PABPC4 Gene Summary [Human]
Poly(A)-binding proteins (PABPs) bind to the poly(A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. This protein has also been found to interact with coronavirus nucleocapsid proteins and is thought to inhibit coronavirus replication. [provided by RefSeq, Nov 2021]
Details
| Type | Protein Coding |
| Official Symbol | PABPC4 |
| Official Name | poly(A) binding protein cytoplasmic 4 [Source:HGNC Symbol;Acc:HGNC:8557] |
| Ensembl ID | ENSG00000090621 |
| Bio databases IDs | |
| Aliases | poly(A) binding protein cytoplasmic 4, activated-platelet protein 1, Inducible poly(A)-binding protein |
| Synonyms | APP-1, iPABP, PABP4, poly(A) binding protein cytoplasmic 4, poly(A) binding protein, cytoplasmic 4, Poly(A)-binding protein, cytoplasmic 4 (inducible form), Polyadenylate-binding |
| Species | Human, Homo sapiens |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in human PABPC4 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- ELAV/HuD family splicing factor
- RNA recognition motif (RRM) superfamily
- RNA recognition motif
- mRNA binding
- poly(A) binding protein
- protein binding
- heterogeneous nuclear ribonucleoprotein R, Q family
- Poly-adenylate binding protein, unique domain
- C-terminal domain of Poly(A)-binding protein
- translation regulator
- poly(U) binding protein
- polyadenylate binding protein, human types 1, 2, 3, 4 family
- RNA binding motif
- poly-U binding splicing factor, half-pint family
Pathways
Biological processes and signaling networks where the PABPC4 gene in human plays a role, providing insight into its function and relevance in health or disease.
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- non-insulin-dependent diabetes mellitus
- gastric adenocarcinoma
- chronic obstructive pulmonary disease
- gastric epithelial cancer
role in cell
- expression in
- translation in
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- detergent resistant lipid raft fraction
- ribosome
- Nucleus
- cytosol
- stress granule
- paraspeckle-like structures
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human PABPC4 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- RNA processing
- regulation of mRNA stability
- blood coagulation
- translation
- RNA catabolic process
Cellular Component
Where in the cell the gene product is active
- nucleus
- cytoplasmic stress granule
- cytoplasm
- cytosol
Molecular Function
What the gene product does at the molecular level
- RNA binding
- protein binding
- poly(A) RNA binding
- poly(C) RNA binding
- poly(U) RNA binding
- mRNA 3'-UTR binding