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HUMAN:RAD51

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) RAD51 (synonyms: RAD51A, RECA)
Protein Name(s) DNA repair protein RAD51 homolog 1

HsRAD51 hRAD51 RAD51 homolog A

External Links
UniProt Q06609
EMBL D13804
D14134
AF165094
AF165088
AF165089
AF165090
AF165091
AF165092
AF165093
AF233744
AF233740
AF233741
AF233742
AF236021
AF233743
EU362635
AY196785
AK131299
AK291969
AK313503
CR536559
AC012476
AC022405
CH471125
CH471125
CH471125
BC001459
CCDS CCDS10062.1
CCDS53931.1
CCDS53932.1
PIR I58295
RefSeq NP_001157741.1
NP_001157742.1
NP_002866.2
NP_597994.3
XP_006720689.1
UniGene Hs.631709
PDB 1B22
1N0W
PDBsum 1B22
1N0W
ProteinModelPortal Q06609
SMR Q06609
BioGrid 111825
DIP DIP-462N
IntAct Q06609
MINT MINT-1374477
STRING 9606.ENSP00000267868
BindingDB Q06609
ChEMBL CHEMBL2034807
PhosphoSite Q06609
DMDM 548663
MaxQB Q06609
PaxDb Q06609
PRIDE Q06609
DNASU 5888
Ensembl ENST00000267868
ENST00000382643
ENST00000423169
ENST00000532743
ENST00000557850
GeneID 5888
KEGG hsa:5888
UCSC uc001zmi.4
uc001zml.4
uc010bbw.3
CTD 5888
GeneCards GC15P040987
HGNC HGNC:9817
HPA CAB010381
HPA039310
MIM 114480
179617
614508
neXtProt NX_Q06609
Orphanet 238722
145
PharmGKB PA34176
eggNOG COG0468
GeneTree ENSGT00770000120539
HOGENOM HOG000227426
HOVERGEN HBG001504
InParanoid Q06609
KO K04482
OMA CQLPIDQ
PhylomeDB Q06609
TreeFam TF101218
Reactome REACT_2141
REACT_27271
REACT_408
SignaLink Q06609
ChiTaRS RAD51
EvolutionaryTrace Q06609
GeneWiki RAD51
GenomeRNAi 5888
NextBio 22896
PMAP-CutDB Q06609
PRO PR:Q06609
Proteomes UP000005640
Bgee Q06609
CleanEx HS_RAD51
ExpressionAtlas Q06609
Genevestigator Q06609
GO GO:0000793
GO:0000794
GO:0005737
GO:0000800
GO:0005815
GO:0005759
GO:0005739
GO:0000228
GO:0005730
GO:0005654
GO:0005634
GO:0048471
GO:0016605
GO:0005524
GO:0003684
GO:0070182
GO:0003690
GO:0042802
GO:0008022
GO:0003697
GO:0043142
GO:0006200
GO:0072757
GO:0006974
GO:0071479
GO:0000730
GO:0006310
GO:0006281
GO:0006268
GO:0006302
GO:0000724
GO:0007126
GO:0006312
GO:0051106
GO:0051260
GO:0007131
GO:0010569
Gene3D 3.40.50.300
InterPro IPR003593
IPR011941
IPR013632
IPR016467
IPR010995
IPR003583
IPR027417
IPR020588
IPR020587
Pfam PF08423
PIRSF PIRSF005856
SMART SM00382
SM00278
SUPFAM SSF47794
SSF52540
TIGRFAMs TIGR02239
PROSITE PS50162
PS50163

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0003682

chromatin binding

PMID:23401855[1]

ECO:0000314

direct assay evidence used in manual assertion

F

happens_during:(GO:0006974)

Seeded From UniProt

complete

enables

GO:0019899

enzyme binding

PMID:23401855[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9NXL9

F

Seeded From UniProt

complete

enables

GO:0019899

enzyme binding

PMID:23401855[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9UJA3

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000730

DNA recombinase assembly

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0043142

single-stranded DNA-dependent ATPase activity

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003690

double-stranded DNA binding

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

PMID:26681308[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:26681308[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:26681308[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000790

nuclear chromatin

PMID:26323318[3]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0006974)

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:26323318[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:16990250[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0036297

interstrand cross-link repair

PMID:26253028[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:25585578[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:25585578[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000785

chromatin

PMID:25585578[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:25585578[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031297

replication fork processing

PMID:25585578[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010833

telomere maintenance via telomere lengthening

PMID:21076401[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

P

Seeded From UniProt

complete

involved_in

GO:0000722

telomere maintenance via recombination

PMID:21076401[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

P

causally_upstream_of:(GO:0016233)

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:22778135[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031297

replication fork processing

PMID:22778135[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

PMID:21076401[7]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0000084)

Seeded From UniProt

complete

enables

GO:0070182

DNA polymerase binding

PMID:19995904[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q7Z5Q5

F

Seeded From UniProt

complete

involved_in

GO:0072757

cellular response to camptothecin

PMID:23509288[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071479

cellular response to ionizing radiation

PMID:23509288[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071479

cellular response to ionizing radiation

PMID:23754376[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051260

protein homooligomerization

PMID:12442171[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

P

Seeded From UniProt

complete

involved_in

GO:0051106

positive regulation of DNA ligation

PMID:8929543[13]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:16215984[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0043142

single-stranded DNA-dependent ATPase activity

PMID:7988572[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043142

single-stranded DNA-dependent ATPase activity

PMID:8929543[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016605

PML body

PMID:11309417[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0010569

regulation of double-strand break repair via homologous recombination

PMID:23754376[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008022

protein C-terminus binding

PMID:17515903[17]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P51587

F

Seeded From UniProt

complete

involved_in

GO:0051321

meiotic cell cycle

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

P

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:23509288[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006268

DNA unwinding involved in DNA replication

PMID:7988572[15]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:20413593[18]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:16215984[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:18417535[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:16215984[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:12442171[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

C

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

PMID:7988572[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003690

double-stranded DNA binding

PMID:7988572[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000794

condensed nuclear chromosome

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

C

Seeded From UniProt

complete

part_of

GO:0000793

condensed chromosome

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08297

C

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:23509288[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0000228

nuclear chromosome

PMID:23754376[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0070192

chromosome organization involved in meiotic cell cycle

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97890
PANTHER:PTN000534635

P

Seeded From UniProt

complete

involved_in

GO:0042148

strand invasion

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC644.14c
PomBase:SPAC8E11.03c
SGD:S000000897

P

Seeded From UniProt

complete

enables

GO:0008094

DNA-dependent ATPase activity

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC8E11.03c
SGD:S000000897
UniProtKB:Q8IIS8
WB:WBGene00004297

F

Seeded From UniProt

complete

involved_in

GO:0007131

reciprocal meiotic recombination

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000534635
SGD:S000000897

P

Seeded From UniProt

complete

involved_in

GO:0006312

mitotic recombination

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC644.14c
UniProtKB:C8VSQ3

P

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97890
PANTHER:PTN001415033
PomBase:SPAC644.14c
PomBase:SPAC8E11.03c
SGD:S000000897
SGD:S000000981
UniProtKB:A0A1D8PFE4
UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0003690

double-stranded DNA binding

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC644.14c
PomBase:SPAC8E11.03c
SGD:S000000981
UniProtKB:A0A1D8PFE4
UniProtKB:Q06609
WB:WBGene00004297

F

Seeded From UniProt

complete

part_of

GO:0000794

condensed nuclear chromosome

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97890
PANTHER:PTN000534635
SGD:S000000897
WB:WBGene00004297

C

Seeded From UniProt

complete

involved_in

GO:0000730

DNA recombinase assembly

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC20H4.07
SGD:S000002411
UniProtKB:Q06609

P

Seeded From UniProt

complete

enables

GO:0000150

recombinase activity

PMID:21873635[20]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001415033
PomBase:SPAC644.14c
PomBase:SPAC8E11.03c
SGD:S000000897
SGD:S000000981
UniProtKB:Q8IIS8
WB:WBGene00004297

F

Seeded From UniProt

complete

part_of

GO:0035861

site of double-strand break

PMID:24550317[21]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:16428451[22]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000800

lateral element

PMID:9774970[23]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:16428451[22]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9660962[24]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9469824[25]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9396801[26]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25282148[27]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19628690[28]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19622740[29]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:12442171[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005730

nucleolus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0000150

recombinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010995

F

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020587
InterPro:IPR020588
InterPro:IPR033925

F

Seeded From UniProt

complete

enables

GO:0003690

double-stranded DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941

F

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020587
InterPro:IPR020588

F

Seeded From UniProt

complete

involved_in

GO:0006259

DNA metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020587

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020588

P

Seeded From UniProt

complete

enables

GO:0008094

DNA-dependent ATPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941
InterPro:IPR020587
InterPro:IPR020588

F

Seeded From UniProt

complete

involved_in

GO:1990426

mitotic recombination-dependent replication fork processing

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011941

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17515904[30]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609-1

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17515903[17]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06609-1

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:18417535[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0007131

reciprocal meiotic recombination

PMID:8358431[31]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006312

mitotic recombination

PMID:8358431[31]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

PMID:8358431[31]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006310

DNA recombination

PMID:7988572[15]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:12427746[32]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-5686483
Reactome:R-HSA-5686469
Reactome:R-HSA-5686440
Reactome:R-HSA-5686410
Reactome:R-HSA-5685838
Reactome:R-HSA-5685341
Reactome:R-HSA-5685230
Reactome:R-HSA-9007582
Reactome:R-HSA-5693620
Reactome:R-HSA-5693593
Reactome:R-HSA-5693589
Reactome:R-HSA-5693584
Reactome:R-HSA-5693564
Reactome:R-HSA-5693561
Reactome:R-HSA-5693539
Reactome:R-HSA-5686657
Reactome:R-HSA-5686642

ECO:0000304

author statement supported by traceable reference used in manual assertion

















C

Seeded From UniProt

complete

involved_in

GO:0070317

negative regulation of G0 to G1 transition

Reactome:R-HSA-8953750

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0227

P

Seeded From UniProt

complete

involved_in

GO:0006310

DNA recombination

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0233

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0234

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005694

chromosome

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0158
UniProtKB-SubCell:SL-0468

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005815

microtubule organizing center

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0048

C

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0198

C

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0170

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

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  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Ameziane, N et al. (2015) A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51. Nat Commun 6 8829 PubMed GONUTS page
  3. 3.0 3.1 Parplys, AC et al. (2015) NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability. Nucleic Acids Res. 43 9817-34 PubMed GONUTS page
  4. Kovalenko, OV et al. (2006) RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51. Nucleic Acids Res. 34 5081-92 PubMed GONUTS page
  5. Wang, AT et al. (2015) A Dominant Mutation in Human RAD51 Reveals Its Function in DNA Interstrand Crosslink Repair Independent of Homologous Recombination. Mol. Cell 59 478-90 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 Chu, WK et al. (2015) FBH1 influences DNA replication fork stability and homologous recombination through ubiquitylation of RAD51. Nat Commun 6 5931 PubMed GONUTS page
  7. 7.0 7.1 7.2 Badie, S et al. (2010) BRCA2 acts as a RAD51 loader to facilitate telomere replication and capping. Nat. Struct. Mol. Biol. 17 1461-9 PubMed GONUTS page
  8. 8.0 8.1 Kim, TM et al. (2012) RAD51 mutants cause replication defects and chromosomal instability. Mol. Cell. Biol. 32 3663-80 PubMed GONUTS page
  9. Moldovan, GL et al. (2010) DNA polymerase POLN participates in cross-link repair and homologous recombination. Mol. Cell. Biol. 30 1088-96 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 Wan, L et al. (2013) Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc. Natl. Acad. Sci. U.S.A. 110 10646-51 PubMed GONUTS page
  11. 11.0 11.1 11.2 Yuan, J & Chen, J (2013) FIGNL1-containing protein complex is required for efficient homologous recombination repair. Proc. Natl. Acad. Sci. U.S.A. 110 10640-5 PubMed GONUTS page
  12. 12.0 12.1 12.2 Pellegrini, L et al. (2002) Insights into DNA recombination from the structure of a RAD51-BRCA2 complex. Nature 420 287-93 PubMed GONUTS page
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  14. 14.0 14.1 14.2 Bennett, BT & Knight, KL (2005) Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51. J. Cell. Biochem. 96 1095-109 PubMed GONUTS page
  15. 15.0 15.1 15.2 15.3 15.4 Benson, FE et al. (1994) Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 13 5764-71 PubMed GONUTS page
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  17. 17.0 17.1 Davies, OR & Pellegrini, L (2007) Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats. Nat. Struct. Mol. Biol. 14 475-83 PubMed GONUTS page
  18. Sage, JM et al. (2010) Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome. J. Biol. Chem. 285 18984-90 PubMed GONUTS page
  19. 19.0 19.1 Park, JY et al. (2008) Identification of a novel human Rad51 variant that promotes DNA strand exchange. Nucleic Acids Res. 36 3226-34 PubMed GONUTS page
  20. 20.0 20.1 20.2 20.3 20.4 20.5 20.6 20.7 20.8 20.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  21. Khoury-Haddad, H et al. (2014) PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair. Proc. Natl. Acad. Sci. U.S.A. 111 E728-37 PubMed GONUTS page
  22. 22.0 22.1 Wesoly, J et al. (2006) Differential contributions of mammalian Rad54 paralogs to recombination, DNA damage repair, and meiosis. Mol. Cell. Biol. 26 976-89 PubMed GONUTS page
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  24. Liu, N et al. (1998) XRCC2 and XRCC3, new human Rad51-family members, promote chromosome stability and protect against DNA cross-links and other damages. Mol. Cell 1 783-93 PubMed GONUTS page
  25. Dosanjh, MK et al. (1998) Isolation and characterization of RAD51C, a new human member of the RAD51 family of related genes. Nucleic Acids Res. 26 1179-84 PubMed GONUTS page
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