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P39928 (SLN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Osmosensing histidine protein kinase SLN1
EC=2.7.13.3
Alternative name(s):
Osmolarity two-component system protein SLN1
Tyrosine phosphatase-dependent protein 2
Gene names
Name:SLN1
Synonyms:YPD2
Ordered Locus Names:YIL147C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histidine kinase that acts as a osmosensor at the plasma membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in resonse to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, the histidine kinase autophosphorylates His-576. This phosphate is subsequently transferred to Asp-1144, from where it is relayed to 'His-64' of the phosphorelay intermediate protein YPD1. Under high osmolarity conditions, the histidine kinase is no longer active. Ref.5 Ref.6

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subunit structure

Interacts with DJP1, MOG1 and YPD1. Ref.5 Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Potential Ref.7.

Post-translational modification

The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-576 (H1) in the histidine kinase domain (transmitter domain) to Asp-1144 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two SLN1 molecules, rather than intramolecularly. The phosphate group is further transferred to 'His-64' (H2) of YPD1 and finally to 'Asp-554' (D2) of SSK1 or 'Asp-427' (D2) of SKN7.

Miscellaneous

Present with 656 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Contains 1 histidine kinase domain.

Contains 1 response regulatory domain.

Ontologies

Keywords
   Biological processTwo-component regulatory system
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processnegative regulation of protein kinase activity

Inferred from mutant phenotype. Source: SGD

osmosensory signaling pathway via two-component system

Inferred from direct assay Ref.5. Source: SGD

peptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: InterPro

protein autophosphorylation

Inferred from direct assay Ref.5. Source: SGD

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.7. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histidine phosphotransfer kinase activity

Inferred from direct assay. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

osmosensor activity

Inferred from direct assay. Source: SGD

protein binding

Inferred from physical interaction Ref.13. Source: IntAct

two-component response regulator activity

Inferred from electronic annotation. Source: InterPro

two-component sensor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YPD1Q076882EBI-17357,EBI-34423

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220Osmosensing histidine protein kinase SLN1
PRO_0000081405

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4624Helical; Potential
Topological domain47 – 333287Extracellular Potential
Transmembrane334 – 35421Helical; Potential
Topological domain355 – 1220866Cytoplasmic Potential
Domain573 – 928356Histidine kinase
Domain1089 – 1210122Response regulatory

Sites

Metal binding10941Magnesium By similarity
Metal binding10951Magnesium By similarity
Metal binding11441Magnesium By similarity
Metal binding11951Magnesium By similarity

Amino acid modifications

Modified residue4731Phosphoserine Ref.12
Modified residue5761Phosphohistidine; by autocatalysis Ref.5
Modified residue8331Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue9801Phosphoserine Ref.11
Modified residue114414-aspartylphosphate
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis5761H → Q: Inactive. Ref.4
Mutagenesis8911G → D in SLN1-1; slow growth.
Mutagenesis11441D → N: Inactive. Ref.4

Secondary structure

1 ....................... 1220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39928 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 45FFE24A8165486B

FASTA1,220134,435
        10         20         30         40         50         60 
MRFGLPSKLE LTPPFRIGIR TQLTALVSIV ALGSLIILAV TTGVYFTSNY KNLRSDRLYI 

        70         80         90        100        110        120 
AAQLKSSQID QTLNYLYYQA YYLASRDALQ SSLTSYVAGN KSADNWVDSL SVIQKFLSSS 

       130        140        150        160        170        180 
NLFYVAKVYD SSFNAVLNAT NNGTGDLIPE DVLDSLFPLS TDTPLPSSLE TIGILTDPVL 

       190        200        210        220        230        240 
NSTDYLMSMS LPIFANPSII LTDSRVYGYI TIIMSAEGLK SVFNDTTALE HSTIAIISAV 

       250        260        270        280        290        300 
YNSQGKASGY HFVFPPYGSR SDLPQKVFSI KNDTFISSAF RNGKGGSLKQ TNILSTRNTA 

       310        320        330        340        350        360 
LGYSPCSFNL VNWVAIVSQP ESVFLSPATK LAKIITGTVI AIGVFVILLT LPLAHWAVQP 

       370        380        390        400        410        420 
IVRLQKATEL ITEGRGLRPS TPRTISRASS FKRGFSSGFA VPSSLLQFNT AEAGSTTSVS 

       430        440        450        460        470        480 
GHGGSGHGSG AAFSANSSMK SAINLGNEKM SPPEEENKIP NNHTDAKISM DGSLNHDLLG 

       490        500        510        520        530        540 
PHSLRHNDTD RSSNRSHILT TSANLTEARL PDYRRLFSDE LSDLTETFNT MTDALDQHYA 

       550        560        570        580        590        600 
LLEERVRART KQLEAAKIEA EAANEAKTVF IANISHELRT PLNGILGMTA ISMEETDVNK 

       610        620        630        640        650        660 
IRNSLKLIFR SGELLLHILT ELLTFSKNVL QRTKLEKRDF CITDVALQIK SIFGKVAKDQ 

       670        680        690        700        710        720 
RVRLSISLFP NLIRTMVLWG DSNRIIQIVM NLVSNALKFT PVDGTVDVRM KLLGEYDKEL 

       730        740        750        760        770        780 
SEKKQYKEVY IKKGTEVTEN LETTDKYDLP TLSNHRKSVD LESSATSLGS NRDTSTIQEE 

       790        800        810        820        830        840 
ITKRNTVANE SIYKKVNDRE KASNDDVSSI VSTTTSSYDN AIFNSQFNKA PGSDDEEGGN 

       850        860        870        880        890        900 
LGRPIENPKT WVISIEVEDT GPGIDPSLQE SVFHPFVQGD QTLSRQYGGT GLGLSICRQL 

       910        920        930        940        950        960 
ANMMHGTMKL ESKVGVGSKF TFTLPLNQTK EISFADMEFP FEDEFNPESR KNRRVKFSVA 

       970        980        990       1000       1010       1020 
KSIKSRQSTS SVATPATNRS SLTNDVLPEV RSKGKHETKD VGNPNMGREE KNDNGGLEQL 

      1030       1040       1050       1060       1070       1080 
QEKNIKPSIC LTGAEVNEQN SLSSKHRSRH EGLGSVNLDR PFLQSTGTAT SSRNIPTVKD 

      1090       1100       1110       1120       1130       1140 
DDKNETSVKI LVVEDNHVNQ EVIKRMLNLE GIENIELACD GQEAFDKVKE LTSKGENYNM 

      1150       1160       1170       1180       1190       1200 
IFMDVQMPKV DGLLSTKMIR RDLGYTSPIV ALTAFADDSN IKECLESGMN GFLSKPIKRP 

      1210       1220 
KLKTILTEFC AAYQGKKNNK

« Hide

References

« Hide 'large scale' references
[1]"A yeast protein similar to bacterial two-component regulators."
Ota I.M., Varshavsky A.
Science 262:566-569(1993) [PubMed: 8211183] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: S288c / YPH1.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed: 9169870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"A two-component system that regulates an osmosensing MAP kinase cascade in yeast."
Maeda T., Wurgler-Murphy S.M., Saito H.
Nature 369:242-245(1994) [PubMed: 8183345] [Abstract]
Cited for: MUTAGENESIS OF HIS-576 AND ASP-1144.
[5]"Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 two-component osmosensor."
Posas F., Wurgler-Murphy S.M., Maeda T., Witten E.A., Thai T.C., Saito H.
Cell 86:865-875(1996) [PubMed: 8808622] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT HIS-576 AND ASP-1144, INTERACTION WITH YPD1.
[6]"The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p."
Li S., Ault A., Malone C.L., Raitt D., Dean S., Johnston L.H., Deschenes R.J., Fassler J.S.
EMBO J. 17:6952-6962(1998) [PubMed: 9843501] [Abstract]
Cited for: FUNCTION.
[7]"Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p."
Lu J.M.-Y., Deschenes R.J., Fassler J.S.
Eukaryot. Cell 2:1304-1314(2003) [PubMed: 14665464] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction."
Lu J.M.-Y., Deschenes R.J., Fassler J.S.
Eukaryot. Cell 3:1544-1556(2004) [PubMed: 15590828] [Abstract]
Cited for: INTERACTION WITH DJP1 AND MOG1.
[10]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, MASS SPECTROMETRY.
Strain: ADR376.
[11]"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: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833 AND SER-980, MASS SPECTROMETRY.
[12]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-833, MASS SPECTROMETRY.
[13]"The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems."
Xu Q., Porter S.W., West A.H.
Structure 11:1569-1581(2003) [PubMed: 14656441] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1087-1220 IN COMPLEX WITH YPD1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U01835 Unassigned DNA. Translation: AAC48912.1.
Z38059 Genomic DNA. Translation: CAA86131.1.
BK006942 Genomic DNA. Translation: DAA08406.1.
PIRS48387.
RefSeqNP_012119.1. NM_001179495.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OXBX-ray2.30B1087-1220[»]
1OXKX-ray2.10B/D/F/H/J/L1087-1220[»]
2R25X-ray1.70B1086-1218[»]
ProteinModelPortalP39928.
SMRP39928. Positions 566-627, 638-711, 852-928, 1087-1214.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2939N.
IntActP39928. 29 interactions.
MINTMINT-682970.
STRINGP39928.

Proteomic databases

PeptideAtlasP39928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL147C; YIL147C; YIL147C.
GeneID854659.
KEGGsce:YIL147C.
NMPDRfig|4932.3.peg.1641.

Organism-specific databases

CYGDYIL147c.
SGDS000001409. SLN1.

Phylogenomic databases

eggNOGfuNOG04349.
GeneTreeEFGT00050000001181.
HOGENOMHBG398244.
OMAFVQGDQT.
OrthoDBEOG4N8VCT.

Enzyme and pathway databases

BRENDA2.7.13.3. 984.

Gene expression databases

ArrayExpressP39928.
GenevestigatorP39928.
GermOnlineYIL147C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR011006. CheY-like_superfamily.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 2 hits.
KOK11231.
PfamPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF52172. CheY_like. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977226.

Entry information

Entry nameSLN1_YEAST
AccessionPrimary (citable) accession number: P39928
Secondary accession number(s): D6VVE0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IX

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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