P40073 · SHO1_YEAST
- ProteinHigh osmolarity signaling protein SHO1
- GeneSHO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids367 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Miscellaneous
Present with 2330 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell periphery | |
Cellular Component | cellular bud | |
Cellular Component | cellular bud neck | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | HICS complex | |
Cellular Component | mating projection tip | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | MAP-kinase scaffold activity | |
Molecular Function | osmosensor activity | |
Biological Process | establishment of cell polarity | |
Biological Process | mitotic cytokinetic process | |
Biological Process | osmosensory signaling pathway | |
Biological Process | osmosensory signaling pathway via Sho1 osmosensor | |
Biological Process | regulation of actin filament polymerization | |
Biological Process | signal transduction involved in filamentous growth |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHigh osmolarity signaling protein SHO1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40073
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localizes at the tip of the mating projection during conjugation.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-32 | Cytoplasmic | ||||
Sequence: MSISSKIRPTPRKPSRMATDHSFKMKKFYADP | ||||||
Transmembrane | 33-53 | Helical | ||||
Sequence: FAISSISLAIVSWVIAIGGSI | ||||||
Topological domain | 54-65 | Extracellular | ||||
Sequence: SSASTNESFPRF | ||||||
Transmembrane | 66-86 | Helical | ||||
Sequence: TWWGIVYQFLIICSLMLFYCF | ||||||
Topological domain | 87-93 | Cytoplasmic | ||||
Sequence: DLVDHYR | ||||||
Transmembrane | 94-114 | Helical | ||||
Sequence: IFITTSIAVAFVYNTNSATNL | ||||||
Topological domain | 115-122 | Extracellular | ||||
Sequence: VYADGPKK | ||||||
Transmembrane | 123-143 | Helical | ||||
Sequence: AAASAGVILLSIINLIWILYY | ||||||
Topological domain | 144-367 | Cytoplasmic | ||||
Sequence: GGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGNRNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLHLNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDNFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDGPEEMHR |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 166 | Diminishes the formation of oligomers, dampens activation of the HOG1 kinase, and impairs growth in high-salt or sorbitol conditions. | ||||
Sequence: S → E | ||||||
Mutagenesis | 309 | Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 317 | Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. | ||||
Sequence: D → I or H | ||||||
Mutagenesis | 355 | Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. | ||||
Sequence: Y → A, F, I, or M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000072231 | 1-367 | High osmolarity signaling protein SHO1 | |||
Sequence: MSISSKIRPTPRKPSRMATDHSFKMKKFYADPFAISSISLAIVSWVIAIGGSISSASTNESFPRFTWWGIVYQFLIICSLMLFYCFDLVDHYRIFITTSIAVAFVYNTNSATNLVYADGPKKAAASAGVILLSIINLIWILYYGGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGNRNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLHLNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDNFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDGPEEMHR | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms homooligomers. Interacts (via the SH3 domain) with PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase II.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40073 | AAD14 P42884 | 2 | EBI-18140, EBI-1994 | |
BINARY | P40073 | BCH2 P36122 | 2 | EBI-18140, EBI-26374 | |
BINARY | P40073 | CYK3 Q07533 | 4 | EBI-18140, EBI-31510 | |
BINARY | P40073 | FUS1 P11710 | 7 | EBI-18140, EBI-7179 | |
BINARY | P40073 | GIP2 P40036 | 2 | EBI-18140, EBI-7612 | |
BINARY | P40073 | HOF1 Q05080 | 5 | EBI-18140, EBI-5412 | |
BINARY | P40073 | INN1 P53901 | 4 | EBI-18140, EBI-28955 | |
BINARY | P40073 | LAS17 Q12446 | 5 | EBI-18140, EBI-10022 | |
BINARY | P40073 | LCL3 P53153 | 2 | EBI-18140, EBI-23857 | |
BINARY | P40073 | MSB1 P21339 | 2 | EBI-18140, EBI-11322 | |
BINARY | P40073 | PBS2 P08018 | 8 | EBI-18140, EBI-12972 | |
BINARY | P40073 | PCF11 P39081 | 2 | EBI-18140, EBI-12980 | |
BINARY | P40073 | RGA1 P39083 | 2 | EBI-18140, EBI-15044 | |
BINARY | P40073 | STE11 P23561 | 3 | EBI-18140, EBI-18259 | |
BINARY | P40073 | STE50 P25344 | 3 | EBI-18140, EBI-18305 | |
BINARY | P40073 | TUS1 Q06412 | 3 | EBI-18140, EBI-37117 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 252-276 | Disordered | ||||
Sequence: SNAKETNDNSNNQTNTNIGNTFDTD | ||||||
Domain | 300-361 | SH3 | ||||
Sequence: NFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDG |
Sequence similarities
Belongs to the SHO1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)41,126
- Last updated1995-02-01 v1
- ChecksumE467A4D50AA3EDB6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U15653 EMBL· GenBank· DDBJ | AAA61904.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L41926 EMBL· GenBank· DDBJ | AAC41664.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18916 EMBL· GenBank· DDBJ | AAC03216.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07778.1 EMBL· GenBank· DDBJ | Genomic DNA |