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P36035 (JEN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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:
Carboxylic acid transporter protein homolog
Gene names
Name:JEN1
Ordered Locus Names:YKL217W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential to lactate transport.

Subcellular location

Membrane; Multi-pass membrane protein.

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.7
Chain2 – 616615Carboxylic acid transporter protein homolog
PRO_0000050460

Regions

Topological domain2 – 140139Cytoplasmic Potential
Transmembrane141 – 16121Helical; Name=1; Potential
Topological domain162 – 17615Extracellular Potential
Transmembrane177 – 19721Helical; Name=2; Potential
Topological domain198 – 2058Cytoplasmic Potential
Transmembrane206 – 22621Helical; Name=3; Potential
Topological domain227 – 2304Extracellular Potential
Transmembrane231 – 25121Helical; Name=4; Potential
Topological domain252 – 26312Cytoplasmic Potential
Transmembrane264 – 28421Helical; Name=5; Potential
Topological domain285 – 29612Extracellular Potential
Transmembrane297 – 31721Helical; Name=6; Potential
Topological domain318 – 36346Cytoplasmic Potential
Transmembrane364 – 38421Helical; Name=7; Potential
Topological domain385 – 40218Extracellular Potential
Transmembrane403 – 42321Helical; Name=8; Potential
Topological domain424 – 4329Cytoplasmic Potential
Transmembrane433 – 45321Helical; Name=9; Potential
Topological domain454 – 4574Extracellular Potential
Transmembrane458 – 47821Helical; Name=10; Potential
Topological domain479 – 48911Cytoplasmic Potential
Transmembrane490 – 51021Helical; Name=11; Potential
Topological domain511 – 53525Extracellular Potential
Transmembrane536 – 55621Helical; Name=12; Potential
Topological domain557 – 61660Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.9
Modified residue41Phosphoserine Ref.7
Modified residue111Phosphoserine Ref.7
Modified residue611Phosphoserine Ref.8
Modified residue661Phosphoserine Ref.8
Modified residue701Phosphothreonine Ref.8
Modified residue5841Phosphoserine Ref.7
Modified residue6031Phosphoserine Ref.8
Modified residue6061Phosphoserine Ref.7 Ref.8
Cross-link9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
Cross-link338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Sequences

Sequence LengthMass (Da)Tools
P36035 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 47926F50842ACD5B

FASTA61669,376
        10         20         30         40         50         60 
MSSSITDEKI SGEQQQPAGR KLYYNTSTFA EPPLVDGEGN PINYEPEVYN PDHEKLYHNP 

        70         80         90        100        110        120 
SLPAQSIQDT RDDELLERVY SQDQGVEYEE DEEDKPNLSA ASIKSYALTR FTSLLHIHEF 

       130        140        150        160        170        180 
SWENVNPIPE LRKMTWQNWN YFFMGYFAWL SAAWAFFCVS VSVAPLAELY DRPTKDITWG 

       190        200        210        220        230        240 
LGLVLFVRSA GAVIFGLWTD KSSRKWPYIT CLFLFVIAQL CTPWCDTYEK FLGVRWITGI 

       250        260        270        280        290        300 
AMGGIYGCAS ATAIEDAPVK ARSFLSGLFF SAYAMGFIFA IIFYRAFGYF RDDGWKILFW 

       310        320        330        340        350        360 
FSIFLPILLI FWRLLWPETK YFTKVLKARK LILSDAVKAN GGEPLPKANF KQKMVSMKRT 

       370        380        390        400        410        420 
VQKYWLLFAY LVVLLVGPNY LTHASQDLLP TMLRAQLGLS KDAVTVIVVV TNIGAICGGM 

       430        440        450        460        470        480 
IFGQFMEVTG RRLGLLIACT MGGCFTYPAF MLRSEKAILG AGFMLYFCVF GVWGILPIHL 

       490        500        510        520        530        540 
AELAPADARA LVAGLSYQLG NLASAAASTI ETQLADRYPL ERDASGAVIK EDYAKVMAIL 

       550        560        570        580        590        600 
TGSVFIFTFA CVFVGHEKFH RDLSSPVMKK YINQVEEYEA DGLSISDIVE QKTECASVKM 

       610 
IDSNVSKTYE EHIETV 

« Hide

References

« Hide 'large scale' references
[1]Davis E.S., Brennan M.B.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204510 / AB320.
[2]"The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein."
Tzermia M., Horaitis O., Alexandraki D.
Yeast 10:663-679(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-338.
Strain: SUB592.
[6]"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.
[7]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11; SER-584 AND SER-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[8]"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-61; SER-66; THR-70; SER-603 AND SER-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24155 Genomic DNA. Translation: AAB60291.1.
X75951 Genomic DNA. Translation: CAA53556.1.
Z28217 Genomic DNA. Translation: CAA82062.1.
BK006944 Genomic DNA. Translation: DAA08952.1.
PIRS38060.
RefSeqNP_012705.1. NM_001179782.1.

3D structure databases

ProteinModelPortalP36035.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33948. 28 interactions.
DIPDIP-8064N.
MINTMINT-4988115.
STRING4932.YKL217W.

Protein family/group databases

TCDB2.A.1.12.2. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbP36035.
PeptideAtlasP36035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL217W; YKL217W; YKL217W.
GeneID853663.
KEGGsce:YKL217W.

Organism-specific databases

CYGDYKL217w.
SGDS000001700. JEN1.

Phylogenomic databases

eggNOGCOG0477.
HOGENOMHOG000259757.
KOK08178.
OMADSMDFFC.
OrthoDBEOG78H430.

Enzyme and pathway databases

BioCycYEAST:G3O-31974-MONOMER.

Gene expression databases

GenevestigatorP36035.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004742. SA_transporter.
IPR005828. Sub_transporter.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 1 hit.
TIGRFAMsTIGR00891. 2A0112. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974593.
PROP36035.

Entry information

Entry nameJEN1_YEAST
AccessionPrimary (citable) accession number: P36035
Secondary accession number(s): D6VWY6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 121 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 XI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families