ID TRI26_HUMAN Reviewed; 539 AA. AC Q12899; A6NG96; Q5SRL2; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 209. DE RecName: Full=Tripartite motif-containing protein 26; DE EC=2.3.2.27 {ECO:0000269|PubMed:26611359, ECO:0000269|PubMed:29203640, ECO:0000269|PubMed:29610152, ECO:0000269|PubMed:34017102}; DE AltName: Full=Acid finger protein; DE Short=AFP; DE AltName: Full=RING finger protein 95; DE AltName: Full=Zinc finger protein 173; GN Name=TRIM26; Synonyms=RNF95, ZNF173; 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]. RX PubMed=8530076; DOI=10.1006/geno.1995.1236; RA Chu T.W., Capossela A., Coleman R., Goei V.L., Nallur G., Gruen J.R.; RT "Cloning of a new 'finger' protein gene (ZNF173) within the class I region RT of the human MHC."; RL Genomics 29:229-239(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.; RT "Genome diversity in HLA: a new strategy for detection of genetic RT polymorphisms in expressed genes within the HLA class III and class I RT regions."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Peripheral blood leukocyte; RX PubMed=16702430; DOI=10.1534/genetics.106.057034; RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A., RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., RA Inoko H., Bahram S.; RT "Rapid evolution of major histocompatibility complex class I genes in RT primates generates new disease alleles in humans via hitchhiking RT diversity."; RL Genetics 173:1555-1570(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Skin; 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 [8] RP INTERACTION WITH INCA1. RX PubMed=21750715; DOI=10.1371/journal.pone.0021505; RA Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E., RA Mueller-Tidow C.; RT "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor RT for its antiproliferative effects."; RL PLoS ONE 6:E21505-E21505(2011). RN [9] RP FUNCTION. RX PubMed=23452852; DOI=10.1016/j.cell.2013.02.006; RA Zhao W., Li Q., Ayers S., Gu Y., Shi Z., Zhu Q., Chen Y., Wang H.Y., RA Wang R.F.; RT "Jmjd3 inhibits reprogramming by upregulating expression of INK4a/Arf and RT targeting PHF20 for ubiquitination."; RL Cell 152:1037-1050(2013). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25763818; DOI=10.1371/journal.ppat.1004726; RA Wang P., Zhao W., Zhao K., Zhang L., Gao C.; RT "TRIM26 negatively regulates interferon-beta production and antiviral RT response through polyubiquitination and degradation of nuclear IRF3."; RL PLoS Pathog. 11:E1004726-E1004726(2015). RN [11] RP FUNCTION, INTERACTION WITH TBK1, AND UBIQUITINATION. RX PubMed=26611359; DOI=10.1093/jmcb/mjv068; RA Ran Y., Zhang J., Liu L.L., Pan Z.Y., Nie Y., Zhang H.Y., Wang Y.Y.; RT "Autoubiquitination of TRIM26 links TBK1 to NEMO in RLR-mediated innate RT antiviral immune response."; RL J. Mol. Cell Biol. 8:31-43(2016). RN [12] RP FUNCTION, INDUCTION BY TGF-BETA, AND CATALYTIC ACTIVITY. RX PubMed=29203640; DOI=10.1128/mcb.00449-17; RA Nakagawa T., Hosogane M., Nakagawa M., Morohoshi A., Funayama R., RA Nakayama K.; RT "Transforming Growth Factor beta-Induced Proliferative Arrest Mediated by RT TRIM26-Dependent TAF7 Degradation and Its Antagonism by MYC."; RL Mol. Cell. Biol. 38:0-0(2018). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29610152; DOI=10.1128/mcb.00616-17; RA Williams S.C., Parsons J.L.; RT "NTH1 Is a New Target for Ubiquitylation-Dependent Regulation by TRIM26 RT Required for the Cellular Response to Oxidative Stress."; RL Mol. Cell. Biol. 38:0-0(2018). RN [14] RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INDUCTION BY RP HERPES SIMPLEX VIRUS TYPE 2. RX PubMed=33419081; DOI=10.3390/v13010070; RA Dhawan T., Zahoor M.A., Heryani N., Workenhe S.T., Nazli A., Kaushic C.; RT "TRIM26 Facilitates HSV-2 Infection by Downregulating Antiviral Responses RT through the IRF3 Pathway."; RL Viruses 13:0-0(2021). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF RP CYS-16. RX PubMed=34017102; DOI=10.1038/s41418-021-00803-1; RA Zhao J., Cai B., Shao Z., Zhang L., Zheng Y., Ma C., Yi F., Liu B., Gao C.; RT "TRIM26 positively regulates the inflammatory immune response through K11- RT linked ubiquitination of TAB1."; RL Cell Death Differ. 28:3077-3091(2021). RN [16] RP FUNCTION, AND INTERACTION WITH SOX2. RX PubMed=34732716; DOI=10.1038/s41467-021-26653-6; RA Mahlokozera T., Patel B., Chen H., Desouza P., Qu X., Mao D.D., Hafez D., RA Yang W., Taiwo R., Paturu M., Salehi A., Gujar A.D., Dunn G.P., RA Mosammaparast N., Petti A.A., Yano H., Kim A.H.; RT "Competitive binding of E3 ligases TRIM26 and WWP2 controls SOX2 in RT glioblastoma."; RL Nat. Commun. 12:6321-6321(2021). RN [17] RP FUNCTION. RX PubMed=36232914; DOI=10.3390/ijms231911613; RA Konis S.M.R., Hughes J.R., Parsons J.L.; RT "TRIM26 Maintains Cell Survival in Response to Oxidative Stress through RT Regulating DNA Glycosylase Stability."; RL Int. J. Mol. Sci. 23:0-0(2022). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY TYPE I INTERFERON. RX PubMed=35872575; DOI=10.1111/apt.17124; RA Luo M., Hou J., Mai H., Chen J., Chen H., Zhou B., Hou J., Jiang D.K.; RT "TRIM26 inhibits hepatitis B virus replication by promoting HBx degradation RT and TRIM26 genetic polymorphism predicts PegIFNalpha treatment response of RT HBeAg-positive chronic hepatitis B Patients."; RL Aliment. Pharmacol. Ther. 56:878-889(2022). CC -!- FUNCTION: E3 ubiquitin-protein ligase which regulates the IFN-beta CC production and antiviral response downstream of various DNA-encoded CC pattern-recognition receptors (PRRs). Plays also a central role in CC determining the response to different forms of oxidative stress by CC controlling levels of DNA glycosylases NEIL1, NEIL3 and NTH1 that are CC involved in repair of damaged DNA (PubMed:29610152, PubMed:36232914). CC Promotes nuclear IRF3 ubiquitination and proteasomal degradation CC (PubMed:25763818). Bridges together TBK1 and NEMO during the innate CC response to viral infection leading to the activation of TBK1. CC Positively regulates LPS-mediated inflammatory innate immune response CC by catalyzing the 'Lys-11'-linked polyubiquitination of TAB1 to enhance CC its activation and subsequent NF-kappa-B and MAPK signaling CC (PubMed:34017102). In a manner independent of its catalytic activity, CC inhibits WWP2, a SOX2-directed E3 ubiquitin ligase, and thus protects CC SOX2 from polyubiquitination and proteasomal degradation CC (PubMed:34732716). Ubiquitinates the histone acetyltransferase protein CC complex component PHF20 and thereby triggers its degradation in the CC nucleus after its recruitment by the histone demethylase KDM6B, serving CC as a scaffold protein (PubMed:23452852). Upon induction by TGF-beta, CC ubiquitinates the TFIID component TAF7 for proteasomal degradation CC (PubMed:29203640). Induces ferroptosis by ubiquitinating SLC7A11, a CC critical protein for lipid reactive oxygen species (ROS) scavenging (By CC similarity). Inhibits directly hepatitis B virus replication by CC mediating HBX ubiquitination and subsequent degradation CC (PubMed:35872575). {ECO:0000250|UniProtKB:Q99PN3, CC ECO:0000269|PubMed:23452852, ECO:0000269|PubMed:25763818, CC ECO:0000269|PubMed:26611359, ECO:0000269|PubMed:29203640, CC ECO:0000269|PubMed:29610152, ECO:0000269|PubMed:34017102, CC ECO:0000269|PubMed:34732716, ECO:0000269|PubMed:35872575, CC ECO:0000269|PubMed:36232914}. CC -!- FUNCTION: (Microbial infection) Promotes herpes simplex virus type CC 2/HHV-2 infection in vaginal epithelial cells by decreasing the nuclear CC localization of IRF3, the primary mediator of type I interferon CC activation. {ECO:0000269|PubMed:33419081}. 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:26611359, CC ECO:0000269|PubMed:29203640, ECO:0000269|PubMed:29610152, CC ECO:0000269|PubMed:34017102}; CC -!- SUBUNIT: Interacts with TBK1; this interaction bridges together TBK1 CC and NEMO in order to activate TBK1 (PubMed:26611359). Interacts with CC INCA1 (PubMed:21750715). {ECO:0000269|PubMed:21750715, CC ECO:0000269|PubMed:26611359}. CC -!- INTERACTION: CC Q12899; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2341136, EBI-10181188; CC Q12899; Q86UB2: BIVM; NbExp=3; IntAct=EBI-2341136, EBI-12191873; CC Q12899; O95208-2: EPN2; NbExp=3; IntAct=EBI-2341136, EBI-12135243; CC Q12899; I6L9I8: EPN3; NbExp=3; IntAct=EBI-2341136, EBI-12866582; CC Q12899; Q0VD86: INCA1; NbExp=2; IntAct=EBI-2341136, EBI-6509505; CC Q12899; O75367: MACROH2A1; NbExp=3; IntAct=EBI-2341136, EBI-2868511; CC Q12899; P43360: MAGEA6; NbExp=4; IntAct=EBI-2341136, EBI-1045155; CC Q12899; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-2341136, EBI-741515; CC Q12899; Q08117: TLE5; NbExp=3; IntAct=EBI-2341136, EBI-717810; CC Q12899; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2341136, EBI-11741437; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25763818, CC ECO:0000269|PubMed:34017102, ECO:0000269|PubMed:35872575}. Nucleus CC {ECO:0000269|PubMed:25763818, ECO:0000269|PubMed:33419081}. Note=Viral CC infection mediates TRIM26 nuclear translocation. CC {ECO:0000269|PubMed:25763818}. CC -!- INDUCTION: By cytokine TGF-beta and binding of activated SMAD3 to the CC TRIM26 promoter (PubMed:29203640). Upon herpes simplex virus type CC 2/HHV-2 infection (PubMed:33419081). By type I interferon CC (PubMed:35872575). {ECO:0000269|PubMed:29203640, CC ECO:0000269|PubMed:33419081, ECO:0000269|PubMed:35872575}. CC -!- PTM: Autoubiquitinates upon viral infection. In turn, autoubiquitinated CC TRIM26 recruits NEMO and bridges TBK1-NEMO interaction. CC {ECO:0000269|PubMed:26611359}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {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; U09825; AAA93131.1; -; mRNA. DR EMBL; BA000025; BAB63330.1; -; Genomic_DNA. DR EMBL; AB088090; BAC54923.1; -; Genomic_DNA. DR EMBL; AB202086; BAE78607.1; -; Genomic_DNA. DR EMBL; AB103596; BAF31258.1; -; Genomic_DNA. DR EMBL; AL844220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248419; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388382; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927189; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927221; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759838; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03272.1; -; Genomic_DNA. DR EMBL; BC024039; AAH24039.1; -; mRNA. DR EMBL; BC032297; AAH32297.1; -; mRNA. DR CCDS; CCDS4678.1; -. DR RefSeq; NP_001229712.1; NM_001242783.1. DR RefSeq; NP_003440.1; NM_003449.4. DR RefSeq; XP_005249431.1; XM_005249374.2. DR RefSeq; XP_005249432.1; XM_005249375.2. DR RefSeq; XP_005249433.1; XM_005249376.2. DR RefSeq; XP_005249434.1; XM_005249377.2. DR RefSeq; XP_005249435.1; XM_005249378.2. DR RefSeq; XP_006715243.1; XM_006715180.2. DR AlphaFoldDB; Q12899; -. DR SMR; Q12899; -. DR BioGRID; 113515; 197. DR DIP; DIP-52853N; -. DR IntAct; Q12899; 75. DR MINT; Q12899; -. DR STRING; 9606.ENSP00000410446; -. DR iPTMnet; Q12899; -. DR PhosphoSitePlus; Q12899; -. DR SwissPalm; Q12899; -. DR BioMuta; TRIM26; -. DR DMDM; 17380344; -. DR EPD; Q12899; -. DR jPOST; Q12899; -. DR MassIVE; Q12899; -. DR PaxDb; 9606-ENSP00000410446; -. DR PeptideAtlas; Q12899; -. DR ProteomicsDB; 59009; -. DR Pumba; Q12899; -. DR Antibodypedia; 26253; 150 antibodies from 22 providers. DR DNASU; 7726; -. DR Ensembl; ENST00000327357.9; ENSP00000331131.5; ENSG00000137313.15. DR Ensembl; ENST00000383607.6; ENSP00000373102.2; ENSG00000137313.15. DR Ensembl; ENST00000396558.5; ENSP00000379806.1; ENSG00000137313.15. DR Ensembl; ENST00000415923.6; ENSP00000415755.2; ENSG00000231002.7. DR Ensembl; ENST00000422349.5; ENSP00000396188.1; ENSG00000234046.7. DR Ensembl; ENST00000425523.5; ENSP00000393011.1; ENSG00000228881.7. DR Ensembl; ENST00000425831.5; ENSP00000394371.1; ENSG00000231641.9. DR Ensembl; ENST00000427535.5; ENSP00000398545.1; ENSG00000234046.7. DR Ensembl; ENST00000428486.5; ENSP00000414248.1; ENSG00000231002.7. DR Ensembl; ENST00000432326.5; ENSP00000407876.1; ENSG00000231641.9. DR Ensembl; ENST00000433314.5; ENSP00000402395.1; ENSG00000226060.7. DR Ensembl; ENST00000436219.5; ENSP00000390258.1; ENSG00000230230.7. DR Ensembl; ENST00000437089.5; ENSP00000395491.1; ENSG00000234127.9. DR Ensembl; ENST00000438384.5; ENSP00000416737.1; ENSG00000231641.9. DR Ensembl; ENST00000438908.5; ENSP00000409182.1; ENSG00000230230.7. DR Ensembl; ENST00000439094.6; ENSP00000389203.2; ENSG00000228881.7. DR Ensembl; ENST00000445259.6; ENSP00000407294.2; ENSG00000234046.7. DR Ensembl; ENST00000447711.6; ENSP00000408233.2; ENSG00000226060.7. DR Ensembl; ENST00000450392.5; ENSP00000394421.1; ENSG00000231002.7. DR Ensembl; ENST00000453195.5; ENSP00000391879.1; ENSG00000234127.9. DR Ensembl; ENST00000454678.7; ENSP00000410446.2; ENSG00000234127.9. DR Ensembl; ENST00000455000.6; ENSP00000392805.2; ENSG00000230230.7. DR Ensembl; ENST00000456093.5; ENSP00000406707.1; ENSG00000226060.7. DR Ensembl; ENST00000456770.5; ENSP00000415328.1; ENSG00000228881.7. DR GeneID; 7726; -. DR KEGG; hsa:7726; -. DR MANE-Select; ENST00000454678.7; ENSP00000410446.2; NM_003449.5; NP_003440.1. DR UCSC; uc003npr.3; human. DR AGR; HGNC:12962; -. DR CTD; 7726; -. DR DisGeNET; 7726; -. DR GeneCards; TRIM26; -. DR HGNC; HGNC:12962; TRIM26. DR HPA; ENSG00000234127; Low tissue specificity. DR MIM; 600830; gene. DR neXtProt; NX_Q12899; -. DR OpenTargets; ENSG00000234127; -. DR PharmGKB; PA37544; -. DR VEuPathDB; HostDB:ENSG00000234127; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000158668; -. DR HOGENOM; CLU_013137_0_3_1; -. DR InParanoid; Q12899; -. DR OMA; PFFWLNW; -. DR OrthoDB; 3453019at2759; -. DR PhylomeDB; Q12899; -. DR TreeFam; TF342569; -. DR PathwayCommons; Q12899; -. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; Q12899; -. DR SIGNOR; Q12899; -. DR BioGRID-ORCS; 7726; 8 hits in 1183 CRISPR screens. DR ChiTaRS; TRIM26; human. DR GenomeRNAi; 7726; -. DR Pharos; Q12899; Tbio. DR PRO; PR:Q12899; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q12899; Protein. DR Bgee; ENSG00000234127; Expressed in granulocyte and 106 other cell types or tissues. DR ExpressionAtlas; Q12899; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProt. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IDA:UniProt. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProt. DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProt. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB. DR CDD; cd19765; Bbox2_TRIM10-like; 1. DR CDD; cd16598; RING-HC_TRIM26_C-IV; 1. DR CDD; cd15826; SPRY_PRY_TRIM15; 1. DR Gene3D; 2.60.120.920; -; 2. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR003877; SPRY_dom. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1. DR PANTHER; PTHR24103:SF369; TRIPARTITE MOTIF-CONTAINING PROTEIN 26; 1. DR Pfam; PF13765; PRY; 1. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF15227; zf-C3HC4_4; 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; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q12899; HS. PE 1: Evidence at protein level; KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus; KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..539 FT /note="Tripartite motif-containing protein 26" FT /id="PRO_0000056235" FT DOMAIN 295..539 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT ZN_FING 16..57 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 97..138 FT /note="B box-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT REGION 376..437 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 188..227 FT /evidence="ECO:0000255" FT COMPBIAS 376..435 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 124 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT VARIANT 197 FT /note="Q -> H (in dbSNP:rs17194565)" FT /id="VAR_052138" FT MUTAGEN 16 FT /note="C->A: Strong loss of ubiquitination activity." FT /evidence="ECO:0000269|PubMed:34017102" SQ SEQUENCE 539 AA; 62166 MW; 842A71C41F2E2348 CRC64; MATSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT TDVRPISGSR PVCPLCKKPF KKENIRPVWQ LASLVENIER LKVDKGRQPG EVTREQQDAK LCERHREKLH YYCEDDGKLL CVMCRESREH RPHTAVLMEK AAQPHREKIL NHLSTLRRDR DKIQGFQAKG EADILAALKK LQDQRQYIVA EFEQGHQFLR EREEHLLEQL AKLEQELTEG REKFKSRGVG ELARLALVIS ELEGKAQQPA AELMQDTRDF LNRYPRKKFW VGKPIARVVK KKTGEFSDKL LSLQRGLREF QGKLLRDLEY KTVSVTLDPQ SASGYLQLSE DWKCVTYTSL YKSAYLHPQQ FDCEPGVLGS KGFTWGKVYW EVEVEREGWS EDEEEGDEEE EGEEEEEEEE AGYGDGYDDW ETDEDEESLG DEEEEEEEEE EEVLESCMVG VARDSVKRKG DLSLRPEDGV WALRLSSSGI WANTSPEAEL FPALRPRRVG IALDYEGGTV TFTNAESQEL IYTFTATFTR RLVPFLWLKW PGTRLLLRP //