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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. 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 XRCC3.9 Publications

Regions

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

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
  • identical protein binding Source: IntAct
  • 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: GO_Central
  • 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
  • homologous recombination-dependent replication fork processing Source: InterPro
  • 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
  • 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 etoposide 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

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: Ensembl
  • 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)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

Defects in RAD51 are found in a patient with microcephaly, mental retardation without bone marrow failure and pediatric cancers.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581K → R: Impaired ubiquitination; when associated with R-64. 1 Publication
Mutagenesisi64 – 641K → R: Impaired ubiquitination; when associated with R-58. 1 Publication
Mutagenesisi86 – 861F → A: Loss of homooligomerization. 1 Publication
Mutagenesisi89 – 891A → E: Loss of homooligomerization. 1 Publication
Mutagenesisi208 – 2092SA → LE: Disrupts interaction with BRCA2, no effect on homooligomerization, promotes interaction with XPO1 and cytoplasmic localization. 2 Publications
Mutagenesisi309 – 3091T → A: Confers hypersensitivity to hydroxyurea. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL2034807.

Polymorphism and mutation databases

BioMutaiRAD51.
DMDMi548663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 339338DNA repair protein RAD51 homolog 1PRO_0000122932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei54 – 541Phosphotyrosine; by ABL11 Publication
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki64 – 64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei309 – 3091Phosphothreonine; by CHEK11 Publication

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.
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

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
  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

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

Chemistry

BindingDBiQ06609.

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 26016Nuclear export signal; masked by the interaction with BRCA21 PublicationAdd
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

GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG091G09QY.
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.
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.
[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)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
Natural varianti293 – 2931A → T Probable disease-associated mutation found in a patient with microcephaly, mental retardation without bone marrow failure and pediatric cancers; dominant negative; impaired DNA-binding; impaired DNA-dependent ATPase activity; impaired function in the formation of nucleoprotein filaments; impaired function in the formation of joint molecule; no effect on subcellular location. 1 Publication
VAR_076593

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_006720626.3. [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
EntryMethodResolution (Å)ChainPositionsPDBsum
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
ProteinModelPortaliQ06609.
SMRiQ06609. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ06609.
ChEMBLiCHEMBL2034807.

PTM databases

iPTMnetiQ06609.
PhosphoSiteiQ06609.

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

Phylogenomic databases

GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ06609.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG091G09QY.
PhylomeDBiQ06609.
TreeFamiTF101218.

Enzyme and pathway databases

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

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.
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: September 7, 2016
This is version 186 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.