RNF32-AS1

Homo sapiens

ASSOCIATED WITH Autism; autistic disorder; Patterson Stevenson Syndrome

LINC00244

Homo sapiens

ASSOCIATED WITH Autism; autistic disorder; Patterson Stevenson Syndrome; INTERACTS WITH aflatoxin B1; benzo[a]pyrene; nickel sulfate

atx-3

Caenorhabditis elegans

Enables cysteine-type deubiquitinase activity. Involved in chemical synaptic transmission. Located in cytoplasm and nucleus. Expressed in coelomocyte; head; somatic nervous system; and tail neurons. Used to study Machado-Joseph disease. Human ortholog(s) of this gene implicated in Machado-Joseph disease and late onset Parkinson's disease. Is an ortholog of human ATXN3 (ataxin 3) and ATXN3L (ataxin 3 like).

Atxn3

Homo sapiens

Machado-Joseph disease, also known as spinocerebellar ataxia-3, is an autosomal dominant neurologic disorder. The protein encoded by this gene contains (CAG)n repeats in the coding region, and the expansion of these repeats from the normal 12-44 to 52-86 is one cause of Machado-Joseph disease. There is a negative correlation between the age of onset and CAG repeat numbers. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Jul 2016]

ATXN3L

Homo sapiens

This intronless gene may be a pseudogene (PMID:11450850). This gene is similar to the multi-exon gene which encodes ataxin 3 and contains a coding region which could encode a protein similar to ataxin 3. Mutations in the gene encoding ataxin 3 are associated with Machado-Joseph disease. [provided by RefSeq, Sep 2011]

bec-1

Caenorhabditis elegans

Predicted to enable phosphatidylinositol 3-kinase binding activity and protein-macromolecule adaptor activity. Involved in several processes, including determination of adult lifespan; gamete generation; and nematode male tail tip morphogenesis. Located in cytoplasmic vesicle and nucleus. Expressed in several structures, including intestine; nervous system; pharynx; tail; and vulva. Human ortholog(s) of this gene implicated in several diseases, including Alzheimer's disease; Barrett's esophagus; Machado-Joseph disease; and adenocarcinoma (multiple). Is an ortholog of human BECN1 (beclin 1).

Dusp18

Homo sapiens

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP18 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]

Dusp14

Homo sapiens

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]

gfat-1

Caenorhabditis elegans

Predicted to enable glutamine-fructose-6-phosphate transaminase (isomerizing) activity. Involved in IRE1-mediated unfolded protein response. Expressed in tail. Used to study Machado-Joseph disease. Human ortholog(s) of this gene implicated in congenital myasthenic syndrome 12; obesity; and type 2 diabetes mellitus. Is an ortholog of human GFPT1 (glutamine--fructose-6-phosphate transaminase 1).

Dusp19

Homo sapiens

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]