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, 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};
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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 Genevisible; Q96F44; HS.
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.
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
//
