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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
  • negative regulation of signal transduction Source: UniProtKB-KW
  • signal transduction Source: SGD
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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR452C.
SGDiS000004444. SST2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • plasma membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002041731 – 698Protein SST2Add BLAST698

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei252PhosphoserineCombined sources1
Modified residuei408PhosphoserineCombined sources1
Modified residuei539Phosphoserine; by MAPK1 Publication1
Modified residuei587PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by FUS3 and KSS1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11972.
PRIDEiP11972.

PTM databases

iPTMnetiP11972.

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 interactors.
DIPiDIP-2354N.
IntActiP11972. 11 interactors.
MINTiMINT-2782980.

Structurei

3D structure databases

ProteinModelPortaliP11972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini273 – 358DEPPROSITE-ProRule annotationAdd BLAST86
Domaini420 – 689RGSPROSITE-ProRule annotationAdd BLAST270

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 203Fungal-DRAdd BLAST194

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

HOGENOMiHOG000248349.
InParanoidiP11972.
KOiK19838.
OMAiAHRFFTN.
OrthoDBiEOG092C22MK.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48097. 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)DescriptionActionsGraphical viewLength
Sequence conflicti616H → D in AAA35104 (PubMed:2830483).Curated1
Sequence conflicti644E → D in AAA35104 (PubMed:2830483).Curated1

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 interactors.
DIPiDIP-2354N.
IntActiP11972. 11 interactors.
MINTiMINT-2782980.

PTM databases

iPTMnetiP11972.

Proteomic databases

MaxQBiP11972.
PRIDEiP11972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR452C.
SGDiS000004444. SST2.

Phylogenomic databases

HOGENOMiHOG000248349.
InParanoidiP11972.
KOiK19838.
OMAiAHRFFTN.
OrthoDBiEOG092C22MK.

Enzyme and pathway databases

BioCyciYEAST:G3O-32505-MONOMER.

Miscellaneous databases

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48097. SSF48097. 3 hits.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 154 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

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 one 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.