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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

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 (PubMed:26681308). 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 (PubMed:26253028).10 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 134ATPBy similarity8

GO - Molecular functioni

  • ATP binding Source: MGI
  • chromatin binding Source: Ensembl
  • DNA polymerase binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • four-way junction DNA binding Source: GO_Central
  • protein C-terminus binding Source: UniProtKB
  • recombinase activity Source: GO_Central
  • 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 cisplatin Source: Ensembl
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to gamma radiation Source: Ensembl
  • cellular response to hydroxyurea Source: Ensembl
  • cellular response to ionizing radiation Source: UniProtKB
  • chromosome organization involved in meiotic cell cycle Source: GO_Central
  • DNA recombinase assembly Source: UniProtKB
  • DNA recombination Source: UniProtKB
  • DNA repair Source: ProtInc
  • DNA synthesis involved in DNA repair Source: Reactome
  • DNA unwinding involved in DNA replication Source: UniProtKB
  • double-strand break repair via homologous recombination Source: UniProtKB
  • interstrand cross-link repair Source: UniProtKB
  • meiotic nuclear division Source: UniProtKB
  • mitotic recombination Source: ProtInc
  • mitotic recombination-dependent replication fork processing Source: InterPro
  • 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
  • regulation of protein phosphorylation Source: Ensembl
  • replication-born double-strand break repair via sister chromatid exchange Source: Ensembl
  • replication fork processing Source: UniProtKB
  • response to drug Source: Ensembl
  • response to toxic substance Source: Ensembl
  • response to X-ray Source: Ensembl
  • strand displacement Source: Reactome
  • strand invasion Source: GO_Central
  • telomere maintenance via recombination Source: BHF-UCL
  • telomere maintenance via telomere lengthening Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000051180-MONOMER.
ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-912446. Meiotic recombination.
SignaLinkiQ06609.
SIGNORiQ06609.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9817. RAD51.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • condensed chromosome Source: UniProtKB
  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • lateral element Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nuclear chromatin Source: ParkinsonsUK-UCL
  • nuclear chromosome Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • PML body Source: UniProtKB
  • site of double-strand break Source: MGI
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_010899150R → Q in BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP. 2 PublicationsCorresponds to variant rs121917739dbSNPEnsembl.1
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

Defects in RAD51 have been found in patients with a Fanconi anemia-like phenotype. Disease features include growth retardation, microcephaly, mental retardation, radial dysplasia, thumb abnormalities, genital and renal defects, and hypersensitivity to DNA cross-linking agents and DNA damage. Affected individuals, however, do not show bone marrow failure and pediatric malignancies.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58K → R: Impaired ubiquitination; when associated with R-64. 1 Publication1
Mutagenesisi64K → R: Impaired ubiquitination; when associated with R-58. 1 Publication1
Mutagenesisi86F → A: Loss of homooligomerization. 1 Publication1
Mutagenesisi89A → E: Loss of homooligomerization. 1 Publication1
Mutagenesisi208 – 209SA → LE: Disrupts interaction with BRCA2, no effect on homooligomerization, promotes interaction with XPO1 and cytoplasmic localization. 2 Publications2
Mutagenesisi309T → A: Confers hypersensitivity to hydroxyurea. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5888.
MalaCardsiRAD51.
MIMi114480. phenotype.
614508. phenotype.
OpenTargetsiENSG00000051180.
Orphaneti238722. Familial congenital mirror movements.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA34176.

Chemistry databases

ChEMBLiCHEMBL2034807.

Polymorphism and mutation databases

BioMutaiRAD51.
DMDMi548663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001229322 – 339DNA repair protein RAD51 homolog 1Add BLAST338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei54Phosphotyrosine; by ABL11 Publication1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei309Phosphothreonine; by CHEK11 Publication1

Post-translational modificationi

Ubiquitinated by the SCF(FBXO18) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA.1 Publication
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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ06609.
MaxQBiQ06609.
PeptideAtlasiQ06609.
PRIDEiQ06609.

PTM databases

iPTMnetiQ06609.
PhosphoSitePlusiQ06609.

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

BgeeiENSG00000051180.
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). Interacts with FBXO18/FBH1 (PubMed:23393192).25 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

GO - Molecular functioni

  • DNA polymerase binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111825. 131 interactors.
DIPiDIP-462N.
IntActiQ06609. 96 interactors.
MINTiMINT-1374477.

Chemistry databases

BindingDBiQ06609.

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 30Combined sources6
Helixi35 – 42Combined sources8
Helixi49 – 51Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 61Combined sources5
Turni62 – 65Combined sources4
Helixi70 – 81Combined sources12
Helixi107 – 112Combined sources6
Turni113 – 115Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi121 – 126Combined sources6
Helixi133 – 143Combined sources11
Helixi148 – 150Combined sources3
Beta strandi154 – 164Combined sources11
Helixi168 – 177Combined sources10
Helixi182 – 187Combined sources6
Beta strandi189 – 193Combined sources5
Helixi197 – 213Combined sources17
Beta strandi216 – 222Combined sources7
Helixi226 – 228Combined sources3
Helixi238 – 259Combined sources22
Beta strandi262 – 267Combined sources6
Beta strandi298 – 304Combined sources7
Beta strandi309 – 314Combined sources6
Beta strandi323 – 330Combined sources8
Beta strandi333 – 335Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
5JZCelectron microscopy4.20A/B/C/D/E/F/G1-339[»]
ProteinModelPortaliQ06609.
SMRiQ06609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 77HhHAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 257Interaction with PALB2Add BLAST74

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi245 – 260Nuclear export signal; masked by the interaction with BRCA21 PublicationAdd BLAST16

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

GeneTreeiENSGT00860000133731.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG091G09QY.
PhylomeDBiQ06609.
TreeFamiTF101218.

Family and domain databases

CDDicd01123. Rad51_DMC1_radA. 1 hit.
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.
IPR027417. P-loop_NTPase.
IPR033925. Rad51_DMC1_RadA.
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.
[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.1 Publication
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)DescriptionActionsGraphical viewLength
Sequence conflicti313K → Q in BAA02962 (PubMed:8358431).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076870131T → P Probable disease-associated mutation found in a patient with a Fanconi anemia-like phenotype; causes dominant negative loss of function in interstrand cross-link repair; shows high basal DNA-independent ATPase activity; results in decreased DNA binding. 1 Publication1
Natural variantiVAR_010899150R → Q in BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP. 2 PublicationsCorresponds to variant rs121917739dbSNPEnsembl.1
Natural variantiVAR_076593293A → T Probable disease-associated mutation found in a patient with a Fanconi anemia-like phenotype; dominant negative; impaired function in DNA repair via homologous recombination; impaired DNA-binding and formation of nucleoprotein filaments; impaired DNA-dependent ATPase activity; no effect on subcellular location. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04365576 – 114AEAAK…DKLLQ → TESRSVARLECNSVILVYCT LRLSGSSDSPASASRVVGTT in isoform 4. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_00555677 – 173Missing in isoform 2. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_041724259 – 284FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_041725285 – 339Missing in isoform 3. 1 PublicationAdd BLAST55

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_006720626.3. [Q06609-1]
XP_011520159.1. XM_011521857.2. [Q06609-1]
XP_011520160.1. XM_011521858.2. [Q06609-1]
XP_011520161.1. XM_011521859.2. [Q06609-1]
XP_011520162.1. XM_011521860.2. [Q06609-1]
XP_011520163.1. XM_011521861.2. [Q06609-3]
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.5. human. [Q06609-1]

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_006720626.3. [Q06609-1]
XP_011520159.1. XM_011521857.2. [Q06609-1]
XP_011520160.1. XM_011521858.2. [Q06609-1]
XP_011520161.1. XM_011521859.2. [Q06609-1]
XP_011520162.1. XM_011521860.2. [Q06609-1]
XP_011520163.1. XM_011521861.2. [Q06609-3]
UniGeneiHs.631709.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
5JZCelectron microscopy4.20A/B/C/D/E/F/G1-339[»]
ProteinModelPortaliQ06609.
SMRiQ06609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111825. 131 interactors.
DIPiDIP-462N.
IntActiQ06609. 96 interactors.
MINTiMINT-1374477.

Chemistry databases

BindingDBiQ06609.
ChEMBLiCHEMBL2034807.

PTM databases

iPTMnetiQ06609.
PhosphoSitePlusiQ06609.

Polymorphism and mutation databases

BioMutaiRAD51.
DMDMi548663.

Proteomic databases

EPDiQ06609.
MaxQBiQ06609.
PeptideAtlasiQ06609.
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.5. human. [Q06609-1]

Organism-specific databases

CTDi5888.
DisGeNETi5888.
GeneCardsiRAD51.
HGNCiHGNC:9817. RAD51.
HPAiCAB010381.
HPA039310.
MalaCardsiRAD51.
MIMi114480. phenotype.
179617. gene.
614508. phenotype.
neXtProtiNX_Q06609.
OpenTargetsiENSG00000051180.
Orphaneti238722. Familial congenital mirror movements.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA34176.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00860000133731.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG091G09QY.
PhylomeDBiQ06609.
TreeFamiTF101218.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000051180-MONOMER.
ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-912446. Meiotic recombination.
SignaLinkiQ06609.
SIGNORiQ06609.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000051180.
CleanExiHS_RAD51.
ExpressionAtlasiQ06609. baseline and differential.
GenevisibleiQ06609. HS.

Family and domain databases

CDDicd01123. Rad51_DMC1_radA. 1 hit.
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.
IPR027417. P-loop_NTPase.
IPR033925. Rad51_DMC1_RadA.
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.
[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...

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: November 30, 2016
This is version 189 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

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 one 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.