SNRPD3 Gene - Small Nuclear Ribonucleoprotein D3 Polypeptide
Core Component of the Spliceosome and U1, U2, U4/U6, U5 snRNPs
Gene Information Card
| Symbol | SNRPD3 |
|---|---|
| Full Name | Small Nuclear Ribonucleoprotein D3 Polypeptide |
| Gene Type | Protein coding |
| Chromosomal Location | 22q11.23 |
| NCBI Gene ID | 6634 ncbi.nlm.nih.gov/gene/6634 |
| Ensembl ID | ENSG00000100181 |
| UniProt ID | P62318 |
| OMIM ID | 601063 |
| HGNC ID | 11162 |
| Aliases | Sm-D3, SMD3, snRNP core protein D3 |
Description
SNRPD3 encodes the Sm-D3 protein, a core component of the spliceosomal U1, U2, U4/U6, and U5 small nuclear ribonucleoproteins (snRNPs). The Sm-D3 protein contains a Sm domain that mediates RNA binding and protein-protein interactions essential for pre-mRNA splicing. SNRPD3 is part of the Sm protein family and is involved in the assembly of the spliceosome, which catalyzes the removal of introns from pre-mRNA. Mutations or altered expression of SNRPD3 have been implicated in various cancers and autoimmune diseases.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Systemic lupus erythematosus | Autoantibodies against Sm proteins, including Sm-D3, are diagnostic markers; immune complex deposition leads to tissue damage. | ClinVar, OMIM |
| Breast cancer | Overexpression of SNRPD3 is associated with poor prognosis and may promote splicing alterations that drive tumorigenesis. | COSMIC, NCBI PubMed |
| Colorectal cancer | SNRPD3 upregulation correlates with advanced stage and metastasis; potential role in alternative splicing of oncogenes. | COSMIC, NCBI PubMed |
| Lung cancer | SNRPD3 mutations and copy number alterations found in lung adenocarcinoma; may affect splicing of tumor suppressor genes. | COSMIC |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Testis | 15.2 | High |
| Lymph node | 12.8 | High |
| Spleen | 11.5 | High |
| Bone marrow | 10.9 | High |
| Brain | 8.3 | Medium |
| Liver | 6.1 | Medium |
| Heart | 5.4 | Medium |
| Kidney | 4.7 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 14.3 | Cervical cancer cell line |
| K562 | 13.1 | Leukemia cell line |
| A549 | 11.8 | Lung cancer cell line |
| MCF7 | 10.5 | Breast cancer cell line |
| HEK293 | 9.2 | Embryonic kidney cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1A>G (p.Met1?) | Missense | <0.01% | Loss of start codon; likely loss of function |
| c.214G>A (p.Gly72Arg) | Missense | <0.01% | Alters Sm domain; potential dominant negative effect |
| c.346C>T (p.Arg116Trp) | Missense | <0.01% | Unknown significance; reported in cancer |
| c.421_423del (p.Lys141del) | Deletion | <0.01% | In-frame deletion; may affect protein stability |
Mutation functional classification
Loss of Function (LOF)
Mutations that disrupt the start codon or introduce premature stop codons are predicted to cause loss of function, impairing snRNP assembly and splicing.
Gain of Function (GOF)
No clear gain-of-function mutations have been reported; overexpression in cancer may act as a functional gain.
Dominant Negative (DN)
Mutations in the Sm domain (e.g., p.Gly72Arg) may interfere with snRNP complex formation, acting in a dominant negative manner.
View complete mutation data：
Gene Ontology (GO)
| • spliceosomal complex assembly (GO:0000245) | • mRNA splicing (GO:0000398) |
| • spliceosomal complex (GO:0005681) | • RNA binding (GO:0003723) |
| • nucleus (GO:0005634) |
Pathways
• hsa03040 - Spliceosome (KEGG)
• R-HSA-72163 - mRNA Splicing - Major Pathway (Reactome)
• R-HSA-72172 - mRNA Splicing (Reactome)
Protein Summary
The SNRPD3 protein (Sm-D3) is a 126-amino acid core component of the spliceosomal snRNPs. It contains a conserved Sm domain that forms a ring structure with other Sm proteins, binding to the Sm site of U1, U2, U4, and U5 snRNAs. Sm-D3 is essential for spliceosome assembly and pre-mRNA splicing. Post-translational modifications include symmetric dimethylation of arginine residues, which may influence protein-protein interactions and autoantibody recognition in autoimmune diseases.
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