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YEAST:TPS2

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) TPS2 (synonyms: PFK3)
Protein Name(s) Trehalose-phosphatase

Trehalose synthase complex catalytic subunit TPS2 Trehalose-6-phosphate phosphatase TPP

External Links
UniProt P31688
EMBL X70694
Z46796
Z74370
X58858
BK006938
PIR S48761
RefSeq NP_010359.1
ProteinModelPortal P31688
SMR P31688
BioGrid 32129
DIP DIP-823N
IntAct P31688
MINT MINT-396338
STRING 4932.YDR074W
CAZy GT20
MaxQB P31688
PaxDb P31688
PeptideAtlas P31688
EnsemblFungi [example_ID YDR074W]
GeneID 851646
KEGG sce:YDR074W
CYGD YDR074w
SGD S000002481
eggNOG COG0380
GeneTree ENSGT00550000075394
HOGENOM HOG000191477
InParanoid P31688
KO K16055
OMA DVAYWAQ
OrthoDB EOG76QFS6
BioCyc MetaCyc:MONOMER-595
YEAST:YDR074W-MONOMER
NextBio 969224
Proteomes UP000002311
Genevestigator P31688
GO GO:0005946
GO:0004805
GO:0034605
GO:0016311
GO:0005992
Gene3D 3.40.50.1000
InterPro IPR001830
IPR023214
IPR006379
IPR003337
Pfam PF00982
PF02358
SUPFAM SSF56784
TIGRFAMs TIGR01484
TIGR00685

Annotations

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

part_of

GO:0005739

mitochondrion

PMID:16823961[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004805

trehalose-phosphatase activity

PMID:9837904[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070413

trehalose metabolism in response to stress

PMID:9837904[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:8203161[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:8444170[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:8444170[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:8203161[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005946

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

PMID:9837904[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P38426
UniProtKB:P38427
UniProtKB:Q00764

C

Seeded From UniProt

complete

enables

GO:0004805

trehalose-phosphatase activity

PMID:8444170[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070413

trehalose metabolism in response to stress

PMID:21873635[6]

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[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082223
SGD:S000002481
UniProtKB:C8VHC8
UniProtKB:Q4WWF5
UniProtKB:Q5AI14

P

Seeded From UniProt

complete

involved_in

GO:0031505

fungal-type cell wall organization

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082223
UniProtKB:C8VHC8
UniProtKB:Q4WWF5

P

Seeded From UniProt

complete

involved_in

GO:0030448

hyphal growth

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082223
UniProtKB:Q4WWF5

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082223
UniProtKB:Q4WWF5

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:21873635[6]

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[6]

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[6]

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[6]

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[6]

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[6]

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

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:0000366

evidence based on logical inference from automatic 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
InterPro:IPR003337

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:IPR003337

P

Seeded From UniProt

complete

enables

GO:0004805

trehalose-phosphatase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.3.12

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: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

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Notes

References

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

  1. ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  2. ↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 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
  4. ↑ 4.0 4.1 Sur, IP et al. (1994) Analysis of PFK3--a gene involved in particulate phosphofructokinase synthesis reveals additional functions of TPS2 in Saccharomyces cerevisiae. Yeast 10 199-209 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 De Virgilio, C et al. (1993) Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur. J. Biochem. 212 315-23 PubMed GONUTS page
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 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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