ArticleDatabase : the journal of biological databases and curation2010
PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae.
Article in Database : the journal of biological databases and curation, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.
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Who cites it
62 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes.GigaScience · 2017Pooled it
- Yeast centrosomes act as organizing centers to promote Polo kinase-mediated adaptation to persistent DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cell growth and nutrient availability control the mitotic exit signaling network in budding yeast.The Journal of cell biology · 2024Article
- The regulatory landscape of the yeast phosphoproteome.Nature structural & molecular biology · 2023Article
- A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition.Mobile DNA · 2022Article
- A global map of associations between types of protein posttranslational modifications and human genetic diseases.iScience · 2021Article
- Article
- Molecular dynamics shows complex interplay and long-range effects of post-translational modifications in yeast protein interactions.PLoS computational biology · 2021Article
- Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021Article
- Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages.Cell communication and signaling : CCS · 2019Article
- Clinically Relevant Post-Translational Modification Analyses-Maturing Workflows and Bioinformatics Tools.International journal of molecular sciences · 2018Review
- Effects of Acetylation and Phosphorylation on Subunit Interactions in Three Large Eukaryotic Complexes.Molecular & cellular proteomics : MCP · 2018Article
- Antagonism between salicylate and the cAMP signal controls yeast cell survival and growth recovery from quiescence.Microbial cell (Graz, Austria) · 2018Article
- Wobble uridine modifications-a reason to live, a reason to die?!RNA biology · 2017Review
- Syp1 regulates the clathrin-mediated and clathrin-independent endocytosis of multiple cargo proteins through a novel sorting motif.Molecular biology of the cell · 2017Article
- Machine Learning of Global Phosphoproteomic Profiles Enables Discrimination of Direct versus Indirect Kinase Substrates.Molecular & cellular proteomics : MCP · 2017Article
- A CDC25 family protein phosphatase gates cargo recognition by the Vps26 retromer subunit.eLife · 2017Article
- Delineating functional principles of the bow tie structure of a kinase-phosphatase network in the budding yeast.BMC systems biology · 2017Article
- Functional Analysis of Kinases and Transcription Factors inG3 (Bethesda, Md.) · 2017Article
- The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.Current genetics · 2017Review
2 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
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Abstract
Protein phosphorylation plays a central role in cellular regulation. Recent proteomics strategies for identifying phosphopeptides have been developed using the model organism Saccharomyces cerevisiae, and consequently, when combined with studies of individual gene products, the number of reported specific phosphorylation sites for this organism has expanded enormously. In order to systematically document and integrate these various data types, we have developed a database of experimentally verified in vivo phosphorylation sites curated from the S. cerevisiae primary literature. PhosphoGRID (www.phosphogrid.org) records the positions of over 5000 specific phosphorylated residues on 1495 gene products. Nearly 900 phosphorylated residues are reported from detailed studies of individual proteins; these in vivo phosphorylation sites are documented by a hierarchy of experimental evidence codes. Where available for specific sites, we have also noted the relevant protein kinases and/or phosphatases, the specific condition(s) under which phosphorylation occurs, and the effect(s) that phosphorylation has on protein function. The unique features of PhosphoGRID that assign both function and specific physiological conditions to each phosphorylated residue will provide a valuable benchmark for proteome-level studies and will facilitate bioinformatic analysis of cellular signal transduction networks. Database URL: http://phosphogrid.org/
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.