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P11972

- SST2_YEAST

UniProt

P11972 - SST2_YEAST

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Protein
Protein SST2
Gene
SST2, YLR452C, L9324.9
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  1. GTPase activator activity Source: SGD
  2. protein binding Source: IntAct

GO - Biological processi

  1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: SGD
  2. intracellular signal transduction Source: InterPro
  3. positive regulation of GTPase activity Source: GOC
  4. signal transduction Source: SGD
  5. 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: Chromosome XII

Organism-specific databases

CYGDiYLR452c.
SGDiS000004444. SST2.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 698698Protein SST2
PRO_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.

Gene expression databases

GenevestigatoriP11972.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi31710. 161 interactions.
DIPiDIP-2354N.
IntActiP11972. 11 interactions.
MINTiMINT-2782980.
STRINGi4932.YLR452C.

Structurei

3D structure databases

ProteinModelPortaliP11972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini273 – 35886DEP
Add
BLAST
Domaini420 – 689270RGS
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 203194Fungal-DR
Add
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.

Sequence similaritiesi

Contains 1 DEP domain.
Contains 1 RGS domain.

Phylogenomic databases

eggNOGiNOG270876.
HOGENOMiHOG000248349.
OMAiKMASERR.
OrthoDBiEOG793BH8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
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

MVDKNRTLHE LSSKNFSRTP NGLIFTNDLK TVYSIFLICL DLKEKKHSSD    50
TKSFLLTAFT KHFHFTFTYQ EAIKAMGQLE LKVDMNTTCI NVSYNIKPSL 100
ARHLLTLFMS SKLLHTPQDR TRGEPKEKVL FQPTPKGVAV LQKYVRDIGL 150
KTMPDILLSS FNSMKLFTFE RSSVTDSIIH SDYLIHILFI KMMGAKPNVW 200
SPTNADDPLP CLSSLLEYTN NDDTFTFEKS KPEQGWQAQI GNIDINDLER 250
VSPLAHRFFT NPDSESHTQY YVSNAGIRLF ENKTFGTSKK IVIKYTFTTK 300
AIWQWIMDCT DIMHVKEAVS LAALFLKTGL IVPVLLQPSR TDKKKFQISR 350
SSFFTLSKRG WDLVSWTGCK SNNIRAPNGS TIDLDFTLRG HMTVRDEKKT 400
LDDSEGFSQD MLISSSNLNK LDYVLTDPGM RYLFRRHLEK ELCVENLDVF 450
IEIKRFLKKM TILKKLIDSK HCDKKSNTST SKNNIVKTID SALMKQANEC 500
LEMAYHIYSS YIMIGSPYQL NIHHNLRQNI SDIMLHPHSP LSEHFPTNLY 550
DPSPASAESA ASSISSTEAD TLGEPPEVSL KPSKNLSNEN CSFKKQGFKH 600
QLKEYKPAPL TLAETHSPNA SVENSHTIVR YGMDNTQNDT KSVESFPATL 650
KVLRKLYPLF EIVSNEMYRL MNNDSFQKFT QSDVYKDASA LIEIQEKC 698
Length:698
Mass (Da):79,716
Last modified:April 16, 2002 - v2
Checksum:i48CF5BB6E456C11C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161H → D in AAA35104. 1 Publication
Sequence conflicti644 – 6441E → D in AAA35104. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M18105 Genomic DNA. Translation: AAA35104.1 .
U22382 Genomic DNA. Translation: AAB67534.1 .
BK006945 Genomic DNA. Translation: DAA09752.1 .
PIRi S55974.
RefSeqi NP_013557.1. NM_001182340.1.

3D structure databases

ProteinModelPortali P11972.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31710. 161 interactions.
DIPi DIP-2354N.
IntActi P11972. 11 interactions.
MINTi MINT-2782980.
STRINGi 4932.YLR452C.

Proteomic databases

MaxQBi P11972.
PaxDbi P11972.
PeptideAtlasi P11972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR452C ; YLR452C ; YLR452C .
GeneIDi 851173.
KEGGi sce:YLR452C.

Organism-specific databases

CYGDi YLR452c.
SGDi S000004444. SST2.

Phylogenomic databases

eggNOGi NOG270876.
HOGENOMi HOG000248349.
OMAi KMASERR.
OrthoDBi EOG793BH8.

Enzyme and pathway databases

BioCyci YEAST:G3O-32505-MONOMER.

Miscellaneous databases

NextBioi 967987.

Gene expression databases

Genevestigatori P11972.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR000591. DEP_dom.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00610. DEP. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view ]
SMARTi SM00049. DEP. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 3 hits.
PROSITEi PS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 134 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.

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

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