Q7TN98 · CPEB4_MOUSE
- ProteinCytoplasmic polyadenylation element-binding protein 4
- GeneCpeb4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids729 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (PubMed:17024188).
RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (By similarity).
Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE-regulated mRNAs in conditions in which global protein synthesis is inhibited (PubMed:28092655).
Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (By similarity).
Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752).
Stimulates proliferation of melanocytes (By similarity).
In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (PubMed:24386439).
RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (By similarity).
Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE-regulated mRNAs in conditions in which global protein synthesis is inhibited (PubMed:28092655).
Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (By similarity).
Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752).
Stimulates proliferation of melanocytes (By similarity).
In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (PubMed:24386439).
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 473 | RNA-binding | ||||
Sequence: K | ||||||
Site | 561 | Important for the positionning of RRM1 relative to RRM2 | ||||
Sequence: W | ||||||
Binding site | 667 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 675 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 684 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 689 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 694 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 697 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 702 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 710 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | dendrite | |
Cellular Component | dendritic spine | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | growth cone | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | postsynaptic density | |
Cellular Component | synapse | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | RNA binding | |
Molecular Function | translation regulator activity | |
Biological Process | cellular response to amino acid stimulus | |
Biological Process | cellular response to decreased oxygen levels | |
Biological Process | cellular response to glucose starvation | |
Biological Process | ionotropic glutamate receptor signaling pathway | |
Biological Process | negative regulation of neuron apoptotic process | |
Biological Process | response to ischemia |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCytoplasmic polyadenylation element-binding protein 4
- Short namesCPE-BP4; CPE-binding protein 4; mCPEB-4
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TN98
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype at young age or under unchallenged conditions (PubMed:24386439, PubMed:28092655).
At 80 weeks or under high fat diet feeding conditions, mutant mice develop hepatosteatosis with excessive liver weight and accumulation of cytosolic lipid droplets sometimes accompanied by fibrosis (PubMed:28092655).
At 80 weeks or under high fat diet feeding conditions, mutant mice develop hepatosteatosis with excessive liver weight and accumulation of cytosolic lipid droplets sometimes accompanied by fibrosis (PubMed:28092655).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 34 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000269265 | 1-729 | Cytoplasmic polyadenylation element-binding protein 4 | |||
Sequence: MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPNPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDSSSENSNGKEKLRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPGASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRSAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPERPRTFDMHSLESSLIDIMRAENDSIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFTHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN | ||||||
Modified residue | 97 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 99 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 137 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 252 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 255 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 326 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 330 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in brain, including hippocampus, amygdala, granule and Purkinje cells of the cerebellum (at protein level) (PubMed:17024188, PubMed:24386439).
Expressed in spinal cord (at protein level) (PubMed:27381259).
Expressed in kidney, lung and heart (at protein level) (PubMed:12871996, PubMed:24386439, PubMed:27381259).
Expressed in liver (at protein level) (PubMed:12871996, PubMed:24386439, PubMed:27381259, PubMed:28092655).
Expressed in spleen and testis (at protein level) (PubMed:12871996, PubMed:24386439).
Weakly expressed in ovary and in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus (PubMed:12871996).
Expressed in spinal cord (at protein level) (PubMed:27381259).
Expressed in kidney, lung and heart (at protein level) (PubMed:12871996, PubMed:24386439, PubMed:27381259).
Expressed in liver (at protein level) (PubMed:12871996, PubMed:24386439, PubMed:27381259, PubMed:28092655).
Expressed in spleen and testis (at protein level) (PubMed:12871996, PubMed:24386439).
Weakly expressed in ovary and in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus (PubMed:12871996).
Induction
Up-regulated in granular cells of the dentate gyrus of CA1 and CA3 after kainate-induced seizures (PubMed:12871996).
Up-regulated by high-fat-diet and aging-induced endoplasmic reticulum stress (PubMed:28092655).
Expression level fluctuation follows the circadian clock amplitude (PubMed:28092655).
Up-regulated by high-fat-diet and aging-induced endoplasmic reticulum stress (PubMed:28092655).
Expression level fluctuation follows the circadian clock amplitude (PubMed:28092655).
Developmental stage
Highly expressed in developing brain, spinal cord and attached dorsal root ganglia (DRG) (at protein level). At embryonic day 18.5 expressed in gray matter of spinal cord, diencephalons, hippocampus and parts of midbrain and hindbrain. At postnatal day 20 expression persists in spinal cord and brain. Expressed in embryonic heart.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 20-50 | Disordered | ||||
Sequence: FPVRFHPHLQPPHHHQNATPNPAAFINNNTA | ||||||
Compositional bias | 33-50 | Polar residues | ||||
Sequence: HHQNATPNPAAFINNNTA | ||||||
Compositional bias | 78-101 | Polar residues | ||||
Sequence: EKAKSQQQEQQDPLEKQQLSPSPG | ||||||
Region | 78-133 | Disordered | ||||
Sequence: EKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDSSSENSNGKEKL | ||||||
Region | 218-324 | Disordered | ||||
Sequence: FGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRSAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRGLNGG | ||||||
Compositional bias | 234-248 | Basic residues | ||||
Sequence: PHHPHFQHHHSQHQQ | ||||||
Compositional bias | 269-301 | Polar residues | ||||
Sequence: NQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSP | ||||||
Domain | 472-563 | RRM 1 | ||||
Sequence: RKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNL | ||||||
Region | 541-543 | RNA-binding | ||||
Sequence: KLY | ||||||
Domain | 580-662 | RRM 2 | ||||
Sequence: KTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVL |
Domain
The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (564-579) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. Unlike in CPEB1, a continuous polar interface is formed between the 2 RRMs.
Sequence similarities
Belongs to the RRM CPEB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q7TN98-1
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
- SynonymsmCPEB-4a
- Length729
- Mass (Da)80,122
- Last updated2003-10-01 v1
- Checksum7CB042EDE4B7C0CA
Q7TN98-2
- Name2
- SynonymsmCPEB-4b
- Differences from canonical
- 420-427: Missing
Q7TN98-3
- Name3
- SynonymsmCPEB-4c
- Differences from canonical
- 402-419: Missing
Q7TN98-4
- Name4
- SynonymsmCPEB-4d
- Differences from canonical
- 402-427: Missing
Q7TN98-5
- Name5
- Differences from canonical
- 404-428: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 33-50 | Polar residues | ||||
Sequence: HHQNATPNPAAFINNNTA | ||||||
Compositional bias | 78-101 | Polar residues | ||||
Sequence: EKAKSQQQEQQDPLEKQQLSPSPG | ||||||
Compositional bias | 234-248 | Basic residues | ||||
Sequence: PHHPHFQHHHSQHQQ | ||||||
Compositional bias | 269-301 | Polar residues | ||||
Sequence: NQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSP | ||||||
Alternative sequence | VSP_022044 | 402-419 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022043 | 402-427 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022045 | 404-428 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022046 | 420-427 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY313775 EMBL· GenBank· DDBJ | AAQ20844.1 EMBL· GenBank· DDBJ | mRNA | ||
AK173229 EMBL· GenBank· DDBJ | BAD32507.1 EMBL· GenBank· DDBJ | mRNA | ||
BC115430 EMBL· GenBank· DDBJ | AAI15431.1 EMBL· GenBank· DDBJ | mRNA | ||
BC115431 EMBL· GenBank· DDBJ | AAI15432.1 EMBL· GenBank· DDBJ | mRNA | ||
BC145863 EMBL· GenBank· DDBJ | AAI45864.1 EMBL· GenBank· DDBJ | mRNA | ||
BC145865 EMBL· GenBank· DDBJ | AAI45866.1 EMBL· GenBank· DDBJ | mRNA |