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Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (hUCRP)

 ISG15_HUMAN             Reviewed;         165 AA.
P05161; Q5SVA4; Q7Z2G2; Q96GF0;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
11-DEC-2019, entry version 216.
RecName: Full=Ubiquitin-like protein ISG15;
AltName: Full=Interferon-induced 15 kDa protein;
AltName: Full=Interferon-induced 17 kDa protein;
Short=IP17;
AltName: Full=Ubiquitin cross-reactive protein;
Short=hUCRP;
Flags: Precursor;
Name=ISG15; Synonyms=G1P2, UCRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3087979;
Blomstrom D.C., Fahey D., Kutny R., Korant B.D., Knight E. Jr.;
"Molecular characterization of the interferon-induced 15-kDa protein.
Molecular cloning and nucleotide and amino acid sequence.";
J. Biol. Chem. 261:8811-8816(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3476954; DOI=10.1073/pnas.84.18.6394;
Reich N., Evans B., Levy D., Fahey D., Knight E. Jr., Darnell J.E. Jr.;
"Interferon-induced transcription of a gene encoding a 15-kDa protein
depends on an upstream enhancer element.";
Proc. Natl. Acad. Sci. U.S.A. 84:6394-6398(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEOLYTIC PROCESSING.
PubMed=3350799;
Knight E. Jr., Fahey D., Cordova B., Hillman M. Jr., Kutny R., Reich N.,
Blomstrom D.C.;
"A 15-kDa interferon-induced protein is derived by COOH-terminal processing
of a 17-kDa precursor.";
J. Biol. Chem. 263:4520-4522(1988).
[4]
ERRATUM.
Knight E. Jr., Fahey D., Cordova B., Hillman M. Jr., Kutny R., Reich N.,
Blomstrom D.C.;
J. Biol. Chem. 263:10040-10040(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-83.
TISSUE=Testis;
Kamitani T., Fukuda-Kamitani T.;
"Conjugation by ubiquitin-like proteins.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-83.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-83.
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-38 AND 151-165, AND PROTEOLYTIC PROCESSING.
PubMed=2477469; DOI=10.1089/jir.1989.9.493;
Feltham N., Hillman M. Jr., Cordova B., Fahey D., Larsen B.,
Blomstrom D.C., Knight E. Jr.;
"A 15-kD interferon-induced protein and its 17-kD precursor: expression in
Escherichia coli, purification, and characterization.";
J. Interferon Res. 9:493-507(1989).
[11]
SIMILARITY TO UBIQUITIN.
PubMed=2440890;
Haas A.L., Ahrens P., Bright P.M., Ankel H.;
"Interferon induces a 15-kilodalton protein exhibiting marked homology to
ubiquitin.";
J. Biol. Chem. 262:11315-11323(1987).
[12]
FUNCTION.
PubMed=1373138;
Loeb K.R., Haas A.L.;
"The interferon-inducible 15-kDa ubiquitin homolog conjugates to
intracellular proteins.";
J. Biol. Chem. 267:7806-7813(1992).
[13]
FUNCTION.
PubMed=7526157; DOI=10.1128/mcb.14.12.8408;
Loeb K.R., Haas A.L.;
"Conjugates of ubiquitin cross-reactive protein distribute in a
cytoskeletal pattern.";
Mol. Cell. Biol. 14:8408-8419(1994).
[14]
FUNCTION.
PubMed=8550581; DOI=10.1074/jbc.271.1.324;
Narasimhan J., Potter J.L., Haas A.L.;
"Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct
from that of ubiquitin.";
J. Biol. Chem. 271:324-330(1996).
[15]
FUNCTION.
PubMed=2005397;
Knight E. Jr., Cordova B.;
"IFN-induced 15-kDa protein is released from human lymphocytes and
monocytes.";
J. Immunol. 146:2280-2284(1991).
[16]
TISSUE SPECIFICITY.
PubMed=7490683; DOI=10.1002/path.1711770210;
Lowe J., McDermott H., Loeb K., Landon M., Haas A.L., Mayer R.J.;
"Immunohistochemical localization of ubiquitin cross-reactive protein in
human tissues.";
J. Pathol. 177:163-169(1995).
[17]
INTERACTION WITH UBE1L AND INFLUENZA B NS1.
PubMed=11157743; DOI=10.1093/emboj/20.3.362;
Yuan W., Krug R.M.;
"Influenza B virus NS1 protein inhibits conjugation of the interferon
(IFN)-induced ubiquitin-like ISG15 protein.";
EMBO J. 20:362-371(2001).
[18]
CHARACTERIZATION.
PubMed=11788588; DOI=10.1074/jbc.m109078200;
Malakhov M.P., Malakhova O.A., Kim K.I., Ritchie K.J., Zhang D.-E.;
"UBP43 (USP18) specifically removes ISG15 from conjugated proteins.";
J. Biol. Chem. 277:9976-9981(2002).
[19]
INTERACTION WITH UBE2E2.
PubMed=15131269; DOI=10.1073/pnas.0402528101;
Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A.,
Huibregtse J.M., Krug R.M.;
"The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-
alpha/beta-induced ubiquitin-like protein.";
Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004).
[20]
FUNCTION IN UBE2N ISGYLATION.
PubMed=16112642; DOI=10.1016/j.bbrc.2005.08.034;
Takeuchi T., Yokosawa H.;
"ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating
activity.";
Biochem. Biophys. Res. Commun. 336:9-13(2005).
[21]
FUNCTION IN UBE2E1 AND UBE2L6 ISGYLATION.
PubMed=16428300; DOI=10.1093/jb/mvi172;
Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.;
"Link between the ubiquitin conjugation system and the ISG15 conjugation
system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme.";
J. Biochem. 138:711-719(2005).
[22]
FUNCTION IN IFIT1; DDX58 AND MX1 ISGYLATION.
PubMed=16009940; DOI=10.1073/pnas.0504754102;
Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.;
"Human ISG15 conjugation targets both IFN-induced and constitutively
expressed proteins functioning in diverse cellular pathways.";
Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005).
[23]
FUNCTION IN PPM1B ISGYLATION.
PubMed=16872604; DOI=10.1016/j.febslet.2006.07.032;
Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.;
"Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation.";
FEBS Lett. 580:4521-4526(2006).
[24]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=16434471; DOI=10.1073/pnas.0510518103;
Okumura A., Lu G., Pitha-Rowe I., Pitha P.M.;
"Innate antiviral response targets HIV-1 release by the induction of
ubiquitin-like protein ISG15.";
Proc. Natl. Acad. Sci. U.S.A. 103:1440-1445(2006).
[25]
DOMAINS UBIQUITIN-LIKE 1 AND 2.
PubMed=18356159; DOI=10.1074/jbc.m800162200;
Chang Y.G., Yan X.Z., Xie Y.Y., Gao X.C., Song A.X., Zhang D.E., Hu H.Y.;
"Different roles for two ubiquitin-like domains of ISG15 in protein
modification.";
J. Biol. Chem. 283:13370-13377(2008).
[26]
S-NITROSYLATION AT CYS-78.
PubMed=18606809; DOI=10.1074/jbc.m803795200;
Okumura F., Lenschow D.J., Zhang D.E.;
"Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization
of ISG15 and contributes to effective ISGylation.";
J. Biol. Chem. 283:24484-24488(2008).
[27]
FUNCTION IN EBOLA VIRUS RESTRICTION, AND INTERACTION WITH NEDD4.
PubMed=18305167; DOI=10.1073/pnas.0710629105;
Okumura A., Pitha P.M., Harty R.N.;
"ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by
blocking Nedd4 ligase activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:3974-3979(2008).
[28]
FUNCTION IN FLNB ISGYLATION.
PubMed=19270716; DOI=10.1038/embor.2009.23;
Jeon Y.J., Choi J.S., Lee J.Y., Yu K.R., Kim S.M., Ka S.H., Oh K.H.,
Kim K.I., Zhang D.E., Bang O.S., Chung C.H.;
"ISG15 modification of filamin B negatively regulates the type I
interferon-induced JNK signalling pathway.";
EMBO Rep. 10:374-380(2009).
[29]
REVIEW.
PubMed=19680460; DOI=10.1159/000226245;
Harty R.N., Pitha P.M., Okumura A.;
"Antiviral activity of innate immune protein ISG15.";
J. Innate Immun. 1:397-404(2009).
[30]
FUNCTION IN INFLUENZA A VIRUS RESTRICTION.
PubMed=19357168; DOI=10.1128/jvi.01667-08;
Hsiang T.Y., Zhao C., Krug R.M.;
"Interferon-induced ISG15 conjugation inhibits influenza A virus gene
expression and replication in human cells.";
J. Virol. 83:5971-5977(2009).
[31]
REVIEW.
PubMed=20153823; DOI=10.1016/j.bbadis.2010.02.006;
Jeon Y.J., Yoo H.M., Chung C.H.;
"ISG15 and immune diseases.";
Biochim. Biophys. Acta 1802:485-496(2010).
[32]
REVIEW.
PubMed=20946978; DOI=10.1016/j.cell.2010.09.033;
Skaug B., Chen Z.J.;
"Emerging role of ISG15 in antiviral immunity.";
Cell 143:187-190(2010).
[33]
FUNCTION.
PubMed=20639253; DOI=10.1136/gut.2009.195545;
Broering R., Zhang X., Kottilil S., Trippler M., Jiang M., Lu M.,
Gerken G., Schlaak J.F.;
"The interferon stimulated gene 15 functions as a proviral factor for the
hepatitis C virus and as a regulator of the IFN response.";
Gut 59:1111-1119(2010).
[34]
FUNCTION IN IRF3 ISGYLATION.
PubMed=20308324; DOI=10.1128/mcb.01466-09;
Shi H.X., Yang K., Liu X., Liu X.Y., Wei B., Shan Y.F., Zhu L.H., Wang C.;
"Positive regulation of interferon regulatory factor 3 activation by Herc5
via ISG15 modification.";
Mol. Cell. Biol. 30:2424-2436(2010).
[35]
FUNCTION IN INFLUENZA A VIRUS NS1 ISGYLATION.
PubMed=20133869; DOI=10.1073/pnas.0909144107;
Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.;
"ISG15 conjugation system targets the viral NS1 protein in influenza A
virus-infected cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010).
[36]
REVIEW.
PubMed=21994614; DOI=10.3390/v2102154;
Lenschow D.J.;
"Antiviral properties of ISG15.";
Viruses 2:2154-2168(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
REVIEW.
PubMed=21190487; DOI=10.1089/jir.2010.0110;
Zhang D., Zhang D.E.;
"Interferon-stimulated gene 15 and the protein ISGylation system.";
J. Interferon Cytokine Res. 31:119-130(2011).
[39]
FUNCTION IN CHMP5; CHMP2A; CHMP4B AND CHMP6 ISGYLATION.
PubMed=21543490; DOI=10.1128/jvi.02610-10;
Kuang Z., Seo E.J., Leis J.;
"Mechanism of inhibition of retrovirus release from cells by interferon-
induced gene ISG15.";
J. Virol. 85:7153-7161(2011).
[40]
REVIEW.
PubMed=22666250; DOI=10.1155/2012/532723;
Seo E.J., Leis J.;
"Budding of enveloped viruses: interferon-induced ISG15-antivirus
mechanisms targeting the release process.";
Adv. Virol. 2012:532723-532723(2012).
[41]
REVIEW.
PubMed=22906767; DOI=10.1016/j.cytogfr.2012.07.003;
Sgorbissa A., Brancolini C.;
"IFNs, ISGylation and cancer: Cui prodest?";
Cytokine Growth Factor Rev. 23:307-314(2012).
[42]
FUNCTION IN UBE2N AND UBA7 ISGYLATION, AND DISULFIDE BOND.
PubMed=22693631; DOI=10.1371/journal.pone.0038294;
Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.;
"Covalent protein modification with ISG15 via a conserved cysteine in the
hinge region.";
PLoS ONE 7:E38294-E38294(2012).
[43]
FUNCTION, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
INVOLVEMENT IN IMD38.
PubMed=22859821; DOI=10.1126/science.1224026;
Bogunovic D., Byun M., Durfee L.A., Abhyankar A., Sanal O., Mansouri D.,
Salem S., Radovanovic I., Grant A.V., Adimi P., Mansouri N., Okada S.,
Bryant V.L., Kong X.F., Kreins A., Velez M.M., Boisson B., Khalilzadeh S.,
Ozcelik U., Darazam I.A., Schoggins J.W., Rice C.M., Al-Muhsen S., Behr M.,
Vogt G., Puel A., Bustamante J., Gros P., Huibregtse J.M., Abel L.,
Boisson-Dupuis S., Casanova J.L.;
"Mycobacterial disease and impaired IFN-gamma immunity in humans with
inherited ISG15 deficiency.";
Science 337:1684-1688(2012).
[44]
REVIEW.
PubMed=22964713; DOI=10.1038/cr.2012.133;
Fan J.B., Zhang D.E.;
"ISG15 regulates IFN-? immunity in human mycobacterial disease.";
Cell Res. 23:173-175(2013).
[45]
REVIEW.
PubMed=23579383; DOI=10.1038/emm.2013.36;
Bogunovic D., Boisson-Dupuis S., Casanova J.L.;
"ISG15: leading a double life as a secreted molecule.";
Exp. Mol. Med. 45:E18-E18(2013).
[46]
FUNCTION IN EIF2AK2 ISGYLATION.
PubMed=23229543; DOI=10.1074/jbc.m112.401851;
Okumura F., Okumura A.J., Uematsu K., Hatakeyama S., Zhang D.E., Kamura T.;
"Activation of double-stranded RNA-activated protein kinase (PKR) by
interferon-stimulated gene 15 (ISG15) modification down-regulates protein
translation.";
J. Biol. Chem. 288:2839-2847(2013).
[47]
REVIEW.
PubMed=23414970; DOI=10.1016/j.tim.2013.01.005;
Zhao C., Collins M.N., Hsiang T.Y., Krug R.M.;
"Interferon-induced ISG15 pathway: an ongoing virus-host battle.";
Trends Microbiol. 21:181-186(2013).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[49]
INTERACTION WITH VACCINIA VIRUS PROTEIN E3.
PubMed=24257616; DOI=10.1128/jvi.03293-13;
Eduardo-Correia B., Martinez-Romero C., Garcia-Sastre A., Guerra S.;
"ISG15 is counteracted by vaccinia virus E3 protein and controls the
proinflammatory response against viral infection.";
J. Virol. 88:2312-2318(2014).
[50]
FUNCTION, AND MUTAGENESIS OF ARG-44; SER-83; TYR-96; ARG-99; THR-101;
GLN-102 AND THR-103.
PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
"Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
receptor.";
Mol. Cell 68:581-590(2017).
[51]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-155 OF MUTANT SER-78.
PubMed=15917233; DOI=10.1074/jbc.m502814200;
Narasimhan J., Wang M., Fu Z., Klein J.M., Haas A.L., Kim J.J.;
"Crystal structure of the interferon-induced ubiquitin-like protein
ISG15.";
J. Biol. Chem. 280:27356-27365(2005).
[52]
STRUCTURE BY NMR OF 79-157.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of the C-terminal domain of the interferon alpha-
inducible ISG15 protein from Homo sapiens.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Ubiquitin-like protein which plays a key role in the innate
immune response to viral infection either via its conjugation to a
target protein (ISGylation) or via its action as a free or unconjugated
protein. ISGylation involves a cascade of enzymatic reactions involving
E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a
lysine residue in the target protein. Its target proteins include
IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6.
Can also isgylate: EIF2AK2/PKR which results in its activation,
DDX58/RIG-I which inhibits its function in antiviral signaling
response, EIF4E2 which enhances its cap structure-binding activity and
translation-inhibition activity, UBE2N and UBE2E1 which negatively
regulates their activity, IRF3 which inhibits its ubiquitination and
degradation and FLNB which prevents its ability to interact with the
upstream activators of the JNK cascade thereby inhibiting IFNA-induced
JNK signaling. Exhibits antiviral activity towards both DNA and RNA
viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1
and ebola virus via disruption of viral budding. Inhibits the
ubiquitination of HIV-1 Gag and host TSG101 and disrupts their
interaction, thereby preventing assembly and release of virions from
infected cells. Inhibits Ebola virus budding mediated by the VP40
protein by disrupting ubiquitin ligase activity of NEDD4 and its
ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein
which causes a loss of function of the protein and the inhibition of
virus replication. The secreted form of ISG15 can: induce natural
killer cell proliferation, act as a chemotactic factor for neutrophils
and act as a IFN-gamma-inducing cytokine playing an essential role in
antimycobacterial immunity. The secreted form acts through the integrin
ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine
kinases including LYN, HCK and FGR which leads to secretion of IFNG and
IL10; the interaction is mediated by ITGAL (PubMed:29100055).
{ECO:0000269|PubMed:1373138, ECO:0000269|PubMed:16009940,
ECO:0000269|PubMed:16112642, ECO:0000269|PubMed:16428300,
ECO:0000269|PubMed:16434471, ECO:0000269|PubMed:16872604,
ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:19270716,
ECO:0000269|PubMed:19357168, ECO:0000269|PubMed:2005397,
ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324,
ECO:0000269|PubMed:20639253, ECO:0000269|PubMed:21543490,
ECO:0000269|PubMed:22693631, ECO:0000269|PubMed:22859821,
ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:29100055,
ECO:0000269|PubMed:7526157, ECO:0000269|PubMed:8550581}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:2440890). Interacts with,
and is conjugated to its targets by UBE1L (E1 enzyme) and UBE2E2 (E2
enzyme) (PubMed:11157743, PubMed:15131269). Interacts with NEDD4
(PubMed:18305167). {ECO:0000269|PubMed:11157743,
ECO:0000269|PubMed:15131269, ECO:0000269|PubMed:18305167,
ECO:0000269|PubMed:2440890}.
-!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
E3. {ECO:0000269|PubMed:24257616}.
-!- SUBUNIT: (Microbial infection) Interaction with influenza B NS1 protein
inhibits its conjugation. {ECO:0000269|PubMed:11157743}.
-!- INTERACTION:
O75369:FLNB; NbExp=4; IntAct=EBI-746466, EBI-352089;
Q6TQR6:L (xeno); NbExp=5; IntAct=EBI-746466, EBI-4403908;
P03495:NS (xeno); NbExp=4; IntAct=EBI-746466, EBI-2548993;
P03502:NS (xeno); NbExp=4; IntAct=EBI-746466, EBI-15938710;
O75688:PPM1B; NbExp=2; IntAct=EBI-746466, EBI-1047039;
P41226:UBA7; NbExp=11; IntAct=EBI-746466, EBI-751921;
Q9UMW8:USP18; NbExp=9; IntAct=EBI-746466, EBI-356206;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22859821}. Secreted
{ECO:0000269|PubMed:22859821}. Note=Exists in three distinct states:
free within the cell, released into the extracellular space, or
conjugated to target proteins.
-!- TISSUE SPECIFICITY: Detected in lymphoid cells, striated and smooth
muscle, several epithelia and neurons. Expressed in neutrophils,
monocytes and lymphocytes. Enhanced expression seen in pancreatic
adenocarcinoma, endometrial cancer, and bladder cancer, as compared to
non-cancerous tissue. In bladder cancer, the increase in expression
exhibits a striking positive correlation with more advanced stages of
the disease. {ECO:0000269|PubMed:22859821, ECO:0000269|PubMed:7490683}.
-!- INDUCTION: Strongly induced upon exposure to type I interferons,
viruses, LPS, and other stresses, including certain genotoxic stresses.
{ECO:0000269|PubMed:22859821}.
-!- DOMAIN: Both the Ubiquitin-like 1 and Ubiquitin-like 2 domains are
required for its efficient conjugation to cellular proteins. The two
domains play different roles in the ISGylation pathway: Ubiquitin-like
2 domain is necessary for the first two steps allowing the linking of
ISG15 to the E1 and E2 enzymes while Ubiquitin-like 1 domain is
essential for the final, E3-mediated transfer of ISG15, from the E2 to
the Lys of the target protein (PubMed:18356159).
{ECO:0000269|PubMed:18356159}.
-!- PTM: S-nitrosylation decreases its dimerization, thereby increasing the
availability as well as the solubility of monomeric ISG15 for its
conjugation to cellular proteins. {ECO:0000269|PubMed:18606809}.
-!- PTM: Induced as an inactive, precursor protein that is cleaved by
specific proteases to expose the C-terminal diglycine (LRLRGG) motif.
This motif is essential not only for its conjugation to substrates but
also for its recognition by the relevant processing proteases.
{ECO:0000269|PubMed:2477469, ECO:0000269|PubMed:3350799}.
-!- DISEASE: Immunodeficiency 38, with basal ganglia calcification (IMD38)
[MIM:616126]: A primary immunodeficiency predisposing individuals to
severe clinical disease upon infection with weakly virulent
mycobacteria, including Mycobacterium bovis Bacille Calmette-Guerin
(BCG) vaccines. Patients are also susceptible to Salmonella and
Mycobacterium tubercolosis infections. Affected individuals have
intracranial calcification. {ECO:0000269|PubMed:22859821}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; M13755; AAA36038.1; -; mRNA.
EMBL; M21786; AAA36128.1; -; Genomic_DNA.
EMBL; AY168648; AAN86983.1; -; mRNA.
EMBL; BT007297; AAP35961.1; -; mRNA.
EMBL; AL645608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471183; EAW56295.1; -; Genomic_DNA.
EMBL; BC009507; AAH09507.1; -; mRNA.
CCDS; CCDS6.1; -.
PIR; A28304; A28138.
RefSeq; NP_005092.1; NM_005101.3.
PDB; 1Z2M; X-ray; 2.50 A; A=1-155.
PDB; 2HJ8; NMR; -; A=79-157.
PDB; 3PHX; X-ray; 1.60 A; B=79-156.
PDB; 3PSE; X-ray; 2.30 A; B=1-156.
PDB; 3R66; X-ray; 2.30 A; C/D=1-157.
PDB; 3RT3; X-ray; 2.01 A; B=1-158.
PDB; 3SDL; X-ray; 2.29 A; C/D=1-157.
PDB; 5TL6; X-ray; 2.62 A; A/C=80-157.
PDB; 5W8T; X-ray; 2.76 A; B/D=80-156.
PDB; 5W8U; X-ray; 2.41 A; B/D=80-156.
PDB; 6BI8; X-ray; 3.00 A; C/D=1-156.
PDB; 6FFA; X-ray; 1.50 A; B=79-155.
PDBsum; 1Z2M; -.
PDBsum; 2HJ8; -.
PDBsum; 3PHX; -.
PDBsum; 3PSE; -.
PDBsum; 3R66; -.
PDBsum; 3RT3; -.
PDBsum; 3SDL; -.
PDBsum; 5TL6; -.
PDBsum; 5W8T; -.
PDBsum; 5W8U; -.
PDBsum; 6BI8; -.
PDBsum; 6FFA; -.
SMR; P05161; -.
BioGrid; 114995; 190.
DIP; DIP-29814N; -.
IntAct; P05161; 52.
MINT; P05161; -.
STRING; 9606.ENSP00000368699; -.
iPTMnet; P05161; -.
PhosphoSitePlus; P05161; -.
BioMuta; ISG15; -.
DMDM; 52001470; -.
EPD; P05161; -.
jPOST; P05161; -.
MassIVE; P05161; -.
MaxQB; P05161; -.
PaxDb; P05161; -.
PeptideAtlas; P05161; -.
PRIDE; P05161; -.
ProteomicsDB; 51809; -.
TopDownProteomics; P05161; -.
DNASU; 9636; -.
Ensembl; ENST00000649529; ENSP00000496832; ENSG00000187608.
GeneID; 9636; -.
KEGG; hsa:9636; -.
UCSC; uc001acj.5; human.
CTD; 9636; -.
DisGeNET; 9636; -.
EuPathDB; HostDB:ENSG00000187608.8; -.
GeneCards; ISG15; -.
HGNC; HGNC:4053; ISG15.
HPA; HPA004627; -.
MalaCards; ISG15; -.
MIM; 147571; gene.
MIM; 616126; phenotype.
neXtProt; NX_P05161; -.
OpenTargets; ENSG00000187608; -.
Orphanet; 319563; Mendelian susceptibility to mycobacterial diseases due to complete ISG15 deficiency.
PharmGKB; PA28465; -.
eggNOG; KOG0001; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00940000162007; -.
HOGENOM; HOG000233942; -.
InParanoid; P05161; -.
KO; K12159; -.
OMA; QCTVFMN; -.
OrthoDB; 1367357at2759; -.
PhylomeDB; P05161; -.
TreeFam; TF338379; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
ChiTaRS; ISG15; human.
EvolutionaryTrace; P05161; -.
GeneWiki; ISG15; -.
GenomeRNAi; 9636; -.
Pharos; P05161; Tbio.
PRO; PR:P05161; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P05161; protein.
Bgee; ENSG00000187608; Expressed in 228 organ(s), highest expression level in epithelium of bronchus.
ExpressionAtlas; P05161; baseline and differential.
Genevisible; P05161; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0031386; F:protein tag; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0072643; P:interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0072608; P:interleukin-10 secretion; IDA:UniProtKB.
GO; GO:0032020; P:ISG15-protein conjugation; IDA:UniProtKB.
GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:0032649; P:regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0034340; P:response to type I interferon; IDA:UniProtKB.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR000626; Ubiquitin-like_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019956; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 2.
PRINTS; PR00348; UBIQUITIN.
SMART; SM00213; UBQ; 2.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50053; UBIQUITIN_2; 2.
1: Evidence at protein level;
3D-structure; Antiviral defense; Cytoplasm; Direct protein sequencing;
Disulfide bond; Host-virus interaction; Immunity; Innate immunity;
Isopeptide bond; Polymorphism; Reference proteome; Repeat; S-nitrosylation;
Secreted; Ubl conjugation pathway.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:2477469"
CHAIN 2..157
/note="Ubiquitin-like protein ISG15"
/id="PRO_0000035986"
PROPEP 158..165
/note="Removed in mature form"
/id="PRO_0000035987"
DOMAIN 2..78
/note="Ubiquitin-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
DOMAIN 79..157
/note="Ubiquitin-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
REGION 153..157
/note="Involved in the ligation of specific target
proteins"
/evidence="ECO:0000250"
MOTIF 152..157
/note="LRLRGG"
BINDING 153
/note="Activating enzyme"
/evidence="ECO:0000250"
MOD_RES 78
/note="S-nitrosocysteine; alternate"
/evidence="ECO:0000269|PubMed:18606809"
DISULFID 78
/note="Interchain (with C-87 in UBE2N); alternate"
/evidence="ECO:0000269|PubMed:22693631"
CROSSLNK 157
/note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
K-? in acceptor proteins)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
VARIANT 83
/note="S -> N (in dbSNP:rs1921)"
/evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5,
ECO:0000269|Ref.6"
/id="VAR_016181"
MUTAGEN 44
/note="R->A: Does not affect ISG15 signaling, interaction
with ITGAL or activation of SRC family tyrosine kinases."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 83
/note="S->A: Does not affect ISG15 signaling, interaction
with ITGAL or activation of SRC family tyrosine kinases."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 96
/note="Y->L: Reduces ISG15 signaling. Strongly reduces
ISG15 signaling and abolishes interaction with ITGAL and
activation of SRC family tyrosine kinases; when associated
with D-102."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 99
/note="R->A: Strongly reduces ISG15 signaling and abolishes
interaction with ITGAL."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 101
/note="T->A: Strongly reduces ISG15 signaling and abolishes
interaction with ITGAL and activation of SRC family
tyrosine kinases."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 102
/note="Q->D: Reduces ISG15 signaling. Strongly reduces
ISG15 signaling and abolishes interaction with ITGAL and
activation of SRC family tyrosine kinases; when associated
with L-96."
/evidence="ECO:0000269|PubMed:29100055"
MUTAGEN 103
/note="T->A: Strongly reduces ISG15 signaling and abolishes
interaction with ITGAL."
/evidence="ECO:0000269|PubMed:29100055"
CONFLICT 35
/note="K -> N (in Ref. 2; AAA36128)"
/evidence="ECO:0000305"
STRAND 4..9
/evidence="ECO:0000244|PDB:3RT3"
STRAND 10..12
/evidence="ECO:0000244|PDB:6BI8"
STRAND 14..18
/evidence="ECO:0000244|PDB:3RT3"
STRAND 20..22
/evidence="ECO:0000244|PDB:6BI8"
HELIX 25..36
/evidence="ECO:0000244|PDB:3RT3"
HELIX 40..42
/evidence="ECO:0000244|PDB:3RT3"
STRAND 43..48
/evidence="ECO:0000244|PDB:3RT3"
STRAND 56..58
/evidence="ECO:0000244|PDB:3SDL"
HELIX 60..63
/evidence="ECO:0000244|PDB:3RT3"
STRAND 66..68
/evidence="ECO:0000244|PDB:6BI8"
STRAND 70..75
/evidence="ECO:0000244|PDB:3RT3"
STRAND 82..87
/evidence="ECO:0000244|PDB:6FFA"
STRAND 93..98
/evidence="ECO:0000244|PDB:6FFA"
HELIX 104..115
/evidence="ECO:0000244|PDB:6FFA"
HELIX 119..121
/evidence="ECO:0000244|PDB:6FFA"
STRAND 122..126
/evidence="ECO:0000244|PDB:6FFA"
STRAND 129..131
/evidence="ECO:0000244|PDB:5TL6"
HELIX 137..140
/evidence="ECO:0000244|PDB:6FFA"
STRAND 147..152
/evidence="ECO:0000244|PDB:6FFA"
SEQUENCE 165 AA; 17888 MW; B6858A15AB0FFFDE CRC64;
MGWDLTVKML AGNEFQVSLS SSMSVSELKA QITQKIGVHA FQQRLAVHPS GVALQDRVPL
ASQGLGPGST VLLVVDKCDE PLSILVRNNK GRSSTYEVRL TQTVAHLKQQ VSGLEGVQDD
LFWLTFEGKP LEDQLPLGEY GLKPLSTVFM NLRLRGGGTE PGGRS


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WP211: BMP signaling pathway
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Related Genes :
[ISG15 G1P2 UCRP] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (hUCRP)
[Isg15 G1p2 Ucrp] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein)
[ISG15 G1P2 ISG17 UCRP] Ubiquitin-like protein ISG15 (Interferon-stimulated gene product 17) (Ubiquitin cross-reactive protein) (BoUCRP)
[UBE2L6 UBCH8] Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L6) (Retinoic acid-induced gene B protein) (RIG-B) (UbcH8) (Ubiquitin carrier protein L6) (Ubiquitin-protein ligase L6)
[IFIT1 G10P1 IFI56 IFNAI1 ISG56] Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Interferon-induced 56 kDa protein) (IFI-56K) (P56)
[MX1] Interferon-induced GTP-binding protein Mx1 (Interferon-induced protein p78) (IFI-78K) (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) [Cleaved into: Interferon-induced GTP-binding protein Mx1, N-terminally processed]
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[Eif2ak2 Prkr] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2)
[IFI27] Interferon alpha-inducible protein 27, mitochondrial (p27) (Interferon alpha-induced 11.5 kDa protein) (Interferon-stimulated gene 12a protein) (ISG12(a)) (ISG12A)
[IFITM1 CD225 IFI17] Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Interferon-induced protein 17) (Interferon-inducible protein 9-27) (Leu-13 antigen) (CD antigen CD225)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX2] Interferon-induced GTP-binding protein Mx2 (Interferon-regulated resistance GTP-binding protein MxB) (Myxovirus resistance protein 2) (p78-related protein)
[Ifit1 Garg16 Ifi56 Isg56] Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Glucocorticoid-attenuated response gene 16 protein) (GARG-16) (Interferon-induced 56 kDa protein) (IFI-56K) (P56)
[Ifitm3] Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1)
[TXNRD1 GRIM12 KDRF] Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Thioredoxin reductase TR1)
[IFIT2 CIG-42 G10P2 IFI54 ISG54] Interferon-induced protein with tetratricopeptide repeats 2 (IFIT-2) (ISG-54 K) (Interferon-induced 54 kDa protein) (IFI-54K) (P54)
[SQSTM1 ORCA OSIL] Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62)
[UBE2K HIP2 LIG] Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase)
[Mx2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[MAVS IPS1 KIAA1271 VISA] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[MX2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[Mx2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[ADAR ADAR1 DSRAD G1P1 IFI4] Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)

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