TRIM6_HUMAN
ID TRIM6_HUMAN Reviewed; 488 AA.
AC Q9C030; A8K2A7; B4DDQ5; Q86WZ8; Q9HCR1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Tripartite motif-containing protein 6;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8BGE7};
DE AltName: Full=RING finger protein 89;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM6 {ECO:0000305};
GN Name=TRIM6; Synonyms=RNF89;
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 [MRNA] (ISOFORM 1).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Astrocyte, Fetal kidney, Kidney, Placenta, and Thalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-300 (ISOFORM 2).
RX PubMed=11013086; DOI=10.1006/geno.2000.6318;
RA Orimo A., Tominaga N., Yoshimura K., Yamauchi Y., Nomura M., Sato M.,
RA Nogi Y., Suzuki M., Suzuki H., Ikeda K., Inoue S., Muramatsu M.;
RT "Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive
RT finger protein (ifp1), which possesses two RING-B box-coiled coil domains
RT in tandem.";
RL Genomics 69:143-149(2000).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH TRIM5.
RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
RA Dean M., Sodroski J.;
RT "Unique features of TRIM5alpha among closely related human TRIM family
RT members.";
RL Virology 360:419-433(2007).
RN [8]
RP INTERACTION WITH TRIM5, AND MUTAGENESIS OF ARG-121.
RX PubMed=21680743; DOI=10.1074/jbc.m111.260406;
RA Li X., Yeung D.F., Fiegen A.M., Sodroski J.;
RT "Determinants of the higher order association of the restriction factor
RT TRIM5alpha and other tripartite motif (TRIM) proteins.";
RL J. Biol. Chem. 286:27959-27970(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IKBKE, AND MUTAGENESIS OF
RP CYS-15.
RX PubMed=24882218; DOI=10.1016/j.immuni.2014.04.018;
RA Rajsbaum R., Versteeg G.A., Schmid S., Maestre A.M., Belicha-Villanueva A.,
RA Martinez-Romero C., Patel J.R., Morrison J., Pisanelli G., Miorin L.,
RA Laurent-Rolle M., Moulton H.M., Stein D.A., Fernandez-Sesma A.,
RA tenOever B.R., Garcia-Sastre A.;
RT "Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase
RT TRIM6 stimulates the interferon-IKKepsilon kinase-mediated antiviral
RT response.";
RL Immunity 40:880-895(2014).
RN [10]
RP INTERACTION WITH NIPAH VIRUS MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=27622505; DOI=10.1371/journal.ppat.1005880;
RA Bharaj P., Wang Y.E., Dawes B.E., Yun T.E., Park A., Yen B., Basler C.F.,
RA Freiberg A.N., Lee B., Rajsbaum R.;
RT "The Matrix Protein of Nipah Virus Targets the E3-Ubiquitin Ligase TRIM6 to
RT Inhibit the IKKepsilon Kinase-Mediated Type-I IFN Antiviral Response.";
RL PLoS Pathog. 12:e1005880-e1005880(2016).
RN [11]
RP INTERACTION WITH EBOLAVIRUS PROTEIN VP35 (MICROBIAL INFECTION).
RX PubMed=28679761; DOI=10.1128/jvi.00833-17;
RA Bharaj P., Atkins C., Luthra P., Giraldo M.I., Dawes B.E., Miorin L.,
RA Johnson J.R., Krogan N.J., Basler C.F., Freiberg A.N., Rajsbaum R.;
RT "The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35
RT Protein and Promotes Virus Replication.";
RL J. Virol. 91:0-0(2017).
RN [12]
RP FUNCTION, AND INTERACTION WITH VAMP8.
RX PubMed=31694946; DOI=10.1128/jvi.01454-19;
RA van Tol S., Atkins C., Bharaj P., Johnson K.N., Hage A., Freiberg A.N.,
RA Rajsbaum R.;
RT "VAMP8 Contributes to the TRIM6-Mediated Type I Interferon Antiviral
RT Response during West Nile Virus Infection.";
RL J. Virol. 94:0-0(2020).
CC -!- FUNCTION: E3 ubiquitin ligase that plays a crucial role in the
CC activation of the IKBKE-dependent branch of the type I interferon
CC signaling pathway (PubMed:24882218, PubMed:31694946). In concert with
CC the ubiquitin-conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-
CC 48'-linked polyubiquitin chains that promote the oligomerization and
CC autophosphorylation of IKBKE leading to stimulation of an antiviral
CC response (PubMed:24882218). Ubiquitinates also MYC and inhibits its
CC transcription activation activity, maintaining the pluripotency of
CC embryonic stem cells (By similarity). {ECO:0000250|UniProtKB:Q8BGE7,
CC ECO:0000269|PubMed:24882218, ECO:0000269|PubMed:31694946}.
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:0000250|UniProtKB:Q8BGE7};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8BGE7}.
CC -!- SUBUNIT: Homotrimer (PubMed:17156811). Forms heteromultimers (via
CC B30.2/SPRY domain) with TRIM5 (PubMed:21680743). Interacts with MYC (By
CC similarity). Interacts (via SPRY domain) with IKBKE (PubMed:24882218).
CC Interacts with VAMP8; this interaction contributes to the activation of
CC the type I interferon antiviral response (PubMed:31694946).
CC {ECO:0000250|UniProtKB:Q8BGE7, ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:21680743, ECO:0000269|PubMed:24882218,
CC ECO:0000269|PubMed:31694946}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP35;
CC this interaction plays an important role in promoting efficient viral
CC replication. {ECO:0000269|PubMed:28679761}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 capsid complexes.
CC {ECO:0000269|PubMed:17156811}.
CC -!- SUBUNIT: (Microbial infection) Interacts with matrix protein of Nipah
CC virus; this interaction inhibits the IKBKE-dependent activation of the
CC type I interferon signaling pathway. {ECO:0000269|PubMed:27622505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:24882218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C030-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C030-2; Sequence=VSP_012087;
CC Name=3;
CC IsoId=Q9C030-3; Sequence=VSP_046924;
CC -!- DOMAIN: The B-box zinc finger and the linker region between the coiled
CC coil and B30.2/SPRY domains contribute to higher order self-
CC association. {ECO:0000269|PubMed:21680743}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB17050.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. The in vivo relevance of this transcript of the TRIM34 (AC Q9BYJ4) and TRIM6 genes that codes for a chimeric protein of 842 residues is uncertain.; Evidence={ECO:0000305};
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DR EMBL; AF220030; AAG53484.1; -; mRNA.
DR EMBL; AK027664; BAB55276.1; -; mRNA.
DR EMBL; AK290172; BAF82861.1; -; mRNA.
DR EMBL; AK293295; BAG56816.1; -; mRNA.
DR EMBL; AK298301; BAG60556.1; -; mRNA.
DR EMBL; AK316178; BAH14549.1; -; mRNA.
DR EMBL; AK316289; BAH14660.1; -; mRNA.
DR EMBL; AC015691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68783.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68785.1; -; Genomic_DNA.
DR EMBL; BC047564; AAH47564.1; -; mRNA.
DR EMBL; AB039903; BAB17050.1; ALT_SEQ; mRNA.
DR CCDS; CCDS31389.1; -. [Q9C030-2]
DR CCDS; CCDS31390.1; -. [Q9C030-1]
DR CCDS; CCDS55738.1; -. [Q9C030-3]
DR RefSeq; NP_001003818.1; NM_001003818.2. [Q9C030-2]
DR RefSeq; NP_001185573.1; NM_001198644.1. [Q9C030-3]
DR RefSeq; NP_001185574.1; NM_001198645.1. [Q9C030-3]
DR RefSeq; NP_477514.1; NM_058166.4. [Q9C030-1]
DR AlphaFoldDB; Q9C030; -.
DR SMR; Q9C030; -.
DR BioGRID; 125596; 56.
DR IntAct; Q9C030; 2.
DR MINT; Q9C030; -.
DR STRING; 9606.ENSP00000369440; -.
DR iPTMnet; Q9C030; -.
DR PhosphoSitePlus; Q9C030; -.
DR BioMuta; TRIM6; -.
DR DMDM; 25009488; -.
DR EPD; Q9C030; -.
DR MassIVE; Q9C030; -.
DR MaxQB; Q9C030; -.
DR PaxDb; Q9C030; -.
DR PeptideAtlas; Q9C030; -.
DR PRIDE; Q9C030; -.
DR ProteomicsDB; 3881; -.
DR ProteomicsDB; 79950; -. [Q9C030-1]
DR ProteomicsDB; 79951; -. [Q9C030-2]
DR Antibodypedia; 11069; 115 antibodies from 27 providers.
DR DNASU; 117854; -.
DR Ensembl; ENST00000278302.9; ENSP00000278302.5; ENSG00000121236.21. [Q9C030-1]
DR Ensembl; ENST00000380097.8; ENSP00000369440.3; ENSG00000121236.21. [Q9C030-2]
DR Ensembl; ENST00000445329.5; ENSP00000399215.1; ENSG00000121236.21. [Q9C030-3]
DR Ensembl; ENST00000506134.5; ENSP00000421079.1; ENSG00000121236.21. [Q9C030-3]
DR Ensembl; ENST00000507320.5; ENSP00000427704.1; ENSG00000121236.21. [Q9C030-3]
DR Ensembl; ENST00000515022.5; ENSP00000421802.1; ENSG00000121236.21. [Q9C030-3]
DR GeneID; 117854; -.
DR KEGG; hsa:117854; -.
DR MANE-Select; ENST00000380097.8; ENSP00000369440.3; NM_001003818.3; NP_001003818.1. [Q9C030-2]
DR UCSC; uc001mbc.3; human. [Q9C030-1]
DR CTD; 117854; -.
DR DisGeNET; 117854; -.
DR GeneCards; TRIM6; -.
DR HGNC; HGNC:16277; TRIM6.
DR HPA; ENSG00000121236; Tissue enhanced (kidney).
DR MIM; 607564; gene.
DR neXtProt; NX_Q9C030; -.
DR OpenTargets; ENSG00000121236; -.
DR PharmGKB; PA38110; -.
DR VEuPathDB; HostDB:ENSG00000121236; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163021; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9C030; -.
DR OMA; EPTYCFN; -.
DR PhylomeDB; Q9C030; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q9C030; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9C030; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 117854; 14 hits in 1111 CRISPR screens.
DR GeneWiki; TRIM6; -.
DR GenomeRNAi; 117854; -.
DR Pharos; Q9C030; Tbio.
DR PRO; PR:Q9C030; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9C030; protein.
DR Bgee; ENSG00000121236; Expressed in oocyte and 133 other tissues.
DR ExpressionAtlas; Q9C030; baseline and differential.
DR Genevisible; Q9C030; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IMP:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR CDD; cd15823; SPRY_PRY_TRIM6; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR035828; PRY/SPRY_TRIM6.
DR InterPro; IPR003877; SPRY_dom.
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; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 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 Alternative splicing; Coiled coil; Cytoplasm; Host-virus interaction;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="Tripartite motif-containing protein 6"
FT /id="PRO_0000056202"
FT DOMAIN 282..488
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..133
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 134..248
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046924"
FT VAR_SEQ 1
FT /note="M -> MCGSERILQAGNILEIRVGQAGARRVATM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11013086,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_012087"
FT VARIANT 154
FT /note="E -> K (in dbSNP:rs57856328)"
FT /id="VAR_061823"
FT MUTAGEN 15
FT /note="C->A: Abolishes binding of polyubiquitin to IKBKE."
FT /evidence="ECO:0000269|PubMed:24882218"
FT MUTAGEN 121
FT /note="R->E: Reduced higher order self-association and
FT association with TRIM5."
FT /evidence="ECO:0000269|PubMed:21680743"
FT CONFLICT 68..69
FT /note="LR -> FG (in Ref. 6; BAB17050)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="Q -> K (in Ref. 5; AAH47564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56400 MW; F6AEC6BF578E9E72 CRC64;
MTSPVLVDIR EEVTCPICLE LLTEPLSIDC GHSFCQACIT PNGRESVIGQ EGERSCPVCQ
TSYQPGNLRP NRHLANIVRR LREVVLGPGK QLKAVLCADH GEKLQLFCQE DGKVICWLCE
RSQEHRGHHT FLVEEVAQEY QEKFQESLKK LKNEEQEAEK LTAFIREKKT SWKNQMEPER
CRIQTEFNQL RNILDRVEQR ELKKLEQEEK KGLRIIEEAE NDLVHQTQSL RELISDLERR
CQGSTMELLQ DVSDVTERSE FWTLRKPEAL PTKLRSMFRA PDLKRMLRVC RELTDVQSYW
VDVTLNPHTA NLNLVLAKNR RQVRFVGAKV SGPSCLEKHY DCSVLGSQHF SSGKHYWEVD
VAKKTAWILG VCSNSLGPTF SFNHFAQNHS AYSRYQPQSG YWVIGLQHNH EYRAYEDSSP
SLLLSMTVPP RRVGVFLDYE AGTVSFYNVT NHGFPIYTFS KYYFPTTLCP YFNPCNCVIP
MTLRRPSS
