SCUBA

CLNS1A — Chloride nucleotide-sensitive channel 1A

CLNS1A belongs to a gene co-expression module in 3 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

CLNS1A's module in each cell type

Cell typeModuleShares the module with
Gamma-delta T cellsGlycolysis & Proteasome
Housekeeping
ACAA2, ANAPC15, APEH, C1QBP, CCDC167, CHMP2A, ENO1, HINT1 +11 more
Innate lymphoid cellsMitochondrial OxPhos
Mitochondrial & OxPhos
AKR7A2, ANXA6, AP2M1, ARL6IP4, ARPC1B, ATP5MC2, ATP5PB, BSG +21 moreView in SCUBA
MacrophagesComplex I / NADH Dehydrogenase
Mitochondrial & OxPhos
AHCY, ANP32A, ANTKMT, APEX1, ARL2, ATIC, ATP5F1A, ATP5ME +31 moreView in SCUBA

About the gene

SynonymsCLCI, ICln
Chromosome11: 77514936-77637794
Predicted locationIntracellular
Essential geneYes
Protein classEssential proteins, Predicted intracellular proteins, Transporters
Biological processmRNA processing, mRNA splicing

Function

Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins. Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and 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 (Sm core). 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.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.