Full text data of ISG20
ISG20
(HEM45)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Interferon-stimulated gene 20 kDa protein; 3.1.13.1 (Estrogen-regulated transcript 45 protein; Promyelocytic leukemia nuclear body-associated protein ISG20)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Interferon-stimulated gene 20 kDa protein; 3.1.13.1 (Estrogen-regulated transcript 45 protein; Promyelocytic leukemia nuclear body-associated protein ISG20)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96AZ6
ID ISG20_HUMAN Reviewed; 181 AA.
AC Q96AZ6; O00441; O00586;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-JAN-2005, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Interferon-stimulated gene 20 kDa protein;
DE EC=3.1.13.1;
DE AltName: Full=Estrogen-regulated transcript 45 protein;
DE AltName: Full=Promyelocytic leukemia nuclear body-associated protein ISG20;
GN Name=ISG20; Synonyms=HEM45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION IN PML NB COMPLEX, AND INDUCTION.
RX PubMed=9235947; DOI=10.1074/jbc.272.31.19457;
RA Gongora C., David G., Pintard L., Tissot C., Hua T.D., Dejean A.,
RA Mechti N.;
RT "Molecular cloning of a new interferon-induced PML nuclear bodies-
RT associated protein.";
RL J. Biol. Chem. 272:19457-19463(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9569007; DOI=10.1016/S0960-0760(97)00140-4;
RA Pentecost B.T.;
RT "Expression and estrogen regulation of the HEM45 mRNA in human tumor
RT lines and in the rat uterus.";
RL J. Steroid Biochem. Mol. Biol. 64:25-33(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND ENZYME REGULATION.
RX PubMed=11401564; DOI=10.1021/bi010141t;
RA Nguyen L.H., Espert L., Mechti N., Wilson D.M. III;
RT "The human interferon- and estrogen-regulated ISG20/HEM45 gene product
RT degrades single-stranded RNA and DNA in vitro.";
RL Biochemistry 40:7174-7179(2001).
RN [7]
RP FUNCTION.
RX PubMed=12594219; DOI=10.1074/jbc.M209628200;
RA Espert L., Degols G., Gongora C., Blondel D., Williams B.R.,
RA Silverman R.H., Mechti N.;
RT "ISG20, a new interferon-induced RNase specific for single-stranded
RT RNA, defines an alternative antiviral pathway against RNA genomic
RT viruses.";
RL J. Biol. Chem. 278:16151-16158(2003).
RN [8]
RP FUNCTION.
RX PubMed=16033969; DOI=10.1099/vir.0.81074-0;
RA Espert L., Degols G., Lin Y.L., Vincent T., Benkirane M., Mechti N.;
RT "Interferon-induced exonuclease ISG20 exhibits an antiviral activity
RT against human immunodeficiency virus type 1.";
RL J. Gen. Virol. 86:2221-2229(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SMN COMPLEX AND SNRNAS.
RX PubMed=16514659; DOI=10.1002/jcb.20869;
RA Espert L., Eldin P., Gongora C., Bayard B., Harper F.,
RA Chelbi-Alix M.K., Bertrand E., Degols G., Mechti N.;
RT "The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal
RT (Coiled) bodies and is associated with nuclear SMN protein-containing
RT complexes.";
RL J. Cell. Biochem. 98:1320-1333(2006).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=17445960; DOI=10.1016/j.biochi.2007.03.006;
RA Degols G., Eldin P., Mechti N.;
RT "ISG20, an actor of the innate immune response.";
RL Biochimie 89:831-835(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION IN HCV; HAV AND YFV RESTRICTION, AND SUBCELLULAR LOCATION.
RX PubMed=21036379; DOI=10.1016/j.virol.2010.10.008;
RA Zhou Z., Wang N., Woodson S.E., Dong Q., Wang J., Liang Y.,
RA Rijnbrand R., Wei L., Nichols J.E., Guo J.T., Holbrook M.R.,
RA Lemon S.M., Li K.;
RT "Antiviral activities of ISG20 in positive-strand RNA virus
RT infections.";
RL Virology 409:175-188(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UMP, COFACTOR,
RP AND MANGANESE-BINDING SITES.
RX PubMed=15527770; DOI=10.1016/j.febslet.2004.09.074;
RA Horio T., Murai M., Inoue T., Hamasaki T., Tanaka T., Ohgi T.;
RT "Crystal structure of human ISG20, an interferon-induced antiviral
RT ribonuclease.";
RL FEBS Lett. 577:111-116(2004).
CC -!- FUNCTION: Interferon-induced antiviral exoribonuclease that acts
CC on single-stranded RNA and also has minor activity towards single-
CC stranded DNA. Exhibits antiviral activity against RNA viruses
CC including hepatitis C virus (HCV), hepatitis A virus (HAV) and
CC yellow fever virus (YFV) in an exonuclease-dependent manner. May
CC also play additional roles in the maturation of snRNAs and rRNAs,
CC and in ribosome biogenesis.
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.
CC -!- COFACTOR: Binds 2 manganese ions per subunit.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0;
CC -!- SUBUNIT: Associates with PML and SP100 in the PML NB complex.
CC Associates with survival motor neuron protein (SMN)-containing
CC macromolecular nuclear complexes and U1 and U2 snRNAs and U3
CC snoRNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm.
CC Nucleus, Cajal body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AZ6-2; Sequence=VSP_012429, VSP_012430;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood
CC leukocytes, spleen, thymus, colon and lung. Up regulated by E2 in
CC estrogen receptor-positive breast cancer lines.
CC -!- INDUCTION: Induced by interferons alpha and beta. Weaker induction
CC was seen with interferon gamma. Increased expression was seen at
CC the transcriptional level.
CC -!- SIMILARITY: Belongs to the exonuclease superfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X89773; CAA61915.2; -; mRNA.
DR EMBL; U88964; AAB53416.1; -; mRNA.
DR EMBL; BT006952; AAP35598.1; -; mRNA.
DR EMBL; CR456942; CAG33223.1; -; mRNA.
DR EMBL; BC007922; AAH07922.1; -; mRNA.
DR EMBL; BC016341; AAH16341.1; -; mRNA.
DR RefSeq; NP_002192.2; NM_002201.4.
DR RefSeq; XP_005254956.1; XM_005254899.1.
DR UniGene; Hs.459265; -.
DR PDB; 1WLJ; X-ray; 1.90 A; A=1-181.
DR PDBsum; 1WLJ; -.
DR ProteinModelPortal; Q96AZ6; -.
DR SMR; Q96AZ6; 6-178.
DR MINT; MINT-4714850; -.
DR STRING; 9606.ENSP00000306565; -.
DR PhosphoSite; Q96AZ6; -.
DR DMDM; 57012967; -.
DR PaxDb; Q96AZ6; -.
DR PRIDE; Q96AZ6; -.
DR DNASU; 3669; -.
DR Ensembl; ENST00000306072; ENSP00000306565; ENSG00000172183.
DR Ensembl; ENST00000560741; ENSP00000453638; ENSG00000172183.
DR GeneID; 3669; -.
DR KEGG; hsa:3669; -.
DR UCSC; uc002bmv.1; human.
DR CTD; 3669; -.
DR GeneCards; GC15P089181; -.
DR HGNC; HGNC:6130; ISG20.
DR MIM; 604533; gene.
DR neXtProt; NX_Q96AZ6; -.
DR PharmGKB; PA29930; -.
DR eggNOG; COG0847; -.
DR HOGENOM; HOG000182422; -.
DR HOVERGEN; HBG052149; -.
DR KO; K12579; -.
DR OMA; MLLWREA; -.
DR OrthoDB; EOG7WHHB0; -.
DR PhylomeDB; Q96AZ6; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ISG20; human.
DR EvolutionaryTrace; Q96AZ6; -.
DR GeneWiki; ISG20; -.
DR GenomeRNAi; 3669; -.
DR NextBio; 14359; -.
DR PRO; PR:Q96AZ6; -.
DR ArrayExpress; Q96AZ6; -.
DR Bgee; Q96AZ6; -.
DR CleanEx; HS_ISG20; -.
DR Genevestigator; Q96AZ6; -.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:UniProtKB.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Immunity;
KW Innate immunity; Manganese; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1 181 Interferon-stimulated gene 20 kDa
FT protein.
FT /FTId=PRO_0000084243.
FT METAL 11 11 Manganese 1.
FT METAL 13 13 Manganese 1.
FT METAL 90 90 Manganese 2.
FT METAL 93 93 Manganese 2.
FT METAL 154 154 Manganese 1.
FT VAR_SEQ 77 86 ILQLLKGKLV -> VPFPSSPTAA (in isoform 2).
FT /FTId=VSP_012429.
FT VAR_SEQ 87 181 Missing (in isoform 2).
FT /FTId=VSP_012430.
FT STRAND 7 17
FT TURN 18 21
FT STRAND 22 31
FT STRAND 37 44
FT STRAND 49 51
FT HELIX 54 57
FT HELIX 61 64
FT HELIX 70 81
FT STRAND 84 90
FT HELIX 91 97
FT STRAND 106 109
FT HELIX 110 112
FT HELIX 114 120
FT HELIX 130 137
FT HELIX 151 171
SQ SEQUENCE 181 AA; 20363 MW; 24519CB52CEA5581 CRC64;
MAGSREVVAM DCEMVGLGPH RESGLARCSL VNVHGAVLYD KFIRPEGEIT DYRTRVSGVT
PQHMVGATPF AVARLEILQL LKGKLVVGHD LKHDFQALKE DMSGYTIYDT STDRLLWREA
KLDHCRRVSL RVLSERLLHK SIQNSLLGHS SVEDARATME LYQISQRIRA RRGLPRLAVS
D
//
ID ISG20_HUMAN Reviewed; 181 AA.
AC Q96AZ6; O00441; O00586;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-JAN-2005, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Interferon-stimulated gene 20 kDa protein;
DE EC=3.1.13.1;
DE AltName: Full=Estrogen-regulated transcript 45 protein;
DE AltName: Full=Promyelocytic leukemia nuclear body-associated protein ISG20;
GN Name=ISG20; Synonyms=HEM45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION IN PML NB COMPLEX, AND INDUCTION.
RX PubMed=9235947; DOI=10.1074/jbc.272.31.19457;
RA Gongora C., David G., Pintard L., Tissot C., Hua T.D., Dejean A.,
RA Mechti N.;
RT "Molecular cloning of a new interferon-induced PML nuclear bodies-
RT associated protein.";
RL J. Biol. Chem. 272:19457-19463(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9569007; DOI=10.1016/S0960-0760(97)00140-4;
RA Pentecost B.T.;
RT "Expression and estrogen regulation of the HEM45 mRNA in human tumor
RT lines and in the rat uterus.";
RL J. Steroid Biochem. Mol. Biol. 64:25-33(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND ENZYME REGULATION.
RX PubMed=11401564; DOI=10.1021/bi010141t;
RA Nguyen L.H., Espert L., Mechti N., Wilson D.M. III;
RT "The human interferon- and estrogen-regulated ISG20/HEM45 gene product
RT degrades single-stranded RNA and DNA in vitro.";
RL Biochemistry 40:7174-7179(2001).
RN [7]
RP FUNCTION.
RX PubMed=12594219; DOI=10.1074/jbc.M209628200;
RA Espert L., Degols G., Gongora C., Blondel D., Williams B.R.,
RA Silverman R.H., Mechti N.;
RT "ISG20, a new interferon-induced RNase specific for single-stranded
RT RNA, defines an alternative antiviral pathway against RNA genomic
RT viruses.";
RL J. Biol. Chem. 278:16151-16158(2003).
RN [8]
RP FUNCTION.
RX PubMed=16033969; DOI=10.1099/vir.0.81074-0;
RA Espert L., Degols G., Lin Y.L., Vincent T., Benkirane M., Mechti N.;
RT "Interferon-induced exonuclease ISG20 exhibits an antiviral activity
RT against human immunodeficiency virus type 1.";
RL J. Gen. Virol. 86:2221-2229(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SMN COMPLEX AND SNRNAS.
RX PubMed=16514659; DOI=10.1002/jcb.20869;
RA Espert L., Eldin P., Gongora C., Bayard B., Harper F.,
RA Chelbi-Alix M.K., Bertrand E., Degols G., Mechti N.;
RT "The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal
RT (Coiled) bodies and is associated with nuclear SMN protein-containing
RT complexes.";
RL J. Cell. Biochem. 98:1320-1333(2006).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=17445960; DOI=10.1016/j.biochi.2007.03.006;
RA Degols G., Eldin P., Mechti N.;
RT "ISG20, an actor of the innate immune response.";
RL Biochimie 89:831-835(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION IN HCV; HAV AND YFV RESTRICTION, AND SUBCELLULAR LOCATION.
RX PubMed=21036379; DOI=10.1016/j.virol.2010.10.008;
RA Zhou Z., Wang N., Woodson S.E., Dong Q., Wang J., Liang Y.,
RA Rijnbrand R., Wei L., Nichols J.E., Guo J.T., Holbrook M.R.,
RA Lemon S.M., Li K.;
RT "Antiviral activities of ISG20 in positive-strand RNA virus
RT infections.";
RL Virology 409:175-188(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UMP, COFACTOR,
RP AND MANGANESE-BINDING SITES.
RX PubMed=15527770; DOI=10.1016/j.febslet.2004.09.074;
RA Horio T., Murai M., Inoue T., Hamasaki T., Tanaka T., Ohgi T.;
RT "Crystal structure of human ISG20, an interferon-induced antiviral
RT ribonuclease.";
RL FEBS Lett. 577:111-116(2004).
CC -!- FUNCTION: Interferon-induced antiviral exoribonuclease that acts
CC on single-stranded RNA and also has minor activity towards single-
CC stranded DNA. Exhibits antiviral activity against RNA viruses
CC including hepatitis C virus (HCV), hepatitis A virus (HAV) and
CC yellow fever virus (YFV) in an exonuclease-dependent manner. May
CC also play additional roles in the maturation of snRNAs and rRNAs,
CC and in ribosome biogenesis.
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.
CC -!- COFACTOR: Binds 2 manganese ions per subunit.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0;
CC -!- SUBUNIT: Associates with PML and SP100 in the PML NB complex.
CC Associates with survival motor neuron protein (SMN)-containing
CC macromolecular nuclear complexes and U1 and U2 snRNAs and U3
CC snoRNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm.
CC Nucleus, Cajal body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AZ6-2; Sequence=VSP_012429, VSP_012430;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood
CC leukocytes, spleen, thymus, colon and lung. Up regulated by E2 in
CC estrogen receptor-positive breast cancer lines.
CC -!- INDUCTION: Induced by interferons alpha and beta. Weaker induction
CC was seen with interferon gamma. Increased expression was seen at
CC the transcriptional level.
CC -!- SIMILARITY: Belongs to the exonuclease superfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X89773; CAA61915.2; -; mRNA.
DR EMBL; U88964; AAB53416.1; -; mRNA.
DR EMBL; BT006952; AAP35598.1; -; mRNA.
DR EMBL; CR456942; CAG33223.1; -; mRNA.
DR EMBL; BC007922; AAH07922.1; -; mRNA.
DR EMBL; BC016341; AAH16341.1; -; mRNA.
DR RefSeq; NP_002192.2; NM_002201.4.
DR RefSeq; XP_005254956.1; XM_005254899.1.
DR UniGene; Hs.459265; -.
DR PDB; 1WLJ; X-ray; 1.90 A; A=1-181.
DR PDBsum; 1WLJ; -.
DR ProteinModelPortal; Q96AZ6; -.
DR SMR; Q96AZ6; 6-178.
DR MINT; MINT-4714850; -.
DR STRING; 9606.ENSP00000306565; -.
DR PhosphoSite; Q96AZ6; -.
DR DMDM; 57012967; -.
DR PaxDb; Q96AZ6; -.
DR PRIDE; Q96AZ6; -.
DR DNASU; 3669; -.
DR Ensembl; ENST00000306072; ENSP00000306565; ENSG00000172183.
DR Ensembl; ENST00000560741; ENSP00000453638; ENSG00000172183.
DR GeneID; 3669; -.
DR KEGG; hsa:3669; -.
DR UCSC; uc002bmv.1; human.
DR CTD; 3669; -.
DR GeneCards; GC15P089181; -.
DR HGNC; HGNC:6130; ISG20.
DR MIM; 604533; gene.
DR neXtProt; NX_Q96AZ6; -.
DR PharmGKB; PA29930; -.
DR eggNOG; COG0847; -.
DR HOGENOM; HOG000182422; -.
DR HOVERGEN; HBG052149; -.
DR KO; K12579; -.
DR OMA; MLLWREA; -.
DR OrthoDB; EOG7WHHB0; -.
DR PhylomeDB; Q96AZ6; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ISG20; human.
DR EvolutionaryTrace; Q96AZ6; -.
DR GeneWiki; ISG20; -.
DR GenomeRNAi; 3669; -.
DR NextBio; 14359; -.
DR PRO; PR:Q96AZ6; -.
DR ArrayExpress; Q96AZ6; -.
DR Bgee; Q96AZ6; -.
DR CleanEx; HS_ISG20; -.
DR Genevestigator; Q96AZ6; -.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:UniProtKB.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Immunity;
KW Innate immunity; Manganese; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1 181 Interferon-stimulated gene 20 kDa
FT protein.
FT /FTId=PRO_0000084243.
FT METAL 11 11 Manganese 1.
FT METAL 13 13 Manganese 1.
FT METAL 90 90 Manganese 2.
FT METAL 93 93 Manganese 2.
FT METAL 154 154 Manganese 1.
FT VAR_SEQ 77 86 ILQLLKGKLV -> VPFPSSPTAA (in isoform 2).
FT /FTId=VSP_012429.
FT VAR_SEQ 87 181 Missing (in isoform 2).
FT /FTId=VSP_012430.
FT STRAND 7 17
FT TURN 18 21
FT STRAND 22 31
FT STRAND 37 44
FT STRAND 49 51
FT HELIX 54 57
FT HELIX 61 64
FT HELIX 70 81
FT STRAND 84 90
FT HELIX 91 97
FT STRAND 106 109
FT HELIX 110 112
FT HELIX 114 120
FT HELIX 130 137
FT HELIX 151 171
SQ SEQUENCE 181 AA; 20363 MW; 24519CB52CEA5581 CRC64;
MAGSREVVAM DCEMVGLGPH RESGLARCSL VNVHGAVLYD KFIRPEGEIT DYRTRVSGVT
PQHMVGATPF AVARLEILQL LKGKLVVGHD LKHDFQALKE DMSGYTIYDT STDRLLWREA
KLDHCRRVSL RVLSERLLHK SIQNSLLGHS SVEDARATME LYQISQRIRA RRGLPRLAVS
D
//
MIM
604533
*RECORD*
*FIELD* NO
604533
*FIELD* TI
*604533 INTERFERON-STIMULATED GENE, 20-KD; ISG20
;;HEM45
*FIELD* TX
Binding of interferons (see IFNA, 147660; IFNB, 147570) to their
read morespecific cell surface receptors triggers the rapid nuclear translocation
of a complex formed by association between the various phosphorylated
STAT (see 600555) proteins. This results in the induction of genes that
mediate the biologic functions of IFNs which may be localized in the
cytoplasm, nucleus, or cell surface. The nuclear proteins may localize
within the nucleolus or within the nuclear matrix, specifically to
nuclear bodies (NBs) or PML (promyelocytic leukemia; 102578) NBs.
Proteins of various oncogenic viruses have been found to associate with
and disrupt PML NBs. In addition, PML, SP100 (604585), and NDP52
(604587) are inducible by IFN.
By screening an IFN-treated Daudi cell cDNA library, Gongora et al.
(1997) obtained a cDNA encoding a deduced 179-amino acid, 20-kD, basic
(pI 9.2) interferon-induced protein, termed ISG20, containing 7 lysine
and 19 arginine residues. Sequence analysis of ISG20 also predicted a
coiled-coil structure in the region of amino acids 78-107, suggesting
that the protein could be a component of a multiprotein complex. The
coiled-coil domain is bordered on both sides by potential
phosphorylation sites. ISG20 shares amino acid cluster homologies with
XPMC2H (602930), suggesting an antigrowth function, which is also a
property of IFNs. On the basis of the lysine- and arginine-rich domains
of ISG20, Gongora et al. (1997) suspected nuclear targeting. Using laser
confocal immunofluorescence, they found speckled nuclear staining with
colocalization of ISG20, PML, and SP100. Northern blot analysis of
IFN-treated Daudi cells determined that expression increases in response
to this stimulus and occurs at the transcriptional level. In the absence
of IFN treatment, Northern blot analysis detected ISG20 expression in
peripheral blood leukocytes, thymus, spleen, colon, and lung.
By use of differential display-PCR and mRNA from a human cervical cell
line, Pentecost (1998) identified a cDNA encoding a 181-amino acid
protein, which they termed HEM45. HEM45 aligns with the C-terminal half
of XPMC2H. The authors found that HEM45 mRNA expression increases in
response to estrogen in estrogen receptor-expressing cells in the
presence of cycloheximide.
By radiolabeled probe in situ hybridization, Mattei et al. (1997) mapped
the ISG20 gene to 15q26.
*FIELD* RF
1. Gongora, C.; David, G.; Pintard, L.; Tissot, C.; Hua, T. D.; Dejean,
A.; Mechti, N.: Molecular cloning of a new interferon-induced PML
nuclear body-associated protein. J. Biol. Chem. 272: 19457-19463,
1997.
2. Mattei, M. G.; Tissot, C.; Gongora, C.; Mechti, N.: Assignment
of ISG20 encoding a new interferon-induced PML nuclear body-associated
protein, to chromosome 15q26 by in situ hybridization. Cytogenet.
Cell Genet. 79: 286-287, 1997.
3. Pentecost, B. T.: Expression and estrogen regulation of the HEM45
mRNA in human tumor lines and in the rat uterus. J. Steroid Biochem.
Molec. Biol. 64: 25-33, 1998.
*FIELD* CD
Paul J. Converse: 2/10/2000
*FIELD* ED
carol: 02/22/2000
carol: 2/10/2000
*RECORD*
*FIELD* NO
604533
*FIELD* TI
*604533 INTERFERON-STIMULATED GENE, 20-KD; ISG20
;;HEM45
*FIELD* TX
Binding of interferons (see IFNA, 147660; IFNB, 147570) to their
read morespecific cell surface receptors triggers the rapid nuclear translocation
of a complex formed by association between the various phosphorylated
STAT (see 600555) proteins. This results in the induction of genes that
mediate the biologic functions of IFNs which may be localized in the
cytoplasm, nucleus, or cell surface. The nuclear proteins may localize
within the nucleolus or within the nuclear matrix, specifically to
nuclear bodies (NBs) or PML (promyelocytic leukemia; 102578) NBs.
Proteins of various oncogenic viruses have been found to associate with
and disrupt PML NBs. In addition, PML, SP100 (604585), and NDP52
(604587) are inducible by IFN.
By screening an IFN-treated Daudi cell cDNA library, Gongora et al.
(1997) obtained a cDNA encoding a deduced 179-amino acid, 20-kD, basic
(pI 9.2) interferon-induced protein, termed ISG20, containing 7 lysine
and 19 arginine residues. Sequence analysis of ISG20 also predicted a
coiled-coil structure in the region of amino acids 78-107, suggesting
that the protein could be a component of a multiprotein complex. The
coiled-coil domain is bordered on both sides by potential
phosphorylation sites. ISG20 shares amino acid cluster homologies with
XPMC2H (602930), suggesting an antigrowth function, which is also a
property of IFNs. On the basis of the lysine- and arginine-rich domains
of ISG20, Gongora et al. (1997) suspected nuclear targeting. Using laser
confocal immunofluorescence, they found speckled nuclear staining with
colocalization of ISG20, PML, and SP100. Northern blot analysis of
IFN-treated Daudi cells determined that expression increases in response
to this stimulus and occurs at the transcriptional level. In the absence
of IFN treatment, Northern blot analysis detected ISG20 expression in
peripheral blood leukocytes, thymus, spleen, colon, and lung.
By use of differential display-PCR and mRNA from a human cervical cell
line, Pentecost (1998) identified a cDNA encoding a 181-amino acid
protein, which they termed HEM45. HEM45 aligns with the C-terminal half
of XPMC2H. The authors found that HEM45 mRNA expression increases in
response to estrogen in estrogen receptor-expressing cells in the
presence of cycloheximide.
By radiolabeled probe in situ hybridization, Mattei et al. (1997) mapped
the ISG20 gene to 15q26.
*FIELD* RF
1. Gongora, C.; David, G.; Pintard, L.; Tissot, C.; Hua, T. D.; Dejean,
A.; Mechti, N.: Molecular cloning of a new interferon-induced PML
nuclear body-associated protein. J. Biol. Chem. 272: 19457-19463,
1997.
2. Mattei, M. G.; Tissot, C.; Gongora, C.; Mechti, N.: Assignment
of ISG20 encoding a new interferon-induced PML nuclear body-associated
protein, to chromosome 15q26 by in situ hybridization. Cytogenet.
Cell Genet. 79: 286-287, 1997.
3. Pentecost, B. T.: Expression and estrogen regulation of the HEM45
mRNA in human tumor lines and in the rat uterus. J. Steroid Biochem.
Molec. Biol. 64: 25-33, 1998.
*FIELD* CD
Paul J. Converse: 2/10/2000
*FIELD* ED
carol: 02/22/2000
carol: 2/10/2000