Q7TN98 · CPEB4_MOUSE

  • Protein
    Cytoplasmic polyadenylation element-binding protein 4
  • Gene
    Cpeb4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for site, binding site.

1729100200300400500600700
TypeIDPosition(s)Description
Site473RNA-binding
Site561Important for the positionning of RRM1 relative to RRM2
Binding site667Zn2+ 1 (UniProtKB | ChEBI)
Binding site675Zn2+ 1 (UniProtKB | ChEBI)
Binding site684Zn2+ 2 (UniProtKB | ChEBI)
Binding site689Zn2+ 2 (UniProtKB | ChEBI)
Binding site694Zn2+ 1 (UniProtKB | ChEBI)
Binding site697Zn2+ 1 (UniProtKB | ChEBI)
Binding site702Zn2+ 2 (UniProtKB | ChEBI)
Binding site710Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentdendritic spine
Cellular Componentendoplasmic reticulum
Cellular Componentgrowth cone
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentpostsynaptic density
Cellular Componentsynapse
Molecular Functionmetal ion binding
Molecular FunctionmRNA 3'-UTR binding
Molecular FunctionRNA binding
Molecular Functiontranslation regulator activity
Biological Processcellular response to amino acid stimulus
Biological Processcellular response to decreased oxygen levels
Biological Processcellular response to glucose starvation
Biological Processionotropic glutamate receptor signaling pathway
Biological Processnegative regulation of neuron apoptotic process
Biological Processresponse to ischemia

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cytoplasmic polyadenylation element-binding protein 4
  • Short names
    CPE-BP4; CPE-binding protein 4; mCPEB-4

Gene names

    • Name
      Cpeb4
    • Synonyms
      Kiaa1673

Organism names

  • Taxonomic identifier
  • Strain
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q7TN98
  • Secondary accessions
    • A6H6G0
    • Q69ZD7

Proteomes

Organism-specific databases

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).

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002692651-729Cytoplasmic polyadenylation element-binding protein 4
Modified residue97Phosphoserine
Modified residue99Phosphoserine
Modified residue137Phosphoserine
Modified residue252Phosphoserine
Modified residue255Phosphoserine
Modified residue326Phosphothreonine
Modified residue330Phosphoserine
Modified residue332Phosphoserine

Keywords

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).

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).

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

Interaction

Subunit

Interacts with TOB1.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region20-50Disordered
Compositional bias33-50Polar residues
Compositional bias78-101Polar residues
Region78-133Disordered
Region218-324Disordered
Compositional bias234-248Basic residues
Compositional bias269-301Polar residues
Domain472-563RRM 1
Region541-543RNA-binding
Domain580-662RRM 2

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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

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.

  • Name
    1
  • Synonyms
    mCPEB-4a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    729
  • Mass (Da)
    80,122
  • Last updated
    2003-10-01 v1
  • Checksum
    7CB042EDE4B7C0CA
MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPNPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDSSSENSNGKEKLRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPGASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRSAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPERPRTFDMHSLESSLIDIMRAENDSIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFTHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN

Q7TN98-2

  • Name
    2
  • Synonyms
    mCPEB-4b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q7TN98-3

  • Name
    3
  • Synonyms
    mCPEB-4c
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q7TN98-4

  • Name
    4
  • Synonyms
    mCPEB-4d
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q7TN98-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q5SU47Q5SU47_MOUSECpeb4392
Q5SU48Q5SU48_MOUSECpeb4712

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias33-50Polar residues
Compositional bias78-101Polar residues
Compositional bias234-248Basic residues
Compositional bias269-301Polar residues
Alternative sequenceVSP_022044402-419in isoform 3
Alternative sequenceVSP_022043402-427in isoform 4
Alternative sequenceVSP_022045404-428in isoform 5
Alternative sequenceVSP_022046420-427in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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