Reviewed,
UniProtKB/Swiss-Prot P32945 (PPQ1_YEAST)
Last modified
November 24, 2009.
Version 88.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serine/threonine-protein phosphatase PPQ EC=3.1.3.16 | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 549 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Phosphatase involved in the regulation of protein synthesis. Affects translational accuracy. |
| Catalytic activity | A phosphoprotein + H2O = a protein + phosphate. |
| Cofactor | Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity. |
| Miscellaneous | Present with 319 molecules/cell in log phase SD medium. Ref.6 |
| Sequence similarities | Belongs to the PPP phosphatase family. PP-Z subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Iron Manganese Metal-binding |
| Molecular function | Hydrolase Protein phosphatase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | regulation of translation Ref.1 Inferred from mutant phenotype. Source: SGD |
| Cellular component | cytoplasm Inferred from direct assay. Source: SGD |
| Molecular function | cofactor binding Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW magnesium-dependent protein serine/threonine phosphatase activityInferred from electronic annotation. Source: InterPro manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 549 | 549 | Serine/threonine-protein phosphatase PPQ | PRO_0000058893 | |||||
Regions | |||||||||
| Compositional bias | 113 – 219 | 107 | Ser-rich | ||||||
Sites | |||||||||
| Active site | 362 | 1 | Proton donor By similarity | ||||||
| Metal binding | 301 | 1 | Iron By similarity | ||||||
| Metal binding | 303 | 1 | Iron By similarity | ||||||
| Metal binding | 329 | 1 | Iron By similarity | ||||||
| Metal binding | 329 | 1 | Manganese By similarity | ||||||
| Metal binding | 361 | 1 | Manganese By similarity | ||||||
| Metal binding | 410 | 1 | Manganese By similarity | ||||||
| Metal binding | 485 | 1 | Manganese By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 80 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 208 | 1 | Phosphoserine Ref.8 Ref.7 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis." Chen M.X., Chen Y.H., Cohen P.T.W. Eur. J. Biochem. 218:689-699(1993) [PubMed: 8269960] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [2] | Erratum Chen M.X., Chen Y.H., Cohen P.T.W. Eur. J. Biochem. 221:1133-1133(1994) |
| [3] | "The yeast translational allosuppressor, SAL6: a new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension." Vincent A., Newnam G.P., Liebman S.W. Genetics 138:597-607(1994) [PubMed: 7851758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88. |
| [4] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. Hani J.Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [5] | "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases." Chen M.X., Chen Y.H., Cohen P.T.W. FEBS Lett. 306:54-58(1992) [PubMed: 1321058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-328. |
| [6] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [7] | "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, MASS SPECTROMETRY. |
| [8] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-208, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X75485 Genomic DNA. Translation: CAA53214.1. U00795 Genomic DNA. Translation: AAC48924.1. Z73535 Genomic DNA. Translation: CAA97886.1. S39958 Genomic DNA. Translation: AAB22461.1. | |
| PIR | S39533. |
| RefSeq | NP_015146.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:5504N. |
| IntAct | P32945. 4 interactions. |
| STRING | P32945. |
Genome annotation databases | |
| Ensembl | YPL179W; YPL179W; YPL179W; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 855923. |
| KEGG | sce:YPL179W. |
| NMPDR | fig|4932.3.peg.6275. |
Organism-specific databases | |
| CYGD | YPL179w. |
| SGD | S000006100. PPQ1. |
Phylogenomic databases | |
| HOGENOM | P32945. |
| OrthoDB | EOG9XD582 |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.16. 250. |
Gene expression databases | |
| ArrayExpress | P32945. |
| Genevestigator | P32945. |
| GermOnline | YPL179W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR004843. M-pesterase. IPR011159. PPPtase_PPZ. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view] |
| PANTHER | PTHR11668. T_phtase_apaH. 1 hit. |
| Pfam | PF00149. Metallophos. 1 hit. [Graphical view] |
| PIRSF | PIRSF000909. PPPtase_PPZ. 1 hit. |
| PRINTS | PR00114. STPHPHTASE. |
| SMART | SM00156. PP2Ac. 1 hit. [Graphical view] |
| PROSITE | PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 980649. |
Entry information
| Entry name | PPQ1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P32945 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


