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YEAST:ENO1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) ENO1 (synonyms: ENOA, HSP48)
Protein Name(s) Enolase 1

2-phospho-D-glycerate hydro-lyase 1 2-phosphoglycerate dehydratase 1

External Links
UniProt P00924
EMBL J01322
X99228
Z73039
BK006941
PIR S64586
RefSeq NP_011770.3
PDB 1EBG
1EBH
1ELS
1L8P
1NEL
1ONE
1P43
1P48
2AL1
2AL2
2ONE
2XGZ
2XH0
2XH2
2XH4
2XH7
3ENL
4ENL
5ENL
6ENL
7ENL
PDBsum 1EBG
1EBH
1ELS
1L8P
1NEL
1ONE
1P43
1P48
2AL1
2AL2
2ONE
2XGZ
2XH0
2XH2
2XH4
2XH7
3ENL
4ENL
5ENL
6ENL
7ENL
ProteinModelPortal P00924
SMR P00924
BioGrid 33505
DIP DIP-5561N
IntAct P00924
MINT MINT-574648
Allergome 786
COMPLUYEAST-2DPAGE P00924
SWISS-2DPAGE P00924
UCD-2DPAGE P00924
MaxQB P00924
PeptideAtlas P00924
PRIDE P00924
EnsemblFungi [example_ID YGR254W]
GeneID 853169
KEGG sce:YGR254W
EuPathDB FungiDB:YGR254W
SGD S000003486
GeneTree ENSGT00550000074560
HOGENOM HOG000072174
InParanoid P00924
KO K01689
OMA EAYAGNQ
OrthoDB EOG7JHMFP
BioCyc YEAST:YGR254W-MONOMER
BRENDA 4.2.1.11
Reactome R-SCE-70171
R-SCE-70263
SABIO-RK P00924
UniPathway UPA00109
EvolutionaryTrace P00924
NextBio 973288
PRO PR:P00924
Proteomes UP000002311
GO GO:0000324
GO:0005739
GO:0000015
GO:0000287
GO:0004634
GO:0006094
GO:0006096
GO:0032889
Gene3D 3.20.20.120
3.30.390.10
HAMAP MF_00318
InterPro IPR000941
IPR020810
IPR029065
IPR020809
IPR020811
IPR029017
PANTHER PTHR11902
Pfam PF00113
PF03952
PIRSF PIRSF001400
PRINTS PR00148
SUPFAM SSF51604
SSF54826
TIGRFAMs TIGR01060
PROSITE PS00164

Annotations

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

part_of

GO:0005829

cytosol

PMID:26928762[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24769239[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:11914276[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:16622836[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0032889

regulation of vacuole fusion, non-autophagic

PMID:16565073[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032889

regulation of vacuole fusion, non-autophagic

PMID:16565073[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:6282834[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

PMID:3313003[7]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:16962558[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

PMID:6282834[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000324

fungal-type vacuole

PMID:16565073[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000015

phosphopyruvate hydratase complex

PMID:6282834[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000015

phosphopyruvate hydratase complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

C

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

F

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

P

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.11

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:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

Notes

References

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

  1. Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page
  2. Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  3. Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
  4. Delom, F et al. (2006) The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor. Proteomics 6 3029-39 PubMed GONUTS page
  5. 5.0 5.1 5.2 Decker, BL & Wickner, WT (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J. Biol. Chem. 281 14523-8 PubMed GONUTS page
  6. 6.0 6.1 6.2 McAlister, L & Holland, MJ (1982) Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes. J. Biol. Chem. 257 7181-8 PubMed GONUTS page
  7. Cohen, R et al. (1987) Transcription of the constitutively expressed yeast enolase gene ENO1 is mediated by positive and negative cis-acting regulatory sequences. Mol. Cell. Biol. 7 2753-61 PubMed GONUTS page
  8. Brandina, I et al. () Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim. Biophys. Acta 1757 1217-28 PubMed GONUTS page