P60228 · EIF3E_HUMAN
- ProteinEukaryotic translation initiation factor 3 subunit E
- GeneEIF3E
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids445 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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, PubMed:27462815).
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).
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).
Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741).
May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924).
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).
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).
Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741).
May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 3 subunit E
- Short nameseIF3e
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP60228
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046480 | 185 | in dbSNP:rs17856554 | |||
Sequence: A → V | ||||||
Mutagenesis | 312 | Promotes nuclear accumulation. | ||||
Sequence: L → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 350 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000123515 | 2-445 | UniProt | Eukaryotic translation initiation factor 3 subunit E | |||
Sequence: AEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY | |||||||
Modified residue | 399 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 399 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 442 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 445 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 445 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.
Gene expression databases
Organism-specific databases
Interaction
Subunit
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, EIF3K and EIF3L. 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. Interacts with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and IFIT2 (PubMed:16023166, PubMed:16973618).
Interacts with BZW2/5MP1 (PubMed:21745818).
Interacts with BZW2/5MP1 (PubMed:21745818).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 4-128 | Sufficient for interaction with EPAS1 | ||||
Sequence: YDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYL | ||||||
Region | 9-195 | Sufficient for interaction with TRIM27 | ||||
Sequence: RIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKET | ||||||
Domain | 221-398 | PCI | ||||
Sequence: VFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAV | ||||||
Region | 351-445 | Sufficient for interaction with MCM7 | ||||
Sequence: ISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY |
Sequence similarities
Belongs to the eIF-3 subunit E family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length445
- Mass (Da)52,221
- Last updated2004-01-16 v1
- ChecksumA5368651DD0DDD0C
Computationally mapped potential isoform sequences
There are 25 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YAW4 | H0YAW4_HUMAN | EIF3E | 84 | ||
H0YBP5 | H0YBP5_HUMAN | EIF3E | 332 | ||
H0YBR5 | H0YBR5_HUMAN | EIF3E | 123 | ||
A0A161SXE1 | A0A161SXE1_HUMAN | EIF3E | 172 | ||
B3KW56 | B3KW56_HUMAN | EIF3E | 396 | ||
E5RIP5 | E5RIP5_HUMAN | EIF3E | 45 | ||
E5RII3 | E5RII3_HUMAN | EIF3E | 75 | ||
E5RJ25 | E5RJ25_HUMAN | EIF3E | 56 | ||
E5RGA2 | E5RGA2_HUMAN | EIF3E | 352 | ||
E5RHS5 | E5RHS5_HUMAN | EIF3E | 318 | ||
A0A7I2V2H9 | A0A7I2V2H9_HUMAN | EIF3E | 452 | ||
A0A7I2V2Q9 | A0A7I2V2Q9_HUMAN | EIF3E | 103 | ||
A0A7I2V2W0 | A0A7I2V2W0_HUMAN | EIF3E | 446 | ||
A0A7I2V2S9 | A0A7I2V2S9_HUMAN | EIF3E | 88 | ||
A0A7I2V3I0 | A0A7I2V3I0_HUMAN | EIF3E | 472 | ||
A0A7I2V3I2 | A0A7I2V3I2_HUMAN | EIF3E | 396 | ||
A0A7I2V429 | A0A7I2V429_HUMAN | EIF3E | 182 | ||
A0A7I2V3S3 | A0A7I2V3S3_HUMAN | EIF3E | 507 | ||
A0A7I2V3W9 | A0A7I2V3W9_HUMAN | EIF3E | 122 | ||
A0A7I2V4B4 | A0A7I2V4B4_HUMAN | EIF3E | 455 | ||
A0A7I2V4G3 | A0A7I2V4G3_HUMAN | EIF3E | 339 | ||
A0A7I2V570 | A0A7I2V570_HUMAN | EIF3E | 172 | ||
A0A7I2V5P9 | A0A7I2V5P9_HUMAN | EIF3E | 334 | ||
A0A7I2V5K7 | A0A7I2V5K7_HUMAN | EIF3E | 79 | ||
A0A7I2V5Z6 | A0A7I2V5Z6_HUMAN | EIF3E | 416 |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U54562 EMBL· GenBank· DDBJ | AAC51760.1 EMBL· GenBank· DDBJ | mRNA | ||
U94174 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94162 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94163 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94164 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94165 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94166 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94167 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94168 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94169 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94170 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94171 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94172 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94173 EMBL· GenBank· DDBJ | AAC51917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U94175 EMBL· GenBank· DDBJ | AAC51919.1 EMBL· GenBank· DDBJ | mRNA | ||
U62962 EMBL· GenBank· DDBJ | AAB58251.1 EMBL· GenBank· DDBJ | mRNA | ||
U85947 EMBL· GenBank· DDBJ | AAB88873.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542275 EMBL· GenBank· DDBJ | CAG47071.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471060 EMBL· GenBank· DDBJ | EAW91918.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000734 EMBL· GenBank· DDBJ | AAH00734.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008419 EMBL· GenBank· DDBJ | AAH08419.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016706 EMBL· GenBank· DDBJ | AAH16706.1 EMBL· GenBank· DDBJ | mRNA | ||
BC017887 EMBL· GenBank· DDBJ | AAH17887.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021679 EMBL· GenBank· DDBJ | AAH21679.1 EMBL· GenBank· DDBJ | mRNA |