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Reviewed, UniProtKB/Swiss-Prot P08018 (PBS2_YEAST)

Last modified November 3, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    MAP kinase kinase PBS2
    EC=2.7.12.2
Alternative name(s):
    Polymyxin B resistance protein 2
    Suppressor of fluoride sensitivity 4
Gene names
Name: PBS2
Synonyms: HOG4, SFS4, SSK4
Ordered Locus Names: YJL128C
ORF Names: J0699
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue. Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with NBP2 and PTC1. Ref.11

Subcellular location

Cytoplasm. Ref.9

Domain

Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1. Ref.6

Post-translational modification

Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.

Miscellaneous

Present with 2160 molecules/cell in log phase SD medium. Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processN-terminal peptidyl-methionine acetylation

Inferred from genetic interaction. Source: UniProtKB

actin filament organization

Inferred from mutant phenotype. Source: SGD

activation of MAPK activity involved in osmosensory signaling pathway Ref.6

Inferred from mutant phenotype. Source: SGD

hyperosmotic response Ref.7

Inferred from mutant phenotype. Source: SGD

negative regulation of transposition, RNA-mediated

Inferred from mutant phenotype. Source: SGD

nuclear translocation of MAPK involved in osmosensory signaling pathway

Inferred from mutant phenotype. Source: SGD

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentNatB complex

Inferred from direct assay. Source: UniProtKB

cellular bud neck

Inferred from direct assay. Source: SGD

cellular bud tip

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity Ref.6

Inferred from mutant phenotype. Source: SGD

MAP-kinase scaffold activity

Inferred from physical interaction. Source: SGD

peptide alpha-N-acetyltransferase activity

Inferred from mutant phenotype. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSU81P400731EBI-12972,EBI-18140

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668MAP kinase kinase PBS2
PRO_0000086483

Regions

Domain360 – 623264Protein kinase
Nucleotide binding366 – 3749ATP By similarity
Compositional bias91 – 10111Pro-rich

Sites

Active site4851Proton acceptor By similarity
Binding site3891ATP By similarity

Amino acid modifications

Modified residue91Phosphoserine Ref.14
Modified residue381Phosphoserine Ref.14 Ref.12
Modified residue661Phosphoserine Ref.13
Modified residue681Phosphoserine Ref.12 Ref.13
Modified residue711Phosphoserine Ref.13 Ref.8
Modified residue811Phosphoserine Ref.13
Modified residue831Phosphoserine Ref.8
Modified residue2481Phosphoserine Ref.14 Ref.13
Modified residue2691Phosphoserine Ref.13
Modified residue5141Phosphoserine Ref.6 Ref.14
Modified residue5181Phosphothreonine Ref.6

Experimental info

Mutagenesis961P → S in PBS2-13; loss of SH3-domain interaction. Ref.6
Mutagenesis3891K → M: Loss of activity. Ref.6
Mutagenesis5141S → A: Loss of phosphorylation. Ref.6
Mutagenesis5181T → A: Loss of phosphorylation. Ref.6
Sequence conflict222 – 2232AV → GL in AAA16819. Ref.3
Sequence conflict222 – 2232AV → GL in AAA20392. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08018-1 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: C7E23A77ABD36267

FASTA66872,720
        10         20         30         40         50         60 
MEDKFANLSL HEKTGKSSIQ LNEQTGSDNG SAVKRTSSTS SHYNNINADL HARVKAFQEQ 

        70         80         90        100        110        120 
RALKRSASVG SNQSEQDKGS SQSPKHIQQI VNKPLPPLPV AGSSKVSQRM SSQVVQASSK 

       130        140        150        160        170        180 
STLKNVLDNQ ETQNITDVNI NIDTTKITAT TIGVNTGLPA TDITPSVSNT ASATHKAQLL 

       190        200        210        220        230        240 
NPNRRAPRRP LSTQHPTRPN VAPHKAPAII NTPKQSLSAR RAVKLPPGGM SLKMPTKTAQ 

       250        260        270        280        290        300 
QPQQFAPSPS NKKHIETLSN SKVVEGKRSN PGSLINGVQS TSTSSSTEGP HDTVGTTPRT 

       310        320        330        340        350        360 
GNSNNSSNSG SSGGGGLFAN FSKYVDIKSG SLNFAGKLSL SSKGIDFSNG SSSRITLDEL 

       370        380        390        400        410        420 
EFLDELGHGN YGNVSKVLHK PTNVIMATKE VRLELDEAKF RQILMELEVL HKCNSPYIVD 

       430        440        450        460        470        480 
FYGAFFIEGA VYMCMEYMDG GSLDKIYDES SEIGGIDEPQ LAFIANAVIH GLKELKEQHN 

       490        500        510        520        530        540 
IIHRDVKPTN ILCSANQGTV KLCDFGVSGN LVASLAKTNI GCQSYMAPER IKSLNPDRAT 

       550        560        570        580        590        600 
YTVQSDIWSL GLSILEMALG RYPYPPETYD NIFSQLSAIV DGPPPRLPSD KFSSDAQDFV 

       610        620        630        640        650        660 
SLCLQKIPER RPTYAALTEH PWLVKYRNQD VHMSEYITER LERRNKILRE RGENGLSKNV 


PALHMGGL 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of a gene conferring polymyxin B resistance on yeast: similarity of the predicted polypeptide to protein kinases."
Boguslawski G., Polazzi J.O.
Proc. Natl. Acad. Sci. U.S.A. 84:5848-5852(1987) [PubMed: 3039511] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"PBS2, a yeast gene encoding a putative protein kinase, interacts with the RAS2 pathway and affects osmotic sensitivity of Saccharomyces cerevisiae."
Boguslawski G.
J. Gen. Microbiol. 138:2425-2432(1992) [PubMed: 1479360] [Abstract]
Cited for: SEQUENCE REVISION TO 222-223 AND 668.
[3]"Mutational analysis of Saccharomyces cerevisiae ARF1."
Kahn R.A., Clark J., Rulka C., Stearns T., Zhang C.J., Randazzo P.A., Terui T., Cavenagh M.
J. Biol. Chem. 270:143-150(1995) [PubMed: 7814365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta elements and a Ty4 transposon."
Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.
Yeast 12:1471-1474(1996) [PubMed: 8948101] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[5]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[6]"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: 7624781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 91-101, DOMAIN, PHOSPHORYLATION AT SER-514 AND THR-518, MUTAGENESIS OF PRO-96; LYS-389; SER-514 AND THR-518.
[7]"An osmosensing signal transduction pathway in yeast."
Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C.
Science 259:1760-1763(1993) [PubMed: 7681220] [Abstract]
Cited for: FUNCTION.
[8]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-83, MASS SPECTROMETRY.
[9]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"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].
[11]"Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway."
Mapes J., Ota I.M.
EMBO J. 23:302-311(2004) [PubMed: 14685261] [Abstract]
Cited for: INTERACTION WITH PTC1 AND PBS2.
[12]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-68, MASS SPECTROMETRY.
[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: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-68; SER-71; SER-81; SER-248 AND SER-269, 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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-38; SER-248 AND SER-514, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

J02946 Unassigned DNA. Translation: AAA16819.1.
U12237 Genomic DNA. Translation: AAA20392.1.
Z49403 Genomic DNA. Translation: CAA89423.1.
PIRS56909.
RefSeqNP_012407.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VKNX-ray2.05C92-103[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2368N.
IntActP08018. 12 interactions.
STRINGP08018.

Proteomic databases

PeptideAtlasP08018.
PRIDEP08018.

Genome annotation databases

EnsemblYJL128C; YJL128C; YJL128C; Saccharomyces cerevisiae. [Genome view]
GeneID853313.
GenomeReviewsGene locus YJL128C in contig Y13136_GR.
KEGGsce:YJL128C.
NMPDRfig|4932.3.peg.3374.

Organism-specific databases

CYGDYJL128c.
SGDS000003664. PBS2.

Phylogenomic databases

HOGENOMP08018.
OMAMELEVLH.

Enzyme and pathway databases

BRENDA2.7.12.2. 250.

Gene expression databases

ArrayExpressP08018.
GenevestigatorP08018.
GermOnlineYJL128C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio973654.

Entry information

Entry namePBS2_YEAST
AccessionPrimary (citable) accession number: P08018
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 6, 2005
Last modified: November 3, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome X

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents