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Protein

Down-regulator of invasive growth 1

Gene

DIG1

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

DIG1 and DIG2 are negative regulators of the filamentation and pheromone induced mating program. DIG1 and DIG2 inhibit the transcriptional activity of STE12 by direct protein-protein interaction. DIG1 colocalizes to promoters with STE12 and redistributes with it during induction of filamentation (by butanol) or mating (by pheromone) to program specific genes, but binding of DIG1 to STE12 is reduced by pheromone treatment.7 Publications

GO - Molecular functioni

  • transcription factor binding Source: SGD

GO - Biological processi

  • negative regulation of invasive growth in response to glucose limitation Source: SGD
  • negative regulation of phenotypic switching Source: SGD
  • negative regulation of pseudohyphal growth Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter by pheromones Source: SGD

Enzyme and pathway databases

BioCyciYEAST:G3O-33962-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Down-regulator of invasive growth 1
Alternative name(s):
Regulator of STE12 protein 1
Regulator of sterile twelve 1
Gene namesi
Name:DIG1
Synonyms:RST1
Ordered Locus Names:YPL049C
ORF Names:P7102.02
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL049C.
SGDiS000005970. DIG1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • Ste12p-Dig1p-Dig2p complex Source: SGD
  • Tec1p-Ste12p-Dig1p complex Source: SGD

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798971 – 452Down-regulator of invasive growth 1Add BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45PhosphoserineCombined sources1
Modified residuei126PhosphoserineCombined sources1
Modified residuei142PhosphoserineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei379PhosphothreonineCombined sources1
Modified residuei395PhosphoserineCombined sources1
Modified residuei428PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by FUS3 and KSS1, in a pheromone-stimulated manner. Phosphorylation reduces the affinity for STE12.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03063.
PRIDEiQ03063.

PTM databases

iPTMnetiQ03063.

Interactioni

Subunit structurei

Forms a complex with DIG2, STE12 and either FUS3 or KSS1. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. DIG1 and DIG2 have also been reported to interact with CLN1 and CLN2.

Binary interactionsi

Show more details

GO - Molecular functioni

  • transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi36131. 196 interactors.
DIPiDIP-1291N.
IntActiQ03063. 63 interactors.
MINTiMINT-393786.

Structurei

3D structure databases

ProteinModelPortaliQ03063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 452Interaction with FUS3 and KSS11 PublicationAdd BLAST241

Phylogenomic databases

InParanoidiQ03063.
KOiK11241.
OMAiADHEDSE.
OrthoDBiEOG092C2EWD.

Sequencei

Sequence statusi: Complete.

Q03063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSARLRTT AEDTSIAKST QDPIGDTEIS VANAKGSSDS NIKNSPGGNS
60 70 80 90 100
VGQESELEHV PEEDDSGDKE ADHEDSETAT AKKRKAQPLK NPKKSLKRGR
110 120 130 140 150
VPAPLNLSDS NTNTHGGNIK DGNLASSNSA HFPPVANQNV KSAPAQVTQH
160 170 180 190 200
SKFQPRVQYL GKASSRQSIQ VNNSSNSYGK PHMPSAGIMS AMNPYMPMNR
210 220 230 240 250
YIMSPYYNPY GIPPPHMLNK PIMTPYVSYP YPMGPRTSIP YAMQGGNARP
260 270 280 290 300
YEENEYSASN YRNKRVNDSY DSPLSGTAST GKTRRSEEGS RNSSVGSSAN
310 320 330 340 350
AGPTQQRADL RPADMIPAEE YHFERDALLS ANTKARSAST STSTSTSTNR
360 370 380 390 400
DRSSWHEAEP NKDEEEGTDL AIEDGAVPTP TFTTFQRTSQ PQQQSPSLLQ
410 420 430 440 450
GEIRLSSHIF AFEFPLSSSN VDKKMFMSIC NKVWNESKEL TKKSSSHHRT

GK
Length:452
Mass (Da):49,356
Last modified:November 1, 1996 - v1
Checksum:i2D27F9878BFADD30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44030 Genomic DNA. Translation: AAB68172.1.
BK006949 Genomic DNA. Translation: DAA11381.1.
PIRiS62027.
RefSeqiNP_015276.1. NM_001183863.1.

Genome annotation databases

EnsemblFungiiYPL049C; YPL049C; YPL049C.
GeneIDi856058.
KEGGisce:YPL049C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44030 Genomic DNA. Translation: AAB68172.1.
BK006949 Genomic DNA. Translation: DAA11381.1.
PIRiS62027.
RefSeqiNP_015276.1. NM_001183863.1.

3D structure databases

ProteinModelPortaliQ03063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36131. 196 interactors.
DIPiDIP-1291N.
IntActiQ03063. 63 interactors.
MINTiMINT-393786.

PTM databases

iPTMnetiQ03063.

Proteomic databases

MaxQBiQ03063.
PRIDEiQ03063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL049C; YPL049C; YPL049C.
GeneIDi856058.
KEGGisce:YPL049C.

Organism-specific databases

EuPathDBiFungiDB:YPL049C.
SGDiS000005970. DIG1.

Phylogenomic databases

InParanoidiQ03063.
KOiK11241.
OMAiADHEDSE.
OrthoDBiEOG092C2EWD.

Enzyme and pathway databases

BioCyciYEAST:G3O-33962-MONOMER.

Miscellaneous databases

PROiQ03063.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiDIG1_YEAST
AccessioniPrimary (citable) accession number: Q03063
Secondary accession number(s): D6W3W5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: March 15, 2017
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5000 molecules/cell in log phase SD medium (5480 according to TAP-tag study).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.