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Entry version 220 (03 Jul 2019)
Sequence version 1 (21 Jul 1986)
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Protein

Elongation factor 1-alpha

Gene

TEF1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells (PubMed:21849502).4 Publications

Miscellaneous

Present with 827 molecules/cell in log phase SD medium.1 Publication
There are two genes for eEF1A in yeast.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.14 mM for GTP1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: polypeptide chain elongation

    This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi14 – 21GTP8
    Nucleotide bindingi91 – 95GTP5
    Nucleotide bindingi153 – 156GTP4

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionActin-binding, Elongation factor
    Biological processProtein biosynthesis
    LigandGTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-29075-MONOMER
    YEAST:G3O-34224-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-156842 Eukaryotic Translation Elongation
    R-SCE-3371511 HSF1 activation
    R-SCE-6798695 Neutrophil degranulation
    R-SCE-8876725 Protein methylation

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00345

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Elongation factor 1-alpha
    Short name:
    EF-1-alpha
    Alternative name(s):
    Eukaryotic elongation factor 1A
    Short name:
    eEF1A
    Translation elongation factor 1A
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:TEF1
    Ordered Locus Names:YPR080W
    ORF Names:P9513.7
    AND
    Name:TEF2
    Ordered Locus Names:YBR118W
    ORF Names:YBR0913
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome II, Chromosome XVI

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000006284 TEF1
    S000000322 TEF2

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi122E → K: Reduces interaction with YEF3. 1 Publication1
    Mutagenesisi153N → D: Increases KM for GTP to 2.7 mM. 2 Publications1
    Mutagenesisi153N → T: Increases KM for GTP to 6.0 mM and reduces translation fidelity. Increases Km for GTP to 10.3 mM and reduces translation fidelity; when associated with E-156. 2 Publications1
    Mutagenesisi156D → E: Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152. 3 Publications1
    Mutagenesisi156D → N: Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. 3 Publications1
    Mutagenesisi156D → W: Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. 3 Publications1
    Mutagenesisi286E → K in TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication1
    Mutagenesisi317E → K in TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000909732 – 458Elongation factor 1-alphaAdd BLAST457

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N,N,N-trimethylglycine; by EFM71 Publication1
    Modified residuei3N6,N6-dimethyllysine; by EFM7; alternate1 Publication1
    Modified residuei3N6-methyllysine; by EFM7; alternate1 Publication1
    Modified residuei18PhosphoserineCombined sources1
    Modified residuei30N6-methyllysine; by EFM13 Publications1
    Modified residuei72PhosphothreonineCombined sources1
    Modified residuei79N6,N6,N6-trimethyllysine; by EFM54 Publications1
    Modified residuei82PhosphothreonineCombined sources1
    Modified residuei163PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Cross-linki242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Cross-linki253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei259PhosphothreonineCombined sources1
    Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei289PhosphoserineCombined sources1
    Modified residuei316N6,N6-dimethyllysine; by EFM4; alternate3 Publications1
    Modified residuei316N6-methyllysine; by EFM4; alternate1 Publication1
    Modified residuei390N6-methyllysine; by EFM64 Publications1
    Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei414PhosphoserineCombined sources1
    Modified residuei430PhosphothreonineCombined sources1
    Cross-linki437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei458Lysine methyl ester1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei298Not modified1
    Sitei372Not modified1

    Keywords - PTMi

    Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P02994

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P02994

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P02994

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    P02994

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P02994

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P02994

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1A interacts directly with eEF1Balpha.

    Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin.

    Interacts with the proteasome, probably via RPT1.

    Interacts with CEX1 and NAP1.

    Interacts with GCN2 (via C-terminus); this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates with ribosomes (PubMed:21849502).

    11 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    32820, 344 interactors
    36251, 229 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-2854 Elongation Factor eEF1 complex, variant CAM1
    CPX-425 Elongation Factor eEF1 complex, variant TEF4

    Database of interacting proteins

    More...
    DIPi
    DIP-2250N

    Protein interaction database and analysis system

    More...
    IntActi
    P02994, 808 interactors

    Molecular INTeraction database

    More...
    MINTi
    P02994

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YPR080W

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1458
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P02994

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P02994

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 240tr-type GAdd BLAST236

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni14 – 21G1By similarity8
    Regioni70 – 74G2By similarity5
    Regioni91 – 94G3By similarity4
    Regioni153 – 156G4By similarity4
    Regioni192 – 194G5By similarity3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000164334

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000229291

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P02994

    KEGG Orthology (KO)

    More...
    KOi
    K03231

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YKGWTKE

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00118_A EF_Tu_A, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004161 EFTu-like_2
    IPR031157 G_TR_CS
    IPR027417 P-loop_NTPase
    IPR000795 TF_GTP-bd_dom
    IPR009000 Transl_B-barrel_sf
    IPR009001 Transl_elong_EF1A/Init_IF2_C
    IPR004539 Transl_elong_EF1A_euk/arc
    IPR004160 Transl_elong_EFTu/EF1A_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00009 GTP_EFTU, 1 hit
    PF03144 GTP_EFTU_D2, 1 hit
    PF03143 GTP_EFTU_D3, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00315 ELONGATNFCT

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50447 SSF50447, 1 hit
    SSF50465 SSF50465, 1 hit
    SSF52540 SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00483 EF-1_alpha, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00301 G_TR_1, 1 hit
    PS51722 G_TR_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P02994-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG
    60 70 80 90 100
    KGSFKYAWVL DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK
    110 120 130 140 150
    NMITGTSQAD CAILIIAGGV GEFEAGISKD GQTREHALLA FTLGVRQLIV
    160 170 180 190 200
    AVNKMDSVKW DESRFQEIVK ETSNFIKKVG YNPKTVPFVP ISGWNGDNMI
    210 220 230 240 250
    EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT DKPLRLPLQD
    260 270 280 290 300
    VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG
    310 320 330 340 350
    VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ
    360 370 380 390 400
    ISAGYSPVLD CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV
    410 420 430 440 450
    KFVPSKPMCV EAFSEYPPLG RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK

    AAQKAAKK
    Length:458
    Mass (Da):50,033
    Last modified:July 21, 1986 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i411C66D830716576
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti86Q → E AA sequence (PubMed:3882705).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X00779 Genomic DNA Translation: CAA25356.1
    X01638 Genomic DNA Translation: CAA25798.1
    M10992 Genomic DNA Translation: AAA34585.1
    M15666 Genomic DNA Translation: AAA34584.1
    M15667 Genomic DNA Translation: AAA34586.1
    X78993 Genomic DNA Translation: CAA55620.1
    Z35987 Genomic DNA Translation: CAA85075.1
    U51033 Genomic DNA Translation: AAB68129.1
    AY692927 Genomic DNA Translation: AAT92946.1
    X73532 Genomic DNA Translation: CAA51936.1
    AF402004 Genomic DNA Translation: AAP86465.1
    AY130810 Genomic DNA Translation: AAM83111.1
    AY130811 Genomic DNA Translation: AAM83112.1
    AY130812 Genomic DNA Translation: AAM83113.1
    AY130813 Genomic DNA Translation: AAM83114.1
    BK006936 Genomic DNA Translation: DAA07236.1
    BK006949 Genomic DNA Translation: DAA11498.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A03522 EFBY1A

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_009676.1, NM_001178466.1
    NP_015405.1, NM_001184177.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YBR118W_mRNA; YBR118W_mRNA; YBR118W
    YPR080W_mRNA; YPR080W_mRNA; YPR080W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    852415
    856195

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YBR118W
    sce:YPR080W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00779 Genomic DNA Translation: CAA25356.1
    X01638 Genomic DNA Translation: CAA25798.1
    M10992 Genomic DNA Translation: AAA34585.1
    M15666 Genomic DNA Translation: AAA34584.1
    M15667 Genomic DNA Translation: AAA34586.1
    X78993 Genomic DNA Translation: CAA55620.1
    Z35987 Genomic DNA Translation: CAA85075.1
    U51033 Genomic DNA Translation: AAB68129.1
    AY692927 Genomic DNA Translation: AAT92946.1
    X73532 Genomic DNA Translation: CAA51936.1
    AF402004 Genomic DNA Translation: AAP86465.1
    AY130810 Genomic DNA Translation: AAM83111.1
    AY130811 Genomic DNA Translation: AAM83112.1
    AY130812 Genomic DNA Translation: AAM83113.1
    AY130813 Genomic DNA Translation: AAM83114.1
    BK006936 Genomic DNA Translation: DAA07236.1
    BK006949 Genomic DNA Translation: DAA11498.1
    PIRiA03522 EFBY1A
    RefSeqiNP_009676.1, NM_001178466.1
    NP_015405.1, NM_001184177.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F60X-ray1.67A1-458[»]
    1G7CX-ray2.05A1-458[»]
    1IJEX-ray2.40A1-458[»]
    1IJFX-ray3.00A1-458[»]
    2B7BX-ray2.60A1-458[»]
    2B7CX-ray1.80A1-458[»]
    5O8WX-ray1.67A1-458[»]
    SMRiP02994
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi32820, 344 interactors
    36251, 229 interactors
    ComplexPortaliCPX-2854 Elongation Factor eEF1 complex, variant CAM1
    CPX-425 Elongation Factor eEF1 complex, variant TEF4
    DIPiDIP-2250N
    IntActiP02994, 808 interactors
    MINTiP02994
    STRINGi4932.YPR080W

    PTM databases

    CarbonylDBiP02994
    iPTMnetiP02994

    Proteomic databases

    MaxQBiP02994
    PaxDbiP02994
    PRIDEiP02994
    TopDownProteomicsiP02994

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYBR118W_mRNA; YBR118W_mRNA; YBR118W
    YPR080W_mRNA; YPR080W_mRNA; YPR080W
    GeneIDi852415
    856195
    KEGGisce:YBR118W
    sce:YPR080W

    Organism-specific databases

    SGDiS000006284 TEF1
    S000000322 TEF2

    Phylogenomic databases

    GeneTreeiENSGT00940000164334
    HOGENOMiHOG000229291
    InParanoidiP02994
    KOiK03231
    OMAiYKGWTKE

    Enzyme and pathway databases

    UniPathwayiUPA00345
    BioCyciYEAST:G3O-29075-MONOMER
    YEAST:G3O-34224-MONOMER
    ReactomeiR-SCE-156842 Eukaryotic Translation Elongation
    R-SCE-3371511 HSF1 activation
    R-SCE-6798695 Neutrophil degranulation
    R-SCE-8876725 Protein methylation

    Miscellaneous databases

    EvolutionaryTraceiP02994

    Protein Ontology

    More...
    PROi
    PR:P02994

    Family and domain databases

    HAMAPiMF_00118_A EF_Tu_A, 1 hit
    InterProiView protein in InterPro
    IPR004161 EFTu-like_2
    IPR031157 G_TR_CS
    IPR027417 P-loop_NTPase
    IPR000795 TF_GTP-bd_dom
    IPR009000 Transl_B-barrel_sf
    IPR009001 Transl_elong_EF1A/Init_IF2_C
    IPR004539 Transl_elong_EF1A_euk/arc
    IPR004160 Transl_elong_EFTu/EF1A_C
    PfamiView protein in Pfam
    PF00009 GTP_EFTU, 1 hit
    PF03144 GTP_EFTU_D2, 1 hit
    PF03143 GTP_EFTU_D3, 1 hit
    PRINTSiPR00315 ELONGATNFCT
    SUPFAMiSSF50447 SSF50447, 1 hit
    SSF50465 SSF50465, 1 hit
    SSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR00483 EF-1_alpha, 1 hit
    PROSITEiView protein in PROSITE
    PS00301 G_TR_1, 1 hit
    PS51722 G_TR_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEF1A_YEAST
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02994
    Secondary accession number(s): D6VQB6
    , Q7Z7U8, Q7Z8Q8, Q7Z8Q9
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: July 3, 2019
    This is version 220 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    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 chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
    5. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    6. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
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