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Entry version 214 (11 Dec 2019)
Sequence version 4 (05 Oct 2010)
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Protein

Elongation factor 3A

Gene

YEF3

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

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. Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells (PubMed:22888004).3 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<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=0.126 mM for ATP1 Publication
  2. KM=0.125 mM for GTP1 Publication
  1. Vmax=15.2 µmol/min/mg enzyme with ATP as substrate1 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 bindingi463 – 470ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi701 – 708ATP 2PROSITE-ProRule annotation8

<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

  • ATPase activity Source: SGD
  • ATP binding Source: GO_Central
  • rRNA binding Source: UniProtKB-KW
  • translation elongation factor activity Source: SGD

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 functionElongation factor, RNA-binding, rRNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32354-MONOMER

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 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
<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:YEF3
Synonyms:EFC1, TEF3, YEF3A
Ordered Locus Names:YLR249W
ORF Names:L9672.5
<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> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR249W

Saccharomyces Genome Database

More...
SGDi
S000004239 YEF3

<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

<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>Mutagenesisi650F → 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 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 methionineiRemovedCombined sources1 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_00000934582 – 1044Elongation factor 3AAdd BLAST1043

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-acetylserineCombined sources1 Publication1
Modified residuei187N6,N6,N6-trimethyllysine1 Publication1
Modified residuei196N6,N6,N6-trimethyllysine1 Publication1
<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-linki350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei642PhosphoserineCombined sources1
Modified residuei789N6,N6,N6-trimethyllysine1 Publication1
Modified residuei972PhosphothreonineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei1039PhosphoserineCombined sources1
Modified residuei1040PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16521

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

More...
PaxDbi
P16521

PRoteomics IDEntifications database

More...
PRIDEi
P16521

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P16521

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16521

<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

Monomer.

Interacts with elongation factor 1A (eEF1A).

Interacts through its N-terminus with 18S rRNA. Associates with ribosomes (PubMed:22888004).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31517, 172 interactors

Database of interacting proteins

More...
DIPi
DIP-2249N

Protein interaction database and analysis system

More...
IntActi
P16521, 83 interactors

Molecular INTeraction database

More...
MINTi
P16521

STRING: functional protein association networks

More...
STRINGi
4932.YLR249W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16521 protein

<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

11044
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
P16521

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P16521

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati5 – 42HEAT 1Add BLAST38
Repeati86 – 123HEAT 2Add BLAST38
Repeati125 – 162HEAT 3Add BLAST38
Repeati166 – 203HEAT 4Add BLAST38
Repeati205 – 241HEAT 5Add BLAST37
Repeati242 – 279HEAT 6Add BLAST38
Repeati285 – 323HEAT 7Add BLAST39
<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>Domaini426 – 641ABC transporter 1PROSITE-ProRule annotationAdd BLAST216
Domaini667 – 993ABC transporter 2PROSITE-ProRule annotationAdd BLAST327

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1009 – 1031Lys-rich (basic)Add BLAST23

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The heat repeats and the C-terminal domain are necessary for impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase activity in amino acid-starved or repleted cells (PubMed:22888004).1 Publication

<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

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000180957

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16521

KEGG Orthology (KO)

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KOi
K03235

Identification of Orthologs from Complete Genome Data

More...
OMAi
EEDQYDA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR040533 4HB
IPR003593 AAA+_ATPase
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR021133 HEAT_type_2
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17947 4HB, 1 hit
PF00005 ABC_tran, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 2 hits
PS50893 ABC_TRANSPORTER_2, 2 hits
PS50077 HEAT_REPEAT, 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.

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
<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:i41E40B8BDD7A4C33
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 conflicti153I → F in AAA35232 (PubMed:2404974).Curated1
Sequence conflicti153I → F no nucleotide entry (PubMed:1976386).Curated1
Sequence conflicti153I → F in AAA35233 (PubMed:2203789).Curated1
Sequence conflicti332V → L in AAA35232 (PubMed:2404974).Curated1
Sequence conflicti332V → L no nucleotide entry (PubMed:1976386).Curated1
Sequence conflicti332V → L in AAA35233 (PubMed:2203789).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
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S59395 DVBYE3

NCBI Reference Sequences

More...
RefSeqi
NP_013350.1, NM_001182136.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR249W_mRNA; YLR249W; YLR249W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850951

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR249W

<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
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

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
2IW3X-ray2.40A/B2-981[»]
2IWHX-ray3.00A/B2-981[»]
2IX3X-ray2.70A/B2-981[»]
2IX8electron microscopy6.00A2-977[»]
SMRiP16521
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31517, 172 interactors
DIPiDIP-2249N
IntActiP16521, 83 interactors
MINTiP16521
STRINGi4932.YLR249W

PTM databases

CarbonylDBiP16521
iPTMnetiP16521

Proteomic databases

MaxQBiP16521
PaxDbiP16521
PRIDEiP16521

Genome annotation databases

EnsemblFungiiYLR249W_mRNA; YLR249W; YLR249W
GeneIDi850951
KEGGisce:YLR249W

Organism-specific databases

EuPathDBiFungiDB:YLR249W
SGDiS000004239 YEF3

Phylogenomic databases

HOGENOMiHOG000180957
InParanoidiP16521
KOiK03235
OMAiEEDQYDA

Enzyme and pathway databases

UniPathwayiUPA00345
BioCyciYEAST:G3O-32354-MONOMER

Miscellaneous databases

EvolutionaryTraceiP16521

Protein Ontology

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PROi
PR:P16521
RNActiP16521 protein

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR040533 4HB
IPR003593 AAA+_ATPase
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR021133 HEAT_type_2
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF17947 4HB, 1 hit
PF00005 ABC_tran, 2 hits
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SUPFAMiSSF48371 SSF48371, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 2 hits
PS50893 ABC_TRANSPORTER_2, 2 hits
PS50077 HEAT_REPEAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiEF3A_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: P16521
Secondary accession number(s): D6VYP7, O93815, Q06558
<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: August 1, 1990
Last sequence update: October 5, 2010
Last modified: December 11, 2019
This is version 214 of the entry and version 4 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, 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
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