STRINGSTRING
LSM8 LSM8 LSM4 LSM4 A0A1L9S6A9 A0A1L9S6A9 LSM5 LSM5 A0A1L9SG17 A0A1L9SG17 A0A1L9SGC1 A0A1L9SGC1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
LSM8U6 snRNA-associated Sm-like protein LSm8; Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. (98 aa)
LSM4U6 snRNA-associated Sm-like protein LSm4; Binds specifically to the 3'-terminal U-tract of U6 snRNA. (122 aa)
A0A1L9S6A9Small nuclear ribonucleoprotein E; Associated with the spliceosome snRNP U1, U2, U4/U6 and U5. Belongs to the snRNP Sm proteins family. (96 aa)
LSM5U6 snRNA-associated Sm-like protein LSm5; Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA. (83 aa)
A0A1L9SG17Small nuclear ribonucleoprotein G. (78 aa)
A0A1L9SGC1U6 snRNA-associated Sm-like protein LSm2; Binds specifically to the 3'-terminal U-tract of U6 snRNA. (98 aa)
Your Current Organism:
Penicilliopsis zonata
NCBI taxonomy Id: 1073090
Other names: Aspergillus zonatus CBS 506.65, P. zonata CBS 506.65, Penicilliopsis zonata CBS 506.65
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