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Q03497

- STE20_YEAST

UniProt

Q03497 - STE20_YEAST

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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: 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

  1. ATP binding Source: UniProtKB-KW
  2. histone kinase activity (H2B-S14 specific) Source: SGD
  3. identical protein binding Source: IntAct
  4. MAP kinase kinase kinase kinase activity Source: SGD

GO - Biological processi

  1. activation of MAPKKK activity Source: SGD
  2. bipolar cellular bud site selection Source: SGD
  3. budding cell apical bud growth Source: SGD
  4. cellular response to heat Source: SGD
  5. histone H2B-S14 phosphorylation Source: GOC
  6. invasive growth in response to glucose limitation Source: SGD
  7. MAPK cascade Source: GOC
  8. negative regulation of gene expression Source: SGD
  9. osmosensory signaling pathway via Sho1 osmosensor Source: SGD
  10. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  11. positive regulation of apoptotic process Source: SGD
  12. protein phosphorylation Source: SGD
  13. pseudohyphal growth Source: SGD
  14. regulation of exit from mitosis Source: SGD
  15. signal transduction involved in filamentous growth Source: SGD
  16. sterol import Source: SGD
  17. stress granule assembly Source: SGD
  18. 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.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189214. Regulation of actin dynamics for phagocytic cup formation.
REACT_191493. FCERI mediated MAPK activation.
REACT_243761. CD28 dependent Vav1 pathway.
REACT_244726. Stimulation of the cell death response by PAK-2p34.

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
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHL007c.
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

  1. cytoplasm Source: SGD
  2. incipient cellular bud site Source: SGD
  3. mating projection tip Source: SGD
  4. 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 methioninei1 – 11Removed1 Publication
Chaini2 – 939938Serine/threonine-protein kinase STE20PRO_0000086686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei167 – 1671Phosphothreonine1 Publication
Modified residuei169 – 1691Phosphoserine3 Publications
Modified residuei203 – 2031Phosphothreonine3 Publications
Modified residuei418 – 4181Phosphoserine1 Publication
Modified residuei502 – 5021Phosphoserine2 Publications
Modified residuei547 – 5471Phosphoserine2 Publications
Modified residuei562 – 5621Phosphoserine4 Publications
Modified residuei573 – 5731Phosphothreonine1 Publication
Modified residuei585 – 5851Phosphoserine3 Publications
Modified residuei773 – 7731Phosphothreonine1 Publication
Modified residuei924 – 9241Phosphoserine1 Publication
Modified residuei927 – 9271Phosphothreonine1 Publication

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.
PaxDbiQ03497.
PeptideAtlasiQ03497.
PRIDEiQ03497.

Expressioni

Gene expression databases

GenevestigatoriQ03497.

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

Protein-protein interaction databases

BioGridi36419. 235 interactions.
DIPiDIP-712N.
IntActiQ03497. 23 interactions.
MINTiMINT-582880.
STRINGi4932.YHL007C.

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000119176.
HOGENOMiHOG000234202.
InParanoidiQ03497.
KOiK04409.
OMAiTDVVTHC.
OrthoDBiEOG708W7W.

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.
IPR002290. Ser/Thr_dual-sp_kinase.
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 .
PIRi S28394.
RefSeqi NP_011856.1. NM_001179087.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KYM NMR - B 468-483 [» ]
2LCS NMR - B 468-483 [» ]
2RQW NMR - B 463-486 [» ]
ProteinModelPortali Q03497.
SMRi Q03497. Positions 337-380, 541-930.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36419. 235 interactions.
DIPi DIP-712N.
IntActi Q03497. 23 interactions.
MINTi MINT-582880.
STRINGi 4932.YHL007C.

Proteomic databases

MaxQBi Q03497.
PaxDbi Q03497.
PeptideAtlasi Q03497.
PRIDEi Q03497.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHL007C ; YHL007C ; YHL007C .
GeneIDi 856382.
KEGGi sce:YHL007C.

Organism-specific databases

CYGDi YHL007c.
SGDi S000000999. STE20.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119176.
HOGENOMi HOG000234202.
InParanoidi Q03497.
KOi K04409.
OMAi TDVVTHC.
OrthoDBi EOG708W7W.

Enzyme and pathway databases

BioCyci YEAST:G3O-31029-MONOMER.
BRENDAi 2.7.11.1. 984.
Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189214. Regulation of actin dynamics for phagocytic cup formation.
REACT_191493. FCERI mediated MAPK activation.
REACT_243761. CD28 dependent Vav1 pathway.
REACT_244726. Stimulation of the cell death response by PAK-2p34.

Miscellaneous databases

EvolutionaryTracei Q03497.
NextBioi 981881.
PROi Q03497.

Gene expression databases

Genevestigatori Q03497.

Family and domain databases

Gene3Di 3.90.810.10. 1 hit.
InterProi IPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The protein kinase homologue Ste20p is required to link the yeast pheromone response G-protein beta gamma subunits to downstream signalling components."
    Leberer E., Dignard D., Harcus D., Thomas D.Y., Whiteway M.
    EMBO J. 11:4815-4824(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "A dominant truncation allele identifies a gene, STE20, that encodes a putative protein kinase necessary for mating in Saccharomyces cerevisiae."
    Ramer S.W., Davis R.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:452-456(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae."
    Truckses D.M., Bloomekatz J.E., Thorner J.
    Mol. Cell. Biol. 26:912-928(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 164-169; 583-591 AND 408-431, PHOSPHORYLATION AT SER-169; SER-585 AND SER-418.
  6. "Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae."
    Wu C., Whiteway M., Thomas D.Y., Leberer E.
    J. Biol. Chem. 270:15984-15992(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, FUNCTION IN PHOSPHORYLATION OF STE11, MUTAGENESIS OF LYS-649 AND THR-777.
  7. "Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast."
    Peter M., Neiman A.M., Park H.-O., van Lohuizen M., Herskowitz I.
    EMBO J. 15:7046-7059(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION.
  8. "Genetic relationships between the G protein beta gamma complex, Ste5p, Ste20p and Cdc42p: investigation of effector roles in the yeast pheromone response pathway."
    Akada R., Kallal L., Johnson D.I., Kurjan J.
    Genetics 143:103-117(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase module to induce filamentous growth in Saccharomyces cerevisiae."
    Moesch H.-U., Roberts R.L., Fink G.R.
    Proc. Natl. Acad. Sci. U.S.A. 93:5352-5356(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BMH1 AND BMH2.
  11. "Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase."
    Leberer E., Wu C., Leeuw T., Fourest-Lieuvin A., Segall J.E., Thomas D.Y.
    EMBO J. 16:83-97(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION.
  12. "The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast."
    Wu C., Lytvyn V., Thomas D.Y., Leberer E.
    J. Biol. Chem. 272:30623-30626(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MYO3.
  13. "Actin cytoskeleton organization regulated by the PAK family of protein kinases."
    Eby J.J., Holly S.P., van Drogen F., Grishin A.V., Peter M., Drubin D.G., Blumer K.J.
    Curr. Biol. 8:967-970(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Cell cycle- and Cln2p-Cdc28p-dependent phosphorylation of the yeast Ste20p protein kinase."
    Wu C., Leeuw T., Leberer E., Thomas D.Y., Whiteway M.
    J. Biol. Chem. 273:28107-28115(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY THE CLN2-CDC28 COMPLEX.
  15. "Interaction of a G-protein beta-subunit with a conserved sequence in Ste20/PAK family protein kinases."
    Leeuw T., Wu C., Schrag J.D., Whiteway M., Thomas D.Y., Leberer E.
    Nature 391:191-195(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STE4.
  16. "PAK-family kinases regulate cell and actin polarization throughout the cell cycle of Saccharomyces cerevisiae."
    Holly S.P., Blumer K.J.
    J. Cell Biol. 147:845-856(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Accurate quantitation of protein expression and site-specific phosphorylation."
    Oda Y., Huang K., Cross F.R., Cowburn D., Chait B.T.
    Proc. Natl. Acad. Sci. U.S.A. 96:6591-6596(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLN2, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-547; SER-562; THR-573; SER-585 AND THR-773.
  18. "Phosphorylation of the MEKK Ste11p by the PAK-like kinase Ste20p is required for MAP kinase signaling in vivo."
    van Drogen F., O'Rourke S.M., Stucke V.M., Jaquenoud M., Neiman A.M., Peter M.
    Curr. Biol. 10:630-639(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STE11.
  19. "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.
  20. "Role of Cdc42p in pheromone-stimulated signal transduction in Saccharomyces cerevisiae."
    Moskow J.J., Gladfelter A.S., Lamson R.E., Pryciak P.M., Lew D.J.
    Mol. Cell. Biol. 20:7559-7571(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION.
  21. "Saccharomyces cerevisiae cdc42p GTPase is involved in preventing the recurrence of bud emergence during the cell cycle."
    Richman T.J., Johnson D.I.
    Mol. Cell. Biol. 20:8548-8559(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC42.
  22. Cited for: INTERACTION WITH CDC42.
  23. "Cdc42 regulation of kinase activity and signaling by the yeast p21-activated kinase Ste20."
    Lamson R.E., Winters M.J., Pryciak P.M.
    Mol. Cell. Biol. 22:2939-2951(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, MUTAGENESIS OF SER-338 AND HIS-345.
  24. "Genetic analysis of the interface between Cdc42p and the CRIB domain of Ste20p in Saccharomyces cerevisiae."
    Ash J., Wu C., Larocque R., Jamal M., Stevens W., Osborne M., Thomas D.Y., Whiteway M.
    Genetics 163:9-20(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC42, MUTAGENESIS OF HIS-345 AND HIS-348, SUBCELLULAR LOCATION.
  25. "Synthetic lethal analysis implicates Ste20p, a p21-activated protein kinase, in polarisome activation."
    Goehring A.S., Mitchell D.A., Tong A.H., Keniry M.E., Boone C., Sprague G.F. Jr.
    Mol. Biol. Cell 14:1501-1516(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "Identification of p21-activated kinase specificity determinants in budding yeast: a single amino acid substitution imparts Ste20 specificity to Cla4."
    Keniry M.E., Sprague G.F. Jr.
    Mol. Cell. Biol. 23:1569-1580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  28. "Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae."
    Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.
    Cell 120:25-36(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H2B, MUTAGENESIS OF LYS-649, SUBCELLULAR LOCATION.
  29. "H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S. cerevisiae."
    Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.
    Cell Cycle 4:780-783(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H2B.
  30. "Interaction with the SH3 domain protein Bem1 regulates signaling by the Saccharomyces cerevisiae p21-activated kinase Ste20."
    Winters M.J., Pryciak P.M.
    Mol. Cell. Biol. 25:2177-2190(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BEM1, MUTAGENESIS OF PRO-475 AND PRO-477, SUBCELLULAR LOCATION.
  31. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  32. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-203; SER-562 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  33. "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-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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-165; THR-167; THR-203; SER-502; SER-924 AND THR-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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-87; SER-169; THR-203; SER-502; SER-547 AND SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

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: November 26, 2014
This is version 163 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

External Data

Dasty 3