PRPF19 Gene Summary [Human]
Enables identical protein binding activity and ubiquitin-ubiquitin ligase activity. Involved in several processes, including DNA damage checkpoint signaling; cellular protein metabolic process; and mRNA splicing, via spliceosome. Acts upstream of or within protein polyubiquitination. Located in cytoplasm; nuclear speck; and site of double-strand break. Part of Prp19 complex and U2-type catalytic step 2 spliceosome. Colocalizes with DNA replication factor A complex. [provided by Alliance of Genome Resources, Apr 2022]
Details
| Type | Protein Coding |
| Official Symbol | PRPF19 |
| Official Name | pre-mRNA processing factor 19 [Source:HGNC Symbol;Acc:HGNC:17896] |
| Ensembl ID | ENSG00000110107 |
| Bio databases IDs | |
| Aliases | pre-mRNA processing factor 19, nuclear matrix protein NMP200 related to splicing factor PRP19, psoralen 4 |
| Synonyms | D19Wsu55e, hPSO4, NMP200, pre-mRNA processing factor 19, PRP19, PSO4, SNEV, UBOX4 |
| 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 PRPF19 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- self-association domain
- low complexity domain
- globular domain
- ubiquitin protein ligase activity
- WD domain, G-beta repeat
- coiled-coil domain
- WD40
- enzyme
- protein binding
- identical protein binding
- Prp19/Pso4-like
- Anaphase-promoting complex subunit 4 WD40 domain
- WD40 repeats
- RING finger (Really Interesting New Gene) domain and U-box domain superfamily
- Modified RING finger domain
Pathways
Biological processes and signaling networks where the PRPF19 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
- colorectal cancer
- urothelial bladder carcinoma
- transitional cell bladder cancer
- organismal death
- plasma cell neoplasm
- B cell cancer
- mature B-cell neoplasia
- major depression
role in cell
- migration
- apoptosis
- cell viability
- expression in
- proliferation
- accumulation in
- activation in
- phosphorylation in
- growth
- differentiation
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Nucleus
- catalytic step 2 spliceosome
- Cytoplasm
- lipid droplets
- spliceosomes
- nuclear foci
- inner nuclear membrane
- nucleoplasm
- nucleoli
- interchromatin granule clusters
- nuclear speckles
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human PRPF19 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- DNA damage checkpoint
- positive regulation of nuclear mRNA splicing, via spliceosome
- protein polyubiquitination
- protein localization
- lipid biosynthetic process
- protein K63-linked ubiquitination
- double-strand break repair via nonhomologous end joining
- spliceosomal complex assembly
- proteasomal protein catabolic process
- nuclear mRNA splicing, via spliceosome
- assembly of spliceosomal tri-snRNP
Cellular Component
Where in the cell the gene product is active
- site of double-strand break
- nuclear speck
- spliceosomal complex
- DNA replication factor A complex
- Prp19 complex
- nucleoplasm
- lipid particle
- nucleus
- catalytic step 2 spliceosome
- cytoplasm
- membrane
- U2-type catalytic step 1 spliceosome
- spindle
- U2-type catalytic step 2 spliceosome
Molecular Function
What the gene product does at the molecular level
- ubiquitin-protein ligase activity
- identical protein binding
- protein binding
- ubiquitin-ubiquitin ligase activity