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Protein

Serine/threonine-protein kinase STE20

Gene

STE20

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

MAP4K component of the MAPK pathway required for the mating pheromone response, haploid invasive growth and diploid pseudohyphal development. Links the pheromone response G-protein beta gamma subunits to downstream signaling components. Needed for mating in haploid cells, induction of a mating-specific gene FUS1, induction of mating-specific morphologies, and pheromone-induced proliferation arrest. Required for the regulation of the actin polarization and bud emergence during cell cycle in G1. Involved in the high osmolarity glycerol (HOG) response. Phosphorylates 'Thr-307' and 'Ser-302' or 'Ser-306' of STE11 and 'Ser-357' of MYO3. Phosphorylates histone H2B to form H2BS10ph during meiosis and H2O(2)-induced apoptosis. Its interaction with CDC42 is required for both invasive growth and the formation of pseudohyphae. Its interaction with STE4 is required for the pheromone signaling.20 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei649 – 6491ATPPROSITE-ProRule annotation
Active sitei739 – 7391Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi626 – 6349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone kinase activity (H2B-S14 specific) Source: SGD
  • identical protein binding Source: IntAct
  • MAP kinase kinase kinase kinase activity Source: SGD

GO - Biological processi

  • activation of MAPKKK activity Source: SGD
  • bipolar cellular bud site selection Source: SGD
  • budding cell apical bud growth Source: SGD
  • cellular response to heat Source: SGD
  • invasive growth in response to glucose limitation Source: SGD
  • negative regulation of gene expression Source: SGD
  • negative regulation of sterol import by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • osmosensory signaling pathway via Sho1 osmosensor Source: SGD
  • pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  • positive regulation of apoptotic process Source: SGD
  • protein phosphorylation Source: SGD
  • pseudohyphal growth Source: SGD
  • regulation of exit from mitosis Source: SGD
  • signal transduction involved in filamentous growth Source: SGD
  • sterol import Source: SGD
  • stress granule assembly Source: SGD
  • vacuole inheritance Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Pheromone response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31029-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-SCE-389359. CD28 dependent Vav1 pathway.
R-SCE-3928662. EPHB-mediated forward signaling.
R-SCE-445144. Signal transduction by L1.
R-SCE-5627123. RHO GTPases activate PAKs.
R-SCE-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase STE20 (EC:2.7.11.1)
Gene namesi
Name:STE20
Ordered Locus Names:YHL007C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHL007C.
SGDiS000000999. STE20.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: The translocation from the cytoplasm to the nucleus is stimulated by H2O2. Localizes at bud emergence during cell cycle and the shmoo top during mating, both localizations requiring an interaction with CDC42.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi338 – 3381S → A: Reduces interaction with CDC42. 1 Publication
Mutagenesisi345 – 3451H → A or D: Reduces interaction with CDC42. 2 Publications
Mutagenesisi348 – 3481H → D: Reduces interaction with CDC42. 1 Publication
Mutagenesisi475 – 4751P → G: Impairs interaction with BEM1; when associated with A-477. 1 Publication
Mutagenesisi477 – 4771P → A: Impairs interaction with BEM1; when associated with G-475. 1 Publication
Mutagenesisi649 – 6491K → R: Impairs phosphorylation of STE11 and histone H2B and mating efficiency. 2 Publications
Mutagenesisi777 – 7771T → A: Impairs autophosphorylation and mating efficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 939938Serine/threonine-protein kinase STE20PRO_0000086686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei167 – 1671PhosphothreonineCombined sources
Modified residuei169 – 1691PhosphoserineCombined sources1 Publication
Modified residuei203 – 2031PhosphothreonineCombined sources
Modified residuei418 – 4181Phosphoserine1 Publication
Modified residuei502 – 5021PhosphoserineCombined sources
Modified residuei547 – 5471PhosphoserineCombined sources1 Publication
Modified residuei562 – 5621PhosphoserineCombined sources1 Publication
Modified residuei573 – 5731Phosphothreonine1 Publication
Modified residuei585 – 5851PhosphoserineCombined sources2 Publications
Modified residuei773 – 7731Phosphothreonine1 Publication
Modified residuei924 – 9241PhosphoserineCombined sources
Modified residuei927 – 9271PhosphothreonineCombined sources

Post-translational modificationi

Autophosphorylated and phosphorylated by the CLN2-CDC28 complex in a cell cycle dependent manner.
Autophosphorylated on serine residues.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ03497.
PRIDEiQ03497.

PTM databases

iPTMnetiQ03497.

Interactioni

Subunit structurei

Interacts with BEM1, CDC42, CLN2, STE4 and the 14-3-3 proteins BMH1 and BMH2.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-18285,EBI-18285
BEM1P2936611EBI-18285,EBI-3508
CDC42P190734EBI-18285,EBI-4274
MYO3P360063EBI-18285,EBI-11670
MYO5Q044394EBI-18285,EBI-11687
NBP2Q121635EBI-18285,EBI-34713
PEX13P806673EBI-18285,EBI-13206
STE4P188513EBI-18285,EBI-7390

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi36419. 238 interactions.
DIPiDIP-712N.
IntActiQ03497. 24 interactions.
MINTiMINT-582880.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KYMNMR-B468-483[»]
2LCSNMR-B468-483[»]
2RQWNMR-B463-486[»]
ProteinModelPortaliQ03497.
SMRiQ03497. Positions 337-380, 541-930.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini337 – 35014CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini620 – 871252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni434 – 49966BEM1-bindingAdd
BLAST

Domaini

The CRIB domain is required for the association with CDC42.

Sequence similaritiesi

Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
InParanoidiQ03497.
KOiK04409.
OMAiTDVVTHC.
OrthoDBiEOG092C2E30.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03497-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDPSAVSE LPDKDSLDNG ISNDNERAMG GNGDGGDGLR LPRTTGTLNV
60 70 80 90 100
NALQKGTNAA HEAGGYKSMD PAKNAETTND DDNNVVSLDD PIQFTRVSSS
110 120 130 140 150
SVISGMSSSM SPHSNIDETK SLEAVTPNIN TSNITPDHSA DNTFSTINAS
160 170 180 190 200
ESDHQFNDTL LSKLSLTDST ETIENNATVK HQQPVASSTV NSNKSSTDIR
210 220 230 240 250
RATPVSTPVI SKPSMTTTPR QINSASHSLS NPKHKQHKPK VKPSKPEAKS
260 270 280 290 300
KPVSVKKSFP SKNPLKNSSP PKKQTEKSYY SSSSKKRKSG SNSGTLRMKD
310 320 330 340 350
VFTSFVQNIK RNSQDDKRAS SSSNNSSSSS ITTALRISTP YNAKHIHHVG
360 370 380 390 400
VDSKTGEYTG LPEEWEKLLT SSGISKREQQ QNMQAVMDIV KFYQDVTETN
410 420 430 440 450
GEDKMFKTFN TTTGLPGSPQ VSTPPANSFN KFPPSTSDSH NYGSRTGTPM
460 470 480 490 500
SNHVMSPTLN TDSSSANGKF IPSRPAPKPP SSASASAPII KSPVMNSAAN
510 520 530 540 550
VSPLKQTHAP TTPNRTSPNR SSISRNATLK KEEQPLPPIP PTKSKTSPII
560 570 580 590 600
STAHTPQQVA QSPKAPAQET VTTPTSKPAQ ARSLSKELNE KKREERERRK
610 620 630 640 650
KQLYAKLNEI CSDGDPSTKY ANLVKIGQGA SGGVYTAYEI GTNVSVAIKQ
660 670 680 690 700
MNLEKQPKKE LIINEILVMK GSKHPNIVNF IDSYVLKGDL WVIMEYMEGG
710 720 730 740 750
SLTDVVTHCI LTEGQIGAVC RETLSGLEFL HSKGVLHRDI KSDNILLSME
760 770 780 790 800
GDIKLTDFGF CAQINELNLK RTTMVGTPYW MAPEVVSRKE YGPKVDIWSL
810 820 830 840 850
GIMIIEMIEG EPPYLNETPL RALYLIATNG TPKLKEPENL SSSLKKFLDW
860 870 880 890 900
CLCVEPEDRA SATELLHDEY ITEIAEANSS LAPLVKLARL KKVAENMDAD
910 920 930
EDNDDDNDNE HINKTNNCDD NNDSKETVNL DVTEDDKQK
Length:939
Mass (Da):102,362
Last modified:October 1, 1993 - v1
Checksum:i69C1C12F5B87733C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191N → S in AAA35038 (PubMed:8421676).Curated
Sequence conflicti134 – 1341I → M in AAA35038 (PubMed:8421676).Curated
Sequence conflicti271 – 2711P → S in AAA35038 (PubMed:8421676).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94719 Genomic DNA. Translation: AAA35111.1.
L04655 Genomic DNA. Translation: AAA35038.1.
L04655 Genomic DNA. Translation: AAA35039.1.
U11581 Genomic DNA. Translation: AAB69747.1.
BK006934 Genomic DNA. Translation: DAA06681.1.
PIRiS28394.
RefSeqiNP_011856.1. NM_001179087.1.

Genome annotation databases

EnsemblFungiiYHL007C; YHL007C; YHL007C.
GeneIDi856382.
KEGGisce:YHL007C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94719 Genomic DNA. Translation: AAA35111.1.
L04655 Genomic DNA. Translation: AAA35038.1.
L04655 Genomic DNA. Translation: AAA35039.1.
U11581 Genomic DNA. Translation: AAB69747.1.
BK006934 Genomic DNA. Translation: DAA06681.1.
PIRiS28394.
RefSeqiNP_011856.1. NM_001179087.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KYMNMR-B468-483[»]
2LCSNMR-B468-483[»]
2RQWNMR-B463-486[»]
ProteinModelPortaliQ03497.
SMRiQ03497. Positions 337-380, 541-930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36419. 238 interactions.
DIPiDIP-712N.
IntActiQ03497. 24 interactions.
MINTiMINT-582880.

PTM databases

iPTMnetiQ03497.

Proteomic databases

MaxQBiQ03497.
PRIDEiQ03497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHL007C; YHL007C; YHL007C.
GeneIDi856382.
KEGGisce:YHL007C.

Organism-specific databases

EuPathDBiFungiDB:YHL007C.
SGDiS000000999. STE20.

Phylogenomic databases

GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
InParanoidiQ03497.
KOiK04409.
OMAiTDVVTHC.
OrthoDBiEOG092C2E30.

Enzyme and pathway databases

BioCyciYEAST:G3O-31029-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-SCE-389359. CD28 dependent Vav1 pathway.
R-SCE-3928662. EPHB-mediated forward signaling.
R-SCE-445144. Signal transduction by L1.
R-SCE-5627123. RHO GTPases activate PAKs.
R-SCE-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

EvolutionaryTraceiQ03497.
PROiQ03497.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTE20_YEAST
AccessioniPrimary (citable) accession number: Q03497
Secondary accession number(s): D3DKQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.