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anti-Human GEMIN5 Antibodies:
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Golden Syrian Hamster Polyclonal GEMIN5 Primary Antibody for IP, WB - ABIN253188
Piñeiro, Ramajo, Bradrick, Martínez-Salas: Gemin5 proteolysis reveals a novel motif to identify L protease targets. in Nucleic acids research 2012
Show all 6 Pubmed References
Human Polyclonal GEMIN5 Primary Antibody for IP, WB - ABIN253187
Pérez-Vilaró, Scheller, Saludes, Díez: Hepatitis C virus infection alters P-body composition but is independent of P-body granules. in Journal of virology 2012
The non-canonical RNA-binding domains of gem nuclear organelle associated protein 5 (Gemin5) recognize distinct RNAs.
study provides direct evidence that Gemin5 is involved in unassembled-U1 snRNA disposal under conditions of SMN deficiency.
the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs
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.
These results reveal the ribosome-binding capacity of the N-ter moiety, enabling Gemin5 to control global protein synthesis.
Gemin5 is dispensable for snRNA identification and snRNP assembly.
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.
The C-terminal region of Gemin5 bears two non-canonical bipartite RNA-binding sites.
The Gemin5's function in delivering pre-snRNAs as substrates for Sm core assembly and processing.
gemin5 has a role as a novel cap-binding protein and WD repeat domains are involved in m(7)G recognition
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
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
Gemin5 functions as a scaffold protein for the ASK1-JNK1 signaling module and thereby potentiates ASK1-mediated signaling events.
Absence of GEMIN5 from SMN complexes in nuclear Cajal bodies is demonstrated.
Gemin5-containing subunits bind small nuclear RNA independently of the SMN complex and without a requirement for exogenous ATP
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.
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.
This gene encodes a WD repeat protein that is a component of the survival of motor neurons (SMN) complex. The SMN complex plays a critical role in mRNA splicing through the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs), and may also mediate the assembly and transport of other classes of ribonucleoproteins. The encoded protein is the snRNA-binding component of the SMN complex. Dysregulation of this gene may play a role in alternative mRNA splicing and tumor cell motility. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
gem-associated protein 5