USP18: Difference between revisions

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'''Ubiquitin specific peptidase 18''' ('''USP18'''), also known as '''UBP43''', is an enzyme that in human is encoded by the ''USP18'' gene.<ref name="entrez">{{cite web | title = Entrez Gene: USP18 ubiquitin specific peptidase 18| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11274| accessdate = }}</ref> USP18 is a member of the [[Deubiquitinating enzyme|deubiquitinating protease]] family of enzymes. It is thought to remove [[ISG15]] adducts from a broad range of protein substrates, a process known as deISGylation.<ref name="entrez"/>
'''Ubiquitin specific peptidase 18''' ('''USP18'''), also known as '''UBP43''', is an [[isopeptidase]] that in human is encoded by the ''USP18'' gene.<ref name="entrez">{{cite web | title = Entrez Gene: USP18 ubiquitin specific peptidase 18| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11274| accessdate = }}</ref> USP18 is a member of the [[Deubiquitinating enzyme|deubiquitinating protease]] family of enzymes. It is thought to remove [[ISG15]] adducts from a broad range of protein substrates, a process known as deISGylation.<ref name="entrez"/> In mice, deletion of this enzyme results in increased inflammatory response to [[type I interferon]]s, suggesting that USP18 may, in part, regulate interferon responsiveness.<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/gene/11274|title=USP18 ubiquitin specific peptidase 18 [Homo sapiens (human)] - Gene - NCBI|website=www.ncbi.nlm.nih.gov|access-date=2018-01-03}}</ref>


==References==
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Li XL, Blackford JA, Judge CS, Liu M, Xiao W, Kalvakolanu DV, Hassel BA | title = RNase-L-dependent destabilization of interferon-induced mRNAs. A role for the 2-5A system in attenuation of the interferon response | journal = The Journal of Biological Chemistry | volume = 275 | issue = 12 | pages = 8880–8 | date = March 2000 | pmid = 10722734 | doi = 10.1074/jbc.275.12.8880 }}
| citations =
* {{cite journal | vauthors = Schwer H, Liu LQ, Zhou L, Little MT, Pan Z, Hetherington CJ, Zhang DE | title = Cloning and characterization of a novel human ubiquitin-specific protease, a homologue of murine UBP43 (Usp18) | journal = Genomics | volume = 65 | issue = 1 | pages = 44–52 | date = April 2000 | pmid = 10777664 | doi = 10.1006/geno.2000.6148 }}
*{{cite journal   |vauthors=Li XL, Blackford JA, Judge CS, etal |title=RNase-L-dependent destabilization of interferon-induced mRNAs. A role for the 2-5A system in attenuation of the interferon response. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8880–8 |year= 2000 |pmid= 10722734 |doi=10.1074/jbc.275.12.8880 }}
* {{cite journal | vauthors = Kang D, Jiang H, Wu Q, Pestka S, Fisher PB | title = Cloning and characterization of human ubiquitin-processing protease-43 from terminally differentiated human melanoma cells using a rapid subtraction hybridization protocol RaSH | journal = Gene | volume = 267 | issue = 2 | pages = 233–42 | date = April 2001 | pmid = 11313150 | doi = 10.1016/S0378-1119(01)00384-5 }}
*{{cite journal   |vauthors=Schwer H, Liu LQ, Zhou L, etal |title=Cloning and characterization of a novel human ubiquitin-specific protease, a homologue of murine UBP43 (Usp18). |journal=Genomics |volume=65 |issue= 1 |pages= 44–52 |year= 2000 |pmid= 10777664 |doi= 10.1006/geno.2000.6148 }}
* {{cite journal | vauthors = Malakhov MP, Malakhova OA, Kim KI, Ritchie KJ, Zhang DE | title = UBP43 (USP18) specifically removes ISG15 from conjugated proteins | journal = The Journal of Biological Chemistry | volume = 277 | issue = 12 | pages = 9976–81 | date = March 2002 | pmid = 11788588 | doi = 10.1074/jbc.M109078200 }}
*{{cite journal   |vauthors=Kang D, Jiang H, Wu Q, etal |title=Cloning and characterization of human ubiquitin-processing protease-43 from terminally differentiated human melanoma cells using a rapid subtraction hybridization protocol RaSH. |journal=Gene |volume=267 |issue= 2 |pages= 233–42 |year= 2001 |pmid= 11313150 |doi=10.1016/S0378-1119(01)00384-5 }}
* {{cite journal | vauthors = Tokarz S, Berset C, La Rue J, Friedman K, Nakayama K, Nakayama K, Zhang DE, Lanker S | title = The ISG15 isopeptidase UBP43 is regulated by proteolysis via the SCFSkp2 ubiquitin ligase | journal = The Journal of Biological Chemistry | volume = 279 | issue = 45 | pages = 46424–30 | date = November 2004 | pmid = 15342634 | doi = 10.1074/jbc.M403189200 }}
*{{cite journal   |vauthors=Malakhov MP, Malakhova OA, Kim KI, etal |title=UBP43 (USP18) specifically removes ISG15 from conjugated proteins. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9976–81 |year= 2002 |pmid= 11788588 |doi= 10.1074/jbc.M109078200 }}
* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = October 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
*{{cite journal   |vauthors=Tokarz S, Berset C, La Rue J, etal |title=The ISG15 isopeptidase UBP43 is regulated by proteolysis via the SCFSkp2 ubiquitin ligase. |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46424–30 |year= 2004 |pmid= 15342634 |doi= 10.1074/jbc.M403189200 }}
* {{cite journal | vauthors = Yan M, Luo JK, Ritchie KJ, Sakai I, Takeuchi K, Ren R, Zhang DE | title = Ubp43 regulates BCR-ABL leukemogenesis via the type 1 interferon receptor signaling | journal = Blood | volume = 110 | issue = 1 | pages = 305–12 | date = July 2007 | pmid = 17374743 | pmc = 1896118 | doi = 10.1182/blood-2006-07-033209 }}
*{{cite journal   |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 }}
* {{cite journal | vauthors = Ketscher L, Hannß R, Morales DJ, Basters A, Guerra S, Goldmann T, Hausmann A, Prinz M, Naumann R, Pekosz A, Utermöhlen O, Lenschow DJ, Knobeloch KP | title = Selective inactivation of USP18 isopeptidase activity in vivo enhances ISG15 conjugation and viral resistance | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 112 | issue = 5 | pages = 1577–82 | date = February 2015 | pmid = 25605921 | pmc = 4321242 | doi = 10.1073/pnas.1412881112 | url = https://repositorio.uam.es/bitstream/10486/672352/1/selective_ketscher_PNAS_2015.pdf }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  |vauthors=Yan M, Luo JK, Ritchie KJ, etal |title=Ubp43 regulates BCR-ABL leukemogenesis via the type 1 interferon receptor signaling. |journal=Blood |volume=110 |issue= 1 |pages= 305–12 |year= 2007 |pmid= 17374743 |doi= 10.1182/blood-2006-07-033209 | pmc=1896118 }}
*{{cite journal   |vauthors=Ketscher L, Hannß R, etal |title=Selective inactivation of USP18 isopeptidase activity in vivo enhances ISG15 conjugation and viral resistance. |journal=Proc Natl Acad Sci U S A |volume=112 |issue= 5 |pages= 1577–82 |year= 2015 |pmid= 25605921 |doi= 10.1073/pnas.1412881112 | pmc=4321242 }}
}}
{{refend}}
{{refend}}


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[[Category:Enzymes]]
[[Category:Enzymes]]


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Latest revision as of 12:26, 9 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Ubiquitin specific peptidase 18 (USP18), also known as UBP43, is an isopeptidase that in human is encoded by the USP18 gene.[1] USP18 is a member of the deubiquitinating protease family of enzymes. It is thought to remove ISG15 adducts from a broad range of protein substrates, a process known as deISGylation.[1] In mice, deletion of this enzyme results in increased inflammatory response to type I interferons, suggesting that USP18 may, in part, regulate interferon responsiveness.[2]

References

  1. 1.0 1.1 "Entrez Gene: USP18 ubiquitin specific peptidase 18".
  2. "USP18 ubiquitin specific peptidase 18 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-01-03.

Further reading