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P32917

- STE5_YEAST

UniProt

P32917 - STE5_YEAST

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Protein

Protein STE5

Gene

STE5

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

Functioni

Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.

GO - Molecular functioni

  1. MAP-kinase scaffold activity Source: SGD
  2. phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. invasive growth in response to glucose limitation Source: SGD
  2. negative regulation of MAPK cascade Source: SGD
  3. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  4. positive regulation of protein phosphorylation Source: SGD
  5. positive regulation of signal transduction Source: GOC
  6. regulation of transposition, RNA-mediated Source: SGD
Complete GO annotation...

Keywords - Biological processi

Pheromone response

Enzyme and pathway databases

BioCyciYEAST:G3O-29705-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein STE5
Gene namesi
Name:STE5
Synonyms:NUL3
Ordered Locus Names:YDR103W
ORF Names:YD8557.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR103w.
SGDiS000002510. STE5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. mating projection tip Source: SGD
  3. nucleus Source: SGD
  4. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917Protein STE5PRO_0000072266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei329 – 3291Phosphoserine1 Publication

Post-translational modificationi

May be regulated at the phosphorylation level, and by the mating type of the cell and depends on an intact pheromone-response pathway.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32917.
PaxDbiP32917.

Expressioni

Gene expression databases

GenevestigatoriP32917.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAGL0J04290gQ6FPF22EBI-18373,EBI-8783845From a different organism.
CEK1Q5A1D32EBI-18373,EBI-8783371From a different organism.
CEK2Q5A2812EBI-18373,EBI-8785242From a different organism.
FUS1P117102EBI-18373,EBI-7179
FUS3P1689210EBI-18373,EBI-7193
KLLA0E10539gQ6CNR32EBI-18373,EBI-8785667From a different organism.
mpkBC8V7D12EBI-18373,EBI-8783425From a different organism.
STE11P235617EBI-18373,EBI-18259
STE4P188512EBI-18373,EBI-7390
STE7P067848EBI-18373,EBI-18389

Protein-protein interaction databases

BioGridi32160. 49 interactions.
DIPiDIP-858N.
IntActiP32917. 20 interactions.
MINTiMINT-1174440.
STRINGi4932.YDR103W.

Structurei

Secondary structure

1
917
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 484
Helixi49 – 513
Turni52 – 543
Helixi55 – 584
Helixi59 – 635
Turni64 – 663
Helixi593 – 60412
Beta strandi608 – 6169
Helixi618 – 6203
Beta strandi622 – 6243
Helixi625 – 64016
Beta strandi645 – 6506
Beta strandi653 – 6608
Helixi661 – 6644
Helixi668 – 6725
Helixi673 – 6764
Helixi685 – 6928
Beta strandi701 – 7077
Turni713 – 7153
Helixi717 – 7193
Helixi723 – 7253
Beta strandi735 – 7417
Turni748 – 7503
Beta strandi755 – 7584
Helixi760 – 77011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KGNNMR-A44-67[»]
2L4UNMR-A44-67[»]
3FZEX-ray1.60A593-786[»]
4F2HX-ray3.19A583-787[»]
ProteinModelPortaliP32917.
SMRiP32917. Positions 584-774.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32917.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi775 – 876102Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

To yeast FAR1.Curated

Phylogenomic databases

eggNOGiNOG44001.
HOGENOMiHOG000065959.
InParanoidiP32917.
KOiK11239.
OMAiTLCDEPI.
OrthoDBiEOG7712HK.

Family and domain databases

InterProiIPR021651. Scaffold_Ste5_Fus5-binding.
IPR021106. Ste5_Fus3-bd.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF11610. Ste5. 1 hit.
PF12194. Ste5_C. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32917-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMETPTDNIV SPFHNFGSST QYSGTLSRTP NQIIELEKPS TLSPLSRGKK
60 70 80 90 100
WTEKLARFQR SSAKKKRFSP SPISSSTFSF SPKSRVTSSN SSGNEDGNLM
110 120 130 140 150
NTPSTVSTDY LPQHPHRTSS LPRPNSNLFH ASNSNLSRAN EPPRAENLSD
160 170 180 190 200
NIPPKVAPFG YPIQRTSIKK SFLNASCTLC DEPISNRRKG EKIIELACGH
210 220 230 240 250
LSHQECLIIS FGTTSKADVR ALFPFCTKCK KDTNKAVQCI PENDELKDIL
260 270 280 290 300
ISDFLIHKIP DSELSITPQS RFPPYSPLLP PFGLSYTPVE RQTIYSQAPS
310 320 330 340 350
LNPNLILAAP PKERNQIPQK KSNYTFLHSP LGHRRIPSGA NSILADTSVA
360 370 380 390 400
LSANDSISAV SNSVRAKDDE TKTTLPLLRS YFIQILLNNF QEELQDWRID
410 420 430 440 450
GDYGLLRLVD KLMISKDGQR YIQCWCFLFE DAFVIAEVDN DVDVLEIRLK
460 470 480 490 500
NLEVFTPIAN LRMTTLEASV LKCTLNKQHC ADLSDLYIVQ NINSDESTTV
510 520 530 540 550
QKWISGILNQ DFVFNEDNIT STLPILPIIK NFSKDVGNGR HETSTFLGLI
560 570 580 590 600
NPNKVVEVGN VHDNDTVIIR RGFTLNSGEC SRQSTVDSIQ SVLTTISSIL
610 620 630 640 650
SLKREKPDNL AIILQIDFTK LKEEDSLIVV YNSLKALTIK FARLQFCFVD
660 670 680 690 700
RNNYVLDYGS VLHKIDSLDS ISNLKSKSSS TQFSPIWLKN TLYPENIHEH
710 720 730 740 750
LGIVAVSNSN MEAKKSILFQ DYRCFTSFGR RRPNELKIKV GYLNVDYSDK
760 770 780 790 800
IDELVEASSW TFVLETLCYS FGLSFDEHDD DDEEDNDDST DNELDNSSGS
810 820 830 840 850
LSDAESTTTI HIDSPFDNEN ATANMVNDRN LLTEGEHSNI ENLETVASSV
860 870 880 890 900
QPALIPNIRF SLHSEEEGTN ENENENDMPV LLLSDMDKGI DGITRRSSFS
910
SLIESGNNNC PLHMDYI
Length:917
Mass (Da):102,727
Last modified:February 1, 1994 - v2
Checksum:i0435BDA0196B2D6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3322LG → W in AAA35108. (PubMed:8516289)Curated
Sequence conflicti341 – 3433NSI → TLS in AAA35108. (PubMed:8516289)Curated
Sequence conflicti821 – 8211A → R in BAA02301. (PubMed:8455598)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12917 Genomic DNA. Translation: BAA02301.1.
L01620 Genomic DNA. Translation: AAA35108.1.
L23856 Genomic DNA. Translation: AAA35115.1.
L07865 Unassigned DNA. Translation: AAA16896.1.
Z47746 Genomic DNA. Translation: CAA87679.1.
BK006938 Genomic DNA. Translation: DAA11949.1.
PIRiS51254.
RefSeqiNP_010388.1. NM_001180411.1.

Genome annotation databases

EnsemblFungiiYDR103W; YDR103W; YDR103W.
GeneIDi851680.
KEGGisce:YDR103W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12917 Genomic DNA. Translation: BAA02301.1 .
L01620 Genomic DNA. Translation: AAA35108.1 .
L23856 Genomic DNA. Translation: AAA35115.1 .
L07865 Unassigned DNA. Translation: AAA16896.1 .
Z47746 Genomic DNA. Translation: CAA87679.1 .
BK006938 Genomic DNA. Translation: DAA11949.1 .
PIRi S51254.
RefSeqi NP_010388.1. NM_001180411.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KGN NMR - A 44-67 [» ]
2L4U NMR - A 44-67 [» ]
3FZE X-ray 1.60 A 593-786 [» ]
4F2H X-ray 3.19 A 583-787 [» ]
ProteinModelPortali P32917.
SMRi P32917. Positions 584-774.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32160. 49 interactions.
DIPi DIP-858N.
IntActi P32917. 20 interactions.
MINTi MINT-1174440.
STRINGi 4932.YDR103W.

Proteomic databases

MaxQBi P32917.
PaxDbi P32917.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR103W ; YDR103W ; YDR103W .
GeneIDi 851680.
KEGGi sce:YDR103W.

Organism-specific databases

CYGDi YDR103w.
SGDi S000002510. STE5.

Phylogenomic databases

eggNOGi NOG44001.
HOGENOMi HOG000065959.
InParanoidi P32917.
KOi K11239.
OMAi TLCDEPI.
OrthoDBi EOG7712HK.

Enzyme and pathway databases

BioCyci YEAST:G3O-29705-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32917.
NextBioi 969315.

Gene expression databases

Genevestigatori P32917.

Family and domain databases

InterProi IPR021651. Scaffold_Ste5_Fus5-binding.
IPR021106. Ste5_Fus3-bd.
IPR001841. Znf_RING.
[Graphical view ]
Pfami PF11610. Ste5. 1 hit.
PF12194. Ste5_C. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Function of the ste signal transduction pathway for mating pheromones sustains MAT alpha 1 transcription in Saccharomyces cerevisiae."
    Mukai Y., Harashima S., Oshima Y.
    Mol. Cell. Biol. 13:2050-2060(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of the STE5 gene of Saccharomyces cerevisiae as a suppressor of the mating defect of cdc25 temperature-sensitive mutants."
    Perlman R., Yablonski D., Simchen G., Levitzki A.
    Proc. Natl. Acad. Sci. U.S.A. 90:5474-5478(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence and characterization of the STE5 gene required for signal transduction and mating in Saccharomyces cerevisiae."
    Mackay V.L., Mathewes S., Bell L., O'Hara P.J.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Cloning of Saccharomyces cerevisiae STE5 as a suppressor of a Ste20 protein kinase mutant: structural and functional similarity of Ste5 to Far1."
    Leberer E., Dignard D., Harcus D., Hougan L., Whiteway M., Thomas D.Y.
    Mol. Gen. Genet. 241:241-254(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DBY939.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTE5_YEAST
AccessioniPrimary (citable) accession number: P32917
Secondary accession number(s): D6VS89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1900 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3