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Protein

Leu/Val/Ile amino-acid permease

Gene

BAP2

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

Functioni

Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan.2 Publications

GO - Molecular functioni

  • amino acid transmembrane transporter activity Source: SGD
  • antiporter activity Source: GO_Central
  • L-amino acid transmembrane transporter activity Source: GO_Central
  • L-phenylalanine transmembrane transporter activity Source: CACAO

GO - Biological processi

  • amino acid transport Source: SGD
  • leucine import into cell Source: CACAO
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29037-MONOMER.

Protein family/group databases

TCDBi2.A.3.10.6. the amino acid-polyamine-organocation (apc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Leu/Val/Ile amino-acid permease
Alternative name(s):
Branched-chain amino-acid permease 2
Gene namesi
Name:BAP2
Ordered Locus Names:YBR068C
ORF Names:YBR0629
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR068C.
SGDiS000000272. BAP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9999CytoplasmicSequence analysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence analysisAdd
BLAST
Topological domaini121 – 1233ExtracellularSequence analysis
Transmembranei124 – 14421HelicalSequence analysisAdd
BLAST
Topological domaini145 – 17329CytoplasmicSequence analysisAdd
BLAST
Transmembranei174 – 19421HelicalSequence analysisAdd
BLAST
Topological domaini195 – 21016ExtracellularSequence analysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence analysisAdd
BLAST
Topological domaini232 – 2354CytoplasmicSequence analysis
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Topological domaini257 – 28933ExtracellularSequence analysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence analysisAdd
BLAST
Topological domaini311 – 32818CytoplasmicSequence analysisAdd
BLAST
Transmembranei329 – 34921HelicalSequence analysisAdd
BLAST
Topological domaini350 – 37425ExtracellularSequence analysisAdd
BLAST
Transmembranei375 – 39521HelicalSequence analysisAdd
BLAST
Topological domaini396 – 42732CytoplasmicSequence analysisAdd
BLAST
Transmembranei428 – 44821HelicalSequence analysisAdd
BLAST
Topological domaini449 – 4513ExtracellularSequence analysis
Transmembranei452 – 47221HelicalSequence analysisAdd
BLAST
Topological domaini473 – 50028CytoplasmicSequence analysisAdd
BLAST
Transmembranei501 – 52121HelicalSequence analysisAdd
BLAST
Topological domaini522 – 53615ExtracellularSequence analysisAdd
BLAST
Transmembranei537 – 55721HelicalSequence analysisAdd
BLAST
Topological domaini558 – 60952CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: SGD
  • vacuole Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 609609Leu/Val/Ile amino-acid permeasePRO_0000054146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineCombined sources
Modified residuei15 – 151PhosphothreonineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38084.

PTM databases

iPTMnetiP38084.
SwissPalmiP38084.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SHR3Q027743EBI-3414,EBI-17099

Protein-protein interaction databases

BioGridi32771. 68 interactions.
DIPiDIP-4910N.
IntActiP38084. 12 interactions.
MINTiMINT-516615.

Structurei

3D structure databases

ProteinModelPortaliP38084.
SMRiP38084. Positions 93-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000049744.
HOGENOMiHOG000261848.
InParanoidiP38084.
KOiK16261.
OMAiDFHRRIY.
OrthoDBiEOG74J9HZ.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSEDFGSS GKKETSPDSI SIRSFSAGNN FQSSSSEKTY SKQKSGSDKL
60 70 80 90 100
IHRFADSFKR AEGSTTRTKQ INENTSDLED GVESITSDSK LKKSMKSRHV
110 120 130 140 150
VMMSLGTGIG TGLLVANAKG LHYGGPAALI IGYILVSFVT YFMIQAAGEM
160 170 180 190 200
AVTYPTLPAN FNAYSSIFIS KSFGFATVWL YCFQWLTVLP LELITASMTI
210 220 230 240 250
QFWNDKINPD IYILIFYVFL VFIHFFGVKA YGETEFIFNC CKILMIAGFI
260 270 280 290 300
ILSIVINCGG AGNDGYIGAT YWHNPGAFAG DTSIGRFKNV CYILVTAYFS
310 320 330 340 350
FGGMELFALS VQEQSNPRKS TPVAAKRSIY RIVVIYLLTM ILIGFNVPYN
360 370 380 390 400
DDQLMGAGGS ATHASPYVLA ASIHGVKIVP HIINAVILIS VVSVANSSLY
410 420 430 440 450
AGPRLICSLA QQGYAPKFLD YVDREGRPLR ALIVCCVFGV IAFVAASSKE
460 470 480 490 500
EIVFTWLAAI AGLSELFTWT SIMLSHLRFR QAMKVQGRSL DELGYKATTG
510 520 530 540 550
IWGSIYGVFF NILVFVAQFW VALAPLGNGG KCDAESFFQN YLAFPIWLAF
560 570 580 590 600
YFGYMVYNRD FTLLNPLDKI DLDFHRRIYD PELMRQEDEE NKEKLRNMSL

MRKAYHFWC
Length:609
Mass (Da):67,769
Last modified:July 27, 2011 - v2
Checksum:iB87FD6A7464E07F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391V → E in CAA85012 (PubMed:7813418).Curated
Sequence conflicti203 – 2031W → G in CAA85012 (PubMed:7813418).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35937 Genomic DNA. Translation: CAA85012.1.
BK006936 Genomic DNA. Translation: DAA07187.2.
PIRiS45930.
RefSeqiNP_009624.4. NM_001178416.4.

Genome annotation databases

EnsemblFungiiYBR068C; YBR068C; YBR068C.
GeneIDi852360.
KEGGisce:YBR068C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35937 Genomic DNA. Translation: CAA85012.1.
BK006936 Genomic DNA. Translation: DAA07187.2.
PIRiS45930.
RefSeqiNP_009624.4. NM_001178416.4.

3D structure databases

ProteinModelPortaliP38084.
SMRiP38084. Positions 93-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32771. 68 interactions.
DIPiDIP-4910N.
IntActiP38084. 12 interactions.
MINTiMINT-516615.

Protein family/group databases

TCDBi2.A.3.10.6. the amino acid-polyamine-organocation (apc) family.

PTM databases

iPTMnetiP38084.
SwissPalmiP38084.

Proteomic databases

MaxQBiP38084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR068C; YBR068C; YBR068C.
GeneIDi852360.
KEGGisce:YBR068C.

Organism-specific databases

EuPathDBiFungiDB:YBR068C.
SGDiS000000272. BAP2.

Phylogenomic databases

GeneTreeiENSGT00510000049744.
HOGENOMiHOG000261848.
InParanoidiP38084.
KOiK16261.
OMAiDFHRRIY.
OrthoDBiEOG74J9HZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29037-MONOMER.

Miscellaneous databases

PROiP38084.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 139 AND 203.
    Strain: ATCC 204508 / S288c.
  3. "BAP2, a gene encoding a permease for branched-chain amino acids in Saccharomyces cerevisiae."
    Grauslund M., Didion T., Kielland-Brandt M.C., Andersen H.A.
    Biochim. Biophys. Acta 1269:275-280(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases."
    During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C., Hansen J.
    Curr. Genet. 35:609-617(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN L-CYSTEINE UPTAKE.
  5. "Substrate specificity and gene expression of the amino-acid permeases in Saccharomyces cerevisiae."
    Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.
    Curr. Genet. 36:317-328(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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.
  9. "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 THR-15 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-3; SER-16; SER-19; SER-21; SER-24; SER-76 AND SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBAP2_YEAST
AccessioniPrimary (citable) accession number: P38084
Secondary accession number(s): D6VQ67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 147 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 8660 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.