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P16521

- EF3A_YEAST

UniProt

P16521 - EF3A_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 residuei187 – 1871N6,N6,N6-trimethyllysine1 Publication
Modified residuei196 – 1961N6,N6,N6-trimethyllysine1 Publication
Modified residuei642 – 6421Phosphoserine2 Publications
Modified residuei789 – 7891N6,N6,N6-trimethyllysine1 Publication
Modified residuei972 – 9721Phosphothreonine3 Publications
Modified residuei974 – 9741Phosphoserine2 Publications
Modified residuei1039 – 10391Phosphoserine4 Publications
Modified residuei1040 – 10401Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Methylation, 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. 135 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 – 1816Combined sources
Turni23 – 253Combined sources
Helixi26 – 3712Combined sources
Beta strandi42 – 454Combined sources
Helixi48 – 5811Combined sources
Helixi61 – 7414Combined sources
Turni77 – 793Combined sources
Turni82 – 843Combined sources
Helixi85 – 895Combined sources
Helixi92 – 987Combined sources
Helixi104 – 12017Combined sources
Helixi123 – 1253Combined sources
Helixi126 – 13914Combined sources
Helixi143 – 15917Combined sources
Helixi161 – 17818Combined sources
Helixi184 – 19714Combined sources
Helixi198 – 2003Combined sources
Turni204 – 2063Combined sources
Helixi207 – 2093Combined sources
Helixi210 – 2189Combined sources
Helixi222 – 2309Combined sources
Helixi241 – 25515Combined sources
Beta strandi257 – 2593Combined sources
Helixi260 – 27415Combined sources
Helixi280 – 2834Combined sources
Helixi284 – 2896Combined sources
Helixi291 – 2977Combined sources
Turni298 – 3003Combined sources
Helixi304 – 32118Combined sources
Turni325 – 3273Combined sources
Helixi338 – 34811Combined sources
Turni349 – 3513Combined sources
Helixi356 – 3583Combined sources
Helixi359 – 37416Combined sources
Helixi380 – 3867Combined sources
Helixi388 – 3914Combined sources
Turni392 – 3943Combined sources
Helixi397 – 41317Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi430 – 44011Combined sources
Beta strandi443 – 45412Combined sources
Beta strandi458 – 4625Combined sources
Helixi469 – 47810Combined sources
Turni487 – 4893Combined sources
Beta strandi492 – 4943Combined sources
Helixi508 – 5136Combined sources
Turni514 – 5163Combined sources
Helixi520 – 52910Combined sources
Helixi534 – 5385Combined sources
Helixi541 – 5433Combined sources
Helixi546 – 55914Combined sources
Beta strandi563 – 5697Combined sources
Turni570 – 5734Combined sources
Helixi576 – 58813Combined sources
Beta strandi591 – 5966Combined sources
Helixi600 – 6067Combined sources
Beta strandi608 – 6147Combined sources
Beta strandi617 – 6237Combined sources
Helixi625 – 6317Combined sources
Helixi633 – 6375Combined sources
Beta strandi638 – 6403Combined sources
Turni641 – 6433Combined sources
Beta strandi664 – 67411Combined sources
Beta strandi679 – 6813Combined sources
Beta strandi683 – 69210Combined sources
Beta strandi696 – 6994Combined sources
Helixi705 – 71410Combined sources
Beta strandi721 – 7277Combined sources
Beta strandi733 – 7364Combined sources
Helixi738 – 7436Combined sources
Helixi744 – 7463Combined sources
Helixi752 – 7598Combined sources
Turni760 – 7623Combined sources
Turni766 – 7727Combined sources
Helixi783 – 7853Combined sources
Beta strandi788 – 7903Combined sources
Beta strandi793 – 80614Combined sources
Beta strandi809 – 82113Combined sources
Beta strandi828 – 8314Combined sources
Helixi834 – 8363Combined sources
Beta strandi838 – 8414Combined sources
Helixi842 – 8443Combined sources
Helixi846 – 86318Combined sources
Helixi872 – 88110Combined sources
Helixi886 – 8916Combined sources
Helixi894 – 8963Combined sources
Helixi899 – 91113Combined sources
Beta strandi916 – 9216Combined sources
Helixi923 – 9253Combined sources
Helixi929 – 94012Combined sources
Beta strandi943 – 9497Combined sources
Helixi953 – 9564Combined sources
Turni957 – 9593Combined sources
Beta strandi962 – 9643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP16521.
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

        10         20         30         40         50
MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF
60 70 80 90 100
FGELAKGIKD KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG
110 120 130 140 150
NKDKEIQSVA SETLISIVNA VNPVAIKALL PHLTNAIVET NKWQEKIAIL
160 170 180 190 200
AAISAMVDAA KDQVALRMPE LIPVLSETMW DTKKEVKAAA TAAMTKATET
210 220 230 240 250
VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT PATLSIMVPL
260 270 280 290 300
LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT
310 320 330 340 350
IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK
360 370 380 390 400
DETVAPRFKI VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA
410 420 430 440 450
KDILDEFRKR AVDNIPVGPN FDDEEDEGED LCNCEFSLAY GAKILLNKTQ
460 470 480 490 500
LRLKRARRYG ICGPNGCGKS TLMRAIANGQ VDGFPTQEEC RTVYVEHDID
510 520 530 540 550
GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP ISALSGGWKM
560 570 580 590 600
KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS
610 620 630 640 650
VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF
660 670 680 690 700
PEPGYLEGVK TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI
710 720 730 740 750
GPNGAGKSTL INVLTGELLP TSGEVYTHEN CRIAYIKQHA FAHIESHLDK
760 770 780 790 800
TPSEYIQWRF QTGEDRETMD RANRQINEND AEAMNKIFKI EGTPRRIAGI
810 820 830 840 850
HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI PRGELVESHS
860 870 880 890 900
KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG
910 920 930 940 950
QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT
960 970 980 990 1000
HSAEFTKNLT EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA
1010 1020 1030 1040
MGNKIAGGKK KKKLSSAELR KKKKERMKKK KELGDAYVSS DEEF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 135 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.
InParanoidi P16521.
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

« Hide 'large scale' publications
  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].
  24. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
    Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
    Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-187; LYS-196 AND LYS-789.

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: November 26, 2014
This is version 166 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