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YEAST:PP4C
Contents
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 |
ECO:0000314 |
P |
Figure 6D. |
complete | |||||
part_of |
GO:0005634 |
nucleus |
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:0034399 |
nuclear periphery |
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 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:2000002 |
negative regulation of DNA damage checkpoint |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:2000002 |
negative regulation of DNA damage checkpoint |
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 |
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 |
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 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0030289 |
protein phosphatase 4 complex |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0030289 |
protein phosphatase 4 complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0030289 |
protein phosphatase 4 complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006470 |
protein dephosphorylation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006470 |
protein dephosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006470 |
protein dephosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004722 |
protein serine/threonine phosphatase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004722 |
protein serine/threonine phosphatase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004722 |
protein serine/threonine phosphatase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
colocalizes_with |
GO:0000794 |
condensed nuclear chromosome |
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 |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
SGD:S000000152 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004721 |
phosphoprotein phosphatase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004721 |
phosphoprotein phosphatase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 | |||
part_of |
GO:0005634 |
nucleus |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information 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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 2.0 2.1 Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
- ↑ 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
- ↑ 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
- ↑ 5.0 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
- ↑ 6.0 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
- ↑ 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
- ↑ 8.0 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
- ↑ Bertram, PG et al. (2000) Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases. J. Biol. Chem. 275 35727-33 PubMed GONUTS page
- ↑ 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
- ↑ 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
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