SHS1/YDL225W Summary Help

Standard Name SHS1 1
Systematic Name YDL225W
Alias SEP7 2
Feature Type ORF, Verified
Description Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble into rod-like hetero-oligomers that can associate with other rods to form filaments; septin rings at the mother-bud neck act as scaffolds for recruiting cell division factors and as barriers to prevent diffusion of specific proteins; undergoes sumoylation and phosphorylation during mitosis; protein abundance increases in response to DNA replication stress (1, 3, 4, 5, 6, 7, 8, 9, 10, 11 and see Summary Paragraph)
Name Description Seventh Homolog of Septin 1
Chromosomal Location
ChrIV:52445 to 54100 | ORF Map | GBrowse
Gene Ontology 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
Regulators 3 genes
Classical genetics
Large-scale survey
251 total interaction(s) for 161 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 49
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 25
  • Biochemical Activity: 11
  • PCA: 5
  • Reconstituted Complex: 1
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Growth Defect: 9
  • Dosage Lethality: 3
  • Dosage Rescue: 2
  • Negative Genetic: 87
  • Phenotypic Enhancement: 9
  • Positive Genetic: 10
  • Synthetic Growth Defect: 10
  • Synthetic Lethality: 20
  • Synthetic Rescue: 2

Expression Summary
Length (a.a.) 551
Molecular Weight (Da) 62,629
Isoelectric Point (pI) 5.31
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:52445 to 54100 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1656 52445..54100 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002384

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 12 and 13). 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 (13, 14).

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, 14). 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, 15). PR, All known septins contain consensus GTP-binding domains, and Drosophila septins hydrolyze GTP in vitro (12, 13). Septin GTPase activity has not been studied extensively in yeast (13).

Last updated: 1999-12-09 Contact SGD

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) Johnson ES and Blobel G  (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 147(5):981-94
4) Takizawa PA, et al.  (2000) Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290(5490):341-4
5) Mortensen EM, et al.  (2002) Cell cycle-dependent assembly of a Gin4-septin complex. Mol Biol Cell 13(6):2091-105
6) Hanrahan J and Snyder M  (2003) Cytoskeletal activation of a checkpoint kinase. Mol Cell 12(3):663-73
7) Conde R, et al.  (2003) Screening for new yeast mutants affected in mannosylphosphorylation of cell wall mannoproteins. Yeast 20(14):1189-211
8) 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
9) Vrabioiu AM, et al.  (2004) The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J Biol Chem 279(4):3111-8
10) McMurray MA, et al.  (2011) Septin filament formation is essential in budding yeast. Dev Cell 20(4):540-9
11) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
12) Longtine MS, et al.  (1996) The septins: roles in cytokinesis and other processes. Curr Opin Cell Biol 8(1):106-19
13) Field CM and Kellogg D  (1999) Septins: cytoskeletal polymers or signalling GTPases? Trends Cell Biol 9(10):387-94
14) Madden K and Snyder M  (1998) Cell polarity and morphogenesis in budding yeast. Annu Rev Microbiol 52():687-744
15) 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