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P38084 (BAP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 106. 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:
Leu/Val/Ile amino-acid permease
Alternative name(s):
Branched-chain amino-acid permease 2
Gene names
Name:BAP2
Ordered Locus Names:YBR068C
ORF Names:YBR0629
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan. Ref.4 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.6.

Miscellaneous

Present with 8660 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family. [View classification]

Ontologies

Keywords
   Biological processAmino-acid transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionamino acid transmembrane transporter activity

Inferred from direct assay Ref.5. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 609609Leu/Val/Ile amino-acid permease
PRO_0000054146

Regions

Topological domain1 – 9999Cytoplasmic Potential
Transmembrane100 – 12021Helical; Potential
Topological domain121 – 1233Extracellular Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 17329Cytoplasmic Potential
Transmembrane174 – 19421Helical; Potential
Topological domain195 – 21016Extracellular Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 2354Cytoplasmic Potential
Transmembrane236 – 25621Helical; Potential
Topological domain257 – 28933Extracellular Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 32818Cytoplasmic Potential
Transmembrane329 – 34921Helical; Potential
Topological domain350 – 37425Extracellular Potential
Transmembrane375 – 39521Helical; Potential
Topological domain396 – 42732Cytoplasmic Potential
Transmembrane428 – 44821Helical; Potential
Topological domain449 – 4513Extracellular Potential
Transmembrane452 – 47221Helical; Potential
Topological domain473 – 50028Cytoplasmic Potential
Transmembrane501 – 52121Helical; Potential
Topological domain522 – 53615Extracellular Potential
Transmembrane537 – 55721Helical; Potential
Topological domain558 – 60952Cytoplasmic Potential

Amino acid modifications

Modified residue31Phosphoserine Ref.11
Modified residue41Phosphoserine Ref.11
Modified residue151Phosphothreonine Ref.9 Ref.11
Modified residue161Phosphoserine Ref.10 Ref.11
Modified residue191Phosphoserine Ref.10 Ref.11
Modified residue211Phosphoserine Ref.11
Modified residue241Phosphoserine Ref.9 Ref.11
Modified residue761Phosphoserine Ref.11

Experimental info

Sequence conflict1391V → E in CAA85012. Ref.1
Sequence conflict2031W → G in CAA85012. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38084 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B87FD6A7464E07F5

FASTA60967,769
        10         20         30         40         50         60 
MLSSEDFGSS GKKETSPDSI SIRSFSAGNN FQSSSSEKTY SKQKSGSDKL IHRFADSFKR 

        70         80         90        100        110        120 
AEGSTTRTKQ INENTSDLED GVESITSDSK LKKSMKSRHV VMMSLGTGIG TGLLVANAKG 

       130        140        150        160        170        180 
LHYGGPAALI IGYILVSFVT YFMIQAAGEM AVTYPTLPAN FNAYSSIFIS KSFGFATVWL 

       190        200        210        220        230        240 
YCFQWLTVLP LELITASMTI QFWNDKINPD IYILIFYVFL VFIHFFGVKA YGETEFIFNC 

       250        260        270        280        290        300 
CKILMIAGFI ILSIVINCGG AGNDGYIGAT YWHNPGAFAG DTSIGRFKNV CYILVTAYFS 

       310        320        330        340        350        360 
FGGMELFALS VQEQSNPRKS TPVAAKRSIY RIVVIYLLTM ILIGFNVPYN DDQLMGAGGS 

       370        380        390        400        410        420 
ATHASPYVLA ASIHGVKIVP HIINAVILIS VVSVANSSLY AGPRLICSLA QQGYAPKFLD 

       430        440        450        460        470        480 
YVDREGRPLR ALIVCCVFGV IAFVAASSKE EIVFTWLAAI AGLSELFTWT SIMLSHLRFR 

       490        500        510        520        530        540 
QAMKVQGRSL DELGYKATTG IWGSIYGVFF NILVFVAQFW VALAPLGNGG KCDAESFFQN 

       550        560        570        580        590        600 
YLAFPIWLAF YFGYMVYNRD FTLLNPLDKI DLDFHRRIYD PELMRQEDEE NKEKLRNMSL 


MRKAYHFWC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
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: 7495881] [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: 10467005] [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: 10654085] [Abstract]
Cited for: FUNCTION.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
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: 16847258] [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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-24, MASS SPECTROMETRY.
Strain: ADR376.
[10]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-19, MASS SPECTROMETRY.
[11]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-4; THR-15; SER-16; SER-19; SER-21; SER-24 AND SER-76, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35937 Genomic DNA. Translation: CAA85012.1.
BK006936 Genomic DNA. Translation: DAA07187.2.
PIRS45930.
RefSeqNP_009624.2. NM_001178416.2.

3D structure databases

ProteinModelPortalP38084.
SMRP38084. Positions 97-152.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4910N.
IntActP38084. 19 interactions.
MINTMINT-516615.
STRINGP38084.

Protein family/group databases

TCDB2.A.3.10.6. amino acid-polyamine-organocation (APC) family.

Proteomic databases

PeptideAtlasP38084.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID852360.
KEGGsce:YBR068C.
NMPDRfig|4932.3.peg.321.

Organism-specific databases

CYGDYBR068c.
SGDS000000272. BAP2.

Phylogenomic databases

eggNOGfuNOG05379.
GeneTreeEFGT00050000001131.
HOGENOMHBG492579.
OMADFHRRIY.
OrthoDBEOG48D43Q.

Gene expression databases

ArrayExpressP38084.
GenevestigatorP38084.
GermOnlineYBR068C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004841. AA-permease_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERPTHR11785. AA/rel_permease1. 1 hit.
PfamPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsTIGR00913. 2A0310. 1 hit.
PROSITEPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971125.

Entry information

Entry nameBAP2_YEAST
AccessionPrimary (citable) accession number: P38084
Secondary accession number(s): D6VQ67
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families