

Domaini

The nuclear localization may reside in the C-terminus (between 259 and 339 AA).

Sequence similaritiesi

Belongs to the RecA family. RAD51 subfamily.Curated
Contains 1 HhH domain.Curated

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
PhylomeDBiQ06609.
TreeFamiTF101218.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06609-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE
60 70 80 90 100
AVAYAPKKEL INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII
110 120 130 140 150
QITTGSKELD KLLQGGIETG SITEMFGEFR TGKTQICHTL AVTCQLPIDR
160 170 180 190 200
GGGEGKAMYI DTEGTFRPER LLAVAERYGL SGSDVLDNVA YARAFNTDHQ
210 220 230 240 250
TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA RQMHLARFLR
260 270 280 290 300
MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
310 320 330
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
Length:339
Mass (Da):36,966
Last modified:June 1, 1994 - v1
Checksum:i26578E6206DEDEDA
GO
Isoform 2 (identifier: Q06609-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-173: Missing.

Note: No experimental confirmation available.
Show »
Length:242
Mass (Da):26,351
Checksum:iDFA9E12DC8429CA2
GO
Isoform 3 (identifier: Q06609-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-284: FGVAVVITNQVVAQVDGAAMFAADPK → IVSEERKRGNQNLQNLRLSLSS
     285-339: Missing.

Note: Mutagenesis of Arg-264 to Ala inhibits nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear localization. Deletion of 254-Arg-Lys-255 inhibits nuclear localization.
Show »
Length:280
Mass (Da):31,001
Checksum:i1DFA22F6C0926FC2
GO
Isoform 4 (identifier: Q06609-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-114: AEAAKLVPMG...GSKELDKLLQ → TESRSVARLE...ASASRVVGTT

Note: No experimental confirmation available.
Show »
Length:340
Mass (Da):36,780
Checksum:iD8E2AAD35400FB04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131K → Q in BAA02962 (PubMed:8358431).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501R → Q in BC; familial. 1 Publication
Corresponds to variant rs121917739 [ dbSNP | Ensembl ].
VAR_010899

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei76 – 11439AEAAK…DKLLQ → TESRSVARLECNSVILVYCT LRLSGSSDSPASASRVVGTT in isoform 4. 1 PublicationVSP_043655Add
BLAST
Alternative sequencei77 – 17397Missing in isoform 2. 1 PublicationVSP_005556Add
BLAST
Alternative sequencei259 – 28426FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3. 1 PublicationVSP_041724Add
BLAST
Alternative sequencei285 – 33955Missing in isoform 3. 1 PublicationVSP_041725Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13804 mRNA. Translation: BAA02962.1.
D14134 mRNA. Translation: BAA03189.1.
AF165094
, AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA. Translation: AAD49705.1.
AF233744
, AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA. Translation: AAF69145.1.
EU362635 mRNA. Translation: ABY59731.1.
AY196785 Genomic DNA. Translation: AAN87149.1.
AK131299 mRNA. Translation: BAD18467.1.
AK291969 mRNA. Translation: BAF84658.1.
AK313503 mRNA. Translation: BAG36283.1.
CR536559 mRNA. Translation: CAG38796.1.
AC012476 Genomic DNA. No translation available.
AC022405 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92434.1.
CH471125 Genomic DNA. Translation: EAW92432.1.
CH471125 Genomic DNA. Translation: EAW92435.1.
BC001459 mRNA. Translation: AAH01459.1.
CCDSiCCDS10062.1. [Q06609-1]
CCDS53931.1. [Q06609-4]
CCDS53932.1. [Q06609-3]
PIRiI58295.
RefSeqiNP_001157741.1. NM_001164269.1. [Q06609-4]
NP_001157742.1. NM_001164270.1. [Q06609-3]
NP_002866.2. NM_002875.4. [Q06609-1]
NP_597994.3. NM_133487.3. [Q06609-4]
XP_006720689.1. XM_006720626.2. [Q06609-1]
UniGeneiHs.631709.

Genome annotation databases

EnsembliENST00000267868; ENSP00000267868; ENSG00000051180. [Q06609-1]
ENST00000382643; ENSP00000372088; ENSG00000051180. [Q06609-4]
ENST00000423169; ENSP00000406602; ENSG00000051180. [Q06609-3]
ENST00000532743; ENSP00000433924; ENSG00000051180. [Q06609-4]
ENST00000557850; ENSP00000454176; ENSG00000051180. [Q06609-2]
GeneIDi5888.
KEGGihsa:5888.
UCSCiuc001zmi.4. human. [Q06609-1]
uc001zml.4. human. [Q06609-4]
uc010bbw.3. human. [Q06609-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13804 mRNA. Translation: BAA02962.1.
D14134 mRNA. Translation: BAA03189.1.
AF165094
, AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA. Translation: AAD49705.1.
AF233744
, AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA. Translation: AAF69145.1.
EU362635 mRNA. Translation: ABY59731.1.
AY196785 Genomic DNA. Translation: AAN87149.1.
AK131299 mRNA. Translation: BAD18467.1.
AK291969 mRNA. Translation: BAF84658.1.
AK313503 mRNA. Translation: BAG36283.1.
CR536559 mRNA. Translation: CAG38796.1.
AC012476 Genomic DNA. No translation available.
AC022405 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92434.1.
CH471125 Genomic DNA. Translation: EAW92432.1.
CH471125 Genomic DNA. Translation: EAW92435.1.
BC001459 mRNA. Translation: AAH01459.1.
CCDSiCCDS10062.1. [Q06609-1]
CCDS53931.1. [Q06609-4]
CCDS53932.1. [Q06609-3]
PIRiI58295.
RefSeqiNP_001157741.1. NM_001164269.1. [Q06609-4]
NP_001157742.1. NM_001164270.1. [Q06609-3]
NP_002866.2. NM_002875.4. [Q06609-1]
NP_597994.3. NM_133487.3. [Q06609-4]
XP_006720689.1. XM_006720626.2. [Q06609-1]
UniGeneiHs.631709.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
ProteinModelPortaliQ06609.
SMRiQ06609. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111825. 66 interactions.
DIPiDIP-462N.
IntActiQ06609. 54 interactions.
MINTiMINT-1374477.
STRINGi9606.ENSP00000372088.

Chemistry

BindingDBiQ06609.
ChEMBLiCHEMBL2034807.

PTM databases

PhosphoSiteiQ06609.

Polymorphism and mutation databases

BioMutaiRAD51.
DMDMi548663.

Proteomic databases

MaxQBiQ06609.
PaxDbiQ06609.
PRIDEiQ06609.

Protocols and materials databases

DNASUi5888.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267868; ENSP00000267868; ENSG00000051180. [Q06609-1]
ENST00000382643; ENSP00000372088; ENSG00000051180. [Q06609-4]
ENST00000423169; ENSP00000406602; ENSG00000051180. [Q06609-3]
ENST00000532743; ENSP00000433924; ENSG00000051180. [Q06609-4]
ENST00000557850; ENSP00000454176; ENSG00000051180. [Q06609-2]
GeneIDi5888.
KEGGihsa:5888.
UCSCiuc001zmi.4. human. [Q06609-1]
uc001zml.4. human. [Q06609-4]
uc010bbw.3. human. [Q06609-3]

Organism-specific databases

CTDi5888.
GeneCardsiGC15P040987.
HGNCiHGNC:9817. RAD51.
HPAiCAB010381.
HPA039310.
MIMi114480. phenotype.
179617. gene.
614508. phenotype.
neXtProtiNX_Q06609.
Orphaneti238722. Familial congenital mirror movements.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA34176.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
PhylomeDBiQ06609.
TreeFamiTF101218.

Enzyme and pathway databases

ReactomeiREACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_27271. Meiotic recombination.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
SignaLinkiQ06609.

Miscellaneous databases

ChiTaRSiRAD51. human.
EvolutionaryTraceiQ06609.
GeneWikiiRAD51.
GenomeRNAii5888.
NextBioi22896.
PMAP-CutDBQ06609.
PROiQ06609.
SOURCEiSearch...

Gene expression databases

BgeeiQ06609.
CleanExiHS_RAD51.
ExpressionAtlasiQ06609. baseline and differential.
GenevisibleiQ06609. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA."
    Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.
    Nat. Genet. 4:239-243(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and sequence of the human RecA-like gene cDNA."
    Yoshimura Y., Morita T., Yamamoto A., Matsushiro A.
    Nucleic Acids Res. 21:1665-1665(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "Characterization of the human Rad51 genomic locus and examination of tumors with 15q14-15 loss of heterozygosity (LOH)."
    Schmutte C., Tombline G., Rhiem K., Sadoff M.M., Schmutzler R., von Deimling A., Fishel R.
    Cancer Res. 59:4564-4569(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers."
    Wang W.W., Spurdle A.B., Kolachana P., Bove B., Modan B., Ebbers S.M., Suthers G., Tucker M.A., Kaufman D.J., Doody M.M., Tarone R.E., Daly M., Levavi H., Pierce H., Chetrit A., Yechezkel G.H., Chenevix-Trench G., Offit K., Godwin A.K., Struewing J.P.
    Cancer Epidemiol. Biomarkers Prev. 10:955-960(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Identification of a novel human Rad51 variant that promotes DNA strand exchange."
    Park J.Y., Yoo H.W., Kim B.R., Park R., Choi S.Y., Kim Y.
    Nucleic Acids Res. 36:3226-3234(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION OF ISOFORMS 1 AND 3, TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MUTAGENESIS (ISOFORM 3).
  6. NIEHS SNPs program
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Brain.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  12. "Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA."
    Benson F.E., Stasiak A., West S.C.
    EMBO J. 13:5764-5771(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  13. "Interaction of human recombination proteins Rad51 and Rad54."
    Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M.
    Nucleic Acids Res. 25:4106-4110(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD54L.
  14. "A novel nucleic acid-binding protein that interacts with human rad51 recombinase."
    Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.
    Nucleic Acids Res. 25:4946-4953(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD51AP1.
  15. "RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein."
    Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H., Copeland N.G., Jenkins N.A., Lalande M., Alt F.W.
    Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD51AP1, SUBCELLULAR LOCATION.
  16. Cited for: INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-54.
  17. "A novel human Rad54 homologue, Rad54B, associates with Rad51."
    Tanaka K., Hiramoto T., Fukuda T., Miyagawa K.
    J. Biol. Chem. 275:26316-26321(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD54B.
  18. "Homologous DNA pairing by human recombination factors Rad51 and Rad54."
    Sigurdsson S., Van Komen S., Petukhova G., Sung P.
    J. Biol. Chem. 277:42790-42794(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells."
    Liu N., Schild D., Thelen M.P., Thompson L.H.
    Nucleic Acids Res. 30:1009-1015(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XRCC3.
  20. "Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro."
    Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.
    J. Biol. Chem. 278:2469-2478(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD51B AND RAD51C.
  21. "Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51."
    Bennett B.T., Knight K.L.
    J. Cell. Biochem. 96:1095-1109(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  22. "The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair."
    Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C., Bartek J., Helleday T.
    Nat. Cell Biol. 7:195-201(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-309, MUTAGENESIS OF THR-309.
  23. "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51."
    Kovalenko O.V., Wiese C., Schild D.
    Nucleic Acids Res. 34:5081-5092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD51AP2.
  24. Cited for: INTERACTION WITH NABP2.
  25. "Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C."
    Gildemeister O.S., Sage J.M., Knight K.L.
    J. Biol. Chem. 284:31945-31952(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  26. "Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity."
    Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R., Shevelev I., Stark J.M., Sung P., Janscak P.
    J. Biol. Chem. 285:15739-15745(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RECQL5, FUNCTION.
  27. "Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome."
    Sage J.M., Gildemeister O.S., Knight K.L.
    J. Biol. Chem. 285:18984-18990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  28. "Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex."
    Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.
    Mol. Cell 39:333-345(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA1.
  29. "RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
    Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
    Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RECQL5, FUNCTION.
  30. "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination."
    Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.
    Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA2, SUBCELLULAR LOCATION.
  31. "Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination."
    Buisson R., Dion-Cote A.M., Coulombe Y., Launay H., Cai H., Stasiak A.Z., Stasiak A., Xia B., Masson J.Y.
    Nat. Struct. Mol. Biol. 17:1247-1254(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PALB2.
  32. "Homologous recombination proteins are associated with centrosomes and are required for mitotic stability."
    Cappelli E., Townsend S., Griffin C., Thacker J.
    Exp. Cell Res. 317:1203-1213(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  33. "The role of human SWI5-MEI5 complex in homologous recombination repair."
    Yuan J., Chen J.
    J. Biol. Chem. 286:9888-9893(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SWI5 AND SFR1.
  34. "hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair."
    Liu T., Wan L., Wu Y., Chen J., Huang J.
    J. Biol. Chem. 286:41758-41766(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SWSAP1.
  35. Cited for: INVOLVEMENT IN MRMV2.
  36. "Inhibition of homologous recombination by the PCNA-interacting protein PARI."
    Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., Boulton S.J., D'Andrea A.D.
    Mol. Cell 45:75-86(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARPBP.
  37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  38. "Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair."
    Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H., Meetei A.R., Andreassen P.R.
    Oncogene 33:4803-4812(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PALB2, IDENTIFICATION IN A PALB2-CONTAINING HR COMPLEX.
  39. "FIGNL1-containing protein complex is required for efficient homologous recombination repair."
    Yuan J., Chen J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FIGNL1; RAD51AP1 AND SWI5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  40. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
    Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH BLM AND SPIDR, INTERACTION WITH SPIDR, SUBCELLULAR LOCATION.
  41. Cited for: INTERACTION WITH POLQ.
  42. "The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR."
    Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T.
    J. Mol. Biol. 290:495-504(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-114.
  43. "Insights into DNA recombination from the structure of a RAD51-BRCA2 complex."
    Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L., Venkitaraman A.R.
    Nature 420:287-293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 97-339 IN COMPLEX WITH BRCA2, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-86 AND ALA-89, SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.
  44. Cited for: VARIANT BC GLN-150.

Entry informationi

Entry nameiRAD51_HUMAN
AccessioniPrimary (citable) accession number: Q06609
Secondary accession number(s): B0FXP0
, B2R8T6, Q6FHX9, Q6ZNA8, Q9BV60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.