SHS1/YDL225W Summary Help

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)
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
Mutant Phenotype All SHS1 Phenotype details and references
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Interactions SHS1 All interactions details and references
107 total interaction(s) for 47 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 36
  • Affinity Capture-Western: 19
  • Biochemical Activity: 9
  • PCA: 3
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Rescue: 2
  • Phenotypic Enhancement: 5
  • Synthetic Growth Defect: 5
  • Synthetic Lethality: 20
  • Synthetic Rescue: 1

Sequence Information
ChrIV:52446 to 54101 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1656 52446..54101 1996-07-31 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002384

SHS1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

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).

Last updated: 1999-12-09

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