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Protein

Seventh homolog of septin 1

Gene

SHS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381GTP; via amide nitrogenBy similarity
Binding sitei288 – 2881GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378GTPBy similarity
Nucleotide bindingi218 – 2269GTPBy similarity

GO - Molecular functioni

  • GTP binding Source: SGD

GO - Biological processi

  • actomyosin contractile ring assembly Source: SGD
  • barrier septum assembly Source: SGD
  • cellular bud neck septin ring organization Source: SGD
  • endoplasmic reticulum polarization Source: SGD
  • exit from mitosis Source: SGD
  • G1/S transition of mitotic cell cycle Source: SGD
  • protein localization to bud neck Source: SGD
  • septin ring assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29605-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Seventh homolog of septin 1
Alternative name(s):
Septation protein 7
Gene namesi
Name:SHS1
Synonyms:SEP7
Ordered Locus Names:YDL225W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL225W.
SGDiS000002384. SHS1.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck septin ring Source: SGD
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi426 – 4261K → R: Abolishes sumoylation in vitro; when associated with R-437. 1 Publication
Mutagenesisi437 – 4371K → R: Abolishes sumoylation in vitro; when associated with R-426. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 551550Seventh homolog of septin 1PRO_0000173545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei400 – 4001PhosphotyrosineCombined sources
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei416 – 4161PhosphoserineCombined sources
Cross-linki426 – 426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki437 – 437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei447 – 4471PhosphoserineCombined sources
Modified residuei460 – 4601PhosphoserineCombined sources
Modified residuei519 – 5191PhosphoserineCombined sources
Modified residuei520 – 5201PhosphoserineCombined sources
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei525 – 5251PhosphoserineCombined sources
Modified residuei539 – 5391PhosphothreonineCombined sources
Modified residuei545 – 5451PhosphoserineCombined sources
Modified residuei548 – 5481PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by GIN4 and CLA4. Phosphorylation state is essential for septin ring dynamics during telophase.2 Publications
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ07657.
PeptideAtlasiQ07657.

PTM databases

iPTMnetiQ07657.

Interactioni

Subunit structurei

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 SPA2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC11P324585EBI-22083,EBI-4178
CDC12P324684EBI-22083,EBI-4182
GIN4Q122637EBI-22083,EBI-7595
SCS2P400754EBI-22083,EBI-16735
YMR124WP395235EBI-22083,EBI-27256

Protein-protein interaction databases

BioGridi31885. 161 interactions.
DIPiDIP-5596N.
IntActiQ07657. 22 interactions.
MINTiMINT-542688.

Structurei

3D structure databases

ProteinModelPortaliQ07657.
SMRiQ07657. Positions 20-47, 141-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 339320Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili418 – 518101Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00740000115641.
HOGENOMiHOG000233586.
InParanoidiQ07657.
KOiK16946.
OMAiYLKQQFD.
OrthoDBiEOG76HQBH.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 3 hits.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07657-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTASTPPIN LFRRKKEHKR GITYTMLLCG PAGTGKTAFA NNLLETKIFP
60 70 80 90 100
HKYQYGKSNA SISSNPEVKV IAPTKVVSFN SKNGIPSYVS EFDPMRANLE
110 120 130 140 150
PGITITSTSL ELGGNKDQGK PEMNEDDTVF FNLIMTHGIG ENLDDSLCSE
160 170 180 190 200
EVMSYLEQQF DIVLAEETRI KRNPRFEDTR VHVALYFIEP TGHGLREVDV
210 220 230 240 250
ELMKSISKYT NVLPIITRAD SFTKEELTQF RKNIMFDVER YNVPIYKFEV
260 270 280 290 300
DPEDDDLESM EENQALASLQ PFAIITSDTR DSEGRYVREY PWGIISIDDD
310 320 330 340 350
KISDLKVLKN VLFGSHLQEF KDTTQNLLYE NYRSEKLSSV ANAEEIGPNS
360 370 380 390 400
TKRQSNAPSL SNFASLISTG QFNSSQTLAN NLRADTPRNQ VSGNFKENEY
410 420 430 440 450
EDNGEHDSAE NEQEMSPVRQ LGREIKQENE NLIRSIKTES SPKFLNSPDL
460 470 480 490 500
PERTKLRNIS ETVPYVLRHE RILARQQKLE ELEAQSAKEL QKRIQELERK
510 520 530 540 550
AHELKLREKL INQNKLNGSS SSINSLQQST RSQIKKNDTY TDLASIASGR

D
Length:551
Mass (Da):62,630
Last modified:November 1, 1997 - v1
Checksum:iBDA2631061A278F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74273 Genomic DNA. Translation: CAA98804.1.
BK006938 Genomic DNA. Translation: DAA11640.1.
PIRiS67788.
RefSeqiNP_010056.1. NM_001180285.1.

Genome annotation databases

EnsemblFungiiYDL225W; YDL225W; YDL225W.
GeneIDi851373.
KEGGisce:YDL225W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74273 Genomic DNA. Translation: CAA98804.1.
BK006938 Genomic DNA. Translation: DAA11640.1.
PIRiS67788.
RefSeqiNP_010056.1. NM_001180285.1.

3D structure databases

ProteinModelPortaliQ07657.
SMRiQ07657. Positions 20-47, 141-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31885. 161 interactions.
DIPiDIP-5596N.
IntActiQ07657. 22 interactions.
MINTiMINT-542688.

PTM databases

iPTMnetiQ07657.

Proteomic databases

MaxQBiQ07657.
PeptideAtlasiQ07657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL225W; YDL225W; YDL225W.
GeneIDi851373.
KEGGisce:YDL225W.

Organism-specific databases

EuPathDBiFungiDB:YDL225W.
SGDiS000002384. SHS1.

Phylogenomic databases

GeneTreeiENSGT00740000115641.
HOGENOMiHOG000233586.
InParanoidiQ07657.
KOiK16946.
OMAiYLKQQFD.
OrthoDBiEOG76HQBH.

Enzyme and pathway databases

BioCyciYEAST:G3O-29605-MONOMER.

Miscellaneous databases

PROiQ07657.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 3 hits.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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, IDENTIFICATION BY 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "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 SER-408; SER-416; SER-447; SER-545 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-400; SER-408; SER-416; SER-447; SER-460; SER-519; SER-520; SER-522; SER-525; THR-539; SER-545 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSHS1_YEAST
AccessioniPrimary (citable) accession number: Q07657
Secondary accession number(s): D6VRD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5620 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.