MAP kinase kinase PBS2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P08018 (PBS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	668 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with NBP2, PTC1, SHO1 AND STE11. Ref.9 Ref.13 Ref.14 Ref.15
Subcellular location	Cytoplasm Ref.11.
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 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 Reference proteome
Gene Ontology (GO)
Biological_process	MAPK 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 response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NatB 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
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Inferred from mutant phenotype Ref.7. Source: SGD peptide alpha-N-acetyltransferase activity Inferred from mutant phenotype 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
SHO1	P40073	2	EBI-12972,EBI-18140

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.18

Modified residue

Phosphoserine Ref.16 Ref.18

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine Ref.16 Ref.17

Modified residue

Phosphoserine Ref.10 Ref.17

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine Ref.10

Modified residue

248

Phosphoserine Ref.17 Ref.18

Modified residue

269

Phosphoserine Ref.17

Modified residue

514

Phosphoserine Ref.7 Ref.18

Modified residue

518

Phosphothreonine Ref.7

Experimental info

Mutagenesis

P → S in PBS2-13; loss of SH3-domain interaction. Ref.7

Mutagenesis

389

K → M: Loss of activity. Ref.7

Mutagenesis

514

S → A: Loss of phosphorylation. Ref.7

Mutagenesis

518

T → A: Loss of phosphorylation. Ref.7

Sequence conflict

222 – 223

GL → AV Ref.4

Sequence conflict

222 – 223

GL → AV in CAA89423. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P08018 [UniParc].

Last modified September 21, 2011. Version 4.
Checksum: 9BC3435BDAFE8019
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 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' 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] [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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-83, MASS SPECTROMETRY. Strain: 2124.
[11]	"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].
[12]	"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].
[13]	"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.
[14]	"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.
[15]	"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.
[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-38 AND SER-68, MASS SPECTROMETRY.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-68; SER-71; SER-81; SER-248 AND SER-269, MASS SPECTROMETRY.
[18]	"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-9; SER-38; SER-248 AND SER-514, MASS SPECTROMETRY.
+	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.

PIR

S56909.

RefSeq

NP_012407.2. NM_001181561.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P08018.

SMR

P08018. Positions 271-630.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2368N.

IntAct

P08018. 19 interactions.

MINT

MINT-546167.

STRING

4932.YJL128C.

Proteomic databases

PaxDb

P08018.

PeptideAtlas

P08018.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJL128C; YJL128C; YJL128C.

GeneID

853313.

KEGG

sce:YJL128C.

Organism-specific databases

CYGD

YJL128c.

SGD

S000003664. PBS2.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00690000101918.

HOGENOM

HOG000234206.

K11227.

OMA

TNILCSA.

OrthoDB

EOG4RV60P.

Enzyme and pathway databases

BioCyc

YEAST:G3O-31578-MONOMER.

BRENDA

2.7.12.2. 984.

Gene expression databases

Genevestigator

P08018.

GermOnline

YJL128C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P08018.

NextBio

973654.

Entry information

Entry name

PBS2_YEAST

Accession

Primary (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:	May 29, 2013
This is version 138 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents