Serine/threonine-protein kinase STE20 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q03497 (STE20_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 146. History...

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

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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:
Serine/threonine-protein kinase STE20
EC=2.7.11.1

Gene names

Name:	STE20
Ordered Locus Names:	YHL007C

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	939 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Pheromone response
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular bud site selection Inferred from mutant phenotype PubMed 11452010. Source: SGD cellular response to heat Inferred from mutant phenotype PubMed 12455951. Source: SGD 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 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_component	cytoplasm 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 PubMed 19793923. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase kinase activity Inferred from direct assay Ref.6. Source: SGD histone serine kinase activity Inferred from direct assay Ref.28. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		2	EBI-18285,EBI-18285
BEM1	P29366	6	EBI-18285,EBI-3508
CDC42	P19073	4	EBI-18285,EBI-4274
NBP2	Q12163	2	EBI-18285,EBI-34713
STE4	P18851	3	EBI-18285,EBI-7390

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 939

939

Serine/threonine-protein kinase STE20

PRO_0000086686

Regions

Domain

337 – 350

CRIB

Domain

620 – 871

252

Protein kinase

Nucleotide binding

626 – 634

ATP By similarity

Region

434 – 499

BEM1-binding

Sites

Active site

739

Proton acceptor By similarity

Binding site

649

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.35

Modified residue

165

Phosphoserine Ref.35

Modified residue

167

Phosphothreonine Ref.35

Modified residue

169

Phosphoserine Ref.5 Ref.31 Ref.32 Ref.35

Modified residue

170

Phosphothreonine Ref.35

Modified residue

172

Phosphothreonine Ref.35

Modified residue

192

Phosphoserine Ref.34

Modified residue

195

Phosphoserine Ref.34

Modified residue

203

Phosphothreonine Ref.32 Ref.34 Ref.35

Modified residue

207

Phosphothreonine Ref.34

Modified residue

217

Phosphothreonine Ref.34

Modified residue

323

Phosphoserine Ref.35

Modified residue

326

Phosphoserine Ref.35

Modified residue

329

Phosphoserine Ref.35

Modified residue

418

Phosphoserine Ref.5 Ref.31 Ref.35

Modified residue

502

Phosphoserine Ref.35

Modified residue

511

Phosphothreonine Ref.34

Modified residue

512

Phosphothreonine Ref.34

Modified residue

516

Phosphothreonine Ref.34

Modified residue

517

Phosphoserine Ref.34

Modified residue

521

Phosphoserine Ref.34

Modified residue

522

Phosphoserine Ref.35

Modified residue

546

Phosphothreonine Ref.33

Modified residue

547

Phosphoserine Ref.17 Ref.34

Modified residue

562

Phosphoserine Ref.17 Ref.32 Ref.34 Ref.35

Modified residue

573

Phosphothreonine Ref.17 Ref.35

Modified residue

585

Phosphoserine Ref.5 Ref.17 Ref.31 Ref.32 Ref.35

Modified residue

773

Phosphothreonine Ref.17

Modified residue

924

Phosphoserine Ref.35

Modified residue

927

Phosphothreonine Ref.35

Experimental info

Mutagenesis

338

S → A: Reduces interaction with CDC42. Ref.23

Mutagenesis

345

H → A or D: Reduces interaction with CDC42. Ref.23 Ref.24

Mutagenesis

348

H → D: Reduces interaction with CDC42. Ref.24

Mutagenesis

475

P → G: Impairs interaction with BEM1; when associated with A-477. Ref.30

Mutagenesis

477

P → A: Impairs interaction with BEM1; when associated with G-475. Ref.30

Mutagenesis

649

K → R: Impairs phosphorylation of STE11 and histone H2B and mating efficiency. Ref.6 Ref.28

Mutagenesis

777

T → A: Impairs autophosphorylation and mating efficiency. Ref.6

Sequence conflict

N → S in AAA35038. Ref.2

Sequence conflict

134

I → M in AAA35038. Ref.2

Sequence conflict

271

P → S in AAA35038. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q03497 [UniParc].

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

FASTA

939

102,362

        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' referencesShow '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. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-418 AND SER-585, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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 THR-546, MASS SPECTROMETRY.
[34]	"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-192; SER-195; THR-203; THR-207; THR-217; THR-511; THR-512; THR-516; SER-517; SER-521; SER-547 AND SER-562, MASS SPECTROMETRY.
[35]	"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-16; SER-165; THR-167; SER-169; THR-170; THR-172; THR-203; SER-323; SER-326; SER-329; SER-418; SER-502; SER-522; SER-562; THR-573; SER-585; SER-924 AND THR-927, MASS SPECTROMETRY.
+	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.

PIR

S28394.

RefSeq

NP_011856.1. NM_001179087.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KYM	NMR	-	B	468-483	[»]
2LCS	NMR	-	B	468-483	[»]
2RQW	NMR	-	B	463-486	[»]

ProteinModelPortal

Q03497.

SMR

Q03497. Positions 337-380, 560-930.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-712N.

IntAct

Q03497. 14 interactions.

MINT

MINT-582880.

STRING

4932.YHL007C.

Proteomic databases

PaxDb

Q03497.

PeptideAtlas

Q03497.

PRIDE

Q03497.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YHL007C; YHL007C; YHL007C.

GeneID

856382.

KEGG

sce:YHL007C.

Organism-specific databases

CYGD

YHL007c.

SGD

S000000999. STE20.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00670000097939.

HOGENOM

HOG000234202.

K04409.

OMA

TDVVTHC.

OrthoDB

EOG4G7G6X.

Enzyme and pathway databases

BRENDA

2.7.11.1. 984.

Gene expression databases

Genevestigator

Q03497.

GermOnline

YHL007C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

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EvolutionaryTrace

Q03497.

NextBio

981881.

Entry information

Entry name

STE20_YEAST

Accession

Primary (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:	May 1, 2013
This is version 146 of the entry and version 1 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 VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: 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