Seventh homolog of septin 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Seventh homolog of septin 1

Alternative name(s):
Septation protein 7

Gene names

Name:	SHS1
Synonyms:	SEP7
Ordered Locus Names:	YDL225W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	551 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. Ref.4
Subunit structure	Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with CDC11 and SPA2. Ref.3 Ref.4 Ref.6 Ref.10
Subcellular location	Membrane; Peripheral membrane protein By similarity. Bud neck. Note: Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate By similarity. Ref.4 Ref.8
Post-translational modification	Phosphorylated by GIN4 and CLA4. Phosphorylation state is essential for septin ring dynamics during telophase. Ref.6 Ref.7 Sumoylated during mitosis on the mother cell side of the bud neck. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle. Ref.5
Miscellaneous	Present with 5620 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Membrane
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Inferred from genetic interaction PubMed 18431499. Source: SGD barrier septum assembly Inferred from mutant phenotype PubMed 17603111. Source: SGD cellular bud neck septin ring organization Inferred from mutant phenotype Ref.7. Source: SGD cytokinesis, actomyosin contractile ring assembly Inferred from mutant phenotype PubMed 17603111. Source: SGD exit from mitosis Inferred from mutant phenotype PubMed 12699621. Source: SGD septin ring assembly Inferred from genetic interaction PubMed 17603111. Source: SGD
Cellular_component	cellular bud neck septin ring Inferred from direct assay PubMed 17603111. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell septin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from direct assay PubMed 14597621. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CDC11	P32458	5	EBI-22083,EBI-4178
CDC12	P32468	4	EBI-22083,EBI-4182
GIN4	Q12263	7	EBI-22083,EBI-7595

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 551

551

Seventh homolog of septin 1

PRO_0000173545

Regions

Nucleotide binding

30 – 37

8

GTP By similarity

Nucleotide binding

218 – 226

9

GTP By similarity

Coiled coil

418 – 518

101

Potential

Sites

Binding site

138

1

GTP; via amide nitrogen By similarity

Binding site

288

1

GTP By similarity

Amino acid modifications

Modified residue

23

1

Phosphothreonine Ref.14

Modified residue

63

1

Phosphoserine Ref.14

Modified residue

64

1

Phosphoserine Ref.14

Modified residue

221

1

Phosphoserine Ref.13 Ref.14

Modified residue

374

1

Phosphoserine Ref.14

Modified residue

408

1

Phosphoserine Ref.13 Ref.14

Modified residue

416

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

447

1

Phosphoserine Ref.11 Ref.12 Ref.14

Modified residue

460

1

Phosphoserine Ref.11

Modified residue

519

1

Phosphoserine Ref.12 Ref.14

Modified residue

520

1

Phosphoserine Ref.14

Modified residue

521

1

Phosphoserine Ref.14

Modified residue

522

1

Phosphoserine Ref.14

Modified residue

525

1

Phosphoserine Ref.12 Ref.14

Modified residue

539

1

Phosphothreonine Ref.11 Ref.13 Ref.14

Modified residue

540

1

Phosphotyrosine Ref.14

Modified residue

541

1

Phosphothreonine Ref.14

Modified residue

545

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

548

1

Phosphoserine Ref.12 Ref.13 Ref.14

Cross-link

426

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5

Cross-link

437

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5

Experimental info

Mutagenesis

426

1

K → R: Abolishes sumoylation in vitro; when associated with R-437. Ref.5

Mutagenesis

437

1

K → R: Abolishes sumoylation in vitro; when associated with R-426. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q07657 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: BDA2631061A278F9
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FASTA

551

62,630

        10         20         30         40         50         60 
MSTASTPPIN LFRRKKEHKR GITYTMLLCG PAGTGKTAFA NNLLETKIFP HKYQYGKSNA 

        70         80         90        100        110        120 
SISSNPEVKV IAPTKVVSFN SKNGIPSYVS EFDPMRANLE PGITITSTSL ELGGNKDQGK 

       130        140        150        160        170        180 
PEMNEDDTVF FNLIMTHGIG ENLDDSLCSE EVMSYLEQQF DIVLAEETRI KRNPRFEDTR 

       190        200        210        220        230        240 
VHVALYFIEP TGHGLREVDV ELMKSISKYT NVLPIITRAD SFTKEELTQF RKNIMFDVER 

       250        260        270        280        290        300 
YNVPIYKFEV DPEDDDLESM EENQALASLQ PFAIITSDTR DSEGRYVREY PWGIISIDDD 

       310        320        330        340        350        360 
KISDLKVLKN VLFGSHLQEF KDTTQNLLYE NYRSEKLSSV ANAEEIGPNS TKRQSNAPSL 

       370        380        390        400        410        420 
SNFASLISTG QFNSSQTLAN NLRADTPRNQ VSGNFKENEY EDNGEHDSAE NEQEMSPVRQ 

       430        440        450        460        470        480 
LGREIKQENE NLIRSIKTES SPKFLNSPDL PERTKLRNIS ETVPYVLRHE RILARQQKLE 

       490        500        510        520        530        540 
ELEAQSAKEL QKRIQELERK AHELKLREKL INQNKLNGSS SSINSLQQST RSQIKKNDTY 

       550 
TDLASIASGR D

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"The septins are required for the mitosis-specific activation of the Gin4 kinase." Carroll C.W., Altman R., Schieltz D., Yates J.R. III, Kellogg D. J. Cell Biol. 143:709-717(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH GIN4.
[4]	"Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in Saccharomyces cerevisiae." Mino A., Tanaka K., Kamei T., Umikawa M., Fujiwara T., Takai Y. Biochem. Biophys. Res. Commun. 251:732-736(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPA2.
[5]	"Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins." Johnson E.S., Blobel G. J. Cell Biol. 147:981-994(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-426 AND LYS-437, MUTAGENESIS OF LYS-426 AND LYS-437.
[6]	"Cell cycle-dependent assembly of a Gin4-septin complex." Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R. Mol. Biol. Cell 13:2091-2105(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY GIN4, MASS SPECTROMETRY, IDENTIFICATION IN THE GIN4 COMPLEX.
[7]	"Phosphorylation-dependent regulation of septin dynamics during the cell cycle." Dobbelaere J., Gentry M.S., Hallberg R.L., Barral Y. Dev. Cell 4:345-357(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae." Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S., Chen R.E., Barth P., Alber T., Thorner J. Mol. Biol. Cell 15:4568-4583(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDC11, ASSEMBLY OF THE SEPTIN FILAMENTS.
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-460 AND THR-539, MASS SPECTROMETRY. Strain: YAL6B.
[12]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-447; SER-519; SER-525; SER-545 AND SER-548, MASS SPECTROMETRY. Strain: ADR376.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-408; SER-416; THR-539; SER-545 AND SER-548, MASS SPECTROMETRY.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; SER-63; SER-64; SER-221; SER-374; SER-408; SER-416; SER-447; SER-519; SER-520; SER-521; SER-522; SER-525; THR-539; TYR-540; THR-541; SER-545 AND SER-548, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74273 Genomic DNA. Translation: CAA98804.1. BK006938 Genomic DNA. Translation: DAA11640.1.
PIR	S67788.
RefSeq	NP_010056.1. NM_001180285.1.
3D structure databases
ProteinModelPortal	Q07657.
SMR	Q07657. Positions 22-337.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5596N.
IntAct	Q07657. 30 interactions.
MINT	MINT-542688.
STRING	4932.YDL225W.
Proteomic databases
PaxDb	Q07657.
PeptideAtlas	Q07657.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL225W; YDL225W; YDL225W.
GeneID	851373.
KEGG	sce:YDL225W.
Organism-specific databases
CYGD	YDL225w.
SGD	S000002384. SHS1.
Phylogenomic databases
eggNOG	COG5019.
GeneTree	ENSGT00550000075461.
HOGENOM	HOG000233586.
OMA	TRIKRNP.
OrthoDB	EOG4CJZRV.
Gene expression databases
Genevestigator	Q07657.
GermOnline	YDL225W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. PTHR18884. 1 hit.
Pfam	PF00735. Septin. 2 hits. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
ProtoNet	Search...
Other
NextBio	968498.

Entry information

Entry name

SHS1_YEAST

Accession

Primary (citable) accession number: Q07657
Secondary accession number(s): D6VRD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents