Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P20459 (IF2A_YEAST)

Entry version 198 (23 Feb 2022)
Sequence version 1 (01 Feb 1991)
Previous versions | rss
Add a publicationFeedback
Protein

Eukaryotic translation initiation factor 2 subunit alpha

Gene

SUI2

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

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.

Curated

Miscellaneous

Present with 17100 molecules/cell in log phase SD medium.1 Publication

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionInitiation factor, RNA-binding
Biological processProtein biosynthesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-381042, PERK regulates gene expression
R-SCE-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-SCE-72702, Ribosomal scanning and start codon recognition
R-SCE-72731, Recycling of eIF2:GDP

<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%5Fand%5Ftaxonomy%5Fsection">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:
Eukaryotic translation initiation factor 2 subunit alpha
Short name:
eIF-2-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:SUI21 PublicationImported
Synonyms:TIF211
Ordered Locus Names:YJR007W
ORF Names:J1429
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 X

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000003767, SUI2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YJR007W

<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

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi52S → A: Inhibits derepression of GCN4 expression in amino acid, purine, and glucose-starved cells. 2 Publications1
Mutagenesisi52S → D: Weakly impairs derepression of GCN4 expression in amino acid-starved cells. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001373891 – 304Eukaryotic translation initiation factor 2 subunit alphaAdd BLAST304

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 residuei52Phosphoserine; by GCN23 Publications1
Modified residuei292PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated; phosphorylation on Ser-52 by the GCN2 protein kinase occurs in response to low amino acid, carbon, or purine availability.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P20459

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

More...PaxDbi		P20459

PRoteomics IDEntifications database

More...PRIDEi		P20459

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P20459

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimer composed of an alpha, a beta and a gamma subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.

Curated

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33763, 320 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-427, Eukaryotic translation initiation factor 2 complex

Database of interacting proteins

More...DIPi		DIP-2327N

Protein interaction database and analysis system

More...IntActi		P20459, 35 interactors

Molecular INTeraction database

More...MINTi		P20459

STRING: functional protein association networks

More...STRINGi		4932.YJR007W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P20459, 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

1304
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		P20459

Database of comparative protein structure models

More...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		P20459

<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%5Fand%5Fdomains%5Fsection">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>Domaini17 – 88S1 motifPROSITE-ProRule annotationAdd BLAST72

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>Regioni283 – 304DisorderedSequence analysisAdd BLAST22

<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 eIF-2-alpha family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2916, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000007015

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_033458_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P20459

Identification of Orthologs from Complete Genome Data

More...OMAi		DVNEHQR

Family and domain databases

Conserved Domains Database

More...CDDi		cd04452, S1_IF2_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.150.190, 1 hit
3.30.70.1130, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50184

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012340, NA-bd_OB-fold
IPR022967, S1_dom
IPR003029, S1_domain
IPR044126, S1_IF2_alpha
IPR024055, TIF2_asu_C
IPR024054, TIF2_asu_middle_sf
IPR011488, TIF_2_asu

The PANTHER Classification System

More...PANTHERi		PTHR10602, PTHR10602, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07541, EIF_2_alpha, 1 hit
PF00575, S1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00316, S1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF110993, SSF110993, 1 hit
SSF116742, SSF116742, 1 hit
SSF50249, SSF50249, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50126, S1, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P20459-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTSHCRFYE NKYPEIDDIV MVNVQQIAEM GAYVKLLEYD NIEGMILLSE 
        60         70         80         90        100
LSRRRIRSIQ KLIRVGKNDV AVVLRVDKEK GYIDLSKRRV SSEDIIKCEE 
       110        120        130        140        150
KYQKSKTVHS ILRYCAEKFQ IPLEELYKTI AWPLSRKFGH AYEAFKLSII 
       160        170        180        190        200
DETVWEGIEP PSKDVLDELK NYISKRLTPQ AVKIRADVEV SCFSYEGIDA 
       210        220        230        240        250
IKDALKSAED MSTEQMQVKV KLVAAPLYVL TTQALDKQKG IEQLESAIEK 
       260        270        280        290        300
ITEVITKYGG VCNITMPPKA VTATEDAELQ ALLESKELDN RSDSEDDEDE 

SDDE
Length:304
Mass (Da):34,718
Last modified:February 1, 1991 - 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:iAF4F1C80303A4E98
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 conflicti258Y → H in AAS56202 (PubMed:17322287).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
M25552 Genomic DNA Translation: AAA70332.1
X87611 Genomic DNA Translation: CAA60929.1
Z49507 Genomic DNA Translation: CAA89529.1
AY557876 Genomic DNA Translation: AAS56202.1
BK006943 Genomic DNA Translation: DAA08798.1

Protein sequence database of the Protein Information Resource

More...PIRi		A32108

NCBI Reference Sequences

More...RefSeqi		NP_012540.3, NM_001181664.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YJR007W_mRNA; YJR007W; YJR007W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853463

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YJR007W

<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
M25552 Genomic DNA Translation: AAA70332.1
X87611 Genomic DNA Translation: CAA60929.1
Z49507 Genomic DNA Translation: CAA89529.1
AY557876 Genomic DNA Translation: AAS56202.1
BK006943 Genomic DNA Translation: DAA08798.1
PIRiA32108
RefSeqiNP_012540.3, NM_001181664.3

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
1Q46X-ray2.86A2-176[»]
2A19X-ray2.50A4-176[»]
2A1AX-ray2.80A4-176[»]
3J81electron microscopy4.00j1-300[»]
3JAPelectron microscopy4.90j1-304[»]
3JAQelectron microscopy6.00j1-304[»]
6FYXelectron microscopy3.05j1-304[»]
6FYYelectron microscopy3.05j1-304[»]
6GSMelectron microscopy5.15j3-265[»]
6GSNelectron microscopy5.75j3-265[»]
6I3Melectron microscopy3.93K/L1-304[»]
6I7Telectron microscopy4.61K/L1-304[»]
6JLYX-ray3.50L/M1-304[»]
6JLZX-ray3.35L/M1-304[»]
6QG0electron microscopy4.20K/L1-304[»]
6QG1electron microscopy4.20K/L1-304[»]
6QG2electron microscopy4.60K/L1-304[»]
6QG3electron microscopy9.40K/L1-304[»]
6QG5electron microscopy10.10K/L1-304[»]
6QG6electron microscopy4.65K/L1-304[»]
SMRiP20459
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33763, 320 interactors
ComplexPortaliCPX-427, Eukaryotic translation initiation factor 2 complex
DIPiDIP-2327N
IntActiP20459, 35 interactors
MINTiP20459
STRINGi4932.YJR007W

PTM databases

iPTMnetiP20459

Proteomic databases

MaxQBiP20459
PaxDbiP20459
PRIDEiP20459

Genome annotation databases

EnsemblFungiiYJR007W_mRNA; YJR007W; YJR007W
GeneIDi853463
KEGGisce:YJR007W

Organism-specific databases

SGDiS000003767, SUI2
VEuPathDBiFungiDB:YJR007W

Phylogenomic databases

eggNOGiKOG2916, Eukaryota
GeneTreeiENSGT00390000007015
HOGENOMiCLU_033458_0_1_1
InParanoidiP20459
OMAiDVNEHQR

Enzyme and pathway databases

ReactomeiR-SCE-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-381042, PERK regulates gene expression
R-SCE-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-SCE-72702, Ribosomal scanning and start codon recognition
R-SCE-72731, Recycling of eIF2:GDP

Miscellaneous databases

EvolutionaryTraceiP20459

Protein Ontology

More...PROi		PR:P20459
RNActiP20459, protein

Family and domain databases

CDDicd04452, S1_IF2_alpha, 1 hit
Gene3Di1.10.150.190, 1 hit
3.30.70.1130, 1 hit
IDEALiIID50184
InterProiView protein in InterPro
IPR012340, NA-bd_OB-fold
IPR022967, S1_dom
IPR003029, S1_domain
IPR044126, S1_IF2_alpha
IPR024055, TIF2_asu_C
IPR024054, TIF2_asu_middle_sf
IPR011488, TIF_2_asu
PANTHERiPTHR10602, PTHR10602, 1 hit
PfamiView protein in Pfam
PF07541, EIF_2_alpha, 1 hit
PF00575, S1, 1 hit
SMARTiView protein in SMART
SM00316, S1, 1 hit
SUPFAMiSSF110993, SSF110993, 1 hit
SSF116742, SSF116742, 1 hit
SSF50249, SSF50249, 1 hit
PROSITEiView protein in PROSITE
PS50126, S1, 1 hit

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 nameiIF2A_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: P20459
Secondary accession number(s): D6VWI2, E9P8T6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 23, 2022
This is version 198 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  3. Translation initiation factors
    List of translation initiation factor entries
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again