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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

EIF3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632, PubMed:11169732). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773, PubMed:27462815).UniRule annotation4 Publications
(Microbial infection) Essential for the initiation of translation on type-1 viral ribosomal entry sites (IRESs), like for HCV, PV, EV71 or BEV translation (PubMed:23766293, PubMed:24357634).2 Publications
(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).1 Publication

GO - Molecular functioni

  • mRNA binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural molecule activity Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107581-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit AUniRule annotation
Short name:
eIF3aUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
eIF-3-thetaUniRule annotation
eIF3 p167
eIF3 p180
eIF3 p185
Gene namesi
Name:EIF3AUniRule annotation
Synonyms:EIF3S10UniRule annotation, KIAA0139
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3271. EIF3A.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi8661.
OpenTargetsiENSG00000107581.
PharmGKBiPA27699.

Polymorphism and mutation databases

BioMutaiEIF3A.
DMDMi6685537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotation2 Publications
ChainiPRO_00001235372 – 1382Eukaryotic translation initiation factor 3 subunit AAdd BLAST1381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-acetyllysineCombined sources1
Modified residuei492PhosphoserineCombined sources1
Modified residuei584PhosphoserineCombined sources1
Modified residuei881PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei882PhosphoserineCombined sources1
Modified residuei895PhosphoserineCombined sources1
Modified residuei949PhosphoserineCombined sources1
Modified residuei1028PhosphoserineCombined sources1
Modified residuei1188PhosphoserineCombined sources1
Modified residuei1198PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei1262PhosphoserineCombined sources1
Modified residuei1336PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei1364PhosphoserineUniRule annotation1 Publication1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14152.
MaxQBiQ14152.
PaxDbiQ14152.
PeptideAtlasiQ14152.
PRIDEiQ14152.

2D gel databases

UCD-2DPAGEQ14152.

PTM databases

iPTMnetiQ14152.
PhosphoSitePlusiQ14152.
SwissPalmiQ14152.

Expressioni

Gene expression databases

BgeeiENSG00000107581.
CleanExiHS_EIF3A.
GenevisibleiQ14152. HS.

Organism-specific databases

HPAiHPA038315.
HPA038316.

Interactioni

Subunit structurei

Interacts with EIF4G1 (By similarity). Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3L and EIF3K. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with KRT7 and PIWIL2.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3BP558846EBI-366617,EBI-366696
KRT7P087293EBI-366617,EBI-297833
ORFQ9Q2G45EBI-366617,EBI-6248094From a different organism.
UPF1Q92900-25EBI-366617,EBI-373492

Protein-protein interaction databases

BioGridi114210. 111 interactors.
DIPiDIP-31114N.
IntActiQ14152. 50 interactors.
MINTiMINT-1519859.
STRINGi9606.ENSP00000358140.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-A1-494[»]
3J8Celectron microscopy-A1-494[»]
ProteinModelPortaliQ14152.
SMRiQ14152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini366 – 494PCIUniRule annotationAdd BLAST129
Repeati925 – 934110
Repeati935 – 9422; truncated8
Repeati943 – 952310
Repeati953 – 962410
Repeati963 – 972510
Repeati973 – 982610
Repeati983 – 992710
Repeati993 – 1002810
Repeati1003 – 1012910
Repeati1013 – 10221010
Repeati1023 – 10321110
Repeati1033 – 10421210
Repeati1043 – 10521310
Repeati1054 – 10631410
Repeati1064 – 10731510
Repeati1074 – 10831610
Repeati1084 – 10931710
Repeati1094 – 11031810
Repeati1104 – 11131910
Repeati1114 – 11232010
Repeati1124 – 11332110
Repeati1134 – 11432210
Repeati1144 – 115223; truncated9
Repeati1153 – 11622410
Repeati1163 – 117225; approximate10

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni664 – 835Interaction with EIF3BAdd BLAST172
Regioni925 – 117225 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT]Add BLAST248

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili82 – 120UniRule annotationAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi576 – 875Glu-richAdd BLAST300
Compositional biasi925 – 1294Asp-richAdd BLAST370

Sequence similaritiesi

Belongs to the eIF-3 subunit A family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiQ14152.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
PhylomeDBiQ14152.
TreeFamiTF101522.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03000. eIF3a. 1 hit.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14152-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI
60 70 80 90 100
MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK
110 120 130 140 150
TEAAKEESQQ MVLDIEDLDN IQTPESVLLS AVSGEDTQDR TDRLLLTPWV
160 170 180 190 200
KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ AFKFCLQYTR KAEFRKLCDN
210 220 230 240 250
LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA ISMELWQEAF
260 270 280 290 300
KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
310 320 330 340 350
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE
360 370 380 390 400
KQRRLATLLG LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP
410 420 430 440 450
LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVSQIYQSI
460 470 480 490 500
EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA
510 520 530 540 550
TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA HILQEKEEQH
560 570 580 590 600
QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
610 620 630 640 650
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA
660 670 680 690 700
KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER
710 720 730 740 750
AKRLEEIPLI KSAYEEQRIK DMDLWEQQEE ERITTMQLER EKALEHKNRM
760 770 780 790 800
SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHNR LEERKRQRKE
810 820 830 840 850
ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK
860 870 880 890 900
LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR
910 920 930 940 950
KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL
960 970 980 990 1000
RPDDDRVPRR GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR
1010 1020 1030 1040 1050
IADEDRGNWR HADDDRPPRR GLDEDRGSWR TADEDRGPRR GMDDDRGPRR
1060 1070 1080 1090 1100
GGADDERSSW RNADDDRGPR RGLDDDRGPR RGMDDDRGPR RGMDDDRGPR
1110 1120 1130 1140 1150
RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW RNMDDDRLSR
1160 1170 1180 1190 1200
RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE
1210 1220 1230 1240 1250
REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR
1260 1270 1280 1290 1300
GPAEESSSWR DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL
1310 1320 1330 1340 1350
RSEREEVSSW RRADDRKDDR VEERDPPRRV PPPALSRDRE RDRDREREGE
1360 1370 1380
KEKASWRAEK DRESLRRTKN ETDEDGWTTV RR
Length:1,382
Mass (Da):166,569
Last modified:November 1, 1996 - v1
Checksum:i485C01B28D67EBBA
GO
Isoform 2 (identifier: Q14152-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Note: No experimental confirmation available.
Show »
Length:1,348
Mass (Da):162,636
Checksum:i97F42E357D8B5405
GO

Sequence cautioni

The sequence BAA09488 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti520R → G in BAG63833 (PubMed:14702039).Curated1
Sequence conflicti983D → G in BAG63833 (PubMed:14702039).Curated1
Sequence conflicti1272D → G in BAG63833 (PubMed:14702039).Curated1

Mass spectrometryi

Molecular mass is 166758.3 Da from positions 1 - 1382. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024438386E → K.1 PublicationCorresponds to variant rs967185dbSNPEnsembl.1
Natural variantiVAR_048921694K → N.Corresponds to variant rs431898dbSNPEnsembl.1
Natural variantiVAR_048922993D → E.Corresponds to variant rs532138dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0554711 – 34Missing in isoform 2. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58046 mRNA. Translation: AAB41584.1.
U58047 Genomic DNA. Translation: AAB41586.1.
U78311 mRNA. Translation: AAB80695.1.
D50929 mRNA. Translation: BAA09488.2. Different initiation.
AK302575 mRNA. Translation: BAG63833.1.
AL355598 Genomic DNA. Translation: CAI14127.1.
CH471066 Genomic DNA. Translation: EAW49408.1.
CCDSiCCDS7608.1. [Q14152-1]
RefSeqiNP_003741.1. NM_003750.2. [Q14152-1]
UniGeneiHs.523299.
Hs.713331.

Genome annotation databases

EnsembliENST00000369144; ENSP00000358140; ENSG00000107581. [Q14152-1]
ENST00000541549; ENSP00000438178; ENSG00000107581. [Q14152-1]
GeneIDi8661.
KEGGihsa:8661.
UCSCiuc001ldu.4. human. [Q14152-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58046 mRNA. Translation: AAB41584.1.
U58047 Genomic DNA. Translation: AAB41586.1.
U78311 mRNA. Translation: AAB80695.1.
D50929 mRNA. Translation: BAA09488.2. Different initiation.
AK302575 mRNA. Translation: BAG63833.1.
AL355598 Genomic DNA. Translation: CAI14127.1.
CH471066 Genomic DNA. Translation: EAW49408.1.
CCDSiCCDS7608.1. [Q14152-1]
RefSeqiNP_003741.1. NM_003750.2. [Q14152-1]
UniGeneiHs.523299.
Hs.713331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-A1-494[»]
3J8Celectron microscopy-A1-494[»]
ProteinModelPortaliQ14152.
SMRiQ14152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114210. 111 interactors.
DIPiDIP-31114N.
IntActiQ14152. 50 interactors.
MINTiMINT-1519859.
STRINGi9606.ENSP00000358140.

PTM databases

iPTMnetiQ14152.
PhosphoSitePlusiQ14152.
SwissPalmiQ14152.

Polymorphism and mutation databases

BioMutaiEIF3A.
DMDMi6685537.

2D gel databases

UCD-2DPAGEQ14152.

Proteomic databases

EPDiQ14152.
MaxQBiQ14152.
PaxDbiQ14152.
PeptideAtlasiQ14152.
PRIDEiQ14152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369144; ENSP00000358140; ENSG00000107581. [Q14152-1]
ENST00000541549; ENSP00000438178; ENSG00000107581. [Q14152-1]
GeneIDi8661.
KEGGihsa:8661.
UCSCiuc001ldu.4. human. [Q14152-1]

Organism-specific databases

CTDi8661.
DisGeNETi8661.
GeneCardsiEIF3A.
H-InvDBHIX0170434.
HGNCiHGNC:3271. EIF3A.
HPAiHPA038315.
HPA038316.
MIMi602039. gene.
neXtProtiNX_Q14152.
OpenTargetsiENSG00000107581.
PharmGKBiPA27699.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiQ14152.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
PhylomeDBiQ14152.
TreeFamiTF101522.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107581-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEIF3A. human.
GeneWikiiEIF3A.
GenomeRNAii8661.
PROiQ14152.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107581.
CleanExiHS_EIF3A.
GenevisibleiQ14152. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03000. eIF3a. 1 hit.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3A_HUMAN
AccessioniPrimary (citable) accession number: Q14152
Secondary accession number(s): B1AMV5
, B4DYS1, F5H335, O00653, Q15778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.