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'''ISG15 ubiquitin-like modifier''', also known as '''ISG15''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ISG15 ISG15 ubiquitin-like modifier| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9636| accessdate = }}</ref> |
'''ISG15 ubiquitin-like modifier''', also known as '''ISG15''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ISG15 ISG15 ubiquitin-like modifier| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9636| accessdate = }}</ref> ISG15 shares several common properties with other ubiquitin-like molecules (UBLs), but its activity is tightly regulated by specific signaling pathways that have a role in innate immunity. ISG15 was identified as an interferon stimulated [[gene]] (ISG) since its expression is induced in response to type I interferons or lipopolysaccharide treatment. Upon interferon treatment, ISG15 can be detected in both free and conjugated forms, and is secreted from monocytes and lymphocytes where it can function as a cytokine. In the cell, ISG15 co-localizes with intermediate filaments and ISGylation may modulate the JAK-STAT pathway or certain aspects of neurological disease. It is also known as UCRP ([[ubiquitin]] cross-reactive protein) since it contains 2 tandem ubiquitin homology domains and is cross-reactive with ubiquitin antibodies. In contrast to other UBLs, ISG15 has not been identified in lower eukaryotes (yeast, nematode, insects, plants) indicating its role in specialized functions. |
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The mechanism of ISGylation and deISGylation is similar to that of [[ubiquitin]], although the complete system components have not yet been identified. The activating E1 enzyme (UBE1L) charges ISG15 by forming a high-energy thiolester intermediate and transfers it to the UbcH8 E2 protein. UbcH8 has been identified as the major E2 for ISGlyation, although it also functions in ubiquitination. The E2 protein subsequently transfers the ISG15 to specific E3 ligases (none have been identified to date) and relevant intracellular substrates. Only one deconjugating protease with specificity to ISG15 has been identified to date: UBP43 (a member of the USP family) cleaves ISG15-peptide fusions and also removes ISG15 (deISGylation) from native conjugates. <ref>{{cite web | title = Boston Biochem ISG15 Overview| url = http://www.bostonbiochem.com/overview.php?prod=isg15| accessdate = 05/21/2008}}</ref> |
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Revision as of 15:49, 21 May 2008
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Aliases | ISG15, G1P2, IFI15, IP17, UCRP, hUCRP, IMD38, ISG15 ubiquitin-like modifier, ISG15 ubiquitin like modifier | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 147571; MGI: 1855694; HomoloGene: 48326; GeneCards: ISG15; OMA:ISG15 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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ISG15 ubiquitin-like modifier, also known as ISG15, is a human gene.[5] ISG15 shares several common properties with other ubiquitin-like molecules (UBLs), but its activity is tightly regulated by specific signaling pathways that have a role in innate immunity. ISG15 was identified as an interferon stimulated gene (ISG) since its expression is induced in response to type I interferons or lipopolysaccharide treatment. Upon interferon treatment, ISG15 can be detected in both free and conjugated forms, and is secreted from monocytes and lymphocytes where it can function as a cytokine. In the cell, ISG15 co-localizes with intermediate filaments and ISGylation may modulate the JAK-STAT pathway or certain aspects of neurological disease. It is also known as UCRP (ubiquitin cross-reactive protein) since it contains 2 tandem ubiquitin homology domains and is cross-reactive with ubiquitin antibodies. In contrast to other UBLs, ISG15 has not been identified in lower eukaryotes (yeast, nematode, insects, plants) indicating its role in specialized functions.
The mechanism of ISGylation and deISGylation is similar to that of ubiquitin, although the complete system components have not yet been identified. The activating E1 enzyme (UBE1L) charges ISG15 by forming a high-energy thiolester intermediate and transfers it to the UbcH8 E2 protein. UbcH8 has been identified as the major E2 for ISGlyation, although it also functions in ubiquitination. The E2 protein subsequently transfers the ISG15 to specific E3 ligases (none have been identified to date) and relevant intracellular substrates. Only one deconjugating protease with specificity to ISG15 has been identified to date: UBP43 (a member of the USP family) cleaves ISG15-peptide fusions and also removes ISG15 (deISGylation) from native conjugates. [6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000187608 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035692 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: ISG15 ISG15 ubiquitin-like modifier".
- ^ "Boston Biochem ISG15 Overview". Retrieved 05/21/2008.
{{cite web}}
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