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P08018 (PBS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 149. 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

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
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.8 Ref.9 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with NBP2, PTC1, SHO1 AND STE11. Ref.9 Ref.12 Ref.13 Ref.14

Subcellular location

Cytoplasm Ref.10.

Domain

Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1. Ref.7

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.

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
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK import into nucleus involved in osmosensory signaling pathway

Inferred from mutant phenotype PubMed 15707964. Source: SGD

N-terminal peptidyl-methionine acetylation

Inferred from genetic interaction PubMed 12783868. Source: UniProtKB

actin filament organization

Inferred from mutant phenotype PubMed 7941729. Source: SGD

activation of MAPK activity involved in osmosensory signaling pathway

Inferred from mutant phenotype Ref.7. Source: SGD

cellular response to heat

Inferred from mutant phenotype PubMed 12455951. Source: SGD

hyperosmotic response

Inferred from mutant phenotype Ref.8. Source: SGD

osmosensory signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNatB complex

Inferred from direct assay PubMed 12783868. Source: UniProtKB

cellular bud neck

Inferred from direct assay PubMed 10980703. Source: SGD

cellular bud tip

Inferred from direct assay PubMed 10980703. Source: SGD

cytoplasm

Inferred from direct assay PubMed 9755161. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from mutant phenotype Ref.7. Source: SGD

MAP-kinase scaffold activity

Inferred from physical interaction Ref.14PubMed 15200959. Source: SGD

peptide alpha-N-acetyltransferase activity

Inferred from mutant phenotype PubMed 12783868. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12783868. 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

NBP2Q121632EBI-12972,EBI-34713
SHO1P400735EBI-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 residue681Phosphoserine Ref.16
Modified residue2691Phosphoserine Ref.18
Modified residue5141Phosphoserine Ref.7 Ref.17
Modified residue5181Phosphothreonine Ref.7

Experimental info

Mutagenesis961P → S in PBS2-13; loss of SH3-domain interaction. Ref.7
Mutagenesis3891K → M: Loss of activity. Ref.7
Mutagenesis5141S → A: Loss of phosphorylation. Ref.7
Mutagenesis5181T → A: Loss of phosphorylation. Ref.7
Sequence conflict222 – 2232GL → AV Ref.4
Sequence conflict222 – 2232GL → AV in CAA89423. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P08018 [UniParc].

Last modified September 21, 2011. Version 4.
Checksum: 9BC3435BDAFE8019

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 RGLKLPPGGM 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 222-223.
Strain: ATCC 204508 / S288c.
[7]"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 OF 91-101, DOMAIN, PHOSPHORYLATION AT SER-514 AND THR-518, MUTAGENESIS OF PRO-96; LYS-389; SER-514 AND THR-518.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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, INTERACTION WITH SHO1.
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"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].
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBP2 AND PTC1.
[13]"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 SHO1.
[14]"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: INTERACTION WITH SHO1 AND STE11.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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 SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02946 Unassigned DNA. Translation: AAA16819.1.
U12237 Genomic DNA. Translation: AAA20392.1.
Z49403 Genomic DNA. Translation: CAA89423.1.
BK006943 Genomic DNA. Translation: DAA08673.2.
PIRS56909.
RefSeqNP_012407.2. NM_001181561.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VKNX-ray2.05C92-103[»]
ProteinModelPortalP08018.
SMRP08018. Positions 271-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33628. 284 interactions.
DIPDIP-2368N.
IntActP08018. 21 interactions.
MINTMINT-546167.
STRING4932.YJL128C.

Proteomic databases

MaxQBP08018.
PaxDbP08018.
PeptideAtlasP08018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL128C; YJL128C; YJL128C.
GeneID853313.
KEGGsce:YJL128C.

Organism-specific databases

CYGDYJL128c.
SGDS000003664. PBS2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00690000101918.
HOGENOMHOG000234206.
KOK11227.
OMATNILCSA.
OrthoDBEOG7380F1.

Enzyme and pathway databases

BioCycYEAST:G3O-31578-MONOMER.
BRENDA2.7.12.2. 984.

Gene expression databases

GenevestigatorP08018.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08018.
NextBio973654.
PROP08018.

Entry information

Entry namePBS2_YEAST
AccessionPrimary (citable) accession number: P08018
Secondary accession number(s): D6VW57
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 21, 2011
Last modified: June 11, 2014
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references