TRIM8_HUMAN
ID TRIM8_HUMAN Reviewed; 551 AA.
AC Q9BZR9; A6NI31; Q9C028;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM8;
DE EC=2.3.2.27;
DE AltName: Full=Glioblastoma-expressed RING finger protein;
DE AltName: Full=RING finger protein 27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM8 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 8;
GN Name=TRIM8; Synonyms=GERP, RNF27;
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].
RC TISSUE=Brain;
RX PubMed=11118312; DOI=10.1006/bbrc.2000.3984;
RA Vincent S.R., Kwasnicka D.A., Fretier P.;
RT "A novel RING finger-B box-coiled-coil protein, GERP.";
RL Biochem. Biophys. Res. Commun. 279:482-486(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuron;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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].
RC TISSUE=Colon;
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 FUNCTION, AND INTERACTION WITH SOCS1.
RX PubMed=12163497; DOI=10.1074/jbc.m205900200;
RA Toniato E., Chen X.P., Losman J., Flati V., Donahue L., Rothman P.;
RT "TRIM8/GERP RING finger protein interacts with SOCS-1.";
RL J. Biol. Chem. 277:37315-37322(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIAS3.
RX PubMed=20516148; DOI=10.1242/jcs.068981;
RA Okumura F., Matsunaga Y., Katayama Y., Nakayama K.I., Hatakeyama S.;
RT "TRIM8 modulates STAT3 activity through negative regulation of PIAS3.";
RL J. Cell Sci. 123:2238-2245(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH MAP3K7.
RX PubMed=22084099; DOI=10.1073/pnas.1110946108;
RA Li Q., Yan J., Mao A.P., Li C., Ran Y., Shu H.B., Wang Y.Y.;
RT "Tripartite motif 8 (TRIM8) modulates TNFalpha- and IL-1beta-triggered NF-
RT kappaB activation by targeting TAK1 for K63-linked polyubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19341-19346(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23152791; DOI=10.1371/journal.pone.0048662;
RA Tomar D., Sripada L., Prajapati P., Singh R., Singh A.K., Singh R.;
RT "Nucleo-cytoplasmic trafficking of TRIM8, a novel oncogene, is involved in
RT positive regulation of TNF induced NF-kappaB pathway.";
RL PLoS ONE 7:E48662-E48662(2012).
RN [10]
RP FUNCTION, INTERACTION WITH MAP3K7, AND MUTAGENESIS OF CYS-15 AND CYS-18.
RX PubMed=27981609; DOI=10.1002/hep.28971;
RA Yan F.J., Zhang X.J., Wang W.X., Ji Y.X., Wang P.X., Yang Y., Gong J.,
RA Shen L.J., Zhu X.Y., Huang Z., Li H.;
RT "The E3 ligase tripartite motif 8 targets TAK1 to promote insulin
RT resistance and steatohepatitis.";
RL Hepatology 65:1492-1511(2017).
RN [11]
RP FUNCTION, INTERACTION WITH TICAM1, AND MUTAGENESIS OF CYS-15; CYS-18 AND
RP CYS-30.
RX PubMed=28747347; DOI=10.4049/jimmunol.1601647;
RA Ye W., Hu M.M., Lei C.Q., Zhou Q., Lin H., Sun M.S., Shu H.B.;
RT "TRIM8 Negatively Regulates TLR3/4-Mediated Innate Immune Response by
RT Blocking TRIF-TBK1 Interaction.";
RL J. Immunol. 199:1856-1864(2017).
RN [12]
RP INVOLVEMENT IN FSGSNEDS, AND VARIANTS FSGSNEDS 423-GLN--SER-551 DEL;
RP 444-SER--SER-551 DEL; 446-TYR--SER-551 DEL AND 459-GLN--SER-551 DEL.
RX PubMed=30244534; DOI=10.1002/ajmg.a.40357;
RA Assoum M., Lines M.A., Elpeleg O., Darmency V., Whiting S., Edvardson S.,
RA Devinsky O., Heinzen E., Hernan R.R., Antignac C., Deleuze J.F.,
RA Des Portes V., Bertholet-Thomas A., Belot A., Geller E., Lemesle M.,
RA Duffourd Y., Thauvin-Robinet C., Thevenon J., Chung W., Lowenstein D.H.,
RA Faivre L.;
RT "Further delineation of the clinical spectrum of de novo TRIM8 truncating
RT mutations.";
RL Am. J. Med. Genet. A 176:2470-2478(2018).
RN [13]
RP VARIANT FSGSNEDS 460-TYR--SER-551 DEL.
RX PubMed=32193649; DOI=10.1007/s00467-020-04525-3;
RA Warren M., Takeda M., Partikian A., Opas L., Fine R., Yano S.;
RT "Association of a de novo nonsense mutation of the TRIM8 gene with
RT childhood-onset focal segmental glomerulosclerosis.";
RL Pediatr. Nephrol. 35:1129-1132(2020).
RN [14]
RP VARIANT 445-GLN--SER-551 DEL.
RX PubMed=28124119; DOI=10.1007/s00439-017-1757-z;
RA Bramswig N.C., Caluseriu O., Luedecke H.J., Bolduc F.V., Noel N.C.,
RA Wieland T., Surowy H.M., Christen H.J., Engels H., Strom T.M.,
RA Wieczorek D.;
RT "Heterozygosity for ARID2 loss-of-function mutations in individuals with a
RT Coffin-Siris syndrome-like phenotype.";
RL Hum. Genet. 136:297-305(2017).
RN [15]
RP VARIANTS FSGSNEDS 401-GLY--SER-551 DEL; 411-GLN--SER-551 DEL;
RP 414-GLN--SER-551 DEL; 423-GLN--SER-551 DEL; 445-GLN--SER-551 DEL;
RP 459-GLN--SER-551 DEL; 460-TYR--SER-551 DEL AND 487-TYR--SER-551 DEL,
RP CHARACTERIZATION OF VARIANTS FSGSNEDS 411-GLN--SER-551 DEL AND
RP 459-GLN--SER-551 DEL, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=33508234; DOI=10.1016/j.ajhg.2021.01.008;
RG Undiagnosed Diseases Network;
RG UCLA Clinical Genomics Center;
RA Weng P.L., Majmundar A.J., Khan K., Lim T.Y., Shril S., Jin G.,
RA Musgrove J., Wang M., Ahram D.F., Aggarwal V.S., Bier L.E., Heinzen E.L.,
RA Onuchic-Whitford A.C., Mann N., Buerger F., Schneider R., Deutsch K.,
RA Kitzler T.M., Klaembt V., Kolb A., Mao Y., Moufawad El Achkar C.,
RA Mitrotti A., Martino J., Beck B.B., Altmueller J., Benz M.R., Yano S.,
RA Mikati M.A., Gunduz T., Cope H., Shashi V., Trachtman H., Bodria M.,
RA Caridi G., Pisani I., Fiaccadori E., AbuMaziad A.S., Martinez-Agosto J.A.,
RA Yadin O., Zuckerman J., Kim A., John-Kroegel U., Tyndall A.V.,
RA Parboosingh J.S., Innes A.M., Bierzynska A., Koziell A.B., Muorah M.,
RA Saleem M.A., Hoefele J., Riedhammer K.M., Gharavi A.G., Jobanputra V.,
RA Pierce-Hoffman E., Seaby E.G., O'Donnell-Luria A., Rehm H.L., Mane S.,
RA D'Agati V.D., Pollak M.R., Ghiggeri G.M., Lifton R.P., Goldstein D.B.,
RA Davis E.E., Hildebrandt F., Sanna-Cherchi S.;
RT "De novo TRIM8 variants impair its protein localization to nuclear bodies
RT and cause developmental delay, epilepsy, and focal segmental
RT glomerulosclerosis.";
RL Am. J. Hum. Genet. 108:357-367(2021).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that participates in multiple
CC biological processes including cell survival, differentiation,
CC apoptosis, and in particular, the innate immune response
CC (PubMed:27981609, PubMed:28747347). Participates in the activation of
CC interferon-gamma signaling by promoting proteasomal degradation of the
CC repressor SOCS1 (PubMed:12163497). Plays a positive role in the
CC TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the
CC 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to
CC the activation of NF-kappa-B (PubMed:22084099, PubMed:23152791,
CC PubMed:27981609). Modulates also STAT3 activity through negative
CC regulation of PIAS3, either by degradation of PIAS3 through the
CC ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus
CC (PubMed:20516148). Negatively regulates TLR3/4-mediated innate immune
CC response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination
CC of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction
CC (PubMed:28747347). {ECO:0000269|PubMed:12163497,
CC ECO:0000269|PubMed:20516148, ECO:0000269|PubMed:22084099,
CC ECO:0000269|PubMed:23152791, ECO:0000269|PubMed:28747347}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with SOCS1 (via) SH2 domain and SOCS box
CC (PubMed:12163497). Interacts with HSP90AB1; prevents nucleus
CC translocation of phosphorylated STAT3 and HSP90AB1. Interacts with
CC MAP3K7/TAK1 (PubMed:22084099). Interacts with PIAS3 (PubMed:20516148).
CC Interacts with TICAM1 (PubMed:28747347). {ECO:0000269|PubMed:12163497,
CC ECO:0000269|PubMed:20516148, ECO:0000269|PubMed:22084099,
CC ECO:0000269|PubMed:28747347}.
CC -!- INTERACTION:
CC Q9BZR9; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-2340370, EBI-744545;
CC Q9BZR9; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-2340370, EBI-740086;
CC Q9BZR9; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-2340370, EBI-11986315;
CC Q9BZR9; P49639: HOXA1; NbExp=3; IntAct=EBI-2340370, EBI-740785;
CC Q9BZR9; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-2340370, EBI-739832;
CC Q9BZR9; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-2340370, EBI-2341787;
CC Q9BZR9; Q8N3F0: MTURN; NbExp=7; IntAct=EBI-2340370, EBI-11980301;
CC Q9BZR9; Q8NFP7: NUDT10; NbExp=3; IntAct=EBI-2340370, EBI-726826;
CC Q9BZR9; Q96DC9: OTUB2; NbExp=7; IntAct=EBI-2340370, EBI-746259;
CC Q9BZR9; P54725: RAD23A; NbExp=3; IntAct=EBI-2340370, EBI-746453;
CC Q9BZR9; Q8IYW5: RNF168; NbExp=3; IntAct=EBI-2340370, EBI-914207;
CC Q9BZR9; Q13148: TARDBP; NbExp=3; IntAct=EBI-2340370, EBI-372899;
CC Q9BZR9; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-2340370, EBI-2509913;
CC Q9BZR9; O14787-2: TNPO2; NbExp=3; IntAct=EBI-2340370, EBI-12076664;
CC Q9BZR9; Q63HR2: TNS2; NbExp=3; IntAct=EBI-2340370, EBI-949753;
CC Q9BZR9; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-2340370, EBI-2340370;
CC Q9BZR9; P57075-2: UBASH3A; NbExp=5; IntAct=EBI-2340370, EBI-7353612;
CC Q9BZR9; P51668: UBE2D1; NbExp=4; IntAct=EBI-2340370, EBI-743540;
CC Q9BZR9; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-2340370, EBI-745527;
CC Q9BZR9; O14933: UBE2L6; NbExp=4; IntAct=EBI-2340370, EBI-2129974;
CC Q9BZR9; O94888: UBXN7; NbExp=3; IntAct=EBI-2340370, EBI-1993627;
CC Q9BZR9; P45974-2: USP5; NbExp=3; IntAct=EBI-2340370, EBI-12072186;
CC Q9BZR9; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-2340370, EBI-2510804;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23152791}. Nucleus
CC {ECO:0000269|PubMed:23152791}. Nucleus, nuclear body
CC {ECO:0000269|PubMed:33508234}. Note=Nucleo-cytoplasmic translocation is
CC involved in regulation of NF-kappa-B. {ECO:0000269|PubMed:23152791}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in glomerular podocytes
CC of kidneys. {ECO:0000269|PubMed:33508234, ECO:0000305}.
CC -!- DOMAIN: The coiled coil domain is required for homodimerization.
CC -!- DOMAIN: The region immediately C-terminal to the RING motif is
CC sufficient to mediate the interaction with SOCS1.
CC {ECO:0000250|UniProtKB:Q99PJ2}.
CC -!- DISEASE: Focal segmental glomerulosclerosis and neurodevelopmental
CC syndrome (FSGSNEDS) [MIM:619428]: An autosomal dominant disorder
CC characterized by global developmental delay associated with variable
CC features of focal segmental glomerulosclerosis, a renal pathology
CC defined by the presence of segmental sclerosis in glomeruli and
CC resulting in proteinuria, reduced glomerular filtration rate and
CC progressive decline in renal function. Some patients have transient
CC proteinuria and others require renal transplant. Neurodevelopmental
CC features are also variable, with some patients having only mildly
CC impaired intellectual development, and others having a severe
CC developmental disorder associated with early-onset refractory seizures
CC or epileptic encephalopathy. Additional features, including feeding
CC difficulties, poor overall growth, and non-specific dysmorphic facial
CC features, are commonly observed. {ECO:0000269|PubMed:30244534,
CC ECO:0000269|PubMed:32193649, ECO:0000269|PubMed:33508234}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF281046; AAG53087.1; -; mRNA.
DR EMBL; AF220034; AAG53488.1; -; mRNA.
DR EMBL; AL391121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49680.1; -; Genomic_DNA.
DR EMBL; BC021925; AAH21925.1; -; mRNA.
DR CCDS; CCDS31274.1; -.
DR PIR; JC7562; JC7562.
DR RefSeq; NP_112174.2; NM_030912.2.
DR AlphaFoldDB; Q9BZR9; -.
DR SMR; Q9BZR9; -.
DR BioGRID; 123541; 93.
DR IntAct; Q9BZR9; 67.
DR STRING; 9606.ENSP00000302120; -.
DR MoonDB; Q9BZR9; Predicted.
DR iPTMnet; Q9BZR9; -.
DR PhosphoSitePlus; Q9BZR9; -.
DR BioMuta; TRIM8; -.
DR DMDM; 18202744; -.
DR EPD; Q9BZR9; -.
DR jPOST; Q9BZR9; -.
DR MassIVE; Q9BZR9; -.
DR MaxQB; Q9BZR9; -.
DR PaxDb; Q9BZR9; -.
DR PeptideAtlas; Q9BZR9; -.
DR PRIDE; Q9BZR9; -.
DR ProteomicsDB; 79898; -.
DR Antibodypedia; 31471; 175 antibodies from 29 providers.
DR DNASU; 81603; -.
DR Ensembl; ENST00000643721.2; ENSP00000496301.1; ENSG00000171206.15.
DR GeneID; 81603; -.
DR KEGG; hsa:81603; -.
DR MANE-Select; ENST00000643721.2; ENSP00000496301.1; NM_030912.3; NP_112174.2.
DR UCSC; uc001kvz.3; human.
DR CTD; 81603; -.
DR DisGeNET; 81603; -.
DR GeneCards; TRIM8; -.
DR HGNC; HGNC:15579; TRIM8.
DR HPA; ENSG00000171206; Low tissue specificity.
DR MalaCards; TRIM8; -.
DR MIM; 606125; gene.
DR MIM; 619428; phenotype.
DR neXtProt; NX_Q9BZR9; -.
DR OpenTargets; ENSG00000171206; -.
DR Orphanet; 1934; Early infantile epileptic encephalopathy.
DR PharmGKB; PA37983; -.
DR VEuPathDB; HostDB:ENSG00000171206; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000157919; -.
DR HOGENOM; CLU_036491_0_0_1; -.
DR InParanoid; Q9BZR9; -.
DR OrthoDB; 364341at2759; -.
DR PhylomeDB; Q9BZR9; -.
DR TreeFam; TF333491; -.
DR PathwayCommons; Q9BZR9; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9BZR9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81603; 17 hits in 1121 CRISPR screens.
DR ChiTaRS; TRIM8; human.
DR GenomeRNAi; 81603; -.
DR Pharos; Q9BZR9; Tbio.
DR PRO; PR:Q9BZR9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BZR9; protein.
DR Bgee; ENSG00000171206; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q9BZR9; baseline and differential.
DR Genevisible; Q9BZR9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Disease variant; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..551
FT /note="E3 ubiquitin-protein ligase TRIM8"
FT /id="PRO_0000056206"
FT ZN_FING 15..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..132
FT /note="B box-type 1"
FT ZN_FING 140..182
FT /note="B box-type 2"
FT COILED 181..249
FT /evidence="ECO:0000255"
FT VARIANT 401..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:33508234"
FT /id="VAR_086209"
FT VARIANT 411..551
FT /note="Missing (in FSGSNEDS; disrupts localization to
FT nuclear bodies)"
FT /evidence="ECO:0000269|PubMed:33508234"
FT /id="VAR_086210"
FT VARIANT 414..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:33508234"
FT /id="VAR_086211"
FT VARIANT 423..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:30244534,
FT ECO:0000269|PubMed:33508234"
FT /id="VAR_086212"
FT VARIANT 444..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:30244534"
FT /id="VAR_086213"
FT VARIANT 445..551
FT /note="Missing (in FSGSNEDS; also found in a patient with
FT Coffin-Siris syndrome carrying a likely pathogenic ARID2
FT mutation)"
FT /evidence="ECO:0000269|PubMed:28124119,
FT ECO:0000269|PubMed:33508234"
FT /id="VAR_080568"
FT VARIANT 446..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:30244534"
FT /id="VAR_086214"
FT VARIANT 459..551
FT /note="Missing (in FSGSNEDS; disrupts localization to
FT nuclear bodies)"
FT /evidence="ECO:0000269|PubMed:30244534,
FT ECO:0000269|PubMed:33508234"
FT /id="VAR_086215"
FT VARIANT 460..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:32193649,
FT ECO:0000269|PubMed:33508234"
FT /id="VAR_086216"
FT VARIANT 487..551
FT /note="Missing (in FSGSNEDS)"
FT /evidence="ECO:0000269|PubMed:33508234"
FT /id="VAR_086217"
FT MUTAGEN 15
FT /note="C->A: Complete loss of ubiquitination activity on
FT MAP3K7/TAK1."
FT /evidence="ECO:0000269|PubMed:27981609"
FT MUTAGEN 15
FT /note="C->S: Complete loss of ubiquitination activity on
FT TICAM1."
FT /evidence="ECO:0000269|PubMed:28747347"
FT MUTAGEN 18
FT /note="C->A: Complete loss of ubiquitination activity on
FT MAP3K7/TAK1."
FT /evidence="ECO:0000269|PubMed:27981609"
FT MUTAGEN 18
FT /note="C->S: Complete loss of ubiquitination activity on
FT TICAM1."
FT /evidence="ECO:0000269|PubMed:28747347"
FT MUTAGEN 30
FT /note="C->S: Complete loss of ubiquitination activity on
FT TICAM1."
FT /evidence="ECO:0000269|PubMed:28747347"
FT CONFLICT 174
FT /note="H -> R (in Ref. 1; AAG53087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 61489 MW; 1FEF89029EB9BACB CRC64;
MAENWKNCFE EELICPICLH VFVEPVQLPC KHNFCRGCIG EAWAKDSGLV RCPECNQAYN
QKPGLEKNLK LTNIVEKFNA LHVEKPPAAL HCVFCRRGPP LPAQKVCLRC EAPCCQSHVQ
THLQQPSTAR GHLLVEADDV RAWSCPQHNA YRLYHCEAEQ VAVCQYCCYY SGAHQGHSVC
DVEIRRNEIR KMLMKQQDRL EEREQDIEDQ LYKLESDKRL VEEKVNQLKE EVRLQYEKLH
QLLDEDLRQT VEVLDKAQAK FCSENAAQAL HLGERMQEAK KLLGSLQLLF DKTEDVSFMK
NTKSVKILMD RTQTCTSSSL SPTKIGHLNS KLFLNEVAKK EKQLRKMLEG PFSTPVPFLQ
SVPLYPCGVS SSGAEKRKHS TAFPEASFLE TSSGPVGGQY GAAGTASGEG QSGQPLGPCS
STQHLVALPG GAQPVHSSPV FPPSQYPNGS AAQQPMLPQY GGRKILVCSV DNCYCSSVAN
HGGHQPYPRS GHFPWTVPSQ EYSHPLPPTP SVPQSLPSLA VRDWLDASQQ PGHQDFYRVY
GQPSTKHYVT S
