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YEAST:RAD51

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) RAD51
Protein Name(s) DNA repair protein RAD51
External Links
UniProt P25454
EMBL X64270
M88470
D10023
U18839
BK006939
PIR A44348
RefSeq NP_011021.3
PDB 1SZP
3LDA
PDBsum 1SZP
3LDA
ProteinModelPortal P25454
SMR P25454
BioGrid 36841
DIP DIP-195N
IntAct P25454
MINT MINT-386096
STRING 4932.YER095W
MaxQB P25454
PaxDb P25454
PeptideAtlas P25454
EnsemblFungi [example_ID YER095W]
GeneID 856831
KEGG sce:YER095W
CYGD YER095w
SGD S000000897
eggNOG COG0468
GeneTree ENSGT00770000120539
HOGENOM HOG000227426
InParanoid P25454
KO K04482
OMA CQLPIDQ
OrthoDB EOG7TN02X
BioCyc YEAST:G3O-30262-MONOMER
Reactome REACT_260604
EvolutionaryTrace P25454
NextBio 983130
PRO PR:P25454
Proteomes UP000002311
Genevestigator P25454
GO GO:0000794
GO:0000228
GO:0005524
GO:0003684
GO:0008094
GO:0042802
GO:0000150
GO:0003697
GO:0006200
GO:0006310
GO:0000724
GO:0030491
GO:0000709
GO:0007131
GO:0042148
GO:0000722
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

involved_in

GO:0000722

telomere maintenance via recombination

PMID:25822194[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042148

strand invasion

PMID:9271413[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042148

strand invasion

PMID:8066464[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030491

heteroduplex formation

PMID:10506208[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008094

DNA-dependent ATPase activity

PMID:8066464[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0007131

reciprocal meiotic recombination

PMID:16581767[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006310

DNA recombination

PMID:22955832[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

PMID:20371520[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000794

condensed nuclear chromosome

PMID:9427283[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000709

meiotic joint molecule formation

PMID:1581961[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0000228

nuclear chromosome

PMID:11459983[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0000150

recombinase activity

PMID:8066464[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070192

chromosome organization involved in meiotic cell cycle

PMID:21873635[11]

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[11]

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[11]

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[11]

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[11]

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[11]

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[11]

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[11]

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[11]

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[11]

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

enables

GO:0042802

identical protein binding

PMID:23624404[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25454

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21738226[13]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25454

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18467557[14]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25454

F

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

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:10422536[15]

ECO:0000304

author statement supported by traceable reference used in manual assertion

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

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

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

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

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

Notes

References

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

  1. Peng, J et al. (2015) Inhibition of telomere recombination by inactivation of KEOPS subunit Cgi121 promotes cell longevity. PLoS Genet. 11 e1005071 PubMed GONUTS page
  2. Namsaraev, E & Berg, P (1997) Characterization of strand exchange activity of yeast Rad51 protein. Mol. Cell. Biol. 17 5359-68 PubMed GONUTS page
  3. 3.0 3.1 3.2 Sung, P (1994) Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science 265 1241-3 PubMed GONUTS page
  4. Petukhova, G et al. (1999) Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation. J. Biol. Chem. 274 29453-62 PubMed GONUTS page
  5. Henry, JM et al. (2006) Mnd1/Hop2 facilitates Dmc1-dependent interhomolog crossover formation in meiosis of budding yeast. Mol. Cell. Biol. 26 2913-23 PubMed GONUTS page
  6. Cloud, V et al. (2012) Rad51 is an accessory factor for Dmc1-mediated joint molecule formation during meiosis. Science 337 1222-5 PubMed GONUTS page
  7. Chen, J et al. (2010) Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant. Nucleic Acids Res. 38 4889-906 PubMed GONUTS page
  8. Shinohara, A et al. (1997) Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination. Genes Cells 2 615-29 PubMed GONUTS page
  9. Shinohara, A et al. (1992) Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell 69 457-70 PubMed GONUTS page
  10. Gasior, SL et al. (2001) Assembly of RecA-like recombinases: distinct roles for mediator proteins in mitosis and meiosis. Proc. Natl. Acad. Sci. U.S.A. 98 8411-8 PubMed GONUTS page
  11. 11.0 11.1 11.2 11.3 11.4 11.5 11.6 11.7 11.8 11.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  12. Bergink, S et al. (2013) Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction. Nat. Cell Biol. 15 526-32 PubMed GONUTS page
  13. Flott, S et al. (2011) Regulation of Rad51 function by phosphorylation. EMBO Rep. 12 833-9 PubMed GONUTS page
  14. Tarassov, K et al. (2008) An in vivo map of the yeast protein interactome. Science 320 1465-70 PubMed GONUTS page
  15. Cui, X et al. (1999) The XRCC2 and XRCC3 repair genes are required for chromosome stability in mammalian cells. Mutat. Res. 434 75-88 PubMed GONUTS page