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YEAST:TPS1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) TPS1 (synonyms: BYP1, CIF1, FDP1, GGS1, GLC6, TSS1)
Protein Name(s) Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit

General glucose sensor subunit 1 Glycogen metabolism control protein GLC6 Trehalose synthase complex catalytic subunit TPS1 Trehalose-6-phosphate synthase UDP-glucose-glucosephosphate glucosyltransferase

External Links
UniProt Q00764
EMBL J04450
X68214
X68496
X67499
X61275
L21999
X78993
X75891
AF061037
AY598966
AY598964
Z35995
AY693147
BK006936
PIR S34979
RefSeq NP_009684.1
ProteinModelPortal Q00764
SMR Q00764
BioGrid 32827
DIP DIP-744N
IntAct Q00764
MINT MINT-618278
STRING 4932.YBR126C
CAZy GT20
MaxQB Q00764
PaxDb Q00764
PeptideAtlas Q00764
PRIDE Q00764
EnsemblFungi [example_ID YBR126C]
GeneID 852423
KEGG sce:YBR126C
CYGD YBR126c
SGD S000000330
eggNOG COG0380
GeneTree ENSGT00550000075557
HOGENOM HOG000191477
InParanoid Q00764
KO K00697
OMA WLAYNEA
OrthoDB EOG76QFS6
BioCyc MetaCyc:MONOMER-563
YEAST:YBR126C-MONOMER
NextBio 971291
PRO PR:Q00764
Proteomes UP000002311
ExpressionAtlas Q00764
Genevestigator Q00764
GO GO:0005946
GO:0003825
GO:0042802
GO:0044262
GO:0034605
GO:0034599
GO:0005992
InterPro IPR001830
IPR012766
Pfam PF00982
TIGRFAMs TIGR02400

Annotations

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

involved_in

GO:1900118

negative regulation of execution phase of apoptosis

PMID:27507670[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004805

trehalose-phosphatase activity

PMID:9837904[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

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

involved_in

GO:0071465

cellular response to desiccation

PMID:25456447[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044262

cellular carbohydrate metabolic process

PMID:1425702[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044262

cellular carbohydrate metabolic process

PMID:1425702[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:9660948[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034599

cellular response to oxidative stress

PMID:11483159[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:1425702[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:1425702[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005946

alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

PMID:9837904[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P31688
UniProtKB:P38426
UniProtKB:P38427

C

Seeded From UniProt

complete

part_of

GO:0005946

alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

PMID:1425702[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005946

alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

PMID:1425702[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:1425702[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:9837904[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

contributes_to

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:1425702[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0090441

trehalose biosynthesis in response to heat stress

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000846253
PomBase:SPAC328.03

P

Seeded From UniProt

complete

involved_in

GO:0070413

trehalose metabolism in response to stress

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082159
PomBase:SPAC328.03
SGD:S000002481

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000846253
SGD:S000000330
UniProtKB:O59921

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
FB:FBgn0027560
PANTHER:PTN000082159
SGD:S000000330
SGD:S000002481
SGD:S000004566
SGD:S000004874
TAIR:locus:2200216
UniProtKB:O59921
UniProtKB:P9WN11
UniProtKB:Q4WHW0
UniProtKB:Q4WLM9
WB:WBGene00001649

P

Seeded From UniProt

complete

part_of

GO:0005946

alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082162
PomBase:SPAC19G12.15c
PomBase:SPAC328.03
SGD:S000000330
SGD:S000002481
SGD:S000004566
SGD:S000004874

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
PANTHER:PTN000082159
TAIR:locus:2054027
TAIR:locus:2202290

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082159
TAIR:locus:2202990
WB:WBGene00001649

C

Seeded From UniProt

complete

contributes_to

GO:0004805

trehalose-phosphatase activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0027560
PANTHER:PTN000082159
PomBase:SPAC19G12.15c
SGD:S000000330
SGD:S000002481
SGD:S000004566
SGD:S000004874
UniProtKB:Q5AI14
WB:WBGene00001649

F

Seeded From UniProt

complete

contributes_to

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000182821
PANTHER:PTN000082159
PomBase:SPAC328.03
SGD:S000000330
SGD:S000004566
SGD:S000004874
TAIR:locus:2202990

F

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004805

P

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004805

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001830

F

Seeded From UniProt

complete

enables

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012766

F

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001830
InterPro:IPR012766

P

Seeded From UniProt

complete

enables

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.15

F

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

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

edit table

Notes

References

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

  1. ↑ Petitjean, M et al. (2017) A new function for the yeast trehalose-6P synthase (Tps1) protein, as key pro-survival factor during growth, chronological ageing, and apoptotic stress. Mech. Ageing Dev. 161 234-246 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Bell, W et al. (1998) Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex. J. Biol. Chem. 273 33311-9 PubMed GONUTS page
  3. ↑ Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
  4. ↑ Tapia, H & Koshland, DE (2014) Trehalose is a versatile and long-lived chaperone for desiccation tolerance. Curr. Biol. 24 2758-66 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 Bell, W et al. (1992) Characterization of the 56-kDa subunit of yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation. Eur. J. Biochem. 209 951-9 PubMed GONUTS page
  6. ↑ Singer, MA & Lindquist, S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1 639-48 PubMed GONUTS page
  7. ↑ Pereira, MD et al. (2001) Acquisition of tolerance against oxidative damage in Saccharomyces cerevisiae. BMC Microbiol. 1 11 PubMed GONUTS page
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 8.7 8.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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