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UniProtKB - Q14152 (EIF3A_HUMAN)

Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

EIF3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • receptor tyrosine kinase binding Source: Ensembl
  • RNA binding Source: UniProtKB
  • structural molecule activity Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-UniRule
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionInitiation factor, RNA-binding
Biological processProtein biosynthesis

Enzyme and pathway databases

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

Protein family/group databases

MoonProtiQ14152

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000107581.12
HGNCiHGNC:3271 EIF3A
MIMi602039 gene
neXtProtiNX_Q14152

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi59854

2D gel databases

UCD-2DPAGEiQ14152

PTM databases

iPTMnetiQ14152
PhosphoSitePlusiQ14152
SwissPalmiQ14152

Expressioni

Gene expression databases

BgeeiENSG00000107581 Expressed in 239 organ(s), highest expression level in substantia nigra
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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114210, 124 interactors
CORUMiQ14152
DIPiDIP-31114N
IntActiQ14152, 71 interactors
MINTiQ14152
STRINGi9606.ENSP00000358140

Structurei

Secondary structure

11382
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ14152
SMRiQ14152
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini315 – 498PCIPROSITE-ProRule annotationAdd BLAST184
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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_03000 eIF3a, 1 hit
InterProiView protein in InterPro
IPR027512 EIF3A
IPR000717 PCI_dom
PANTHERiPTHR14005 PTHR14005, 2 hits
PfamiView protein in Pfam
PF01399 PCI, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit

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 → K1 PublicationCorresponds to variant dbSNP:rs967185Ensembl.1
Natural variantiVAR_048921694K → N. Corresponds to variant dbSNP:rs431898Ensembl.1
Natural variantiVAR_048922993D → E. Corresponds to variant dbSNP:rs532138Ensembl.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 No translation available.
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

Similar proteinsi

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 No translation available.
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, 124 interactors
CORUMiQ14152
DIPiDIP-31114N
IntActiQ14152, 71 interactors
MINTiQ14152
STRINGi9606.ENSP00000358140

Protein family/group databases

MoonProtiQ14152

PTM databases

iPTMnetiQ14152
PhosphoSitePlusiQ14152
SwissPalmiQ14152

Polymorphism and mutation databases

BioMutaiEIF3A
DMDMi6685537

2D gel databases

UCD-2DPAGEiQ14152

Proteomic databases

EPDiQ14152
MaxQBiQ14152
PaxDbiQ14152
PeptideAtlasiQ14152
PRIDEiQ14152
ProteomicsDBi59854

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
EuPathDBiHostDB:ENSG00000107581.12
GeneCardsiEIF3A
H-InvDBiHIX0170434
HGNCiHGNC:3271 EIF3A
HPAiHPA038315
HPA038316
MIMi602039 gene
neXtProtiNX_Q14152
OpenTargetsiENSG00000107581
PharmGKBiPA27699
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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
PROiPR:Q14152
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107581 Expressed in 239 organ(s), highest expression level in substantia nigra
CleanExiHS_EIF3A
GenevisibleiQ14152 HS

Family and domain databases

HAMAPiMF_03000 eIF3a, 1 hit
InterProiView protein in InterPro
IPR027512 EIF3A
IPR000717 PCI_dom
PANTHERiPTHR14005 PTHR14005, 2 hits
PfamiView protein in Pfam
PF01399 PCI, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3A_HUMAN
AccessioniPrimary (citable) accession number: Q14152
Secondary accession number(s): B1AMV5
, B4DYS1, F5H335, O00653, Q15778
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 186 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Translation initiation factors
    List of translation initiation factor entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
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