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P16521

- EF3A_YEAST

UniProt

P16521 - EF3A_YEAST

Protein

Elongation factor 3A

Gene

YEF3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis. Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied.2 Publications

    Enzyme regulationi

    Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity.1 Publication

    Kineticsi

    1. KM=0.126 mM for ATP1 Publication
    2. KM=0.125 mM for GTP1 Publication

    Vmax=15.2 µmol/min/mg enzyme with ATP as substrate1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi463 – 4708ATP 1PROSITE-ProRule annotation
    Nucleotide bindingi701 – 7088ATP 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. rRNA binding Source: UniProtKB-KW
    4. translation elongation factor activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. translational elongation Source: SGD
    3. translational termination Source: SGD

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32354-MONOMER.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 3A
    Short name:
    EF-3
    Short name:
    EF-3A
    Alternative name(s):
    Eukaryotic elongation factor 3
    Short name:
    eEF3
    Translation elongation factor 3A
    Yeast elongation factor 3
    Gene namesi
    Name:YEF3
    Synonyms:EFC1, TEF3, YEF3A
    Ordered Locus Names:YLR249W
    ORF Names:L9672.5
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004239. YEF3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasmic stress granule Source: SGD
    2. cytosolic ribosome Source: SGD
    3. ribosome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi650 – 6501F → S: Reduces ATPase activity and interaction with eEF1A. Required for growth at 37 degrees Celsius and causes a 50% reduction of total protein synthesis at permissive temperatures. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 10441043Elongation factor 3APRO_0000093458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei642 – 6421Phosphoserine2 Publications
    Modified residuei972 – 9721Phosphothreonine3 Publications
    Modified residuei974 – 9741Phosphoserine2 Publications
    Modified residuei1039 – 10391Phosphoserine4 Publications
    Modified residuei1040 – 10401Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16521.
    PaxDbiP16521.
    PeptideAtlasiP16521.
    PRIDEiP16521.

    Expressioni

    Gene expression databases

    GenevestigatoriP16521.

    Interactioni

    Subunit structurei

    Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA.3 Publications

    Protein-protein interaction databases

    BioGridi31517. 134 interactions.
    DIPiDIP-2249N.
    IntActiP16521. 84 interactions.
    MINTiMINT-8285353.

    Structurei

    Secondary structure

    1
    1044
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1816
    Turni23 – 253
    Helixi26 – 3712
    Beta strandi42 – 454
    Helixi48 – 5811
    Helixi61 – 7414
    Turni77 – 793
    Turni82 – 843
    Helixi85 – 895
    Helixi92 – 987
    Helixi104 – 12017
    Helixi123 – 1253
    Helixi126 – 13914
    Helixi143 – 15917
    Helixi161 – 17818
    Helixi184 – 19714
    Helixi198 – 2003
    Turni204 – 2063
    Helixi207 – 2093
    Helixi210 – 2189
    Helixi222 – 2309
    Helixi241 – 25515
    Beta strandi257 – 2593
    Helixi260 – 27415
    Helixi280 – 2834
    Helixi284 – 2896
    Helixi291 – 2977
    Turni298 – 3003
    Helixi304 – 32118
    Turni325 – 3273
    Helixi338 – 34811
    Turni349 – 3513
    Helixi356 – 3583
    Helixi359 – 37416
    Helixi380 – 3867
    Helixi388 – 3914
    Turni392 – 3943
    Helixi397 – 41317
    Beta strandi426 – 4283
    Beta strandi430 – 44011
    Beta strandi443 – 45412
    Beta strandi458 – 4625
    Helixi469 – 47810
    Turni487 – 4893
    Beta strandi492 – 4943
    Helixi508 – 5136
    Turni514 – 5163
    Helixi520 – 52910
    Helixi534 – 5385
    Helixi541 – 5433
    Helixi546 – 55914
    Beta strandi563 – 5697
    Turni570 – 5734
    Helixi576 – 58813
    Beta strandi591 – 5966
    Helixi600 – 6067
    Beta strandi608 – 6147
    Beta strandi617 – 6237
    Helixi625 – 6317
    Helixi633 – 6375
    Beta strandi638 – 6403
    Turni641 – 6433
    Beta strandi664 – 67411
    Beta strandi679 – 6813
    Beta strandi683 – 69210
    Beta strandi696 – 6994
    Helixi705 – 71410
    Beta strandi721 – 7277
    Beta strandi733 – 7364
    Helixi738 – 7436
    Helixi744 – 7463
    Helixi752 – 7598
    Turni760 – 7623
    Turni766 – 7727
    Helixi783 – 7853
    Beta strandi788 – 7903
    Beta strandi793 – 80614
    Beta strandi809 – 82113
    Beta strandi828 – 8314
    Helixi834 – 8363
    Beta strandi838 – 8414
    Helixi842 – 8443
    Helixi846 – 86318
    Helixi872 – 88110
    Helixi886 – 8916
    Helixi894 – 8963
    Helixi899 – 91113
    Beta strandi916 – 9216
    Helixi923 – 9253
    Helixi929 – 94012
    Beta strandi943 – 9497
    Helixi953 – 9564
    Turni957 – 9593
    Beta strandi962 – 9643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IW3X-ray2.40A/B2-981[»]
    2IWHX-ray3.00A/B2-981[»]
    2IX3X-ray2.70A/B2-981[»]
    2IX8electron microscopy6.00A2-977[»]
    ProteinModelPortaliP16521.
    SMRiP16521. Positions 2-977.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16521.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati5 – 4238HEAT 1Add
    BLAST
    Repeati86 – 12338HEAT 2Add
    BLAST
    Repeati125 – 16238HEAT 3Add
    BLAST
    Repeati166 – 20338HEAT 4Add
    BLAST
    Repeati205 – 24137HEAT 5Add
    BLAST
    Repeati242 – 27938HEAT 6Add
    BLAST
    Repeati285 – 32339HEAT 7Add
    BLAST
    Domaini426 – 641216ABC transporter 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini667 – 993327ABC transporter 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1009 – 103123Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Contains 2 ABC transporter domains.PROSITE-ProRule annotation
    Contains 7 HEAT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0488.
    GeneTreeiENSGT00550000075671.
    HOGENOMiHOG000180957.
    KOiK03235.
    OMAiFPTQEEC.
    OrthoDBiEOG7Q2NDN.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015688. Elongation_fac_3.
    IPR021133. HEAT_type_2.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR19211:SF5. PTHR19211:SF5. 1 hit.
    PfamiPF00005. ABC_tran. 2 hits.
    [Graphical view]
    SMARTiSM00382. AAA. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 6 hits.
    SSF52540. SSF52540. 3 hits.
    PROSITEiPS00211. ABC_TRANSPORTER_1. 2 hits.
    PS50893. ABC_TRANSPORTER_2. 2 hits.
    PS50077. HEAT_REPEAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16521-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF     50
    FGELAKGIKD KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG 100
    NKDKEIQSVA SETLISIVNA VNPVAIKALL PHLTNAIVET NKWQEKIAIL 150
    AAISAMVDAA KDQVALRMPE LIPVLSETMW DTKKEVKAAA TAAMTKATET 200
    VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT PATLSIMVPL 250
    LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT 300
    IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK 350
    DETVAPRFKI VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA 400
    KDILDEFRKR AVDNIPVGPN FDDEEDEGED LCNCEFSLAY GAKILLNKTQ 450
    LRLKRARRYG ICGPNGCGKS TLMRAIANGQ VDGFPTQEEC RTVYVEHDID 500
    GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP ISALSGGWKM 550
    KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS 600
    VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF 650
    PEPGYLEGVK TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI 700
    GPNGAGKSTL INVLTGELLP TSGEVYTHEN CRIAYIKQHA FAHIESHLDK 750
    TPSEYIQWRF QTGEDRETMD RANRQINEND AEAMNKIFKI EGTPRRIAGI 800
    HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI PRGELVESHS 850
    KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG 900
    QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT 950
    HSAEFTKNLT EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA 1000
    MGNKIAGGKK KKKLSSAELR KKKKERMKKK KELGDAYVSS DEEF 1044
    Length:1,044
    Mass (Da):115,945
    Last modified:October 5, 2010 - v4
    Checksum:i41E40B8BDD7A4C33
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531I → F in AAA35232. (PubMed:2404974)Curated
    Sequence conflicti153 – 1531I → F no nucleotide entry (PubMed:1976386)Curated
    Sequence conflicti153 – 1531I → F in AAA35233. (PubMed:2203789)Curated
    Sequence conflicti332 – 3321V → L in AAA35232. (PubMed:2404974)Curated
    Sequence conflicti332 – 3321V → L no nucleotide entry (PubMed:1976386)Curated
    Sequence conflicti332 – 3321V → L in AAA35233. (PubMed:2203789)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05197 Genomic DNA. Translation: AAA35232.1.
    J05583 Genomic DNA. Translation: AAA35233.1.
    U20865 Genomic DNA. Translation: AAB67391.1.
    AB018539 Genomic DNA. Translation: BAA33897.1.
    BK006945 Genomic DNA. Translation: DAA09563.1.
    PIRiS59395. DVBYE3.
    RefSeqiNP_013350.1. NM_001182136.1.

    Genome annotation databases

    EnsemblFungiiYLR249W; YLR249W; YLR249W.
    GeneIDi850951.
    KEGGisce:YLR249W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05197 Genomic DNA. Translation: AAA35232.1 .
    J05583 Genomic DNA. Translation: AAA35233.1 .
    U20865 Genomic DNA. Translation: AAB67391.1 .
    AB018539 Genomic DNA. Translation: BAA33897.1 .
    BK006945 Genomic DNA. Translation: DAA09563.1 .
    PIRi S59395. DVBYE3.
    RefSeqi NP_013350.1. NM_001182136.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IW3 X-ray 2.40 A/B 2-981 [» ]
    2IWH X-ray 3.00 A/B 2-981 [» ]
    2IX3 X-ray 2.70 A/B 2-981 [» ]
    2IX8 electron microscopy 6.00 A 2-977 [» ]
    ProteinModelPortali P16521.
    SMRi P16521. Positions 2-977.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31517. 134 interactions.
    DIPi DIP-2249N.
    IntActi P16521. 84 interactions.
    MINTi MINT-8285353.

    Proteomic databases

    MaxQBi P16521.
    PaxDbi P16521.
    PeptideAtlasi P16521.
    PRIDEi P16521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR249W ; YLR249W ; YLR249W .
    GeneIDi 850951.
    KEGGi sce:YLR249W.

    Organism-specific databases

    SGDi S000004239. YEF3.

    Phylogenomic databases

    eggNOGi COG0488.
    GeneTreei ENSGT00550000075671.
    HOGENOMi HOG000180957.
    KOi K03235.
    OMAi FPTQEEC.
    OrthoDBi EOG7Q2NDN.

    Enzyme and pathway databases

    UniPathwayi UPA00345 .
    BioCyci YEAST:G3O-32354-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P16521.
    NextBioi 967419.

    Gene expression databases

    Genevestigatori P16521.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015688. Elongation_fac_3.
    IPR021133. HEAT_type_2.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR19211:SF5. PTHR19211:SF5. 1 hit.
    Pfami PF00005. ABC_tran. 2 hits.
    [Graphical view ]
    SMARTi SM00382. AAA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 6 hits.
    SSF52540. SSF52540. 3 hits.
    PROSITEi PS00211. ABC_TRANSPORTER_1. 2 hits.
    PS50893. ABC_TRANSPORTER_2. 2 hits.
    PS50077. HEAT_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae."
      Qin S., Xie A., Bonato M.C.M., McLaughlin C.S.
      J. Biol. Chem. 265:1903-1912(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation and characterization of the structural gene encoding elongation factor 3."
      Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.
      Biochim. Biophys. Acta 1050:230-234(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3."
      Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.
      J. Biol. Chem. 265:15838-15844(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Detection and analysis of translation elongation factor 3 genes from various yeasts."
      Uritani M., Shoumura Y., Yamada S.
      Biosci. Biotechnol. Biochem. 63:769-772(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955.
      Strain: ATCC 208279 / BJ926.
    7. Cited for: PROTEIN SEQUENCE OF 959-967.
      Strain: ATCC 204508 / S288c.
    8. "Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae."
      Dasmahapatra B., Chakraburtty K.
      J. Biol. Chem. 256:9999-10004(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor."
      Triana-Alonso F.J., Chakraburtty K., Nierhaus K.H.
      J. Biol. Chem. 270:20473-20478(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Comparative analysis of ribosome-associated adenosinetriphosphatase (ATPase) from pig liver and the ATPase of elongation factor 3 from Saccharomyces cerevisiae."
      Kovalchuke O., Chakraburtty K.
      Eur. J. Biochem. 226:133-140(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    12. "Competition and cooperation amongst yeast elongation factors."
      Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.
      Eur. J. Biochem. 258:986-993(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EEF1A.
    13. "Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 in Saccharomyces cerevisiae."
      Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R., Moehle C.M., Goldman R.C.
      Yeast 14:239-253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    14. "The N-terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes."
      Gontarek R.R., Li H., Nurse K., Prescott C.D.
      J. Biol. Chem. 273:10249-10252(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 18S RRNA.
    15. "A sampling of the yeast proteome."
      Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.
      Mol. Cell. Biol. 19:7357-7368(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    16. "Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3."
      Anand M., Chakraburtty K., Marton M.J., Hinnebusch A.G., Kinzy T.G.
      J. Biol. Chem. 278:6985-6991(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-650, INTERACTION WITH EEF1A.
    17. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    18. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    19. "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-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    20. "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-972; SER-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-642; THR-972; SER-974; SER-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEF3A_YEAST
    AccessioniPrimary (citable) accession number: P16521
    Secondary accession number(s): D6VYP7, O93815, Q06558
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 164 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 870578 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3