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Description:
Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterised by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin3, also known as DP103, DDX20, DEAD-box protein DP130 and DEAD/H box 20, is a protein product of human chromosome 1p13.2. It associates directly with SMN and is a part of the SMN complex containing Gemin2, Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (for Gemini of the coiled bodies). Gemin3 also interacts with SmB, SmD2 and SmD3. It contains the conserved motif Asp-Glu-Ala-Asp (DEAD) characteristic of DEAD-box proteins. Gemin3 is a putative RNA helicase and shows ATPase activity. It is expressed in B and T cell neuroblastoma-derived cell lines, malignant melanoma tumour, normal testis and is expressed in low levels in colon, skeletal muscle, liver, kidney and lung.
Description:
Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterized by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin3, also known as DP103, DDX20, DEAD-box protein DP130 and DEAD/H box 20, is a protein product of human chromosome 1p13.2. It associates directly with SMN and is a part of the SMN complex containing Gemin2, Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (for Gemini of the coiled bodies). Gemin3 also interacts with SmB, SmD2 and SmD3. It contains the conserved motif Asp-Glu-Ala-Asp (DEAD) characteristic of DEAD-box proteins. Gemin3 is a putative RNA helicase and shows ATPase activity. It is expressed in B and T cell neuroblastoma-derived cell lines, malignant melanoma tumor, normal testis and is expressed in low levels in colon, skeletal muscle, liver, kidney and lung.
Description:
Abhydrolase domain containing 3 (ABHD3) belongs to the AB hydrolase superfamily. It has a central core predicted to form alpha/beta hydrolase folds and has a ser-ala-his catalytic triad characteristic of peroxidases.
Description:
This gene encodes a bitter taste receptor; bitter taste receptors are members of the G protein-coupled receptor superfamily and are specifically expressed by taste receptor cells of the tongue and palate epithelia. Each of these apparently intronless taste receptor genes encodes a 7-transmembrane receptor protein, functioning as a bitter taste receptor. This gene is clustered with another 3 candidate taste receptor genes on chromosome 7 and is genetically linked to loci that influence bitter perception.
Description:
CLN8, a 286 amino acid transmembrane protein, localizes mainly to the endoplasmic reticulum, but also partially to the ER-Golgi intermediate compartment (ERGIC). Mutations in the CLN8 gene cause neuronal ceroid lipofuscinosis 8 and progressive epilepsy with mental retardation (EPMR). Both disorders are forms of neuronal ceroid-lipofuscinose (NCL), a group of progressive neurodegenerative diseases found in children, characterized by failure of psychomotor development, impaired vision, seizures and premature death. The CLN8 protein is one of eight proteins in the CLN family, including CLN1-CLN7, which are associated with NCL.
Description:
CLN8, a 286 amino acid transmembrane protein, localizes mainly to the endoplasmic reticulum, but also partially to the ER-Golgi intermediate compartment (ERGIC). Mutations in the CLN8 gene cause neuronal ceroid lipofuscinosis 8 and progressive epilepsy with mental retardation (EPMR). Both disorders are forms of neuronal ceroid-lipofuscinose (NCL), a group of progressive neurodegenerative diseases found in children, characterized by failure of psychomotor development, impaired vision, seizures and premature death. The CLN8 protein is one of eight proteins in the CLN family, including CLN1-CLN7, which are associated with NCL.
Description:
Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterized by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin2 (formerly known as SIP1 for SMN interacting protein) associates directly with SMN and is a part of the SMN complex containing Gemin3 (a DEAD-box RNA helicase), Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in splicesomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (Gemini of the coiled bodies). The SMN-Gemin2 complex is associated with spliceosomal snRNAs U1 and U5. Gemin2 is expressed in spinal cord. It can be induced by TGF∫ treatment and expression is high in several E-cadherin negative human carcinoma cell lines. SMN is expressed in a wide variety of tissues including brain, kidney, liver and spinal cord, and moderately in skeletal and cardiac muscle. The gene encoding Gemin2 maps to human chromosome 14q13.
Description:
Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.Tissue specificity:Ubiquitously expressed. Expressed at higher levels in the cerebellum and putamen than in other brain regions. Abundant expression seen in the Purkinje cells and pontine neurons.
Description:
Microtubules, the primary component of the cytoskeletal network, are highly dynamic structures composed of Alpha/Beta Tubulin heterodimers. Biosynthesis of functional microtubules involve the participation of several chaperones, termed Tubulin folding cofactors A (TBCA), B (TBCB), D (TBCD), E (TBCE) and C (TBCC), that act on folding intermediates downstream of the cytosolic chaperon, alternatively named TCP. TBCB (tubulin folding cofactor B), also known as CG22, CKAP1 or CKAPI, is a 244 amino acid cytoplasmic protein containing one CAP-Gly domain and in widely expressed. TBCB is involved in the regulation of tubulin heterodimer dissociation and may function as a negative regulator of axonal growth.
Description:
MSK1 is a mitogen and stress activated protein kinase 1 which belongs to the AGC family of kinases and is related in structure to the ribosomal p70 S6 kinase subfamily. MSK1 can be activated by ERK1/2 and SAPK2/p38 MAP kinase. It is also known to be required for the phosphorylation of CREB, ATF1 H3 and HMG14 in response to mitogen and stress. Similar to RSK, MSK1 contains two kinase domains (N term and a C term). Once phosphorylated on Thr581 and Ser360 by ERK1/2 and SAPK2/p38, MSK1 autophosphorylate on at least 5 sites. Of these autophosphorylation sites Ser212 and Ser376 get phosphorylated by the C terminal kinase domain of MSK1 which is essential for the catalytic activity of the N terminal kinase domain.
Description:
MSK1 is a mitogen and stress activated protein kinase 1 which belongs to the AGC family of kinases and is related in structure to the ribosomal p70 S6 kinase subfamily. MSK1 can be activated by ERK1/2 and SAPK2/p38 MAP kinase. It is also known to be required for the phosphorylation of CREB, ATF1 H3 and HMG14 in response to mitogen and stress. Similar to RSK, MSK1 contains two kinase domains (N term and a C term). Once phosphorylated on Thr581 and Ser360 by ERK1/2 and SAPK2/p38, MSK1 autophosphorylate on at least 5 sites. Of these autophosphorylation sites Ser212 and Ser376 get phosphorylated by the C terminal kinase domain of MSK1 which is essential for the catalytic activity of the N terminal kinase domain.
Description:
Sm and Sm-like (LSm) proteins form donut-shaped, ubiquitously expressed heptameric complexes that are involved in various steps of RNA metabolism, including RNA-protein interactions and structural changes that are required during ribosomal subunit assembly. LSm14B, also known as C20orf40, FAM61B or LSM13, is a 385 amino acid protein that exists as multiple alternatively spliced isoforms and may play a role in RNA-related events. The gene encoding LSm14B maps to human chromosome 20. Comprising approximately 2% of the human genome, chromosome 20 contains nearly 63 million bases that encode over 600 genes, some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.
Description:
Sm and Sm-like (LSm) proteins form donut-shaped, ubiquitously expressed heptameric complexes that are involved in various steps of RNA metabolism, including RNA-protein interactions and structural changes that are required during ribosomal subunit assembly. LSm14B, also known as C20orf40, FAM61B or LSM13, is a 385 amino acid protein that exists as multiple alternatively spliced isoforms and may play a role in RNA-related events. The gene encoding LSm14B maps to human chromosome 20. Comprising approximately 2% of the human genome, chromosome 20 contains nearly 63 million bases that encode over 600 genes, some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.
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