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YEAST:KPYK1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) CDC19 (synonyms: PYK1)
Protein Name(s) Pyruvate kinase 1

PK 1 cell division cycle protein 19

External Links
UniProt P00549
EMBL V01321
X14400
AY949862
AY949863
AY949864
AY949865
AY949866
AY949867
AY949868
AY949869
AY949870
AY949871
AY949872
AY949873
AY949874
AY949875
AY949876
AY949877
AY949878
AY949879
AY949880
AY949881
AY949882
AY949883
AY949884
AY949885
AY949886
AY949887
AY949888
AY949889
AY949890
U12980
AY693107
BK006935
PIR S05764
RefSeq NP_009362.1
PDB 1A3W
1A3X
PDBsum 1A3W
1A3X
ProteinModelPortal P00549
SMR P00549
BioGrid 31727
DIP DIP-4124N
IntAct P00549
MINT MINT-565419
STRING 4932.YAL038W
COMPLUYEAST-2DPAGE P00549
MaxQB P00549
PaxDb P00549
PeptideAtlas P00549
EnsemblFungi [example_ID YAL038W]
GeneID 851193
KEGG sce:YAL038W
CYGD YAL038w
SGD S000000036
eggNOG COG0469
GeneTree ENSGT00390000008859
HOGENOM HOG000021559
InParanoid P00549
KO K00873
OMA ISKKCAY
OrthoDB EOG7M6DJC
BioCyc YEAST:YAL038W-MONOMER
Reactome REACT_229625
REACT_237953
REACT_241476
SABIO-RK P00549
UniPathway UPA00109
EvolutionaryTrace P00549
NextBio 968037
Proteomes UP000002311
Genevestigator P00549
GO GO:0005737
GO:0005524
GO:0000287
GO:0030955
GO:0004743
GO:0006096
GO:0006090
Gene3D 2.40.33.10
3.20.20.60
3.40.1380.20
InterPro IPR001697
IPR015813
IPR011037
IPR015794
IPR018209
IPR015793
IPR015795
IPR015806
PANTHER PTHR11817
Pfam PF00224
PF02887
PRINTS PR01050
SUPFAM SSF50800
SSF51621
SSF52935
TIGRFAMs TIGR01064
PROSITE PS00110

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004743

pyruvate kinase activity

PMID:21907146[1]

ECO:0000316

UniProtKB:P52489


F

Figure 1B and 1C Pyruvate kinase activity of TEFpr-PYK1 and CYCpr-PYK1.

TEFpr is a strong promotor, CYCpr is a weak promotor.

complete
CACAO 10958

GO:0006098

pentose-phosphate shunt

PMID:21907146[1]

ECO:0000314

P

Figure 5B Cells with low PYK activity have increased concentrations of PPP intermediates

complete
CACAO 10960

part_of

GO:0005886

plasma membrane

PMID:16622836[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:27385335[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:323230[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006090

pyruvate metabolic process

PMID:323230[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:14718557[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004743

pyruvate kinase activity

PMID:323230[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004743

pyruvate kinase activity

PMID:12063246[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032869

cellular response to insulin stimulus

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000212861
RGD:3336

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10803
EcoGene:EG10804
MGI:MGI:97591
PANTHER:PTN000212670
RGD:3336
RGD:3337
SGD:S000000036
UniProtKB:Q2RAK2

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000212670
SGD:S000000036
UniProtKB:P14618

C

Seeded From UniProt

complete

enables

GO:0004743

pyruvate kinase activity

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10803
EcoGene:EG10804
MGI:MGI:97591
MGI:MGI:97604
PANTHER:PTN000212670
PomBase:SPAC4H3.10c
RGD:3336
RGD:3337
SGD:S000000036
SGD:S000005874
TAIR:locus:2033760
TAIR:locus:2084583
TAIR:locus:2176912
UniProtKB:C6KTA4
UniProtKB:P14618
UniProtKB:P30613
UniProtKB:Q2RAK2

F

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:IPR001697
InterPro:IPR015793

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015813

F

Seeded From UniProt

complete

enables

GO:0004743

pyruvate kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001697
InterPro:IPR015793
InterPro:IPR015806
InterPro:IPR018209

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:IPR001697
InterPro:IPR015793
InterPro:IPR015806
InterPro:IPR018209

P

Seeded From UniProt

complete

enables

GO:0030955

potassium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001697
InterPro:IPR015793

F

Seeded From UniProt

complete

enables

GO:0004743

pyruvate kinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.1.40

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

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

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

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

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

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Grüning, NM et al. (2011) Pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cells. Cell Metab. 14 415-27 PubMed GONUTS page
  2. 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
  3. Finnigan, GC et al. (2016) Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system. Mol. Biol. Cell 27 2708-25 PubMed GONUTS page
  4. 4.0 4.1 4.2 Sprague, GF Jr (1977) Isolation and characterization of a Saccharomyces cerevisiae mutant deficient in pyruvate kinase activity. J. Bacteriol. 130 232-41 PubMed GONUTS page
  5. Jablonowski, D et al. (2004) The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity. Mol. Biol. Cell 15 1459-69 PubMed GONUTS page
  6. Portela, P et al. (2002) In vivo and in vitro phosphorylation of two isoforms of yeast pyruvate kinase by protein kinase A. J. Biol. Chem. 277 30477-87 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page