Q9BY44 · EIF2A_HUMAN

  • Protein
    Eukaryotic translation initiation factor 2A
  • Gene
    EIF2A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner.

Caution

This gene should not be confused with EIF2S1, frequently called eIF2-alpha in the literature, and with which it shares the alias EIF2A. EIF2S1 is the alpha subunit of the eIF2 translation initiation complex. Although both of these proteins function in binding initiator tRNA to the 40S ribosomal subunit, the EIF2A protein does so in a codon-dependent manner, whereas eIF2 complex requires GTP. Was initially thought to constitute the ortholog of prokaryotic IF-2 (infB) protein.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentblood microparticle
Cellular Componentcytoplasm
Cellular Componentcytosolic small ribosomal subunit
Cellular Componenteukaryotic translation initiation factor 2 complex
Cellular Componentextracellular space
Molecular Functioncadherin binding
Molecular FunctionmRNA binding
Molecular Functionribosome binding
Molecular Functiontranslation initiation factor activity
Molecular FunctiontRNA binding
Biological Processpositive regulation of signal transduction
Biological Processregulation of translation
Biological Processresponse to amino acid starvation
Biological Processribosome assembly
Biological ProcessSREBP signaling pathway
Biological Processtranslational initiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      EIF2A
    • ORF names
      CDA02, MSTP004, MSTP089

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BY44
  • Secondary accessions
    • A8MPS6
    • B4DF96
    • B4DQ14
    • D3DNI9
    • Q5QTR2

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_03206697in dbSNP:rs1132979
Natural variantVAR_032067582in dbSNP:rs17850813

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 562 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved; alternate
Modified residue1UniProtN-acetylmethionine
ChainPRO_00004244661-585UniProtEukaryotic translation initiation factor 2A
Modified residue2UniProtN-acetylalanine; in Eukaryotic translation initiation factor 2A, N-terminally processed
ChainPRO_00002860762-585UniProtEukaryotic translation initiation factor 2A, N-terminally processed
Modified residue (large scale data)4PRIDEPhosphoserine
Modified residue5UniProtPhosphothreonine
Modified residue (large scale data)5PRIDEPhosphothreonine
Modified residue (large scale data)103PRIDEPhosphothreonine
Modified residue (large scale data)250PRIDEPhosphotyrosine
Modified residue (large scale data)446PRIDEPhosphotyrosine
Modified residue503UniProtPhosphoserine
Modified residue (large scale data)503PRIDEPhosphoserine
Modified residue506UniProtPhosphoserine
Modified residue (large scale data)506PRIDEPhosphoserine
Modified residue (large scale data)512PRIDEPhosphothreonine
Modified residue517UniProtPhosphoserine
Modified residue (large scale data)517PRIDEPhosphoserine
Modified residue518UniProtPhosphothreonine
Modified residue (large scale data)518PRIDEPhosphothreonine
Modified residue (large scale data)524PRIDEPhosphoserine
Modified residue526UniProtPhosphoserine
Modified residue (large scale data)526PRIDEPhosphoserine
Modified residue (large scale data)528PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed. Expressed at higher level in pancreas, heart, brain and placenta.

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for repeat, region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Repeat56-100WD 1
Repeat101-159WD 2
Repeat160-210WD 3
Repeat211-264WD 4
Repeat265-306WD 5
Repeat307-348WD 6
Repeat349-391WD 7
Region434-534Disordered
Compositional bias515-529Polar residues
Coiled coil531-582

Sequence similarities

Belongs to the WD repeat EIF2A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q9BY44-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    585
  • Mass (Da)
    64,990
  • Last updated
    2008-10-14 v3
  • Checksum
    63D63C0676F232C9
MAPSTPLLTVRGSEGLYMVNGPPHFTESTVFPRESGKNCKVCIFSKDGTLFAWGNGEKVNIISVTNKGLLHSFDLLKAVCLEFSPKNTVLATWQPYTTSKDGTAGIPNLQLYDVKTGTCLKSFIQKKMQNWCPSWSEDETLCARNVNNEVHFFENNNFNTIANKLHLQKINDFVLSPGPQPYKVAVYVPGSKGAPSFVRLYQYPNFAGPHAALANKSFFKADKVTMLWNKKATAVLVIASTDVDKTGASYYGEQTLHYIATNGESAVVQLPKNGPIYDVVWNSSSTEFCAVYGFMPAKATIFNLKCDPVFDFGTGPRNAAYYSPHGHILVLAGFGNLRGQMEVWDVKNYKLISKPVASDSTYFAWCPDGEHILTATCAPRLRVNNGYKIWHYTGSILHKYDVPSNAELWQVSWQPFLDGIFPAKTITYQAVPSEVPNEEPKVATAYRPPALRNKPITNSKLHEEEPPQNMKPQSGNDKPLSKTALKNQRKHEAKKAAKQEARSDKSPDLAPTPAPQSTPRNTVSQSISGDPEIDKKIKNLKKKLKAIEQLKEQAATGKQLEKNQLEKIQKETALLQELEDLELGI

Q9BY44-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9BY44-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9BY44-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9IZE1C9IZE1_HUMANEIF2A236
F8WF18F8WF18_HUMANEIF2A59
F8WAT3F8WAT3_HUMANEIF2A75
F8WAE5F8WAE5_HUMANEIF2A580
H7C5Q3H7C5Q3_HUMANEIF2A158
H7C5Q4H7C5Q4_HUMANEIF2A40
H7C5R5H7C5R5_HUMANEIF2A316

Sequence caution

The sequence AAK14926.1 differs from that shown. Reason: Erroneous initiation
The sequence AAM83402.1 differs from that shown. Reason: Frameshift
The sequence AAQ13506.1 differs from that shown. Reason: Frameshift
The sequence AAQ13612.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0249751-213in isoform 2
Sequence conflict7in Ref. 4; AAQ13612
Sequence conflict14-16in Ref. 4; AAQ13612
Alternative sequenceVSP_05604734-58in isoform 3
Sequence conflict54in Ref. 1; AAM83402
Sequence conflict55in Ref. 1; AAM83402
Sequence conflict84in Ref. 2; BAB55058
Alternative sequenceVSP_05604898-158in isoform 4
Sequence conflict150in Ref. 4; AAQ13612
Sequence conflict173in Ref. 4; AAQ13612
Alternative sequenceVSP_024976214-219in isoform 2
Sequence conflict261in Ref. 1; AAM83402
Sequence conflict263in Ref. 1; AAM83402
Sequence conflict268in Ref. 1; AAM83402
Sequence conflict292in Ref. 1; AAM83402
Compositional bias515-529Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF497978
EMBL· GenBank· DDBJ
AAM83402.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK027356
EMBL· GenBank· DDBJ
BAB55058.1
EMBL· GenBank· DDBJ
mRNA
AK298586
EMBL· GenBank· DDBJ
BAG60776.1
EMBL· GenBank· DDBJ
mRNA
AK293993
EMBL· GenBank· DDBJ
BAG57357.1
EMBL· GenBank· DDBJ
mRNA
AF212241
EMBL· GenBank· DDBJ
AAK14926.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AF109358
EMBL· GenBank· DDBJ
AAQ13506.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AF172818
EMBL· GenBank· DDBJ
AAQ13612.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AC107426
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471052
EMBL· GenBank· DDBJ
EAW78830.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW78831.1
EMBL· GenBank· DDBJ
Genomic DNA
BC011885
EMBL· GenBank· DDBJ
AAH11885.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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