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YEAST:ENO1
Contents
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 |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005886 |
plasma membrane |
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 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0032889 |
regulation of vacuole fusion, non-autophagic |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006094 |
gluconeogenesis |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0004634 |
phosphopyruvate hydratase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0000324 |
fungal-type vacuole |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0000015 |
phosphopyruvate hydratase complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0000015 |
phosphopyruvate hydratase complex |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004634 |
phosphopyruvate hydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004634 |
phosphopyruvate hydratase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0324 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 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
- ↑ Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
- ↑ 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
- ↑ 5.0 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
- ↑ 6.0 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
- ↑ 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
- ↑ 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