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P13045

- GAL3_YEAST

UniProt

P13045 - GAL3_YEAST

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Protein

Protein GAL3

Gene
GAL3, YDR009W, YD8119.14
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

The GAL3 regulatory function is required for rapid induction of the galactose system. At normal induction, galactose in the presence of the GAL3 protein may lead to the induction of the GAL genes, including GAL1. Then the galactokinase protein (GAL1) in the presence of galactose may reinforce the induction leading to a higher expression level. Upon depletion of galactose, the inducing activity of the galactokinase protein may decrease, after which transcription of the GAL genes, including GAL1, may decrease.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. galactokinase activity Source: InterPro
  3. protein binding Source: SGD

GO - Biological processi

  1. galactose metabolic process Source: SGD
  2. maintenance of protein location Source: SGD
  3. positive regulation of transcription from RNA polymerase II promoter by galactose Source: SGD
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29629-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein GAL3
Gene namesi
Name:GAL3
Ordered Locus Names:YDR009W
ORF Names:YD8119.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR009w.
SGDiS000002416. GAL3.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Protein GAL3PRO_0000184658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP13045.
PaxDbiP13045.

Expressioni

Inductioni

The GAL3 gene is a member of the family of galactose inducible, glucose-repressible genes (which include GAL1, GAL2, GAL7, GAL10, GAL80, and MELI).

Gene expression databases

GenevestigatoriP13045.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
URE2P232021EBI-7282,EBI-20138

Protein-protein interaction databases

BioGridi32061. 47 interactions.
DIPiDIP-5725N.
IntActiP13045. 2 interactions.
MINTiMINT-4480213.
STRINGi4932.YDR009W.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Helixi20 – 3415
Beta strandi39 – 5113
Helixi56 – 583
Beta strandi62 – 7716
Beta strandi84 – 918
Beta strandi97 – 1004
Beta strandi112 – 1143
Helixi119 – 13517
Helixi137 – 1404
Beta strandi141 – 1433
Beta strandi148 – 1547
Helixi162 – 17918
Helixi187 – 1959
Helixi198 – 2014
Helixi208 – 2158
Beta strandi220 – 2256
Beta strandi227 – 2293
Beta strandi231 – 2366
Beta strandi244 – 2518
Helixi258 – 2614
Turni263 – 2653
Helixi266 – 28318
Beta strandi296 – 2994
Helixi302 – 31312
Helixi324 – 34219
Helixi343 – 3453
Helixi351 – 3577
Helixi362 – 3698
Beta strandi370 – 3734
Beta strandi378 – 3803
Helixi382 – 40423
Helixi411 – 43121
Helixi438 – 44912
Beta strandi453 – 47321
Helixi478 – 48811
Helixi490 – 4934
Helixi499 – 5057
Beta strandi506 – 5094
Beta strandi515 – 5195

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V2UX-ray2.10C/D2-520[»]
3V5RX-ray2.10A/B17-520[»]
ProteinModelPortaliP13045.
SMRiP13045. Positions 2-520.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0153.
GeneTreeiENSGT00530000063433.
HOGENOMiHOG000241099.
KOiK00849.
OMAiCREAGAY.
OrthoDBiEOG7FZ075.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 2 hits.
InterProiIPR000705. Galactokinase.
IPR019741. Galactokinase_CS.
IPR019539. GalKase_gal-bd.
IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PfamiPF10509. GalKase_gal_bdg. 1 hit.
PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000530. Galactokinase. 1 hit.
PRINTSiPR00473. GALCTOKINASE.
PR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 2 hits.
TIGRFAMsiTIGR00131. gal_kin. 1 hit.
PROSITEiPS00106. GALACTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13045-1 [UniParc]FASTAAdd to Basket

« Hide

MNTNVPIFSS PVRDLPRSFE QKHLAVVDAF FQTYHVKPDF IARSPGRVNL    50
IGEHIDYCDF SVLPLAIDVD MLCAVKILDE KNPSITLTNA DPKFAQRKFD 100
LPLDGSYMAI DPSVSEWSNY FKCGLHVAHS YLKKIAPERF NNTPLVGAQI 150
FCQSDIPTGG GLSSAFTCAA ALATIRANMG KNFDISKKDL TRITAVAEHY 200
VGVNNGGMDQ ATSVYGEEDH ALYVEFRPKL KATPFKFPQL KNHEISFVIA 250
NTLVKSNKFE TAPTNYNLRV IEVTVAANAL ATRYSVALPS HKDNSNSERG 300
NLRDFMDAYY ARYENQAQPW NGDIGTGIER LLKMLQLVEE SFSRKKSGFT 350
VHEASTALNC SREEFTRDYL TTFPVRFQVL KLYQRAKHVY SESLRVLKAL 400
KMMTSATFHT DEDFFTDFGR LMNESQASCD KLYECSCIET NQICSIALAN 450
GSFGSRLTGA GWGGCTIHLV PSGANGNVEQ VRKALIEKFY NVRYPDLTDE 500
ELKDAIIVSK PALGTCLYEQ 520
Length:520
Mass (Da):58,129
Last modified:February 1, 1996 - v2
Checksum:i5852028EBDDC0F3B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 459KPDFIARSP → NLILSLGLL in AAA34625. 1 Publication
Sequence conflicti170 – 1712AA → GR in AAA34625. 1 Publication
Sequence conflicti192 – 21120RITAV…GMDQA → ASQRLRSTMLESIMVVWIKQ in AAA34625. 1 PublicationAdd
BLAST
Sequence conflicti227 – 24115RPKLK…FPQLK → MAKTKWPHFQVSSIE in AAA34625. 1 PublicationAdd
BLAST
Sequence conflicti251 – 29444NTLVK…SHKDN → ILCTRSNNRTLLHISLSCSL LTLLYISTFAREPCGPDTLG LTISQGQ in AAA34625. 1 PublicationAdd
BLAST
Sequence conflicti303 – 33836RDFMD…MLQLV → EIYGCLLRPDTKTKPNHGME ISELVLNVYSRCYNWY in AAA34625. 1 PublicationAdd
BLAST
Sequence conflicti407 – 42519TFHTD…LMNES → IFTRTRFLYRFWPTNE in AAA34625. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21615 Genomic DNA. Translation: AAA34625.1.
X95966 Genomic DNA. Translation: CAA65201.1.
Z48008 Genomic DNA. Translation: CAA88069.1.
Z74305 Genomic DNA. Translation: CAA98829.1.
AY723766 Genomic DNA. Translation: AAU09683.1.
BK006938 Genomic DNA. Translation: DAA11856.1.
PIRiS50990.
RefSeqiNP_010292.1. NM_001180317.1.

Genome annotation databases

EnsemblFungiiYDR009W; YDR009W; YDR009W.
GeneIDi851572.
KEGGisce:YDR009W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21615 Genomic DNA. Translation: AAA34625.1 .
X95966 Genomic DNA. Translation: CAA65201.1 .
Z48008 Genomic DNA. Translation: CAA88069.1 .
Z74305 Genomic DNA. Translation: CAA98829.1 .
AY723766 Genomic DNA. Translation: AAU09683.1 .
BK006938 Genomic DNA. Translation: DAA11856.1 .
PIRi S50990.
RefSeqi NP_010292.1. NM_001180317.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V2U X-ray 2.10 C/D 2-520 [» ]
3V5R X-ray 2.10 A/B 17-520 [» ]
ProteinModelPortali P13045.
SMRi P13045. Positions 2-520.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32061. 47 interactions.
DIPi DIP-5725N.
IntActi P13045. 2 interactions.
MINTi MINT-4480213.
STRINGi 4932.YDR009W.

Proteomic databases

MaxQBi P13045.
PaxDbi P13045.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR009W ; YDR009W ; YDR009W .
GeneIDi 851572.
KEGGi sce:YDR009W.

Organism-specific databases

CYGDi YDR009w.
SGDi S000002416. GAL3.

Phylogenomic databases

eggNOGi COG0153.
GeneTreei ENSGT00530000063433.
HOGENOMi HOG000241099.
KOi K00849.
OMAi CREAGAY.
OrthoDBi EOG7FZ075.

Enzyme and pathway databases

BioCyci YEAST:G3O-29629-MONOMER.

Miscellaneous databases

NextBioi 969025.

Gene expression databases

Genevestigatori P13045.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.890. 2 hits.
InterProi IPR000705. Galactokinase.
IPR019741. Galactokinase_CS.
IPR019539. GalKase_gal-bd.
IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view ]
Pfami PF10509. GalKase_gal_bdg. 1 hit.
PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000530. Galactokinase. 1 hit.
PRINTSi PR00473. GALCTOKINASE.
PR00959. MEVGALKINASE.
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 2 hits.
TIGRFAMsi TIGR00131. gal_kin. 1 hit.
PROSITEi PS00106. GALACTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast regulatory gene GAL3: carbon regulation; UASGal elements in common with GAL1, GAL2, GAL7, GAL10, GAL80, and MEL1; encoded protein strikingly similar to yeast and Escherichia coli galactokinases."
    Bajwa W., Torchia T.E., Hopper J.E.
    Mol. Cell. Biol. 8:3439-3447(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-425.
  2. "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames."
    Eide L.G., Sander C., Prydz H.
    Yeast 12:1085-1090(1996) [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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGAL3_YEAST
AccessioniPrimary (citable) accession number: P13045
Secondary accession number(s): D6VRZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 132 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 721 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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