ID TRI11_HUMAN Reviewed; 468 AA. AC Q96F44; A6NKE2; B2RB82; B3KUS3; B4DX88; Q5VSU1; Q8NCA6; Q9C022; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=E3 ubiquitin-protein ligase TRIM11; DE EC=2.3.2.27 {ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:27498865}; DE AltName: Full=Protein BIA1 {ECO:0000303|Ref.1}; DE AltName: Full=RING finger protein 92; DE AltName: Full=Tripartite motif-containing protein 11 {ECO:0000303|PubMed:16904669}; GN Name=TRIM11 {ECO:0000303|PubMed:16904669, GN ECO:0000312|HGNC:HGNC:16281}; GN Synonyms=RNF92 {ECO:0000312|HGNC:HGNC:16281}; 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). RC TISSUE=Placenta; RA Piecha D., Petersohn D., Eckes B., Krieg T.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 97-468 (ISOFORM 3). RC TISSUE=Fetal brain, Teratocarcinoma, and Testis; 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 395-468 (ISOFORM 1), AND INTERACTION WITH RP INTEGRIN ALPHA-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 [6] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION. RX PubMed=16904669; DOI=10.1016/j.febslet.2006.07.066; RA Ishikawa H., Tachikawa H., Miura Y., Takahashi N.; RT "TRIM11 binds to and destabilizes a key component of the activator-mediated RT cofactor complex (ARC105) through the ubiquitin-proteasome system."; RL FEBS Lett. 580:4784-4792(2006). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18248090; DOI=10.1371/journal.ppat.0040016; RA Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W.; RT "TRIM E3 ligases interfere with early and late stages of the retroviral RT life cycle."; RL PLoS Pathog. 4:E16-E16(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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 [9] RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, INTERACTION WITH RP AIM2 AND SQSTM1, AND MUTAGENESIS OF CYS-53; CYS-56; LYS-169; LYS-366 AND RP LYS-458. RX PubMed=27498865; DOI=10.1016/j.celrep.2016.07.019; RA Liu T., Tang Q., Liu K., Xie W., Liu X., Wang H., Wang R.F., Cui J.; RT "TRIM11 suppresses AIM2 inflammasome by degrading AIM2 via p62-dependent RT selective autophagy."; RL Cell Rep. 16:1988-2002(2016). CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of CC insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln CC repeat expanded HTT and poly-Ala repeat expanded ARX (By similarity). CC Mediates PAX6 ubiquitination leading to proteasomal degradation, CC thereby modulating cortical neurogenesis (By similarity). May also CC inhibit PAX6 transcriptional activity, possibly in part by preventing CC the binding of PAX6 to its consensus sequences (By similarity). May CC contribute to the regulation of the intracellular level of HN (humanin) CC or HN-containing proteins through the proteasomal degradation pathway CC (By similarity). Mediates MED15 ubiquitination leading to proteasomal CC degradation (PubMed:16904669). May contribute to the innate restriction CC of retroviruses (PubMed:18248090). Upon overexpression, reduces HIV-1 CC and murine leukemia virus infectivity, by suppressing viral gene CC expression (PubMed:18248090). Antiviral activity depends on a CC functional E3 ubiquitin-protein ligase domain (PubMed:18248090). May CC regulate TRIM5 turnover via the proteasome pathway, thus counteracting CC the TRIM5-mediated cross-species restriction of retroviral infection at CC early stages of the retroviral life cycle (PubMed:18248090). Acts as an CC inhibitor of the AIM2 inflammasome by promoting autophagy-dependent CC degradation of AIM2 (PubMed:27498865). Mechanistically, undergoes CC autoubiquitination upon DNA stimulation, promoting interaction with CC AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes CC (PubMed:27498865). {ECO:0000250|UniProtKB:Q99PQ2, CC ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:18248090, CC ECO:0000269|PubMed:27498865}. 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:16904669, CC ECO:0000269|PubMed:27498865}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:27498865}. CC -!- SUBUNIT: Binds cytoplasmic tail of integrin alpha-1 (PubMed:11331580). CC Interacts with the HN peptide (By similarity). Interacts with PHOX2B CC (By similarity). Interacts (when autoubiquitinated) with SQSTM1/p62; CC promoting AIM2 recruitment to autophagosomes (PubMed:27498865). CC Interacts with AIM2; promoting its autophagy-dependent degradation CC (PubMed:27498865). {ECO:0000250|UniProtKB:Q99PQ2, CC ECO:0000269|PubMed:11331580, ECO:0000269|PubMed:27498865}. CC -!- INTERACTION: CC Q96F44; Q96RN5: MED15; NbExp=5; IntAct=EBI-851809, EBI-394506; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16904669, CC ECO:0000269|PubMed:18248090}. Nucleus {ECO:0000269|PubMed:16904669}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96F44-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96F44-2; Sequence=VSP_012057, VSP_012058; CC Name=3; CC IsoId=Q96F44-3; Sequence=VSP_039628; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305|PubMed:16904669}. CC -!- DOMAIN: The coiled-coil domain and the B30.2 domain are both necessary CC for interaction with HN and PAX6 (By similarity). They are also CC involved in MED15-binding (PubMed:16904669). CC {ECO:0000250|UniProtKB:Q99PQ2, ECO:0000269|PubMed:16904669}. CC -!- DOMAIN: The B30.2 domain may be involved cellular protein quality CC control by promoting the degradation of insoluble ubiquitinated CC proteins. {ECO:0000250|UniProtKB:Q99PQ2}. CC -!- PTM: Autoubiquitinated upon DNA stimulation; autoubiquitination at Lys- CC 458 promotes interaction with SQSTM1/p62 and recruitment of AIM2 to CC autophagosomes. {ECO:0000269|PubMed:27498865}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH11629.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG53535.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG63300.1; 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; AF327056; AAM63957.1; -; mRNA. DR EMBL; AK074866; BAC11254.1; -; mRNA. DR EMBL; AK314539; BAG37129.1; -; mRNA. DR EMBL; AK097825; BAG53535.1; ALT_INIT; mRNA. DR EMBL; AK301859; BAG63300.1; ALT_INIT; mRNA. DR EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011629; AAH11629.1; ALT_INIT; mRNA. DR EMBL; BC069227; AAH69227.1; -; mRNA. DR EMBL; AF220125; AAG53498.1; -; mRNA. DR CCDS; CCDS31048.1; -. [Q96F44-1] DR RefSeq; NP_660215.1; NM_145214.2. [Q96F44-1] DR RefSeq; XP_016857901.1; XM_017002412.1. [Q96F44-3] DR PDB; 7QS1; X-ray; 1.93 A; A/B=277-461. DR PDBsum; 7QS1; -. DR AlphaFoldDB; Q96F44; -. DR SMR; Q96F44; -. DR BioGRID; 123523; 182. DR IntAct; Q96F44; 62. DR MINT; Q96F44; -. DR STRING; 9606.ENSP00000284551; -. DR iPTMnet; Q96F44; -. DR PhosphoSitePlus; Q96F44; -. DR BioMuta; TRIM11; -. DR DMDM; 26400672; -. DR EPD; Q96F44; -. DR jPOST; Q96F44; -. DR MassIVE; Q96F44; -. DR MaxQB; Q96F44; -. DR PaxDb; 9606-ENSP00000284551; -. DR PeptideAtlas; Q96F44; -. DR ProteomicsDB; 76490; -. [Q96F44-1] DR ProteomicsDB; 76491; -. [Q96F44-2] DR ProteomicsDB; 76492; -. [Q96F44-3] DR Pumba; Q96F44; -. DR TopDownProteomics; Q96F44-1; -. [Q96F44-1] DR Antibodypedia; 34665; 294 antibodies from 30 providers. DR DNASU; 81559; -. DR Ensembl; ENST00000284551.11; ENSP00000284551.6; ENSG00000154370.16. [Q96F44-1] DR Ensembl; ENST00000366699.3; ENSP00000355660.3; ENSG00000154370.16. [Q96F44-2] DR GeneID; 81559; -. DR KEGG; hsa:81559; -. DR MANE-Select; ENST00000284551.11; ENSP00000284551.6; NM_145214.3; NP_660215.1. DR UCSC; uc001hss.4; human. [Q96F44-1] DR AGR; HGNC:16281; -. DR CTD; 81559; -. DR DisGeNET; 81559; -. DR GeneCards; TRIM11; -. DR HGNC; HGNC:16281; TRIM11. DR HPA; ENSG00000154370; Tissue enhanced (brain). DR MIM; 607868; gene. DR neXtProt; NX_Q96F44; -. DR OpenTargets; ENSG00000154370; -. DR PharmGKB; PA38112; -. DR VEuPathDB; HostDB:ENSG00000154370; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000160371; -. DR HOGENOM; CLU_013137_0_3_1; -. DR InParanoid; Q96F44; -. DR OMA; RECIGRC; -. DR OrthoDB; 3453019at2759; -. DR PhylomeDB; Q96F44; -. DR TreeFam; TF338674; -. DR PathwayCommons; Q96F44; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q96F44; -. DR SIGNOR; Q96F44; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 81559; 18 hits in 1197 CRISPR screens. DR GeneWiki; TRIM11; -. DR GenomeRNAi; 81559; -. DR Pharos; Q96F44; Tbio. DR PRO; PR:Q96F44; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96F44; Protein. DR Bgee; ENSG00000154370; Expressed in cerebellar hemisphere and 165 other cell types or tissues. DR ExpressionAtlas; Q96F44; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB. DR GO; GO:0140972; P:negative regulation of AIM2 inflammasome complex assembly; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB. DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB. DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProt. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB. DR CDD; cd19766; Bbox2_TRIM11_C-IV; 1. DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1. DR CDD; cd15811; SPRY_PRY_TRIM11; 1. DR Gene3D; 2.60.120.920; -; 1. 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 InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1. DR PANTHER; PTHR24103:SF648; E3 UBIQUITIN-PROTEIN LIGASE TRIM11; 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; 1. DR SUPFAM; SSF57850; RING/U-box; 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. DR Genevisible; Q96F44; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Coiled coil; KW Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT CHAIN 1..468 FT /note="E3 ubiquitin-protein ligase TRIM11" FT /id="PRO_0000056215" FT DOMAIN 268..461 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 87..128 FT /note="B box-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT COILED 129..208 FT /evidence="ECO:0000255" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 458 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:27498865" FT VAR_SEQ 169 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039628" FT VAR_SEQ 288..385 FT /note="DVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTS FT GRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGS -> RCGGPRWGD FT DSRRGPAKDLGSQPRVLCPATASSKLTVSWWWVVGKTSSAHTSDISCVGIFTPNNSSTS FT GNELGIQGFHSALNRIASADTTGVSTDPTD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012057" FT VAR_SEQ 386..468 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012058" FT MUTAGEN 53 FT /note="C->A: Abolished E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:27498865" FT MUTAGEN 56 FT /note="C->A: Abolished E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:27498865" FT MUTAGEN 169 FT /note="K->R: Does not affect autoubiquitination." FT /evidence="ECO:0000269|PubMed:27498865" FT MUTAGEN 366 FT /note="K->R: Does not affect autoubiquitination." FT /evidence="ECO:0000269|PubMed:27498865" FT MUTAGEN 458 FT /note="K->R: Reduced autoubiquitination, leading to abolish FT interaction with SQSTM1/p62." FT /evidence="ECO:0000269|PubMed:27498865" FT CONFLICT 234 FT /note="G -> D (in Ref. 2; BAG53535)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="Q -> R (in Ref. 2; BAG37129)" FT /evidence="ECO:0000305" FT CONFLICT 289 FT /note="V -> M (in Ref. 2; BAG53535)" FT /evidence="ECO:0000305" FT CONFLICT 319 FT /note="P -> S (in Ref. 2; BAG53535)" FT /evidence="ECO:0000305" FT CONFLICT 395..398 FT /note="APLR -> GSIP (in Ref. 5; AAG53498)" FT /evidence="ECO:0000305" FT CONFLICT 467 FT /note="P -> A (in Ref. 5; AAG53498)" FT /evidence="ECO:0000305" FT HELIX 278..282 FT /evidence="ECO:0007829|PDB:7QS1" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:7QS1" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 337..347 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 354..360 FT /evidence="ECO:0007829|PDB:7QS1" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 391..398 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 402..409 FT /evidence="ECO:0007829|PDB:7QS1" FT TURN 410..413 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 414..419 FT /evidence="ECO:0007829|PDB:7QS1" FT TURN 420..423 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 424..428 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 438..444 FT /evidence="ECO:0007829|PDB:7QS1" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:7QS1" SQ SEQUENCE 468 AA; 52774 MW; 8DE4BDF79F221739 CRC64; MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQKM VESQRQNVLG EFERLRRLLA EEEQQLLQRL EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA LGLLQDIKDA LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD RTSWALGVCR ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP PRRVGIFLDY EAGHLSFYSA TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT PMTICRPKGG SGDTLAPQ //