Q9Y262 · EIF3L_HUMAN
- ProteinEukaryotic translation initiation factor 3 subunit L
- GeneEIF3L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids564 (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).
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).
(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | eukaryotic 43S preinitiation complex | |
Cellular Component | eukaryotic 48S preinitiation complex | |
Cellular Component | eukaryotic translation initiation factor 3 complex | |
Cellular Component | fibrillar center | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | synapse | |
Molecular Function | RNA binding | |
Molecular Function | translation initiation factor activity | |
Biological Process | formation of cytoplasmic translation initiation complex | |
Biological Process | translational initiation | |
Biological Process | viral translational termination-reinitiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 3 subunit L
- Short nameseIF3l
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y262
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 481 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-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000084162 | 2-564 | UniProt | Eukaryotic translation initiation factor 3 subunit L | |||
Sequence: SYPADDYESEAAYDPYAYPSDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAEAIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEEEIDFLRSNPKIWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYSCPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP | |||||||
Modified residue | 21 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 465 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 549 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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 RRN3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y262 | EIF3B P55884 | 6 | EBI-373519, EBI-366696 | |
BINARY | Q9Y262 | EIF3E P60228 | 9 | EBI-373519, EBI-347740 | |
BINARY | Q9Y262 | EIF3K Q9UBQ5 | 17 | EBI-373519, EBI-354344 | |
BINARY | Q9Y262 | KLF11 O14901 | 3 | EBI-373519, EBI-948266 | |
XENO | Q9Y262 | ORF Q9Q2G4 | 5 | EBI-373519, EBI-6248094 | |
BINARY | Q9Y262 | PPP1R18 Q6NYC8 | 3 | EBI-373519, EBI-2557469 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 331-537 | PCI | ||||
Sequence: DAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYSCPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVAR |
Sequence similarities
Belongs to the eIF-3 subunit L family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y262-1
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.
- Name1
- Length564
- Mass (Da)66,727
- Last updated1999-11-01 v1
- ChecksumECBD32192D96E3FE
Q9Y262-2
- Name2
- Differences from canonical
- 146-193: Missing
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045881 | 146-193 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 353 | in Ref. 2; AAQ13507 | ||||
Sequence: T → I | ||||||
Sequence conflict | 377 | in Ref. 5; BAD96249 | ||||
Sequence: M → V | ||||||
Sequence conflict | 432 | in Ref. 5; BAD96216 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 434 | in Ref. 5; BAD96249 | ||||
Sequence: N → D | ||||||
Sequence conflict | 513 | in Ref. 4; BAG63674 | ||||
Sequence: F → L | ||||||
Sequence conflict | 528 | in Ref. 4; BAG63674 | ||||
Sequence: I → T | ||||||
Sequence conflict | 558 | in Ref. 4; BAG63674 | ||||
Sequence: K → R |
Mass Spectrometry
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF077207 EMBL· GenBank· DDBJ | AAD27002.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083243 EMBL· GenBank· DDBJ | AAD39841.1 EMBL· GenBank· DDBJ | mRNA | ||
AF109359 EMBL· GenBank· DDBJ | AAQ13507.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456436 EMBL· GenBank· DDBJ | CAG30322.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK302346 EMBL· GenBank· DDBJ | BAG63674.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315533 EMBL· GenBank· DDBJ | BAG37913.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222496 EMBL· GenBank· DDBJ | BAD96216.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222529 EMBL· GenBank· DDBJ | BAD96249.1 EMBL· GenBank· DDBJ | mRNA | ||
AL022311 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z97630 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471095 EMBL· GenBank· DDBJ | EAW60198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001101 EMBL· GenBank· DDBJ | AAH01101.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007510 EMBL· GenBank· DDBJ | AAH07510.1 EMBL· GenBank· DDBJ | mRNA | ||
BC029265 EMBL· GenBank· DDBJ | AAH29265.1 EMBL· GenBank· DDBJ | mRNA |