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Entry version 161 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Elongator complex protein 3

Gene

ELP3

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

Catalytic subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation (PubMed:10024884, PubMed:11296232, PubMed:11689709, PubMed:13680368). Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD) (PubMed:10024884, PubMed:11296232, PubMed:11689709, PubMed:13680368). The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15138274, PubMed:15769872, PubMed:17018299, PubMed:18755837, PubMed:21912530). ELP3 acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Independently, ELP3 may be involved in polarized exocytosis (PubMed:15780940).By similarity10 Publications

Miscellaneous

Present with 4760 molecules/cell in log phase SD medium.1 Publication

Caution

Was initially thought to display histone acetyltransferase activity and reported to acetylate histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8' (PubMed:10445034, PubMed:11904415). However, it was later shown that the effect on histone acetylation and chromatin regulation is indirect and that the elongator complex is primarily involved in tRNA modification (PubMed:17018299, PubMed:18986986, PubMed:21912530).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster (PubMed:16420352). The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:16420352). The cluster is required for structural integrity of the elongator complex, while it is not required for catalytic activity (PubMed:18986986).2 Publications

<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: 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.3 Publications
View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi108Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi118Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi121Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei173Acetyl-CoABy similarity1
Binding sitei541Acetyl-CoABy similarity1

<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 functionAcyltransferase, RNA-binding, Transferase, tRNA-binding
Biological processTranscription, Transcription regulation, tRNA processing
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33992-MONOMER

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

More...
UniPathwayi
UPA00988

<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:
Elongator complex protein 3Curated
Alternative name(s):
Gamma-toxin target 3
tRNA uridine(34) acetyltransferaseCurated (EC:2.3.1.-By similarity)
<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:ELP31 PublicationImported
Synonyms:HPA1, TOT3
Ordered Locus Names:YPL086C
<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 XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPL086C

Saccharomyces Genome Database

More...
SGDi
S000006007 ELP3

<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, Nucleus

<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>Mutagenesisi53K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi56K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi57K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi59K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi61K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi65R → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi78K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi79K → A: Does not affect tRNA modification. 1 Publication1
Mutagenesisi86 – 88KAK → AAA: Decreased tRNA modification. 1 Publication3
Mutagenesisi91R → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi103C → A: Impaired tRNA wobble uridine modification. 2 Publications1
Mutagenesisi108C → A: Dissociation of the elongator complex following assembly. Abolished interaction with KTI11 and KTI12. 1 Publication1
Mutagenesisi108C → S: Eliminates iron contents; when associated with S-118 and S-121. 1 Publication1
Mutagenesisi110H → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi118 – 121CVYC → SVYS: Decreased tRNA modification. 1 Publication4
Mutagenesisi118C → A: Dissociation of the elongator complex following assembly. 1 Publication1
Mutagenesisi118C → S: Eliminates iron contents; when associated with S-108 and S-121. 1 Publication1
Mutagenesisi119 – 120VY → AA: Decreased tRNA modification. 1 Publication2
Mutagenesisi121C → A: Dissociation of the elongator complex following assembly. 1 Publication1
Mutagenesisi121C → S: Eliminates iron contents; when associated with S-108 and S-118. 1 Publication1
Mutagenesisi136Y → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi168G → R: Impaired tRNA wobble uridine modification. 1 Publication1
Mutagenesisi232R → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi251R → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi269R → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi271H → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi289K → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi325K → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi341W → A: Decreased tRNA modification. 1 Publication1
Mutagenesisi373R → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi376R → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi411R → A: Abolished tRNA modification. 1 Publication1
Mutagenesisi540Y → A: Does not affect interaction with KTI11 and KTI12. 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 ‘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_00002358111 – 557Elongator complex protein 3Add BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q02908

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

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PaxDbi
Q02908

PRoteomics IDEntifications database

More...
PRIDEi
Q02908

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q02908

<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

Component of the RNA polymerase II elongator complex, which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:10445034, PubMed:11435442, PubMed:11689709, PubMed:18986986, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two-lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). ELP3 interacts with KTI11 (PubMed:18986986). ELP3 interacts with KTI12 (PubMed:15772087).

7 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

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
36095, 536 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-779 Elongator holoenzyme complex

Database of interacting proteins

More...
DIPi
DIP-2385N

Protein interaction database and analysis system

More...
IntActi
Q02908, 18 interactors

Molecular INTeraction database

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MINTi
Q02908

STRING: functional protein association networks

More...
STRINGi
4932.YPL086C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q02908 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

1557
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

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SMRi
Q02908

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini405 – 557N-acetyltransferasePROSITE-ProRule annotationAdd BLAST153

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>Regioni485 – 488Acetyl-CoA bindingBy similarity4
Regioni508 – 510Acetyl-CoA bindingBy 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

Belongs to the ELP3 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000227514

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q02908

KEGG Orthology (KO)

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KOi
K07739

Identification of Orthologs from Complete Genome Data

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OMAi
TFETRPD

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.30.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR039661 ELP3
IPR034687 ELP3-like
IPR006638 Elp3/MiaB/NifB
IPR000182 GNAT_dom
IPR032432 Radical_SAM_C
IPR007197 rSAM
IPR023404 rSAM_horseshoe

The PANTHER Classification System

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PANTHERi
PTHR11135 PTHR11135, 1 hit
PTHR11135:SF0 PTHR11135:SF0, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00583 Acetyltransf_1, 1 hit
PF04055 Radical_SAM, 1 hit
PF16199 Radical_SAM_C, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF005669 Hist_AcTrfase_ELP3, 1 hit

Structure-Function Linkage Database

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SFLDi
SFLDF00344 ELP3-like, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00729 Elp3, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55729 SSF55729, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01211 ELP3, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51186 GNAT, 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.

Q02908-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARHGKGPKT NKKKLAPEKE RFIQCCADIT LELTDSLTSG TTREINLNGL
60 70 80 90 100
ITKYSKKYKL KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA
110 120 130 140 150
VMCKPHRCPH IAYTGNICVY CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR
160 170 180 190 200
YDPYEQARGR VEQLKQLGHS IDKVEYVLMG GTFMSLPKEY REDFIVKLHN
210 220 230 240 250
ALSGFNGNDI DEAILYSQQS LTKCVGITIE TRPDYCTQTH LDDMLKYGCT
260 270 280 290 300
RLEIGVQSLY EDVARDTNRG HTVRSVCETF AVSKDAGYKV VSHMMPDLPN
310 320 330 340 350
VGMERDIEQF KEYFENPDFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYS
360 370 380 390 400
ANALVDLVAR ILALVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM
410 420 430 440 450
KDLGTTCRDV RTREVGIQEV HHKVQPDQVE LIRRDYYANG GWETFLSYED
460 470 480 490 500
PKKDILIGLL RLRKASKKYT YRKEFTSQRT SIVRELHVYG SVVPLHSRDP
510 520 530 540 550
RKFQHQGFGT LLMEEAERIA KEEHGSEKIS VISGVGVRNY YGKLGYELDG

PYMSKRI
Length:557
Mass (Da):63,657
Last modified:November 1, 1996 - 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:i64EF8B42D3C3102E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U43281 Genomic DNA Translation: AAB68213.1
BK006949 Genomic DNA Translation: DAA11347.1

Protein sequence database of the Protein Information Resource

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PIRi
S61980

NCBI Reference Sequences

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RefSeqi
NP_015239.1, NM_001183900.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL086C_mRNA; YPL086C; YPL086C

Database of genes from NCBI RefSeq genomes

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GeneIDi
856019

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL086C

<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
U43281 Genomic DNA Translation: AAB68213.1
BK006949 Genomic DNA Translation: DAA11347.1
PIRiS61980
RefSeqiNP_015239.1, NM_001183900.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6QK7electron microscopy3.30C1-557[»]
SMRiQ02908
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi36095, 536 interactors
ComplexPortaliCPX-779 Elongator holoenzyme complex
DIPiDIP-2385N
IntActiQ02908, 18 interactors
MINTiQ02908
STRINGi4932.YPL086C

PTM databases

iPTMnetiQ02908

Proteomic databases

MaxQBiQ02908
PaxDbiQ02908
PRIDEiQ02908

Genome annotation databases

EnsemblFungiiYPL086C_mRNA; YPL086C; YPL086C
GeneIDi856019
KEGGisce:YPL086C

Organism-specific databases

EuPathDBiFungiDB:YPL086C
SGDiS000006007 ELP3

Phylogenomic databases

HOGENOMiHOG000227514
InParanoidiQ02908
KOiK07739
OMAiTFETRPD

Enzyme and pathway databases

UniPathwayiUPA00988
BioCyciYEAST:G3O-33992-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:Q02908
RNActiQ02908 protein

Family and domain databases

Gene3Di3.80.30.20, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR039661 ELP3
IPR034687 ELP3-like
IPR006638 Elp3/MiaB/NifB
IPR000182 GNAT_dom
IPR032432 Radical_SAM_C
IPR007197 rSAM
IPR023404 rSAM_horseshoe
PANTHERiPTHR11135 PTHR11135, 1 hit
PTHR11135:SF0 PTHR11135:SF0, 1 hit
PfamiView protein in Pfam
PF00583 Acetyltransf_1, 1 hit
PF04055 Radical_SAM, 1 hit
PF16199 Radical_SAM_C, 1 hit
PIRSFiPIRSF005669 Hist_AcTrfase_ELP3, 1 hit
SFLDiSFLDF00344 ELP3-like, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
SUPFAMiSSF55729 SSF55729, 1 hit
TIGRFAMsiTIGR01211 ELP3, 1 hit
PROSITEiView protein in PROSITE
PS51186 GNAT, 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 nameiELP3_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: Q02908
Secondary accession number(s): D6W3T1
<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: May 16, 2006
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 161 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, 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
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