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Protein

Protein STE50

Gene

STE50

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

Involved in growth arrest during conjugation. May interact with the G protein alpha subunit.

GO - Molecular functioni

  1. protein kinase regulator activity Source: SGD
  2. SAM domain binding Source: SGD

GO - Biological processi

  1. cell cycle arrest Source: UniProtKB-KW
  2. cellular response to heat Source: SGD
  3. MAPK cascade involved in osmosensory signaling pathway Source: SGD
  4. osmosensory signaling pathway via Sho1 osmosensor Source: SGD
  5. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  6. regulation of protein kinase activity Source: GOC
  7. signal transduction involved in filamentous growth Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Growth arrest, Pheromone response

Enzyme and pathway databases

BioCyciYEAST:G3O-29292-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein STE50
Gene namesi
Name:STE50
Ordered Locus Names:YCL032W
ORF Names:YCL32W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCL032w.
EuPathDBiFungiDB:YCL032W.
SGDiS000000537. STE50.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Protein STE50PRO_0000072265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021Phosphoserine3 Publications
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei248 – 2481Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25344.
PaxDbiP25344.
PeptideAtlasiP25344.

Expressioni

Gene expression databases

GenevestigatoriP25344.

Interactioni

Subunit structurei

Interacts with STE11 through the respective SAM domains.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SHO1P400733EBI-18305,EBI-18140
STE11P235616EBI-18305,EBI-18259

Protein-protein interaction databases

BioGridi30951. 384 interactions.
DIPiDIP-667N.
IntActiP25344. 37 interactions.
MINTiMINT-408633.
STRINGi4932.YCL032W.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni32 – 343Combined sources
Helixi37 – 4812Combined sources
Helixi56 – 627Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8011Combined sources
Beta strandi82 – 843Combined sources
Helixi86 – 10116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UQVNMR-A27-108[»]
1Z1VNMR-A32-107[»]
ProteinModelPortaliP25344.
SMRiP25344. Positions 27-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 10885SAMAdd
BLAST
Domaini233 – 32795Ras-associatingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Ras-associating domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG46436.
HOGENOMiHOG000057098.
InParanoidiP25344.
OMAiGLHPAIM.
OrthoDBiEOG7GFBFJ.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR000159. Ras-assoc.
IPR013761. SAM/pointed.
IPR015316. SAM_Ste50p.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00788. RA. 1 hit.
PF09235. Ste50p-SAM. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50200. RA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDGKQAINE GSNDASPDLD VNGTILMNNE DFSQWSVDDV ITWCISTLEV
60 70 80 90 100
EETDPLCQRL RENDIVGDLL PELCLQDCQD LCDGDLNKAI KFKILINKMR
110 120 130 140 150
DSKLEWKDDK TQEDMITVLK NLYTTTSAKL QEFQSQYTRL RMDVLDVMKT
160 170 180 190 200
SSSSSPINTH GVSTTVPSSN NTIIPSSDGV SLSQTDYFDT VHNRQSPSRR
210 220 230 240 250
ESPVTVFRQP SLSHSKSLHK DSKNKVPQIS TNQSHPSAVS TANTPGPSPN
260 270 280 290 300
EALKQLRASK EDSCERILKN AMKRHNLADQ DWRQYVLVIC YGDQERLLEL
310 320 330 340
NEKPVIIFKN LKQQGLHPAI MLRRRGDFEE VAMMNGSDNV TPGGRL
Length:346
Mass (Da):38,971
Last modified:May 1, 1992 - v1
Checksum:iEFC7D14F2940C779
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11116 Genomic DNA. Translation: CAA77462.1.
S54312 Genomic DNA. Translation: AAA13629.1.
X59720 Genomic DNA. Translation: CAA42384.1.
BK006937 Genomic DNA. Translation: DAA07452.1.
PIRiS17475.
RefSeqiNP_009898.1. NM_001178677.1.

Genome annotation databases

EnsemblFungiiYCL032W; YCL032W; YCL032W.
GeneIDi850325.
KEGGisce:YCL032W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11116 Genomic DNA. Translation: CAA77462.1.
S54312 Genomic DNA. Translation: AAA13629.1.
X59720 Genomic DNA. Translation: CAA42384.1.
BK006937 Genomic DNA. Translation: DAA07452.1.
PIRiS17475.
RefSeqiNP_009898.1. NM_001178677.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UQVNMR-A27-108[»]
1Z1VNMR-A32-107[»]
ProteinModelPortaliP25344.
SMRiP25344. Positions 27-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30951. 384 interactions.
DIPiDIP-667N.
IntActiP25344. 37 interactions.
MINTiMINT-408633.
STRINGi4932.YCL032W.

Proteomic databases

MaxQBiP25344.
PaxDbiP25344.
PeptideAtlasiP25344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCL032W; YCL032W; YCL032W.
GeneIDi850325.
KEGGisce:YCL032W.

Organism-specific databases

CYGDiYCL032w.
EuPathDBiFungiDB:YCL032W.
SGDiS000000537. STE50.

Phylogenomic databases

eggNOGiNOG46436.
HOGENOMiHOG000057098.
InParanoidiP25344.
OMAiGLHPAIM.
OrthoDBiEOG7GFBFJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29292-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25344.
NextBioi965745.
PROiP25344.

Gene expression databases

GenevestigatoriP25344.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR000159. Ras-assoc.
IPR013761. SAM/pointed.
IPR015316. SAM_Ste50p.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00788. RA. 1 hit.
PF09235. Ste50p-SAM. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50200. RA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "STE50, a novel gene required for activation of conjugation at an early step in mating in Saccharomyces cerevisiae."
    Rad M.R., Xu G., Hollenberg C.P.
    Mol. Gen. Genet. 236:145-154(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames."
    Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.
    Yeast 7:533-538(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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-202 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-202; THR-244 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structure of the sterile alpha motif (SAM) domain of the Saccharomyces cerevisiae mitogen-activated protein kinase pathway-modulating protein STE50 and analysis of its interaction with the STE11 SAM."
    Grimshaw S.J., Mott H.R., Stott K.M., Nielsen P.R., Evetts K.A., Hopkins L.J., Nietlispach D., Owen D.
    J. Biol. Chem. 279:2192-2201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 27-108, INTERACTION WITH STE11.
  10. "Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction."
    Kwan J.J., Warner N., Maini J., Chan Tung K.W., Zakaria H., Pawson T., Donaldson L.W.
    J. Mol. Biol. 356:142-154(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 32-107, INTERACTION WITH STE11.

Entry informationi

Entry nameiSTE50_YEAST
AccessioniPrimary (citable) accession number: P25344
Secondary accession number(s): D6VQY3, Q3S1N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 29, 2015
This is version 138 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 1670 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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 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.