SHS1/YDL225W Protein Information Help

Standard Name Shs1p 1
Systematic Name Ydl225wp
Alias Sep7p 2
ORF Classification 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, 10, 11, 3, 4, 5, 6, 7, 8, 9)
Name Description Seventh Homolog of Septin 1
Experimental Data
Molecules/cell 5620 12
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 551
Molecular Weight (Da) 62,629
Isoelectric Point (pI) 5.31

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Shs1p (InterPro)
Physical Interactions There are 94 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000004F0AD | Q07657
MIPS: YDL225W
NCBI: 1431379 | 2500772 | 6319976 | NP_010056.1
GenBank/EMBL/DDBJ: DAA11640.1 | Z74273
Amino Acid Sequence (or in FASTA format)
       1  MSTASTPPIN LFRRKKEHKR GITYTMLLCG PAGTGKTAFA NNLLETKIFP
      51  HKYQYGKSNA SISSNPEVKV IAPTKVVSFN SKNGIPSYVS EFDPMRANLE
     101  PGITITSTSL ELGGNKDQGK PEMNEDDTVF FNLIMTHGIG ENLDDSLCSE
     151  EVMSYLEQQF DIVLAEETRI KRNPRFEDTR VHVALYFIEP TGHGLREVDV
     201  ELMKSISKYT NVLPIITRAD SFTKEELTQF RKNIMFDVER YNVPIYKFEV
     251  DPEDDDLESM EENQALASLQ PFAIITSDTR DSEGRYVREY PWGIISIDDD
     301  KISDLKVLKN VLFGSHLQEF KDTTQNLLYE NYRSEKLSSV ANAEEIGPNS
     351  TKRQSNAPSL SNFASLISTG QFNSSQTLAN NLRADTPRNQ VSGNFKENEY
     401  EDNGEHDSAE NEQEMSPVRQ LGREIKQENE NLIRSIKTES SPKFLNSPDL
     451  PERTKLRNIS ETVPYVLRHE RILARQQKLE ELEAQSAKEL QKRIQELERK
     501  AHELKLREKL INQNKLNGSS SSINSLQQST RSQIKKNDTY TDLASIASGR
     551  D*                                                    

external links for Shs1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Shs1p
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) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41