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Protein

Protein SST2

Gene

SST2

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

Desensitization to alpha-factor pheromone. Is involved in regulating the signaling pathway for responding to mating pheromone.

GO - Molecular functioni

  • GTPase activator activity Source: SGD

GO - Biological processi

  • adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: SGD
  • intracellular signal transduction Source: InterPro
  • positive regulation of GTPase activity Source: GOC
  • signal transduction Source: SGD
  • termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Pheromone response

Enzyme and pathway databases

BioCyciYEAST:G3O-32505-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SST2
Gene namesi
Name:SST2
Ordered Locus Names:YLR452C
ORF Names:L9324.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR452c.
EuPathDBiFungiDB:YLR452C.
SGDiS000004444. SST2.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
  • plasma membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 698698Protein SST2PRO_0000204173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521Phosphoserine1 Publication
Modified residuei408 – 4081Phosphoserine1 Publication
Modified residuei539 – 5391Phosphoserine; by MAPK1 Publication
Modified residuei587 – 5871Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by FUS3 and KSS1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11972.
PaxDbiP11972.
PeptideAtlasiP11972.

Expressioni

Inductioni

By exposure to pheromone.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GPA1P085393EBI-18232,EBI-7376
STE2P0CI394EBI-18232,EBI-18360From a different organism.

Protein-protein interaction databases

BioGridi31710. 165 interactions.
DIPiDIP-2354N.
IntActiP11972. 11 interactions.
MINTiMINT-2782980.
STRINGi4932.YLR452C.

Structurei

3D structure databases

ProteinModelPortaliP11972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini273 – 35886DEPPROSITE-ProRule annotationAdd
BLAST
Domaini420 – 689270RGSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 203194Fungal-DRAdd
BLAST

Domaini

The fungal-differentiation regulator (Fungal-DR) domain is only found in fungal regulator of G-protein signaling (RGS) proteins that regulate differentiation pathways. It is required for function (By similarity).By similarity

Sequence similaritiesi

Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG270876.
HOGENOMiHOG000248349.
InParanoidiP11972.
OMAiKMASERR.
OrthoDBiEOG793BH8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR016137. RGS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 3 hits.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDKNRTLHE LSSKNFSRTP NGLIFTNDLK TVYSIFLICL DLKEKKHSSD
60 70 80 90 100
TKSFLLTAFT KHFHFTFTYQ EAIKAMGQLE LKVDMNTTCI NVSYNIKPSL
110 120 130 140 150
ARHLLTLFMS SKLLHTPQDR TRGEPKEKVL FQPTPKGVAV LQKYVRDIGL
160 170 180 190 200
KTMPDILLSS FNSMKLFTFE RSSVTDSIIH SDYLIHILFI KMMGAKPNVW
210 220 230 240 250
SPTNADDPLP CLSSLLEYTN NDDTFTFEKS KPEQGWQAQI GNIDINDLER
260 270 280 290 300
VSPLAHRFFT NPDSESHTQY YVSNAGIRLF ENKTFGTSKK IVIKYTFTTK
310 320 330 340 350
AIWQWIMDCT DIMHVKEAVS LAALFLKTGL IVPVLLQPSR TDKKKFQISR
360 370 380 390 400
SSFFTLSKRG WDLVSWTGCK SNNIRAPNGS TIDLDFTLRG HMTVRDEKKT
410 420 430 440 450
LDDSEGFSQD MLISSSNLNK LDYVLTDPGM RYLFRRHLEK ELCVENLDVF
460 470 480 490 500
IEIKRFLKKM TILKKLIDSK HCDKKSNTST SKNNIVKTID SALMKQANEC
510 520 530 540 550
LEMAYHIYSS YIMIGSPYQL NIHHNLRQNI SDIMLHPHSP LSEHFPTNLY
560 570 580 590 600
DPSPASAESA ASSISSTEAD TLGEPPEVSL KPSKNLSNEN CSFKKQGFKH
610 620 630 640 650
QLKEYKPAPL TLAETHSPNA SVENSHTIVR YGMDNTQNDT KSVESFPATL
660 670 680 690
KVLRKLYPLF EIVSNEMYRL MNNDSFQKFT QSDVYKDASA LIEIQEKC
Length:698
Mass (Da):79,716
Last modified:April 16, 2002 - v2
Checksum:i48CF5BB6E456C11C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161H → D in AAA35104 (PubMed:2830483).Curated
Sequence conflicti644 – 6441E → D in AAA35104 (PubMed:2830483).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18105 Genomic DNA. Translation: AAA35104.1.
U22382 Genomic DNA. Translation: AAB67534.1.
BK006945 Genomic DNA. Translation: DAA09752.1.
PIRiS55974.
RefSeqiNP_013557.1. NM_001182340.1.

Genome annotation databases

EnsemblFungiiYLR452C; YLR452C; YLR452C.
GeneIDi851173.
KEGGisce:YLR452C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18105 Genomic DNA. Translation: AAA35104.1.
U22382 Genomic DNA. Translation: AAB67534.1.
BK006945 Genomic DNA. Translation: DAA09752.1.
PIRiS55974.
RefSeqiNP_013557.1. NM_001182340.1.

3D structure databases

ProteinModelPortaliP11972.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31710. 165 interactions.
DIPiDIP-2354N.
IntActiP11972. 11 interactions.
MINTiMINT-2782980.
STRINGi4932.YLR452C.

Proteomic databases

MaxQBiP11972.
PaxDbiP11972.
PeptideAtlasiP11972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR452C; YLR452C; YLR452C.
GeneIDi851173.
KEGGisce:YLR452C.

Organism-specific databases

CYGDiYLR452c.
EuPathDBiFungiDB:YLR452C.
SGDiS000004444. SST2.

Phylogenomic databases

eggNOGiNOG270876.
HOGENOMiHOG000248349.
InParanoidiP11972.
OMAiKMASERR.
OrthoDBiEOG793BH8.

Enzyme and pathway databases

BioCyciYEAST:G3O-32505-MONOMER.

Miscellaneous databases

NextBioi967987.
PROiP11972.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR016137. RGS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 3 hits.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone."
    Dietzel C., Kurjan J.
    Mol. Cell. Biol. 7:4169-4177(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Feedback phosphorylation of an RGS protein by MAP kinase in yeast."
    Garrison T.R., Zhang Y., Pausch M., Apanovitch D., Aebersold R., Dohlman H.G.
    J. Biol. Chem. 274:36387-36391(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-539.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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.
  7. "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-252 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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-408 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 nameiSST2_YEAST
AccessioniPrimary (citable) accession number: P11972
Secondary accession number(s): D6VZ86, Q06207
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 16, 2002
Last modified: June 24, 2015
This is version 140 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 5980 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.