MAP kinase kinase PBS2 - Saccharomyces cerevisiae (Baker's yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P08018 (PBS2_YEAST)

Last modified November 3, 2009. Version 104. 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

Hide | Top

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length	668 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	N-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 component	NatB 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 function	ATP 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...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SSU81	P40073	1	EBI-12972,EBI-18140

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 668

668

MAP kinase kinase PBS2

PRO_0000086483

Regions

Domain

360 – 623

264

Protein kinase

Nucleotide binding

366 – 374

ATP By similarity

Compositional bias

91 – 101

Pro-rich

Sites

Active site

485

Proton acceptor By similarity

Binding site

389

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.14 Ref.12

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.12 Ref.13

Modified residue

Phosphoserine Ref.13 Ref.8

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.8

Modified residue

248

Phosphoserine Ref.14 Ref.13

Modified residue

269

Phosphoserine Ref.13

Modified residue

514

Phosphoserine Ref.6 Ref.14

Modified residue

518

Phosphothreonine Ref.6

Experimental info

Mutagenesis

P → S in PBS2-13; loss of SH3-domain interaction. Ref.6

Mutagenesis

389

K → M: Loss of activity. Ref.6

Mutagenesis

514

S → A: Loss of phosphorylation. Ref.6

Mutagenesis

518

T → A: Loss of phosphorylation. Ref.6

Sequence conflict

222 – 223

AV → GL in AAA16819. Ref.3

Sequence conflict

222 – 223

AV → GL in AAA20392. Ref.3

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P08018-1 [UniParc].

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

FASTA

668

72,720

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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. 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.

Hide | Top

Cross-references

Sequence databases

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

PIR

S56909.

RefSeq

NP_012407.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VKN	X-ray	2.05	C	92-103	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2368N.

IntAct

P08018. 12 interactions.

STRING

P08018.

Proteomic databases

PeptideAtlas

P08018.

PRIDE

P08018.

Genome annotation databases

Ensembl

YJL128C; YJL128C; YJL128C; Saccharomyces cerevisiae. [Genome view]

GeneID

853313.

GenomeReviews

Gene locus YJL128C in contig Y13136_GR.

KEGG

sce:YJL128C.

NMPDR

fig|4932.3.peg.3374.

Organism-specific databases

CYGD

YJL128c.

SGD

S000003664. PBS2.

Phylogenomic databases

HOGENOM

P08018.

OMA

MELEVLH.

Enzyme and pathway databases

BRENDA

2.7.12.2. 250.

Gene expression databases

ArrayExpress

P08018.

Genevestigator

P08018.

GermOnline

YJL128C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

973654.

Hide | Top

Entry information

Entry name

PBS2_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents