Browse our anti-GEMIN5 (GEMIN5) Antibodies

Human Gem (Nuclear Organelle) Associated Protein 5 (GEMIN5) interaction partners

1. The non-canonical RNA-binding domains of gem nuclear organelle associated protein 5 (Gemin5) recognize distinct RNAs.

2. study provides direct evidence that Gemin5 is involved in unassembled-U1 snRNA disposal under conditions of SMN deficiency.

3. the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs

4. provide mechanistic understandings of Gemin5's snRNA-binding specificity as well as valuable insights into the molecular mechanism of RNA binding by WD40 repeat proteins in general.

5. These results reveal the ribosome-binding capacity of the N-ter moiety, enabling Gemin5 to control global protein synthesis.

6. Gemin5 is dispensable for snRNA identification and snRNP assembly.

7. This work both reveals a new autoregulatory pathway governing SMN expression, and identifies a new mechanism through which SMN can modulate specific mRNA expression via Gemin5.

8. The C-terminal region of Gemin5 bears two non-canonical bipartite RNA-binding sites.

9. The Gemin5's function in delivering pre-snRNAs as substrates for Sm core assembly and processing.

10. gemin5 has a role as a novel cap-binding protein and WD repeat domains are involved in m(7)G recognition

11. we report the identification of an additional component of the SMN complex, a novel WD repeat protein termed Gemin5. Gemin5 binds SMN directly and is a component of the SMN complex

12. Gemin5 is the snRNA binding protein of the SMN complex, binding directly and specifically to the unique features of snRNAs and is the factor that allows the SMN complex to distinguish snRNAs from other cellular RNAs for snRNP biogenesis

13. Gemin5 functions as a scaffold protein for the ASK1-JNK1 signaling module and thereby potentiates ASK1-mediated signaling events.

14. Absence of GEMIN5 from SMN complexes in nuclear Cajal bodies is demonstrated.

15. Gemin5-containing subunits bind small nuclear RNA independently of the SMN complex and without a requirement for exogenous ATP

16. The data provide the first demonstration that alterations in the expression of Gemin5, a spliceosome protein, can effect both specific splicing events and tumor cell motility.

17. The entire WD repeat domain, comprising 13 WD motifs, is both necessary and sufficient for sequence-specific, high-affinity binding of Gemin5 to its RNA targets.

Mouse (Murine) Gem (Nuclear Organelle) Associated Protein 5 (GEMIN5) interaction partners

1. This work both reveals a new autoregulatory pathway governing SMN expression, and identifies a new mechanism through which SMN can modulate specific mRNA expression via Gemin5.