SHS1 BASIC INFORMATION
| Standard Name | SHS1 1 |
|---|---|
| Systematic Name | YDL225W |
| Alias | SEP7 2 |
| Feature Type | ORF, Verified |
| Description | One of five related septins (Cdc3p, Cdc10p, Cdc11p, Cdc12p, Shs1p) that form a cortical filamentous collar at the mother-bud neck which is necessary for normal morphogenesis and cytokinesis (1, 3, 4 and see Summary Paragraph)
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| Name Description | Seventh Homolog of Septin 1 |
| GO Annotations | All SHS1 GO evidence and references |
|---|---|
| View Computational GO annotations for SHS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Interactions | SHS1 All interactions details and references |
|---|---|
| 107 total interaction(s) for 47 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
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| Primary SGDID | S000002384 |
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ADDITIONAL INFORMATION for SHS1
SUMMARY PARAGRAPH for SHS1
SHS1 encodes a septin (1). Septins are a family of conserved proteins first identified in yeast and subsequently found in numerous other fungi and animals, including human, mouse, Drosophila, and C. elegans (reviewed in 5 and 6). Four yeast septins, Cdc3p Cdc10p, Cdc11p, and Cdc12p, have been studied extensively; they are required for cytokinesis, axial bud site selection, and the correct localization of several other proteins involved in cytokinesis, morphogenesis, and bud site selection (6, 7).
Shs1p was identified by its two-hybrid interaction with Spa2p, a protein implicated in the control of polarized bud growth (1). Shs1p contains a C-terminal domain not found in the other yeast septins, and is not essential (2). Like other yeast septins, Shs1p localizes to a ring around the bud neck (1, 7). Shs1p associates with the Cdc3p, Cdc10p, Cdc11p, and Cdc12p septins on a Gin4p affinity column (2). Gin4p and two related protein kinases, Hsl1p and Kcc4p are involved in cell cycle progression (2, 8). PR, All known septins contain consensus GTP-binding domains, and Drosophila septins hydrolyze GTP in vitro (5, 6). Septin GTPase activity has not been studied extensively in yeast (6).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for SHS1]
| 1) | Mino A, et al. (1998) Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in saccharomyces cerevisiae. Biochem Biophys Res Commun 251(3):732-6 |
| 2) | Carroll CW, et al. (1998) The septins are required for the mitosis-specific activation of the Gin4 kinase. J Cell Biol 143(3):709-17 |
| 3) | Conde R, et al. (2003) Screening for new yeast mutants affected in mannosylphosphorylation of cell wall mannoproteins. Yeast 20(14):1189-211 |
| 4) | Versele M, et al. (2004) Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol Biol Cell 15(10):4568-83 |
| 5) | Longtine MS, et al. (1996) The septins: roles in cytokinesis and other processes. Curr Opin Cell Biol 8(1):106-19 |
| 6) | Field CM and Kellogg D (1999) Septins: cytoskeletal polymers or signalling GTPases? Trends Cell Biol 9(10):387-94 |
| 7) | Madden K and Snyder M (1998) Cell polarity and morphogenesis in budding yeast. Annu Rev Microbiol 52():687-744 |
| 8) | Barral Y, et al. (1999) Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev 13(2):176-87 |





