TRI56_HUMAN
ID TRI56_HUMAN Reviewed; 755 AA.
AC Q9BRZ2; Q6PJS5; Q86VT6; Q8N2H8; Q8NAC0; Q9H031;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM56 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:21289118};
DE AltName: Full=RING finger protein 109;
DE AltName: Full=Tripartite motif-containing protein 56;
GN Name=TRIM56 {ECO:0000303|PubMed:21289118, ECO:0000312|HGNC:HGNC:19028};
GN Synonyms=RNF109;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 429-755 (ISOFORM 1).
RC TISSUE=Spleen, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-755 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418; THR-442 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP FUNCTION, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AUTOUBIQUITINATION, INDUCTION BY IFN-ALPHA, AND MUTAGENESIS OF CYS-21 AND
RP CYS-24.
RX PubMed=21289118; DOI=10.1128/jvi.02546-10;
RA Wang J., Liu B., Wang N., Lee Y.M., Liu C., Li K.;
RT "TRIM56 is a virus- and interferon-inducible E3 ubiquitin ligase that
RT restricts pestivirus infection.";
RL J. Virol. 85:3733-3745(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH TICAM1.
RX PubMed=22948160; DOI=10.1074/jbc.m112.397075;
RA Shen Y., Li N.L., Wang J., Liu B., Lester S., Li K.;
RT "TRIM56 is an essential component of the TLR3 antiviral signaling
RT pathway.";
RL J. Biol. Chem. 287:36404-36413(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418 AND THR-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-21 AND CYS-24.
RX PubMed=25253338; DOI=10.1128/jvi.02505-14;
RA Liu B., Li N.L., Wang J., Shi P.Y., Wang T., Miller M.A., Li K.;
RT "Overlapping and distinct molecular determinants dictating the antiviral
RT activities of TRIM56 against flaviviruses and coronavirus.";
RL J. Virol. 88:13821-13835(2014).
RN [12]
RP FUNCTION, AND PATHWAY.
RX PubMed=29426904; DOI=10.1038/s41467-018-02936-3;
RA Seo G.J., Kim C., Shin W.J., Sklan E.H., Eoh H., Jung J.U.;
RT "TRIM56-mediated monoubiquitination of cGAS for cytosolic DNA sensing.";
RL Nat. Commun. 9:613-613(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in innate
CC antiviral immunity by mediating ubiquitination of CGAS and STING1
CC (PubMed:21289118, PubMed:29426904). In response to pathogen- and host-
CC derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked
CC ubiquitination, thereby promoting its homodimerization, a step required
CC for the production of type I interferon IFN-beta (By similarity). Also
CC mediate monoubiquitination of CGAS, thereby promoting CGAS
CC oligomerization and subsequent activation (PubMed:29426904).
CC Independently of its E3 ubiquitin ligase activity, positive regulator
CC of TLR3 signaling. Potentiates extracellular double stranded RNA
CC (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes
CC ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (PubMed:22948160).
CC Promotes establishment of an antiviral state by TLR3 ligand and TLR3-
CC mediated chemokine induction following infection by hepatitis C virus
CC (PubMed:22948160). {ECO:0000250|UniProtKB:Q80VI1,
CC ECO:0000269|PubMed:21289118, ECO:0000269|PubMed:22948160,
CC ECO:0000269|PubMed:29426904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:21289118};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:21289118, ECO:0000269|PubMed:29426904}.
CC -!- SUBUNIT: Homooligomer. Interacts with STING1 (By similarity). Interacts
CC with TICAM1 (PubMed:22948160). {ECO:0000250|UniProtKB:Q80VI1,
CC ECO:0000269|PubMed:22948160}.
CC -!- INTERACTION:
CC Q9BRZ2; Q8IUC6: TICAM1; NbExp=2; IntAct=EBI-1048636, EBI-525995;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21289118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRZ2-2; Sequence=VSP_029111, VSP_029112;
CC Name=3;
CC IsoId=Q9BRZ2-3; Sequence=VSP_029109, VSP_029110;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:21289118}.
CC -!- INDUCTION: Up-regulated by IFN-alpha. {ECO:0000269|PubMed:21289118}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:21289118}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11882.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11500.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK075255; BAC11500.1; ALT_INIT; mRNA.
DR EMBL; AK092927; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC105446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005847; AAH05847.3; -; mRNA.
DR EMBL; BC011882; AAH11882.1; ALT_INIT; mRNA.
DR EMBL; BC048194; AAH48194.1; -; mRNA.
DR EMBL; AL512757; CAC21676.1; -; mRNA.
DR CCDS; CCDS43625.1; -. [Q9BRZ2-1]
DR RefSeq; NP_112223.1; NM_030961.2. [Q9BRZ2-1]
DR RefSeq; XP_011514891.1; XM_011516589.2. [Q9BRZ2-1]
DR PDB; 5JW7; X-ray; 2.85 A; B=1-93.
DR PDBsum; 5JW7; -.
DR AlphaFoldDB; Q9BRZ2; -.
DR SMR; Q9BRZ2; -.
DR BioGRID; 123596; 145.
DR IntAct; Q9BRZ2; 25.
DR STRING; 9606.ENSP00000305161; -.
DR iPTMnet; Q9BRZ2; -.
DR PhosphoSitePlus; Q9BRZ2; -.
DR BioMuta; TRIM56; -.
DR DMDM; 56749788; -.
DR EPD; Q9BRZ2; -.
DR jPOST; Q9BRZ2; -.
DR MassIVE; Q9BRZ2; -.
DR MaxQB; Q9BRZ2; -.
DR PaxDb; Q9BRZ2; -.
DR PeptideAtlas; Q9BRZ2; -.
DR PRIDE; Q9BRZ2; -.
DR ProteomicsDB; 78854; -. [Q9BRZ2-1]
DR ProteomicsDB; 78855; -. [Q9BRZ2-2]
DR ProteomicsDB; 78856; -. [Q9BRZ2-3]
DR Antibodypedia; 9103; 165 antibodies from 23 providers.
DR DNASU; 81844; -.
DR Ensembl; ENST00000306085.11; ENSP00000305161.6; ENSG00000169871.13. [Q9BRZ2-1]
DR GeneID; 81844; -.
DR KEGG; hsa:81844; -.
DR MANE-Select; ENST00000306085.11; ENSP00000305161.6; NM_030961.3; NP_112223.1.
DR UCSC; uc003uxq.4; human. [Q9BRZ2-1]
DR CTD; 81844; -.
DR DisGeNET; 81844; -.
DR GeneCards; TRIM56; -.
DR HGNC; HGNC:19028; TRIM56.
DR HPA; ENSG00000169871; Low tissue specificity.
DR MIM; 616996; gene.
DR neXtProt; NX_Q9BRZ2; -.
DR OpenTargets; ENSG00000169871; -.
DR PharmGKB; PA134958549; -.
DR VEuPathDB; HostDB:ENSG00000169871; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162489; -.
DR HOGENOM; CLU_008645_6_1_1; -.
DR InParanoid; Q9BRZ2; -.
DR OMA; LQGCPWM; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q9BRZ2; -.
DR TreeFam; TF338323; -.
DR PathwayCommons; Q9BRZ2; -.
DR Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR SignaLink; Q9BRZ2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81844; 10 hits in 1122 CRISPR screens.
DR ChiTaRS; TRIM56; human.
DR GenomeRNAi; 81844; -.
DR Pharos; Q9BRZ2; Tbio.
DR PRO; PR:Q9BRZ2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BRZ2; protein.
DR Bgee; ENSG00000169871; Expressed in tendon of biceps brachii and 194 other tissues.
DR ExpressionAtlas; Q9BRZ2; baseline and differential.
DR Genevisible; Q9BRZ2; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Coiled coil;
KW Cytoplasm; Immunity; Innate immunity; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..755
FT /note="E3 ubiquitin-protein ligase TRIM56"
FT /id="PRO_0000056288"
FT ZN_FING 21..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 98..149
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 164..205
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 371..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..314
FT /evidence="ECO:0000255"
FT COMPBIAS 421..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976"
FT VAR_SEQ 259..269
FT /note="AEGVLRALLAQ -> CLLRTESCKAE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029109"
FT VAR_SEQ 270..755
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029110"
FT VAR_SEQ 273..308
FT /note="VLGQLRAHVEAAEEAARERLAELEGREQVARAAAAF -> NHLNPGGGSCSE
FT LRSHHCTPAWVTRMKLHLKKKKKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029111"
FT VAR_SEQ 309..755
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029112"
FT MUTAGEN 21
FT /note="C->A: Complete loss of autoubiquitination. Complete
FT loss of autoubiquitination, loss of antiviral activity
FT against yellow fever virus and human coronavirus virus
FT OC43, but normal induction of interferon-beta following
FT Sendai virus infection; when associated with A-24."
FT /evidence="ECO:0000269|PubMed:21289118"
FT MUTAGEN 24
FT /note="C->A: Complete loss of autoubiquitination, loss of
FT antiviral activity against yellow fever virus and human
FT coronavirus virus OC43, but normal induction of interferon-
FT beta following Sendia virus infection; when associated with
FT A-24."
FT /evidence="ECO:0000269|PubMed:21289118"
FT CONFLICT 230
FT /note="L -> P (in Ref. 1; AK092927)"
FT /evidence="ECO:0000305"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5JW7"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:5JW7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5JW7"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5JW7"
SQ SEQUENCE 755 AA; 81488 MW; CF72D0C8EC9F69E7 CRC64;
MVSHGSSPSL LEALSSDFLA CKICLEQLRA PKTLPCLHTY CQDCLAQLAD GGRVRCPECR
ETVPVPPEGV ASFKTNFFVN GLLDLVKARA CGDLRAGKPA CALCPLVGGT STGGPATARC
LDCADDLCQA CADGHRCTRQ THTHRVVDLV GYRAGWYDEE ARERQAAQCP QHPGEALRFL
CQPCSQLLCR ECRLDPHLDH PCLPLAEAVR ARRPGLEGLL AGVDNNLVEL EAARRVEKEA
LARLREQAAR VGTQVEEAAE GVLRALLAQK QEVLGQLRAH VEAAEEAARE RLAELEGREQ
VARAAAAFAR RVLSLGREAE ILSLEGAIAQ RLRQLQGCPW APGPAPCLLP QLELHPGLLD
KNCHLLRLSF EEQQPQKDGG KDGAGTQGGE ESQSRREDEP KTERQGGVQP QAGDGAQTPK
EEKAQTTREE GAQTLEEDRA QTPHEDGGPQ PHRGGRPNKK KKFKGRLKSI SREPSPALGP
NLDGSGLLPR PIFYCSFPTR MPGDKRSPRI TGLCPFGPRE ILVADEQNRA LKRFSLNGDY
KGTVPVPEGC SPCSVAALQS AVAFSASARL YLINPNGEVQ WRRALSLSQA SHAVAALPSG
DRVAVSVAGH VEVYNMEGSL ATRFIPGGKA SRGLRALVFL TTSPQGHFVG SDWQQNSVVI
CDGLGQVVGE YKGPGLHGCQ PGSVSVDKKG YIFLTLREVN KVVILDPKGS LLGDFLTAYH
GLEKPRVTTM VDGRYLVVSL SNGTIHIFRV RSPDS
