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YEAST:RAD55

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) RAD55
Protein Name(s) DNA repair protein RAD55
External Links
UniProt P38953
EMBL Z46796
D10481
U01144
X82086
Z74372
AY723773
BK006938
PIR S48763
RefSeq NP_010361.3
ProteinModelPortal P38953
BioGrid 32131
DIP DIP-1554N
IntAct P38953
MINT MINT-386077
STRING 4932.YDR076W
MaxQB P38953
PaxDb P38953
EnsemblFungi [example_ID YDR076W]
GeneID 851648
KEGG sce:YDR076W
CYGD YDR076w
SGD S000002483
eggNOG COG0467
InParanoid P38953
KO K10957
OMA ANIASFP
OrthoDB EOG7SV16X
BioCyc YEAST:G3O-29681-MONOMER
NextBio 969230
Proteomes UP000002311
Genevestigator P38953
GO GO:0005634
GO:0033062
GO:0005524
GO:0003677
GO:0008094
GO:0046982
GO:0006200
GO:0000730
GO:0030491
GO:0000707
Gene3D 3.40.50.300
InterPro IPR014774
IPR027417
IPR020588
Pfam PF06745
SUPFAM SSF52540
PROSITE PS50162

Annotations

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

enables

GO:0046982

protein heterodimerization activity

PMID:9159392[1]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000002411

F

Seeded From UniProt

complete

enables

GO:0046982

protein heterodimerization activity

PMID:7624345[2]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000002411

F

Seeded From UniProt

complete

enables

GO:0046982

protein heterodimerization activity

PMID:7651402[3]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000002411

F

Seeded From UniProt

complete

part_of

GO:0033062

Rhp55-Rhp57 complex

PMID:9159392[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030491

heteroduplex formation

PMID:9159392[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008094

DNA-dependent ATPase activity

PMID:8181742[4]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P25454

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:10943844[5]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000730

DNA recombinase assembly

PMID:12887906[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000730

DNA recombinase assembly

PMID:14765116[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000730

DNA recombinase assembly

PMID:11459983[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000707

meiotic DNA recombinase assembly

PMID:9679065[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

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:IPR020588

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:IPR020588

F

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:IPR020588

F

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

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

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: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

Notes

References

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

  1. 1.0 1.1 1.2 Sung, P (1997) Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev. 11 1111-21 PubMed GONUTS page
  2. Hays, SL et al. (1995) Complex formation in yeast double-strand break repair: participation of Rad51, Rad52, Rad55, and Rad57 proteins. Proc. Natl. Acad. Sci. U.S.A. 92 6925-9 PubMed GONUTS page
  3. Johnson, RD & Symington, LS (1995) Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57. Mol. Cell. Biol. 15 4843-50 PubMed GONUTS page
  4. Lovett, ST (1994) Sequence of the RAD55 gene of Saccharomyces cerevisiae: similarity of RAD55 to prokaryotic RecA and other RecA-like proteins. Gene 142 103-6 PubMed GONUTS page
  5. Agarwal, S & Roeder, GS (2000) Zip3 provides a link between recombination enzymes and synaptonemal complex proteins. Cell 102 245-55 PubMed GONUTS page
  6. Sugawara, N et al. (2003) In vivo roles of Rad52, Rad54, and Rad55 proteins in Rad51-mediated recombination. Mol. Cell 12 209-19 PubMed GONUTS page
  7. Miyazaki, T et al. (2004) In vivo assembly and disassembly of Rad51 and Rad52 complexes during double-strand break repair. EMBO J. 23 939-49 PubMed GONUTS page
  8. 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
  9. Gasior, SL et al. (1998) Rad52 associates with RPA and functions with rad55 and rad57 to assemble meiotic recombination complexes. Genes Dev. 12 2208-21 PubMed GONUTS page