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P23585 (HXT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High-affinity glucose transporter HXT2
Gene names
Name:HXT2
Ordered Locus Names:YMR011W
ORF Names:YM8270.15
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High-affinity glucose transporter. Is only indispensable for growth on low glucose-containing media, because S.cerevisiae possesses other sugar transporters.

Subcellular location

Membrane; Multi-pass membrane protein.

Induction

Repressed at high glucose concentrations.

Miscellaneous

Glucose transport is thought to be mediated by two kinetically distinct systems, a glucose-repressible high-affinity system and a constitutive low-affinity system.

Sequence similarities

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 541540High-affinity glucose transporter HXT2
PRO_0000050392

Regions

Topological domain2 – 4948Cytoplasmic Potential
Transmembrane50 – 7021Helical; Name=1; Potential
Topological domain71 – 10737Extracellular Potential
Transmembrane108 – 12821Helical; Name=2; Potential
Topological domain129 – 1346Cytoplasmic Potential
Transmembrane135 – 15521Helical; Name=3; Potential
Topological domain156 – 1627Extracellular Potential
Transmembrane163 – 18321Helical; Name=4; Potential
Topological domain184 – 1929Cytoplasmic Potential
Transmembrane193 – 21321Helical; Name=5; Potential
Topological domain214 – 22714Extracellular Potential
Transmembrane228 – 24821Helical; Name=6; Potential
Topological domain249 – 32779Cytoplasmic Potential
Transmembrane328 – 34720Helical; Name=7; Potential
Topological domain348 – 3503Extracellular Potential
Transmembrane351 – 37121Helical; Name=8; Potential
Topological domain372 – 3798Cytoplasmic Potential
Transmembrane380 – 40021Helical; Name=9; Potential
Topological domain401 – 41818Extracellular Potential
Transmembrane419 – 43921Helical; Name=10; Potential
Topological domain440 – 45617Cytoplasmic Potential
Transmembrane457 – 47721Helical; Name=11; Potential
Topological domain478 – 4847Extracellular Potential
Transmembrane485 – 50521Helical; Name=12; Potential
Topological domain506 – 54136Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue111Phosphoserine Ref.5
Modified residue131Phosphoserine Ref.5
Modified residue171Phosphoserine Ref.5 Ref.7
Modified residue201Phosphoserine Ref.5 Ref.7
Modified residue291Phosphothreonine Ref.5 Ref.6 Ref.7
Modified residue321Phosphoserine Ref.5 Ref.7
Modified residue2661Phosphoserine; by PKA Potential
Modified residue5391Phosphoserine; by PKA Potential
Glycosylation821N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P23585 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 6AEFEC0A87391CA7

FASTA54159,841
        10         20         30         40         50         60 
MSEFATSRVE SGSQQTSIHS TPIVQKLETD ESPIQTKSEY TNAELPAKPI AAYWTVICLC 

        70         80         90        100        110        120 
LMIAFGGFVF GWDTGTISGF VNQTDFKRRF GQMKSDGTYY LSDVRTGLIV GIFNIGCAFG 

       130        140        150        160        170        180 
GLTLGRLGDM YGRRIGLMCV VLVYIVGIVI QIASSDKWYQ YFIGRIISGM GVGGIAVLSP 

       190        200        210        220        230        240 
TLISETAPKH IRGTCVSFYQ LMITLGIFLG YCTNYGTKDY SNSVQWRVPL GLNFAFAIFM 

       250        260        270        280        290        300 
IAGMLMVPES PRFLVEKGRY EDAKRSLAKS NKVTIEDPSI VAEMDTIMAN VETERLAGNA 

       310        320        330        340        350        360 
SWGELFSNKG AILPRVIMGI MIQSLQQLTG NNYFFYYGTT IFNAVGMKDS FQTSIVLGIV 

       370        380        390        400        410        420 
NFASTFVALY TVDKFGRRKC LLGGSASMAI CFVIFSTVGV TSLYPNGKDQ PSSKAAGNVM 

       430        440        450        460        470        480 
IVFTCLFIFF FAISWAPIAY VIVAESYPLR VKNRAMAIAV GANWIWGFLI GFFTPFITSA 

       490        500        510        520        530        540 
IGFSYGYVFM GCLVFSFFYV FFFVCETKGL TLEEVNEMYV EGVKPWKSGS WISKEKRVSE 


E 

« Hide

References

« Hide 'large scale' references
[1]"The HXT2 gene of Saccharomyces cerevisiae is required for high-affinity glucose transport."
Kruckeberg A.L., Bisson L.F.
Mol. Cell. Biol. 10:5903-5913(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[5]"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-11; SER-13; SER-17; SER-20; THR-29 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[6]"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 THR-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; THR-29 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33270 Genomic DNA. Translation: AAA34701.1.
Z48613 Genomic DNA. Translation: CAA88528.1.
BK006946 Genomic DNA. Translation: DAA09909.1.
PIRMMBYH2. A36380.
RefSeqNP_013724.1. NM_001182507.1.

3D structure databases

ProteinModelPortalP23585.
SMRP23585. Positions 56-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35180. 96 interactions.
DIPDIP-7912N.
IntActP23585. 6 interactions.
MINTMINT-4497394.
STRING4932.YMR011W.

Protein family/group databases

TCDB2.A.1.1.111. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbP23585.
PeptideAtlasP23585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR011W; YMR011W; YMR011W.
GeneID855023.
KEGGsce:YMR011W.

Organism-specific databases

CYGDYMR011w.
SGDS000004613. HXT2.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00720000108754.
HOGENOMHOG000202870.
KOK08139.
OMACAFGGLT.
OrthoDBEOG73JM4H.

Enzyme and pathway databases

BioCycYEAST:G3O-32719-MONOMER.

Gene expression databases

GenevestigatorP23585.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSPR00171. SUGRTRNSPORT.
SUPFAMSSF103473. SSF103473. 1 hit.
TIGRFAMsTIGR00879. SP. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978213.

Entry information

Entry nameHXT2_YEAST
AccessionPrimary (citable) accession number: P23585
Secondary accession number(s): D6VZI5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families