Rabbit anti-Human SMN2 Polyclonal Antibody

Uniprot Id

Q16637

Target Species

Human

Target Name

SMN1

Target Full Name

Survival motor neuron protein

Target 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. 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits. 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. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).

Target Involvement

Spinal muscular atrophy 1 (SMA1); Spinal muscular atrophy 2 (SMA2); Spinal muscular atrophy 3 (SMA3); Spinal muscular atrophy 4 (SMA4)

Target Subcellular Location

Nucleus, gem. Nucleus, Cajal body. Cytoplasm. Cytoplasmic granule. Perikaryon. Cell projection, neuron projection. Cell projection, axon. Cytoplasm, myofibril, sarcomere, Z line.

Target Protein Families

SMN family

Target Tissue Specificity

Expressed in a wide variety of tissues. Expressed at high levels in brain, kidney and liver, moderate levels in skeletal and cardiac muscle, and low levels in fibroblasts and lymphocytes. Also seen at high levels in spinal cord. Present in osteoclasts and

Target Research Area

Epigenetics and Nuclear Signaling

Target Synonyms

BCD541; Component of gems 1; Gemin 1; Gemin-1; OTTHUMP00000125198; OTTHUMP00000223567; OTTHUMP00000223568; OTTHUMP00000224066; OTTHUMP00000226924; SMA 1; SMA 2; SMA 3; SMA 4; SMA; SMA@; SMA1; SMA2; SMA3; SMA4; SMN; SMN_HUMAN; SMN1; SMN2; SMNT; Survival motor neuron protein; Survival of motor neuron 1, telomeric; T-BCD541

Target Background

This gene is part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. The telomeric and centromeric copies of this gene are nearly identical and encode the same protein. While mutations in the telomeric copy are associated with spinal muscular atrophy, mutations in this gene, the centromeric copy, do not lead to disease. This gene may be a modifier of disease caused by mutation in the telomeric copy. The critical sequence difference between the two genes is a single nucleotide in exon 7, which is thought to be an exon splice enhancer. Note that the nine exons of both the telomeric and centromeric copies are designated historically as exon 1, 2a, 2b, and 3-8. It is thought that gene conversion events may involve the two genes, leading to varying copy numbers of each gene. The full length protein encoded by this gene localizes to both the cytoplasm and the nucleus. Within the nucleus, the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs). This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN4, and also interacts with several proteins known to be involved in the biogenesis of snRNPs, such as hnRNP U protein and the small nucleolar RNA binding protein. Four transcript variants encoding distinct isoforms have been described.