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Protein

Protein INO2

Gene

INO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Positive regulatory factor required for depression of the coregulated phospholipid biosynthetic enzymes. Also involved in the expression of ITR1.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: SGD

GO - Biological processi

  1. phospholipid biosynthetic process Source: SGD
  2. positive regulation of transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29723-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein INO2
Gene namesi
Name:INO2
Synonyms:DIE1, SCS1
Ordered Locus Names:YDR123C
ORF Names:YD9727.18C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR123c.
SGDiS000002530. INO2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Protein INO2PRO_0000127253Add
BLAST

Proteomic databases

PaxDbiP26798.

Expressioni

Gene expression databases

GenevestigatoriP26798.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
INO4P139022EBI-9262,EBI-9270

Protein-protein interaction databases

BioGridi32179. 163 interactions.
DIPiDIP-680N.
IntActiP26798. 3 interactions.
MINTiMINT-410234.
STRINGi4932.YDR123C.

Structurei

3D structure databases

ProteinModelPortaliP26798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini236 – 29055bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG42426.
InParanoidiP26798.
KOiK09102.
OMAiSAHIHEN.
OrthoDBiEOG7HXD47.

Family and domain databases

InterProiIPR011598. bHLH_dom.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26798-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQQATGNELL GILDLDNDID FETAYQMLSS NFDDQMSAHI HENTFSATSP
60 70 80 90 100
PLLTHELGII PNVATVQPSH VETIPADNQT HHAPLHTHAH YLNHNPHQPS
110 120 130 140 150
MGFDQALGLK LSPSSSGLLS TNESNAIEQF LDNLISQDMM SSNASMNSES
160 170 180 190 200
HLHIRSPKKQ HRYTELNQRY PETHPHSNTG ELPTNTADVP TEFTTREGPH
210 220 230 240 250
QPIGNDHYNP PPFSVPEIRI PDSDIPANIE DDPVKVRKWK HVQMEKIRRI
260 270 280 290 300
NTKEAFERLI KSVRTPPKEN GKRIPKHILL TCVMNDIKSI RSANEALQHI

LDDS
Length:304
Mass (Da):34,234
Last modified:August 1, 1992 - v1
Checksum:iADF0F0D745A12CE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66066 Genomic DNA. Translation: CAA46866.1.
D90460 Genomic DNA. Translation: BAA14424.1.
Z48758 Genomic DNA. Translation: CAA88676.1.
AY557685 Genomic DNA. Translation: AAS56011.1.
BK006938 Genomic DNA. Translation: DAA11969.1.
PIRiS21570.
RefSeqiNP_010408.1. NM_001180431.1.

Genome annotation databases

EnsemblFungiiYDR123C; YDR123C; YDR123C.
GeneIDi851701.
KEGGisce:YDR123C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66066 Genomic DNA. Translation: CAA46866.1.
D90460 Genomic DNA. Translation: BAA14424.1.
Z48758 Genomic DNA. Translation: CAA88676.1.
AY557685 Genomic DNA. Translation: AAS56011.1.
BK006938 Genomic DNA. Translation: DAA11969.1.
PIRiS21570.
RefSeqiNP_010408.1. NM_001180431.1.

3D structure databases

ProteinModelPortaliP26798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32179. 163 interactions.
DIPiDIP-680N.
IntActiP26798. 3 interactions.
MINTiMINT-410234.
STRINGi4932.YDR123C.

Proteomic databases

PaxDbiP26798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR123C; YDR123C; YDR123C.
GeneIDi851701.
KEGGisce:YDR123C.

Organism-specific databases

CYGDiYDR123c.
SGDiS000002530. INO2.

Phylogenomic databases

eggNOGiNOG42426.
InParanoidiP26798.
KOiK09102.
OMAiSAHIHEN.
OrthoDBiEOG7HXD47.

Enzyme and pathway databases

BioCyciYEAST:G3O-29723-MONOMER.

Miscellaneous databases

NextBioi969374.

Gene expression databases

GenevestigatoriP26798.

Family and domain databases

InterProiIPR011598. bHLH_dom.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis."
    Nikoloff D.M., McGraw P., Henry S.A.
    Nucleic Acids Res. 20:3253-3253(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and characterization of the SCS1 gene required for the expression of genes in yeast phospholipid synthesis."
    Hosaka K., Nikawa J., Kodaki T., Yamashita S.
    J. Biochem. 115:131-136(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Functional characterization of the INO2 gene of Saccharomyces cerevisiae. A positive regulator of phospholipid biosynthesis."
    Nikoloff D.M., Henry S.A.
    J. Biol. Chem. 269:7402-7411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae."
    Nikawa J., Hosaka K.
    Mol. Microbiol. 16:301-308(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiINO2_YEAST
AccessioniPrimary (citable) accession number: P26798
Secondary accession number(s): D6VSA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 4, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 784 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.