ISG15 (interferon-induced 15 kDa protein; also known as IP17) is a 15 kDa ubiquitin family protein that is expressed by a wide variety of cell types. ISG15 is induced by type-I IFN, and like ubiquitin, becomes conjugated to intracellular proteins. Unlike ubiquitin, it does not target proteins for degradation. Instead, it is part of the antivirus response. Human proISG15 is 165 amino acids (aa) in length. There are two ubiquitin-like domains (aa 2-78 and 79-157) and a propeptide (aa 158-165) that is cleaved intracellularly. Select blood mononuclear cells secrete mature ISG15, which is chemotactic for neutrophils. Mature human ISG15 is 66% aa identical to mouse ISG15.
Interferon-stimulated 20 kDa protein (ISG20) is an exoribonuclease that functions as part of the host innate immune response to RNA-based viruses. Indeed, expression of ISG20 can be induced by type-I and type-II interferons following cellular exposure to RNA-based viruses. Mechanistically, ISG20 localizes to the nucleolus and is believed to inhibit the replication of RNA-based viruses, in part, by employing 3'-5' exonuclease activity toward viral RNAs.
This gene encodes a member of the LIM/homeodomain family of transcription factors. The encoded protein binds to the enhancer region of the insulin gene, among others, and may play an important role in regulating insulin gene expression. The encoded protein is central to the development of pancreatic cell lineages and may also be required for motor neuron generation. Mutations in this gene have been associated with maturity-onset diabetes of the young.
This gene encodes a protein that is a member of the integrin superfamily. Members of this family are adhesion receptors that function in signaling from the extracellular matrix to the cell. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The encoded protein forms a dimer with an alpha v chain and this heterodimer can bind to ligands like fibronectin and transforming growth factor beta 1. Alternate splicing results in multiple transcript variants.
This gene encodes a member of the NF-kappa-B inhibitor family, which contain multiple ankrin repeat domains. The encoded protein interacts with REL dimers to inhibit NF-kappa-B/REL complexes which are involved in inflammatory responses. The encoded protein moves between the cytoplasm and the nucleus via a nuclear localization signal and CRM1-mediated nuclear export. Mutations in this gene have been found in ectodermal dysplasia anhidrotic with T-cell immunodeficiency autosomal dominant disease.
This gene encodes a membrane protein that is a member of a class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The encoded kinase phosphorylates STAT proteins (signal transducers and activators of transcription) and plays a key role in interferon-alpha/beta and interferon-gamma signal transduction. Alternative splicing results in multiple transcript variants.
This gene product is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. It has been found to be constituitively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis.
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