K6ZZH2 · K6ZZH2_PANTR
- ProteinEukaryotic translation initiation factor 3 subunit C
- GeneEIF3C
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids913 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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. 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. 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.
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 | eukaryotic 43S preinitiation complex | |
Cellular Component | eukaryotic 48S preinitiation complex | |
Cellular Component | eukaryotic translation initiation factor 3 complex | |
Molecular Function | RNA binding | |
Molecular Function | translation initiation factor activity | |
Molecular Function | translation initiation factor binding | |
Biological Process | formation of cytoplasmic translation initiation complex |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 3 subunit C
- Short nameseIF3c
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan
Accessions
- Primary accessionK6ZZH2
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 9 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 13 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 15 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 16 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 18 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 39 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 524 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 909 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated. Phosphorylation is enhanced upon serum stimulation.
Keywords
- PTM
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.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Polar residues | ||||
Sequence: MSRFFTTGSDSESESSLSGE | ||||||
Region | 1-44 | Disordered | ||||
Sequence: MSRFFTTGSDSESESSLSGEELVTKPVGGNYGKQPLLLSEDEED | ||||||
Region | 157-301 | Disordered | ||||
Sequence: TSYKQNPEQSADEDAEKNEEDSEGSSDEDEDEDGVSAATFLKKKSEAPSGESRKFLKKMDDEDEDSEDSEDDEDWDTGSTSSDSDSEEEEGKQTALASRFLKKAPTTDEDKKAAEKKREDKAKKKHDRKSKRLDEEEEDNEGGEW | ||||||
Compositional bias | 169-190 | Acidic residues | ||||
Sequence: EDAEKNEEDSEGSSDEDEDEDG | ||||||
Compositional bias | 202-217 | Basic and acidic residues | ||||
Sequence: EAPSGESRKFLKKMDD | ||||||
Compositional bias | 218-240 | Acidic residues | ||||
Sequence: EDEDSEDSEDDEDWDTGSTSSDS | ||||||
Compositional bias | 259-277 | Basic and acidic residues | ||||
Sequence: KAPTTDEDKKAAEKKREDK | ||||||
Region | 522-542 | Disordered | ||||
Sequence: QLTPPEGSSKSEQDQAENEGE | ||||||
Domain | 673-849 | PCI | ||||
Sequence: FHLHINLELLECVYLVSAMLLEIPYMAAHESDARRRMISKQFHHQLRVGERQPLLGPPESMREHVVAASKAMKMGDWKTCHSFIINEKMNGKVWDLFPEADKVRTMLVRKIQEESLRTYLFTYSSVYDSISMETLSDMFELDLPTVHSIISKMIINEELMASLDQPTQTVVMHRTEP | ||||||
Region | 885-913 | Disordered | ||||
Sequence: FRDQKDGYRKNEGYMRRGGYRQQQSQTAY |
Sequence similarities
Belongs to the eIF-3 subunit C family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length913
- Mass (Da)105,344
- Last updated2013-01-09 v1
- ChecksumCE5029F4EB51C1AA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Polar residues | ||||
Sequence: MSRFFTTGSDSESESSLSGE | ||||||
Compositional bias | 169-190 | Acidic residues | ||||
Sequence: EDAEKNEEDSEGSSDEDEDEDG | ||||||
Compositional bias | 202-217 | Basic and acidic residues | ||||
Sequence: EAPSGESRKFLKKMDD | ||||||
Compositional bias | 218-240 | Acidic residues | ||||
Sequence: EDEDSEDSEDDEDWDTGSTSSDS | ||||||
Compositional bias | 259-277 | Basic and acidic residues | ||||
Sequence: KAPTTDEDKKAAEKKREDK |