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E3 ubiquitin/ISG15 ligase TRIM25 (EC 6.3.2.n3) (Estrogen-responsive finger protein) (RING finger protein 147) (RING-type E3 ubiquitin transferase) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM25) (Tripartite motif-containing protein 25) (Ubiquitin/ISG15-conjugating enzyme TRIM25) (Zinc finger protein 147)

 TRI25_HUMAN             Reviewed;         630 AA.
Q14258;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
18-JUL-2018, entry version 191.
RecName: Full=E3 ubiquitin/ISG15 ligase TRIM25;
EC=6.3.2.n3 {ECO:0000269|PubMed:16352599};
AltName: Full=Estrogen-responsive finger protein;
AltName: Full=RING finger protein 147;
AltName: Full=RING-type E3 ubiquitin transferase;
EC=2.3.2.27 {ECO:0000269|PubMed:17392790};
AltName: Full=RING-type E3 ubiquitin transferase TRIM25 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 25;
AltName: Full=Ubiquitin/ISG15-conjugating enzyme TRIM25;
AltName: Full=Zinc finger protein 147;
Name=TRIM25; Synonyms=EFP, RNF147, ZNF147;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-358.
TISSUE=Placenta;
PubMed=8248217; DOI=10.1073/pnas.90.23.11117;
Inoue S., Orimo A., Hosoi T., Kondo S., Toyoshima H., Kondo T.,
Ikegami A., Ouchi Y., Orimo H., Muramatsu M.;
"Genomic binding-site cloning reveals an estrogen-responsive gene that
encodes a RING finger protein.";
Proc. Natl. Acad. Sci. U.S.A. 90:11117-11121(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-358.
TISSUE=Lymph;
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).
[4]
TISSUE SPECIFICITY.
PubMed=15130519; DOI=10.1016/j.mce.2003.12.008;
Shimada N., Suzuki T., Inoue S., Kato K., Imatani A., Sekine H.,
Ohara S., Shimosegawa T., Sasano H.;
"Systemic distribution of estrogen-responsive finger protein (Efp) in
human tissues.";
Mol. Cell. Endocrinol. 218:147-153(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
INDUCTION, AND FUNCTION.
PubMed=17069755; DOI=10.1016/j.bbrc.2006.10.061;
Nakasato N., Ikeda K., Urano T., Horie-Inoue K., Takeda S., Inoue S.;
"A ubiquitin E3 ligase Efp is up-regulated by interferons and
conjugated with ISG15.";
Biochem. Biophys. Res. Commun. 351:540-546(2006).
[7]
FUNCTION AS A ISG15 E3 LIGASE, CATALYTIC ACTIVITY, AND INDUCTION.
PubMed=16352599; DOI=10.1074/jbc.M510787200;
Zou W., Zhang D.-E.;
"The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP
also functions as an ISG15 E3 ligase.";
J. Biol. Chem. 281:3989-3994(2006).
[8]
ISGYLATION AT LYS-117, MUTAGENESIS OF LYS-21; LYS-65; LYS-112 AND
LYS-117, AND AUTOISGYLATION.
PubMed=17222803; DOI=10.1016/j.bbrc.2006.12.210;
Zou W., Wang J., Zhang D.-E.;
"Negative regulation of ISG15 E3 ligase EFP through its
autoISGylation.";
Biochem. Biophys. Res. Commun. 354:321-327(2007).
[9]
FUNCTION AS AN UBIQUITIN LIGASE, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND INTERACTION WITH DDX58.
PubMed=17392790; DOI=10.1038/nature05732;
Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L.,
Takeuchi O., Akira S., Chen Z., Inoue S., Jung J.U.;
"TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-
mediated antiviral activity.";
Nature 446:916-920(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INTERACTION WITH INFLUENZA VIRUS PROTEIN NS1 (MICROBIAL INFECTION).
PubMed=19454348; DOI=10.1016/j.chom.2009.04.006;
Gack M.U., Albrecht R.A., Urano T., Inn K.-S., Huang I.-C.,
Carnero E., Farzan M., Inoue S., Jung J.U., Garcia-Sastre A.;
"Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade
recognition by the host viral RNA sensor RIG-I.";
Cell Host Microbe 5:439-449(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-273 AND LYS-567, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
FUNCTION, INTERACTION WITH ZFHX3, AND TISSUE SPECIFICITY.
PubMed=22452784; DOI=10.1042/BJ20111890;
Dong X.Y., Fu X., Fan S., Guo P., Su D., Dong J.T.;
"Oestrogen causes ATBF1 protein degradation through the oestrogen-
responsive E3 ubiquitin ligase EFP.";
Biochem. J. 444:581-590(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91 AND SER-100, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, AND 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).
[18]
VARIANT [LARGE SCALE ANALYSIS] LEU-358, AND 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).
-!- FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3
ligase. Involved in innate immune defense against viruses by
mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked
polyubiquitination of the DDX58 N-terminal CARD-like region which
is crucial for triggering the cytosolic signal transduction that
leads to the production of interferons in response to viral
infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter
protein implicated in the regulation of a large spectrum signaling
pathway. Mediates estrogen action in various target organs.
Mediates the ubiquitination and subsequent proteasomal degradation
of ZFHX3 (PubMed:22452784). {ECO:0000269|PubMed:16352599,
ECO:0000269|PubMed:17069755, ECO:0000269|PubMed:17392790,
ECO:0000269|PubMed:22452784}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17392790}.
-!- CATALYTIC ACTIVITY: ATP + [ISG15] + [protein]-lysine = AMP +
diphosphate + [protein]-N-ISGyllysine.
{ECO:0000269|PubMed:16352599}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via SPRY domain) with DDX58 (via CARD domain).
Interacts with ZFHX3. {ECO:0000269|PubMed:17392790,
ECO:0000269|PubMed:22452784}.
-!- SUBUNIT: (Microbial infection) Interacts (via coiled coil) with
influenza A virus NS1 protein; this interaction specifically
inhibits TRIM25 multimerization and TRIM25-mediated DDX58 CARD
ubiquitination, thereby suppressing DDX58 signal transduction.
{ECO:0000269|PubMed:19454348}.
-!- INTERACTION:
F1BA49:- (xeno); NbExp=5; IntAct=EBI-2341129, EBI-9687469;
O95786:DDX58; NbExp=4; IntAct=EBI-2341129, EBI-995350;
P03496:NS (xeno); NbExp=3; IntAct=EBI-2341129, EBI-2547442;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17392790}.
Note=Colocalized with DDX58 at cytoplasmic perinuclear bodies.
-!- TISSUE SPECIFICITY: Expressed in breast tumors (at protein level).
Ubiquitous. {ECO:0000269|PubMed:15130519,
ECO:0000269|PubMed:22452784}.
-!- INDUCTION: By interferons. {ECO:0000269|PubMed:16352599,
ECO:0000269|PubMed:17069755}.
-!- DOMAIN: The RING-type zinc finger is important for ISG15 E3 ligase
activity and autoISGylation. AutoISGylation negatively regulates
ISG15 E3 ligase activity.
-!- DOMAIN: The C-terminal B30.2/SPRY domain interacts with the first
N-terminal CARD domain of DDX58.
-!- PTM: Auto-ISGylated. {ECO:0000269|PubMed:17222803}.
-!- WEB RESOURCE: Name=Wikipedia; Note=TRIM25 entry;
URL="https://en.wikipedia.org/wiki/TRIM25";
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EMBL; D21205; BAA04747.1; -; mRNA.
EMBL; AC015912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016924; AAH16924.1; -; mRNA.
EMBL; BC042541; AAH42541.1; -; mRNA.
CCDS; CCDS11591.1; -.
PIR; A49656; A49656.
RefSeq; NP_005073.2; NM_005082.4.
UniGene; Hs.528952; -.
PDB; 4CFG; X-ray; 2.80 A; A/B=1-630.
PDB; 4LTB; X-ray; 2.59 A; A/B=189-379.
PDB; 5EYA; X-ray; 2.40 A; F/G=1-83.
PDB; 5FER; X-ray; 2.34 A; A/D=1-82.
PDB; 5NT1; X-ray; 2.82 A; A/E/I=190-379.
PDB; 5NT2; X-ray; 4.26 A; A/I/N/V=190-379.
PDB; 6FLM; X-ray; 2.01 A; A/B/C=435-630.
PDB; 6FLN; X-ray; 3.60 A; A/B/E=189-630.
PDBsum; 4CFG; -.
PDBsum; 4LTB; -.
PDBsum; 5EYA; -.
PDBsum; 5FER; -.
PDBsum; 5NT1; -.
PDBsum; 5NT2; -.
PDBsum; 6FLM; -.
PDBsum; 6FLN; -.
ProteinModelPortal; Q14258; -.
SMR; Q14258; -.
BioGrid; 113500; 2388.
CORUM; Q14258; -.
IntAct; Q14258; 31.
MINT; Q14258; -.
STRING; 9606.ENSP00000323889; -.
iPTMnet; Q14258; -.
PhosphoSitePlus; Q14258; -.
SwissPalm; Q14258; -.
BioMuta; TRIM25; -.
DMDM; 313104033; -.
EPD; Q14258; -.
MaxQB; Q14258; -.
PaxDb; Q14258; -.
PeptideAtlas; Q14258; -.
PRIDE; Q14258; -.
ProteomicsDB; 59953; -.
Ensembl; ENST00000316881; ENSP00000323889; ENSG00000121060.
Ensembl; ENST00000537230; ENSP00000445961; ENSG00000121060.
GeneID; 7706; -.
KEGG; hsa:7706; -.
UCSC; uc002iut.4; human.
CTD; 7706; -.
DisGeNET; 7706; -.
EuPathDB; HostDB:ENSG00000121060.14; -.
GeneCards; TRIM25; -.
HGNC; HGNC:12932; TRIM25.
HPA; HPA005909; -.
MIM; 600453; gene.
neXtProt; NX_Q14258; -.
OpenTargets; ENSG00000121060; -.
PharmGKB; PA37519; -.
eggNOG; ENOG410ITFP; Eukaryota.
eggNOG; ENOG410XQS1; LUCA.
GeneTree; ENSGT00760000118995; -.
HOVERGEN; HBG101063; -.
InParanoid; Q14258; -.
KO; K10652; -.
OMA; SPAFQDH; -.
OrthoDB; EOG091G05F6; -.
PhylomeDB; Q14258; -.
TreeFam; TF351086; -.
BRENDA; 2.3.2.B10; 2681.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
UniPathway; UPA00143; -.
ChiTaRS; TRIM25; human.
GeneWiki; TRIM25; -.
GenomeRNAi; 7706; -.
PRO; PR:Q14258; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000121060; -.
CleanEx; HS_TRIM25; -.
ExpressionAtlas; Q14258; baseline and differential.
Genevisible; Q14258; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
GO; GO:1902187; P:negative regulation of viral release from host cell; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IMP:ParkinsonsUK-UCL.
GO; GO:0046596; P:regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:1902186; P:regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00589; PRY; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antiviral defense; Coiled coil;
Complete proteome; Cytoplasm; Host-virus interaction; Immunity;
Innate immunity; Isopeptide bond; Ligase; Metal-binding;
Phosphoprotein; Polymorphism; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 630 E3 ubiquitin/ISG15 ligase TRIM25.
/FTId=PRO_0000056233.
DOMAIN 439 630 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 13 54 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 180 450 Interaction with influenza A virus NS1.
COILED 217 307 {ECO:0000255}.
MOD_RES 91 91 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 278 278 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 567 567 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000269|PubMed:17222803}.
VARIANT 89 89 V -> G (in dbSNP:rs7212260).
/FTId=VAR_024614.
VARIANT 358 358 P -> L (in dbSNP:rs205498).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8248217}.
/FTId=VAR_024615.
MUTAGEN 21 21 K->R: No effect on ISGylation.
{ECO:0000269|PubMed:17222803}.
MUTAGEN 65 65 K->R: No effect on ISGylation.
{ECO:0000269|PubMed:17222803}.
MUTAGEN 112 112 K->R: No effect on ISGylation.
{ECO:0000269|PubMed:17222803}.
MUTAGEN 117 117 K->R: No ISGylation.
{ECO:0000269|PubMed:17222803}.
HELIX 2 5 {ECO:0000244|PDB:5EYA}.
HELIX 7 10 {ECO:0000244|PDB:5FER}.
TURN 14 16 {ECO:0000244|PDB:5FER}.
STRAND 17 19 {ECO:0000244|PDB:5FER}.
STRAND 21 25 {ECO:0000244|PDB:5FER}.
STRAND 31 33 {ECO:0000244|PDB:5FER}.
HELIX 34 43 {ECO:0000244|PDB:5FER}.
STRAND 46 49 {ECO:0000244|PDB:5FER}.
TURN 51 53 {ECO:0000244|PDB:5FER}.
STRAND 56 59 {ECO:0000244|PDB:5FER}.
HELIX 67 78 {ECO:0000244|PDB:5FER}.
HELIX 191 300 {ECO:0000244|PDB:4LTB}.
HELIX 307 316 {ECO:0000244|PDB:4LTB}.
HELIX 331 358 {ECO:0000244|PDB:4LTB}.
SEQUENCE 630 AA; 70973 MW; EB0AB353F0AD4C80 CRC64;
MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC PQCRAVYQAR
PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS PNAQVACDHC LKEAAVKTCL
VCMASFCQEH LQPHFDSPAF QDHPLQPPVR DLLRRKCSQH NRLREFFCPE HSECICHICL
VEHKTCSPAS LSQASADLEA TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ
LQQEYTEMKA LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT
KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ CIGRLQEPTP
SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP SKLPTFGAPE QLVDLKQAGL
EAAAKATSSH PNSTSLKAKV LETFLAKSRP ELLEYYIKVI LDYNTAHNKV ALSECYTVAS
VAEMPQNYRP HPQRFTYCSQ VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES
RLGRNSASWC VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM
YKFRVDFTEA LYPAFWVFSA GATLSICSPK


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