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SIP1 Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O14893 |
|---|
| Gene ID | 8487 |
|---|---|
| Other Names | Gem-associated protein 2, Gemin-2, Component of gems 2, Survival of motor neuron protein-interacting protein 1, SMN-interacting protein 1, GEMIN2, SIP1 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 244-257 of HUMAN GEMIN2 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | GEMIN2 (HGNC:10884) |
|---|---|
| Synonyms | SIP1 |
| Function | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs (PubMed:18984161, PubMed:9323129). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A (PubMed:18984161, PubMed:9323129). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound (PubMed:31799625, PubMed:21816274, PubMed:16314521). |
| Cellular Location | Nucleus, gem. Cytoplasm. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm |
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Provided below are standard protocols that you may find useful for product applications.
Background
The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.
References
Liu Q.,et al.Cell 90:1013-1021(1997).
Aerbajinai W.,et al.Int. J. Biochem. Cell Biol. 34:699-707(2002).
Helmken C.,et al.Eur. J. Hum. Genet. 8:493-499(2000).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Gubitz A.K.,et al.J. Biol. Chem. 277:5631-5636(2002).
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