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Q03497 (STE20_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase STE20

EC=2.7.11.1
Gene names
Name:STE20
Ordered Locus Names:YHL007C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length939 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with BEM1, CDC42, CLN2, STE4 and the 14-3-3 proteins BMH1 and BMH2. Ref.7 Ref.10 Ref.11 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.30

Subcellular location

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. Ref.7 Ref.11 Ref.20 Ref.24 Ref.28 Ref.30

Domain

The CRIB domain is required for the association with CDC42.

Post-translational modification

Autophosphorylated and phosphorylated by the CLN2-CDC28 complex in a cell cycle dependent manner. Ref.5 Ref.6 Ref.14 Ref.17

Autophosphorylated on serine residues. Ref.5 Ref.6 Ref.14 Ref.17

Miscellaneous

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

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Pheromone response
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.6. Source: GOC

activation of MAPKKK activity

Inferred from direct assay Ref.6. Source: SGD

bipolar cellular bud site selection

Inferred from mutant phenotype PubMed 10866679. Source: SGD

budding cell apical bud growth

Inferred from mutant phenotype PubMed 10866679. Source: SGD

cellular response to heat

Inferred from mutant phenotype PubMed 12455951. Source: SGD

histone H2B-S14 phosphorylation

Inferred from direct assay Ref.28. Source: GOC

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 8001818. Source: SGD

negative regulation of gene expression

Inferred from mutant phenotype PubMed 19793923. Source: SGD

osmosensory signaling pathway via Sho1 osmosensor

Inferred from mutant phenotype Ref.19. Source: SGD

pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype Ref.1. Source: SGD

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.28. Source: SGD

protein phosphorylation

Inferred from direct assay Ref.6. Source: SGD

pseudohyphal growth

Inferred from mutant phenotype PubMed 8259520. Source: SGD

regulation of exit from mitosis

Inferred from mutant phenotype PubMed 12234925. Source: SGD

signal transduction involved in filamentous growth

Inferred from mutant phenotype PubMed 8259520. Source: SGD

sterol import

Inferred from mutant phenotype PubMed 19793923. Source: SGD

stress granule assembly

Inferred from mutant phenotype PubMed 20513766. Source: SGD

vacuole inheritance

Inferred from mutant phenotype PubMed 19218422. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

incipient cellular bud site

Inferred from direct assay Ref.7. Source: SGD

mating projection tip

Inferred from direct assay Ref.7. Source: SGD

nucleus

Inferred from direct assay Ref.28PubMed 19793923. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase kinase activity

Inferred from direct assay Ref.6. Source: SGD

histone kinase activity (H2B-S14 specific)

Inferred from direct assay Ref.28. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 11805826Ref.23. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.36
Chain2 – 939938Serine/threonine-protein kinase STE20
PRO_0000086686

Regions

Domain337 – 35014CRIB
Domain620 – 871252Protein kinase
Nucleotide binding626 – 6349ATP By similarity
Region434 – 49966BEM1-binding

Sites

Active site7391Proton acceptor By similarity
Binding site6491ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.36
Modified residue871Phosphoserine Ref.35
Modified residue1651Phosphoserine Ref.34
Modified residue1671Phosphothreonine Ref.34
Modified residue1691Phosphoserine Ref.5 Ref.32 Ref.35
Modified residue2031Phosphothreonine Ref.32 Ref.34 Ref.35
Modified residue4181Phosphoserine Ref.5
Modified residue5021Phosphoserine Ref.34 Ref.35
Modified residue5471Phosphoserine Ref.17 Ref.35
Modified residue5621Phosphoserine Ref.17 Ref.32 Ref.33 Ref.35
Modified residue5731Phosphothreonine Ref.17
Modified residue5851Phosphoserine Ref.5 Ref.17 Ref.32
Modified residue7731Phosphothreonine Ref.17
Modified residue9241Phosphoserine Ref.34
Modified residue9271Phosphothreonine Ref.34

Experimental info

Mutagenesis3381S → A: Reduces interaction with CDC42. Ref.23
Mutagenesis3451H → A or D: Reduces interaction with CDC42. Ref.23 Ref.24
Mutagenesis3481H → D: Reduces interaction with CDC42. Ref.24
Mutagenesis4751P → G: Impairs interaction with BEM1; when associated with A-477. Ref.30
Mutagenesis4771P → A: Impairs interaction with BEM1; when associated with G-475. Ref.30
Mutagenesis6491K → R: Impairs phosphorylation of STE11 and histone H2B and mating efficiency. Ref.6 Ref.28
Mutagenesis7771T → A: Impairs autophosphorylation and mating efficiency. Ref.6
Sequence conflict191N → S in AAA35038. Ref.2
Sequence conflict1341I → M in AAA35038. Ref.2
Sequence conflict2711P → S in AAA35038. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q03497 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 69C1C12F5B87733C

FASTA939102,362
        10         20         30         40         50         60 
MSNDPSAVSE LPDKDSLDNG ISNDNERAMG GNGDGGDGLR LPRTTGTLNV NALQKGTNAA 

        70         80         90        100        110        120 
HEAGGYKSMD PAKNAETTND DDNNVVSLDD PIQFTRVSSS SVISGMSSSM SPHSNIDETK 

       130        140        150        160        170        180 
SLEAVTPNIN TSNITPDHSA DNTFSTINAS ESDHQFNDTL LSKLSLTDST ETIENNATVK 

       190        200        210        220        230        240 
HQQPVASSTV NSNKSSTDIR RATPVSTPVI SKPSMTTTPR QINSASHSLS NPKHKQHKPK 

       250        260        270        280        290        300 
VKPSKPEAKS KPVSVKKSFP SKNPLKNSSP PKKQTEKSYY SSSSKKRKSG SNSGTLRMKD 

       310        320        330        340        350        360 
VFTSFVQNIK RNSQDDKRAS SSSNNSSSSS ITTALRISTP YNAKHIHHVG VDSKTGEYTG 

       370        380        390        400        410        420 
LPEEWEKLLT SSGISKREQQ QNMQAVMDIV KFYQDVTETN GEDKMFKTFN TTTGLPGSPQ 

       430        440        450        460        470        480 
VSTPPANSFN KFPPSTSDSH NYGSRTGTPM SNHVMSPTLN TDSSSANGKF IPSRPAPKPP 

       490        500        510        520        530        540 
SSASASAPII KSPVMNSAAN VSPLKQTHAP TTPNRTSPNR SSISRNATLK KEEQPLPPIP 

       550        560        570        580        590        600 
PTKSKTSPII STAHTPQQVA QSPKAPAQET VTTPTSKPAQ ARSLSKELNE KKREERERRK 

       610        620        630        640        650        660 
KQLYAKLNEI CSDGDPSTKY ANLVKIGQGA SGGVYTAYEI GTNVSVAIKQ MNLEKQPKKE 

       670        680        690        700        710        720 
LIINEILVMK GSKHPNIVNF IDSYVLKGDL WVIMEYMEGG SLTDVVTHCI LTEGQIGAVC 

       730        740        750        760        770        780 
RETLSGLEFL HSKGVLHRDI KSDNILLSME GDIKLTDFGF CAQINELNLK RTTMVGTPYW 

       790        800        810        820        830        840 
MAPEVVSRKE YGPKVDIWSL GIMIIEMIEG EPPYLNETPL RALYLIATNG TPKLKEPENL 

       850        860        870        880        890        900 
SSSLKKFLDW CLCVEPEDRA SATELLHDEY ITEIAEANSS LAPLVKLARL KKVAENMDAD 

       910        920        930 
EDNDDDNDNE HINKTNNCDD NNDSKETVNL DVTEDDKQK 

« Hide

References

« Hide 'large scale' references
[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]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"GTPase-activating proteins for Cdc42."
Smith G.R., Givan S.A., Cullen P., Sprague G.F. Jr.
Eukaryot. Cell 1:469-480(2002) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS28394.
RefSeqNP_011856.1. NM_001179087.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KYMNMR-B468-483[»]
2LCSNMR-B468-483[»]
2RQWNMR-B463-486[»]
ProteinModelPortalQ03497.
SMRQ03497. Positions 337-380, 560-930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36419. 234 interactions.
DIPDIP-712N.
IntActQ03497. 23 interactions.
MINTMINT-582880.
STRING4932.YHL007C.

Proteomic databases

PaxDbQ03497.
PeptideAtlasQ03497.
PRIDEQ03497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHL007C; YHL007C; YHL007C.
GeneID856382.
KEGGsce:YHL007C.

Organism-specific databases

CYGDYHL007c.
SGDS000000999. STE20.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00670000097939.
HOGENOMHOG000234202.
KOK04409.
OMATDVVTHC.
OrthoDBEOG708W7W.

Enzyme and pathway databases

BioCycYEAST:G3O-31029-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorQ03497.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03497.
NextBio981881.
PROQ03497.

Entry information

Entry nameSTE20_YEAST
AccessionPrimary (citable) accession number: Q03497
Secondary accession number(s): D3DKQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references