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Protein

MAP kinase kinase PBS2

Gene

PBS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.3 Publications

Miscellaneous

Present with 2160 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei389ATPPROSITE-ProRule annotation1
Active sitei485Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi366 – 374ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase activity Source: SGD
  • MAP-kinase scaffold activity Source: SGD
  • peptide alpha-N-acetyltransferase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • actin filament organization Source: SGD
  • activation of MAPK activity Source: SGD
  • cellular response to heat Source: SGD
  • hyperosmotic response Source: SGD
  • osmosensory signaling pathway Source: UniProtKB
  • protein import into nucleus Source: SGD
  • protein phosphorylation Source: UniProtKB
  • regulation of apoptotic process Source: GO_Central
  • regulation of mitotic cell cycle Source: GO_Central
  • response to antibiotic Source: UniProtKB-KW
  • stress-activated protein kinase signaling cascade Source: GO_Central

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processAntibiotic resistance
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31578-MONOMER
BRENDAi2.7.12.2 984
ReactomeiR-SCE-110056 MAPK3 (ERK1) activation
R-SCE-112411 MAPK1 (ERK2) activation
R-SCE-168638 NOD1/2 Signaling Pathway
R-SCE-2559580 Oxidative Stress Induced Senescence
R-SCE-2871796 FCERI mediated MAPK activation
R-SCE-445144 Signal transduction by L1
R-SCE-450302 activated TAK1 mediates p38 MAPK activation
R-SCE-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-SCE-5674135 MAP2K and MAPK activation
R-SCE-5674499 Negative feedback regulation of MAPK pathway
R-SCE-6811555 PI5P Regulates TP53 Acetylation

Names & Taxonomyi

Protein namesi
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 namesi
Name:PBS2
Synonyms:HOG4, SFS4, SSK4
Ordered Locus Names:YJL128C
ORF Names:J0699
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL128C
SGDiS000003664 PBS2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96P → S in PBS2-13; loss of SH3-domain interaction. 1 Publication1
Mutagenesisi389K → M: Loss of activity. 1 Publication1
Mutagenesisi514S → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi518T → A: Loss of phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000864831 – 668MAP kinase kinase PBS2Add BLAST668

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68PhosphoserineCombined sources1
Modified residuei269PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1 Publication1
Modified residuei518Phosphothreonine1 Publication1

Post-translational modificationi

Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08018
PaxDbiP08018
PRIDEiP08018

PTM databases

iPTMnetiP08018

Interactioni

Subunit structurei

Interacts with NBP2, PTC1, SHO1 AND STE11.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • MAP-kinase scaffold activity Source: SGD

Protein-protein interaction databases

BioGridi33628, 478 interactors
DIPiDIP-2368N
ELMiP08018
IntActiP08018, 45 interactors
MINTiP08018
STRINGi4932.YJL128C

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VKNX-ray2.05C92-103[»]
ProteinModelPortaliP08018
SMRiP08018
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08018

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini360 – 623Protein kinasePROSITE-ProRule annotationAdd BLAST264

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi91 – 101Pro-richAdd BLAST11

Domaini

Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1.1 Publication

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119199
HOGENOMiHOG000234206
InParanoidiP08018
KOiK11227
OMAiGAFFIEG
OrthoDBiEOG092C3RSG

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

P08018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDKFANLSL HEKTGKSSIQ LNEQTGSDNG SAVKRTSSTS SHYNNINADL
60 70 80 90 100
HARVKAFQEQ RALKRSASVG SNQSEQDKGS SQSPKHIQQI VNKPLPPLPV
110 120 130 140 150
AGSSKVSQRM SSQVVQASSK STLKNVLDNQ ETQNITDVNI NIDTTKITAT
160 170 180 190 200
TIGVNTGLPA TDITPSVSNT ASATHKAQLL NPNRRAPRRP LSTQHPTRPN
210 220 230 240 250
VAPHKAPAII NTPKQSLSAR RGLKLPPGGM SLKMPTKTAQ QPQQFAPSPS
260 270 280 290 300
NKKHIETLSN SKVVEGKRSN PGSLINGVQS TSTSSSTEGP HDTVGTTPRT
310 320 330 340 350
GNSNNSSNSG SSGGGGLFAN FSKYVDIKSG SLNFAGKLSL SSKGIDFSNG
360 370 380 390 400
SSSRITLDEL EFLDELGHGN YGNVSKVLHK PTNVIMATKE VRLELDEAKF
410 420 430 440 450
RQILMELEVL HKCNSPYIVD FYGAFFIEGA VYMCMEYMDG GSLDKIYDES
460 470 480 490 500
SEIGGIDEPQ LAFIANAVIH GLKELKEQHN IIHRDVKPTN ILCSANQGTV
510 520 530 540 550
KLCDFGVSGN LVASLAKTNI GCQSYMAPER IKSLNPDRAT YTVQSDIWSL
560 570 580 590 600
GLSILEMALG RYPYPPETYD NIFSQLSAIV DGPPPRLPSD KFSSDAQDFV
610 620 630 640 650
SLCLQKIPER RPTYAALTEH PWLVKYRNQD VHMSEYITER LERRNKILRE
660
RGENGLSKNV PALHMGGL
Length:668
Mass (Da):72,720
Last modified:September 21, 2011 - v4
Checksum:i9BC3435BDAFE8019
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222 – 223GL → AV (PubMed:8948101).Curated2
Sequence conflicti222 – 223GL → AV in CAA89423 (PubMed:8641269).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02946 Unassigned DNA Translation: AAA16819.1
U12237 Genomic DNA Translation: AAA20392.1
Z49403 Genomic DNA Translation: CAA89423.1
BK006943 Genomic DNA Translation: DAA08673.2
PIRiS56909
RefSeqiNP_012407.2, NM_001181561.2

Genome annotation databases

EnsemblFungiiYJL128C; YJL128C; YJL128C
GeneIDi853313
KEGGisce:YJL128C

Similar proteinsi

Entry informationi

Entry nameiPBS2_YEAST
AccessioniPrimary (citable) accession number: P08018
Secondary accession number(s): D6VW57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 21, 2011
Last modified: May 23, 2018
This is version 187 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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