High osmolarity signaling protein SHO1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40073 (SHO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
High osmolarity signaling protein SHO1

Alternative name(s):
Osmosensor SHO1
Suppressor of SUA8-1 mutation
Synthetic high osmolarity-sensitive protein 1

Gene names

Name:	SHO1
Synonyms:	SSU81
Ordered Locus Names:	YER118C

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	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway. Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.27 Ref.28 Ref.29
Subunit structure	Forms homooligomers. Interacts (via the SH3 domain) with PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase II. Ref.5 Ref.7 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25
Subcellular location	Cell membrane; Multi-pass membrane protein. Bud. Bud neck. Cell projection. Note: Localizes at the tip of the mating projection during conjugation. Ref.7 Ref.11 Ref.14 Ref.23
Miscellaneous	Present with 2330 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SHO1 family. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cell membrane Cell projection Membrane
Domain	SH3 domain Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to heat Inferred from mutant phenotype Ref.13. Source: SGD cytokinesis Inferred from mutant phenotype PubMed 22623719. Source: SGD establishment of cell polarity Inferred from genetic interaction Ref.28. Source: SGD osmosensory signaling pathway Inferred from genetic interaction Ref.2. Source: SGD signal transduction involved in filamentous growth Inferred from mutant phenotype Ref.6. Source: SGD
Cellular_component	HICS complex Inferred from physical interaction PubMed 22623719. Source: SGD cellular bud neck Inferred from direct assay Ref.11. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD mating projection tip Inferred from direct assay Ref.14. Source: SGD plasma membrane part Inferred from direct assay Ref.11. Source: SGD
Molecular_function	MAP-kinase scaffold activity Inferred from mutant phenotype Ref.21. Source: SGD osmosensor activity Inferred from physical interaction Ref.2. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
FUS1	P11710	3	EBI-18140,EBI-7179
LAS17	Q12446	8	EBI-18140,EBI-10022
PBS2	P08018	2	EBI-18140,EBI-12972

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

High osmolarity signaling protein SHO1

PRO_0000072231

Regions

Topological domain

1 – 32

Cytoplasmic Potential

Transmembrane

33 – 53

Helical; Potential

Topological domain

54 – 65

Extracellular Potential

Transmembrane

66 – 86

Helical; Potential

Topological domain

87 – 93

Cytoplasmic Potential

Transmembrane

94 – 114

Helical; Potential

Topological domain

115 – 122

Extracellular Potential

Transmembrane

123 – 143

Helical; Potential

Topological domain

144 – 367

224

Cytoplasmic Potential

Domain

300 – 361

SH3

Amino acid modifications

Modified residue

166

Phosphoserine Ref.25

Modified residue

184

Phosphothreonine Ref.26

Glycosylation

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

166

S → E: Diminishes the formation of oligomers, dampens activation of the HOG1 kinase, and impairs growth in high-salt or sorbitol conditions. Ref.25

Mutagenesis

309

Y → A: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Ref.21

Mutagenesis

317

D → I or H: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Ref.21

Mutagenesis

355

Y → A, F, I or M: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Ref.21

Secondary structure

367

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40073 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E467A4D50AA3EDB6
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FASTA

367

41,126

        10         20         30         40         50         60 
MSISSKIRPT PRKPSRMATD HSFKMKKFYA DPFAISSISL AIVSWVIAIG GSISSASTNE 

        70         80         90        100        110        120 
SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI AVAFVYNTNS ATNLVYADGP 

       130        140        150        160        170        180 
KKAAASAGVI LLSIINLIWI LYYGGDNASP TNRWIDSFSI KGIRPSPLEN SLHRARRRGN 

       190        200        210        220        230        240 
RNTTPYQNNV YNDAIRDSGY ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH 

       250        260        270        280        290        300 
LNTLQQRINS ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN 

       310        320        330        340        350        360 
FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI IPSNYVQLID 


GPEEMHR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Berroteran R.W., Hampsey M. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor." Maeda T., Takekawa M., Saito H. Science 269:554-558(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK." Posas F., Saito H. Science 276:1702-1705(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PBS2.
[6]	"The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae." O'Rourke S.M., Herskowitz I. Genes Dev. 12:2874-2886(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway." Raitt D.C., Posas F., Saito H. EMBO J. 19:4623-4631(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PBS2.
[8]	"The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion." Singh K.K. Free Radic. Biol. Med. 29:1043-1050(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Calcofluor antifungal action depends on chitin and a functional high-osmolarity glycerol response (HOG) pathway: evidence for a physiological role of the Saccharomyces cerevisiae HOG pathway under noninducing conditions." Garcia-Rodriguez L.J., Duran A., Roncero C. J. Bacteriol. 182:2428-2437(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway." Van Wuytswinkel O., Reiser V., Siderius M., Kelders M.C., Ammerer G., Ruis H., Mager W.H. Mol. Microbiol. 37:382-397(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42." Reiser V., Salah S.M., Ammerer G. Nat. Cell Biol. 2:620-627(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance in Saccharomyces cerevisisae." Toh-e A., Oguchi T. Genes Genet. Syst. 76:393-410(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress." Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K., Ota I.M. Eukaryot. Cell 1:163-173(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Cell surface polarization during yeast mating." Bagnat M., Simons K. Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"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].
[16]	"Optimization of specificity in a cellular protein interaction network by negative selection." Zarrinpar A., Park S.H., Lim W.A. Nature 426:676-680(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, INTERACTION WITH PBS2.
[17]	"Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms." Park S.H., Zarrinpar A., Lim W.A. Science 299:1061-1064(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous growth pathway in yeast." Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K., Neal C., Delrow J., Bardwell L., Sprague G.F. Jr. Genes Dev. 18:1695-1708(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MSB2.
[19]	"Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating." Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K., Ritchie S., Petryshen T.L., Boone C. Genetics 166:67-77(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FUS1.
[20]	"Unique and redundant roles for HOG MAPK pathway components as revealed by whole-genome expression analysis." O'Rourke S.M., Herskowitz I. Mol. Biol. Cell 15:532-542(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast." Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R. Mol. Cell 14:813-823(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PBS2, DOMAIN, MUTAGENESIS OF TYR-309; ASP-317 AND TYR-355.
[22]	"Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway." Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A. Mol. Cell 14:825-832(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH STE11.
[23]	"Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway." Tatebayashi K., Yamamoto K., Tanaka K., Tomida T., Maruoka T., Kasukawa E., Saito H. EMBO J. 25:3033-3044(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STE11 AND STE50.
[24]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[25]	"A systems-biology analysis of feedback inhibition in the Sho1 osmotic-stress-response pathway." Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H., Elston T.C., Dohlman H.G. Curr. Biol. 17:659-667(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, SUBUNIT.
[26]	"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-184, MASS SPECTROMETRY.
[27]	"Signal processing by the HOG MAP kinase pathway." Hersen P., McClean M.N., Mahadevan L., Ramanathan S. Proc. Natl. Acad. Sci. U.S.A. 105:7165-7170(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"The signaling mucins Msb2 and Hkr1 differentially regulate the filamentation mitogen-activated protein kinase pathway and contribute to a multimodal response." Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J. Mol. Biol. Cell 20:3101-3114(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[29]	"Dynamic signaling in the Hog1 MAPK pathway relies on high basal signal transduction." Macia J., Regot S., Peeters T., Conde N., Sole R., Posas F. Sci. Signal. 2:RA13-RA13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Structural genomics of yeast SH3 domains." Kursula P., Kursula I., Song Y.H., Paraskevopoulos M., Wilmanns M. Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 298-367.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U15653 Genomic DNA. Translation: AAA61904.1.
L41926 Genomic DNA. Translation: AAC41664.1.
U18916 Genomic DNA. Translation: AAC03216.1.
BK006939 Genomic DNA. Translation: DAA07778.1.

PIR

S50621.

RefSeq

NP_011043.1. NM_001179008.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VKN	X-ray	2.05	A	298-367	[»]

ProteinModelPortal

P40073.

SMR

P40073. Positions 299-364.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2472N.

IntAct

P40073. 43 interactions.

MINT

MINT-518897.

STRING

4932.YER118C.

Proteomic databases

PaxDb

P40073.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YER118C; YER118C; YER118C.

GeneID

856854.

KEGG

sce:YER118C.

Organism-specific databases

CYGD

YER118c.

SGD

S000000920. SHO1.

Phylogenomic databases

eggNOG

NOG44108.

HOGENOM

HOG000174182.

K11246.

OMA

DAYEISF.

OrthoDB

EOG42VCRD.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30282-MONOMER.

Gene expression databases

Genevestigator

P40073.

GermOnline

YER118C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40073.

NextBio

983195.

Entry information

Entry name

SHO1_YEAST

Accession

Primary (citable) accession number: P40073
Secondary accession number(s): D3DM24

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 116 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 V

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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

Amino acid modifications

Experimental info

Secondary structure

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents