| Standard Name | SDS22 1 |
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| Systematic Name | YKL193C |
| Alias | EGP1 2 |
| Feature Type | ORF, Verified |
| Description | Regulatory subunit of the type 1 protein phosphatase (PP1) Glc7p; whether it functions as a positive or negative regulator of Glc7p is controversial; involved in the regulation of Glc7p nuclear localization and function (1, 2, 3, 4, 5, 6, 7 and see Summary Paragraph) |
| Name Description | homolog of S. pombe SDS22 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
| View Computational GO annotations for SDS22 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Regulatory modules | predicted: stressResponse (643, 607, 595, 445, 379) predicted: cellcycle (341) predicted: stressResponse (643, 607, 595, 445, 379) predicted: cellcycle (341) |
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| Classical genetics | |
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| conditional | |
| Large-scale survey | |
| conditional | |
| null | |
| overexpression | |
| reduction of function | |
| repressible | |
| Resources |
| 147 total interaction(s) for 105 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000001676 |
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SDS22 encodes a leucine-rich repeat protein that is a positive regulatory subunit of protein phosphatase type 1 (Glc7p) (2). Sds22p forms a stable 1:1 complex with Glc7p (8), and is required for normal nuclear localization of Glc7p (5). Sds22p and Glc7p appear to be involved in regulating microtubule-related functions (2), and seem to function in an interdependent manner (5). Sds22p/Glc7p complexes appear more abundant in early stationary phase extracts than in exponential phase extracts (8), but SDS22 expression appears continuous throughout the cell cycle (2).
SDS22 is an essential gene, and roughly 60% of Sds22p-depleted cells arrest in the large-bud stage of the cell cycle, with approximately 7% of the Sds22p-depleted cells being multinucleate or aploid (2). Some Sds22p-depleted large-budded cells also exhibit abnormal spindle structures (2). Some temperature-sensitive loss-of-function sds22 mutations confer a chromosome loss phenotype at higher growth temperatures (5).
SDS22 is the budding yeast homologue of Schizosaccharomyces pombe sds22 and human SDS22 (5).
| 1) | MacKelvie SH, et al. (1995) The Saccharomyces cerevisiae gene SDS22 encodes a potential regulator of the mitotic function of yeast type 1 protein phosphatase. Mol Cell Biol 15(7):3777-85 |
| 2) | Hisamoto N, et al. (1995) The EGP1 gene may be a positive regulator of protein phosphatase type 1 in the growth control of Saccharomyces cerevisiae. Mol Cell Biol 15(7):3767-76 |
| 3) | Hong G, et al. (2000) Sds22p is a subunit of a stable isolatable form of protein phosphatase 1 (Glc7p) from Saccharomyces cerevisiae. Arch Biochem Biophys 376(2):288-98 |
| 4) | Ramaswamy NT, et al. (1998) Regulation of yeast glycogen metabolism and sporulation by Glc7p protein phosphatase. Genetics 149(1):57-72 |
| 5) | Peggie MW, et al. (2002) Essential functions of Sds22p in chromosome stability and nuclear localization of PP1. J Cell Sci 115(Pt 1):195-206 |
| 6) | Pedelini L, et al. (2007) YPI1 and SDS22 proteins regulate the nuclear localization and function of yeast type 1 phosphatase Glc7. J Biol Chem 282(5):3282-92 |
| 7) | Bharucha JP, et al. (2008) Ypi1, a Positive Regulator of Nuclear Protein Phosphatase Type 1 Activity in Saccharomyces cerevisiae. Mol Biol Cell 19(3):1032-45 |
| 8) | Walsh EP, et al. (2002) Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single-step affinity purification and mass spectrometry. Biochemistry 41(7):2409-20 |





