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YEAST:DUG2

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) DUG2
Protein Name(s) Probable di- and tripeptidase DUG2

Deficient in utilization of glutathione protein 2 GSH degradosomal complex subunit DUG2

External Links
UniProt P38149
EMBL X76053
Z36150
BK006936
PIR S44543
RefSeq NP_009840.3
ProteinModelPortal P38149
SMR P38149
BioGrid 32975
DIP DIP-1612N
IntAct P38149
MINT MINT-399156
STRING 4932.YBR281C
MaxQB P38149
PaxDb P38149
PeptideAtlas P38149
EnsemblFungi [example_ID YBR281C]
GeneID 852584
KEGG sce:YBR281C
CYGD YBR281c
SGD S000000485
eggNOG COG0624
HOGENOM HOG000183136
InParanoid P38149
KO K14262
OMA PAAHLPC
OrthoDB EOG7NW6JF
BioCyc YEAST:G3O-29201-MONOMER
NextBio 971733
Proteomes UP000002311
Genevestigator P38149
GO GO:0005737
GO:0005634
GO:0016805
GO:0046872
GO:0008237
GO:0008242
GO:0008233
GO:0006751
Gene3D 2.130.10.10
3.30.70.360
InterPro IPR020472
IPR017149
IPR002933
IPR011650
IPR015943
IPR001680
IPR019775
IPR017986
Pfam PF07687
PF01546
PF00400
PIRSF PIRSF037237
PRINTS PR00320
SMART SM00320
SUPFAM SSF50978
SSF55031
PROSITE PS00678
PS50082
PS50294

Annotations

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

part_of

GO:0005634

nucleus

PMID:14562095[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:14562095[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0034399

nuclear periphery

PMID:25817432[2]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0006974)

Seeded From UniProt

complete

part_of

GO:0061672

glutathione hydrolase complex

PMID:22277648[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008242

omega peptidase activity

PMID:17179087[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004290
SGD:S000004294

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

PMID:17179087[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004294

F

Seeded From UniProt

complete

involved_in

GO:0006751

glutathione catabolic process

PMID:22277648[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006751

glutathione catabolic process

PMID:17179087[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006751

glutathione catabolic process

PMID:22277648[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:17179087[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0036374

glutathione hydrolase activity

PMID:22277648[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22277648[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P38149

F

Seeded From UniProt

complete

involved_in

GO:0006751

glutathione catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017149

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002933

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0224

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

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:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

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

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
  2. Gallina, I et al. (2015) Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat Commun 6 6533 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Kaur, H et al. (2012) Glutathione degradation by the alternative pathway (DUG pathway) in Saccharomyces cerevisiae is initiated by (Dug2p-Dug3p)2 complex, a novel glutamine amidotransferase (GATase) enzyme acting on glutathione. J. Biol. Chem. 287 8920-31 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Ganguli, D et al. (2007) The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae. Genetics 175 1137-51 PubMed GONUTS page