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YEAST:PP4C

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) PPH3
Protein Name(s) Serine/threonine-protein phosphatase 4 catalytic subunit

PP4C Phosphatase PP2A-like catalytic subunit PPH3

External Links
UniProt P32345
EMBL Z46796
X58858
X82086
Z74371
AY557686
BK006938
PIR S44331
RefSeq NP_010360.1
ProteinModelPortal P32345
SMR P32345
BioGrid 32130
DIP DIP-3905N
IntAct P32345
MINT MINT-509529
MaxQB P32345
PeptideAtlas P32345
TopDownProteomics P32345
EnsemblFungi YDR075W
GeneID 851647
KEGG sce:YDR075W
EuPathDB FungiDB:YDR075W
SGD S000002482
GeneTree ENSGT00840000131875
HOGENOM HOG000172696
InParanoid P32345
KO K15423
OMA LRQEYKV
OrthoDB EOG7FFN29
BioCyc YEAST:G3O-29680-MONOMER
PRO PR:P32345
Proteomes UP000002311
GO GO:0005737
GO:0034399
GO:0030289
GO:0046872
GO:0004722
GO:0000724
GO:2000002
GO:1902660
GO:2001034
GO:0051173
GO:0006470
GO:0072462
Gene3D 3.60.21.10
InterPro IPR004843
IPR029052
IPR006186
Pfam PF00149
PRINTS PR00114
SMART SM00156
SUPFAM SSF56300
PROSITE PS00125

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006470

protein dephosphorylation

PMID:22333918[1]

ECO:0000314

P

Figure 6D.

complete
CACAO 12197

part_of

GO:0005634

nucleus

PMID:14562095[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:14562095[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0034399

nuclear periphery

PMID:25817432[3]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0006974)

Seeded From UniProt

complete

involved_in

GO:2001034

positive regulation of double-strand break repair via nonhomologous end joining

PMID:24498054[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000002

negative regulation of DNA damage checkpoint

PMID:16299494[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000002

negative regulation of DNA damage checkpoint

PMID:17517611[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1902660

negative regulation of glucose mediated signaling pathway

PMID:24277933[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0072462

signal transduction involved in meiotic recombination checkpoint

PMID:20951350[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051173

positive regulation of nitrogen compound metabolic process

PMID:10940301[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030289

protein phosphatase 4 complex

PMID:16299494[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030289

protein phosphatase 4 complex

PMID:17517611[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030289

protein phosphatase 4 complex

PMID:16299494[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

PMID:16299494[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

PMID:7941742[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

PMID:16299494[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004722

protein serine/threonine phosphatase activity

PMID:16299494[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004722

protein serine/threonine phosphatase activity

PMID:7941742[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004722

protein serine/threonine phosphatase activity

PMID:16299494[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

colocalizes_with

GO:0000794

condensed nuclear chromosome

PMID:20951350[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000724

double-strand break repair via homologous recombination

PMID:21135129[11]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000000152
SGD:S000000891

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004843
InterPro:IPR006186

F

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.3.16

F

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0904

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

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

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

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

Notes

References

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

  1. Oler, AJ & Cairns, BR (2012) PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression. EMBO J. 31 1440-52 PubMed GONUTS page
  2. 2.0 2.1 Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
  3. Gallina, I et al. (2015) Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat Commun 6 6533 PubMed GONUTS page
  4. Omidi, K et al. (2014) Phosphatase complex Pph3/Psy2 is involved in regulation of efficient non-homologous end-joining pathway in the yeast Saccharomyces cerevisiae. PLoS ONE 9 e87248 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Keogh, MC et al. (2006) A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery. Nature 439 497-501 PubMed GONUTS page
  6. 6.0 6.1 O'Neill, BM et al. (2007) Pph3-Psy2 is a phosphatase complex required for Rad53 dephosphorylation and replication fork restart during recovery from DNA damage. Proc. Natl. Acad. Sci. U.S.A. 104 9290-5 PubMed GONUTS page
  7. Ma, H et al. (2014) Psy2 targets the PP4 family phosphatase Pph3 to dephosphorylate Mth1 and repress glucose transporter gene expression. Mol. Cell. Biol. 34 452-63 PubMed GONUTS page
  8. 8.0 8.1 Falk, JE et al. (2010) A Mec1- and PP4-dependent checkpoint couples centromere pairing to meiotic recombination. Dev. Cell 19 599-611 PubMed GONUTS page
  9. Bertram, PG et al. (2000) Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases. J. Biol. Chem. 275 35727-33 PubMed GONUTS page
  10. 10.0 10.1 Hoffmann, R et al. (1994) The Saccharomyces cerevisiae gene PPH3 encodes a protein phosphatase with properties different from PPX, PP1 and PP2A. Yeast 10 567-78 PubMed GONUTS page
  11. Kim, JA et al. (2011) Protein phosphatases pph3, ptc2, and ptc3 play redundant roles in DNA double-strand break repair by homologous recombination. Mol. Cell. Biol. 31 507-16 PubMed GONUTS page