TRI69_HUMAN
ID TRI69_HUMAN Reviewed; 500 AA.
AC Q86WT6; A8MX03; Q309B0; Q4G1A5; Q6W897; Q8IYY3; Q8WY16; Q8WY17;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM69;
DE EC=2.3.2.27;
DE AltName: Full=RFP-like domain-containing protein trimless;
DE AltName: Full=RING finger protein 36;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM69 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 69;
GN Name=TRIM69; Synonyms=RNF36; ORFNames=HSD-34, HSD34;
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] (ISOFORMS 3 AND 4).
RA Merla G., Zanaria E., Cairo S., Meroni G., Reymond A.;
RT "TRIMLESS defines a new class of RFP-like domain containing proteins.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Corcoran M., Lerner M., Sangfelt O., Grander D.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Fan M.M., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis related gene.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ASN-15 AND MET-161.
RC TISSUE=Brain, and 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 SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF CYS-61 AND CYS-64.
RX PubMed=23131556; DOI=10.1016/j.bbrc.2012.10.109;
RA Han Y., Li R., Gao J., Miao S., Wang L.;
RT "Characterisation of human RING finger protein TRIM69, a novel testis E3
RT ubiquitin ligase and its subcellular localisation.";
RL Biochem. Biophys. Res. Commun. 429:6-11(2012).
CC -!- FUNCTION: May have E3 ubiquitin-protein ligase activity. May play a
CC role in apoptosis. {ECO:0000269|PubMed:23131556}.
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: Interacts with PML. {ECO:0000250|UniProtKB:Q80X56}.
CC -!- INTERACTION:
CC Q86WT6; P08243: ASNS; NbExp=4; IntAct=EBI-749955, EBI-722989;
CC Q86WT6; P05496: ATP5MC1; NbExp=4; IntAct=EBI-749955, EBI-10194585;
CC Q86WT6; Q86TH3: DVL1; NbExp=3; IntAct=EBI-749955, EBI-10185025;
CC Q86WT6; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-749955, EBI-1752811;
CC Q86WT6; P68106: FKBP1B; NbExp=3; IntAct=EBI-749955, EBI-6693977;
CC Q86WT6; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-749955, EBI-2514791;
CC Q86WT6; Q6PHW0: IYD; NbExp=3; IntAct=EBI-749955, EBI-10253668;
CC Q86WT6; F5GWP8: KRT17; NbExp=3; IntAct=EBI-749955, EBI-10177711;
CC Q86WT6; Q659C4: LARP1B; NbExp=3; IntAct=EBI-749955, EBI-3940258;
CC Q86WT6; P43358: MAGEA4; NbExp=3; IntAct=EBI-749955, EBI-743122;
CC Q86WT6; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-749955, EBI-10194128;
CC Q86WT6; Q86SG6: NEK8; NbExp=3; IntAct=EBI-749955, EBI-1752987;
CC Q86WT6; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-749955, EBI-2557469;
CC Q86WT6; Q6P9E2: RECK; NbExp=3; IntAct=EBI-749955, EBI-10253121;
CC Q86WT6; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-749955, EBI-748350;
CC Q86WT6; Q15637: SF1; NbExp=3; IntAct=EBI-749955, EBI-744603;
CC Q86WT6; Q12874: SF3A3; NbExp=3; IntAct=EBI-749955, EBI-1051880;
CC Q86WT6; Q8N205: SYNE4; NbExp=3; IntAct=EBI-749955, EBI-7131783;
CC Q86WT6; Q96DX7: TRIM44; NbExp=3; IntAct=EBI-749955, EBI-8787399;
CC Q86WT6; Q6P088: ZNF483; NbExp=3; IntAct=EBI-749955, EBI-10196963;
CC Q86WT6-2; P01023: A2M; NbExp=3; IntAct=EBI-11525489, EBI-640741;
CC Q86WT6-2; P08319: ADH4; NbExp=3; IntAct=EBI-11525489, EBI-3927856;
CC Q86WT6-2; Q9BRQ8: AIFM2; NbExp=3; IntAct=EBI-11525489, EBI-3956936;
CC Q86WT6-2; P02768-3: ALB; NbExp=3; IntAct=EBI-11525489, EBI-25830928;
CC Q86WT6-2; P08243: ASNS; NbExp=3; IntAct=EBI-11525489, EBI-722989;
CC Q86WT6-2; P05496: ATP5MC1; NbExp=3; IntAct=EBI-11525489, EBI-10194585;
CC Q86WT6-2; P54253: ATXN1; NbExp=6; IntAct=EBI-11525489, EBI-930964;
CC Q86WT6-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-11525489, EBI-10988864;
CC Q86WT6-2; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-11525489, EBI-745073;
CC Q86WT6-2; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-11525489, EBI-2653038;
CC Q86WT6-2; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-11525489, EBI-12020542;
CC Q86WT6-2; P55212: CASP6; NbExp=3; IntAct=EBI-11525489, EBI-718729;
CC Q86WT6-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-11525489, EBI-25837549;
CC Q86WT6-2; P09172: DBH; NbExp=3; IntAct=EBI-11525489, EBI-8589586;
CC Q86WT6-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11525489, EBI-742054;
CC Q86WT6-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-11525489, EBI-10976677;
CC Q86WT6-2; Q16134: ETFDH; NbExp=3; IntAct=EBI-11525489, EBI-2870454;
CC Q86WT6-2; Q9BQ89: FAM110A; NbExp=6; IntAct=EBI-11525489, EBI-1752811;
CC Q86WT6-2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-11525489, EBI-719941;
CC Q86WT6-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11525489, EBI-6658203;
CC Q86WT6-2; P22607: FGFR3; NbExp=3; IntAct=EBI-11525489, EBI-348399;
CC Q86WT6-2; P68106-2: FKBP1B; NbExp=3; IntAct=EBI-11525489, EBI-11998976;
CC Q86WT6-2; P55040: GEM; NbExp=3; IntAct=EBI-11525489, EBI-744104;
CC Q86WT6-2; P14136: GFAP; NbExp=3; IntAct=EBI-11525489, EBI-744302;
CC Q86WT6-2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-11525489, EBI-1955541;
CC Q86WT6-2; P06396: GSN; NbExp=3; IntAct=EBI-11525489, EBI-351506;
CC Q86WT6-2; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-11525489, EBI-2514791;
CC Q86WT6-2; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-11525489, EBI-16429135;
CC Q86WT6-2; O14964: HGS; NbExp=6; IntAct=EBI-11525489, EBI-740220;
CC Q86WT6-2; P30519: HMOX2; NbExp=3; IntAct=EBI-11525489, EBI-712096;
CC Q86WT6-2; P01112: HRAS; NbExp=3; IntAct=EBI-11525489, EBI-350145;
CC Q86WT6-2; Q6PHW0: IYD; NbExp=3; IntAct=EBI-11525489, EBI-10253668;
CC Q86WT6-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-11525489, EBI-10975473;
CC Q86WT6-2; O14901: KLF11; NbExp=3; IntAct=EBI-11525489, EBI-948266;
CC Q86WT6-2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-11525489, EBI-6426443;
CC Q86WT6-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11525489, EBI-21591415;
CC Q86WT6-2; P02545: LMNA; NbExp=3; IntAct=EBI-11525489, EBI-351935;
CC Q86WT6-2; Q96S90: LYSMD1; NbExp=3; IntAct=EBI-11525489, EBI-10293291;
CC Q86WT6-2; P43358: MAGEA4; NbExp=3; IntAct=EBI-11525489, EBI-743122;
CC Q86WT6-2; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-11525489, EBI-18015780;
CC Q86WT6-2; P51608: MECP2; NbExp=3; IntAct=EBI-11525489, EBI-1189067;
CC Q86WT6-2; Q9H944: MED20; NbExp=3; IntAct=EBI-11525489, EBI-394644;
CC Q86WT6-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11525489, EBI-10172526;
CC Q86WT6-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-11525489, EBI-713665;
CC Q86WT6-2; Q86SG6: NEK8; NbExp=3; IntAct=EBI-11525489, EBI-1752987;
CC Q86WT6-2; P35240: NF2; NbExp=3; IntAct=EBI-11525489, EBI-1014472;
CC Q86WT6-2; P29474: NOS3; NbExp=3; IntAct=EBI-11525489, EBI-1391623;
CC Q86WT6-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11525489, EBI-741158;
CC Q86WT6-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-11525489, EBI-2811583;
CC Q86WT6-2; Q9Y2Y1: POLR3K; NbExp=3; IntAct=EBI-11525489, EBI-11023785;
CC Q86WT6-2; P62826: RAN; NbExp=3; IntAct=EBI-11525489, EBI-286642;
CC Q86WT6-2; Q6P9E2: RECK; NbExp=3; IntAct=EBI-11525489, EBI-10253121;
CC Q86WT6-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-11525489, EBI-726876;
CC Q86WT6-2; Q9UHP6: RSPH14; NbExp=5; IntAct=EBI-11525489, EBI-748350;
CC Q86WT6-2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11525489, EBI-2623095;
CC Q86WT6-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-11525489, EBI-5235340;
CC Q86WT6-2; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-11525489, EBI-725557;
CC Q86WT6-2; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-11525489, EBI-11958386;
CC Q86WT6-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-11525489, EBI-372899;
CC Q86WT6-2; P45379-11: TNNT2; NbExp=3; IntAct=EBI-11525489, EBI-17559309;
CC Q86WT6-2; Q86WT6-2: TRIM69; NbExp=4; IntAct=EBI-11525489, EBI-11525489;
CC Q86WT6-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11525489, EBI-12806590;
CC Q86WT6-2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-11525489, EBI-12040603;
CC Q86WT6-2; A0A1U9X8X8; NbExp=3; IntAct=EBI-11525489, EBI-17234977;
CC Q86WT6-2; Q9Y649; NbExp=3; IntAct=EBI-11525489, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23131556}. Nucleus
CC {ECO:0000269|PubMed:23131556}. Nucleus speckle
CC {ECO:0000269|PubMed:23131556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86WT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WT6-2; Sequence=VSP_023201;
CC Name=3; Synonyms=Trimless alpha;
CC IsoId=Q86WT6-3; Sequence=VSP_023200;
CC Name=4; Synonyms=Trimless beta;
CC IsoId=Q86WT6-4; Sequence=VSP_023200, VSP_023202;
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity and for nuclear localization and aggregation.
CC -!- PTM: Phosphorylated. Phosphorylation is necessary for nuclear
CC localization. {ECO:0000250|UniProtKB:Q80X56}.
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; AF302088; AAL55810.1; -; mRNA.
DR EMBL; AF302089; AAL55811.1; -; mRNA.
DR EMBL; DQ232883; ABB18376.1; -; mRNA.
DR EMBL; AY305385; AAQ75551.1; -; mRNA.
DR EMBL; AC122108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024199; AAH24199.1; ALT_TERM; mRNA.
DR EMBL; BC033314; AAH33314.1; -; mRNA.
DR EMBL; BC047945; AAH47945.1; -; mRNA.
DR CCDS; CCDS10114.1; -. [Q86WT6-2]
DR CCDS; CCDS32220.1; -. [Q86WT6-1]
DR CCDS; CCDS73719.1; -. [Q86WT6-3]
DR CCDS; CCDS76746.1; -. [Q86WT6-4]
DR RefSeq; NP_001288073.1; NM_001301144.1. [Q86WT6-3]
DR RefSeq; NP_001288074.1; NM_001301145.1. [Q86WT6-4]
DR RefSeq; NP_001288075.1; NM_001301146.1.
DR RefSeq; NP_542783.2; NM_080745.4. [Q86WT6-2]
DR RefSeq; NP_892030.3; NM_182985.4. [Q86WT6-1]
DR PDB; 4NQJ; X-ray; 2.15 A; A/B/C=143-321.
DR PDB; 6YXE; X-ray; 2.10 A; A/B=1-110.
DR PDBsum; 4NQJ; -.
DR PDBsum; 6YXE; -.
DR AlphaFoldDB; Q86WT6; -.
DR SMR; Q86WT6; -.
DR BioGRID; 126654; 76.
DR IntAct; Q86WT6; 88.
DR MINT; Q86WT6; -.
DR STRING; 9606.ENSP00000453177; -.
DR iPTMnet; Q86WT6; -.
DR PhosphoSitePlus; Q86WT6; -.
DR BioMuta; TRIM69; -.
DR DMDM; 229462760; -.
DR MassIVE; Q86WT6; -.
DR PaxDb; Q86WT6; -.
DR PeptideAtlas; Q86WT6; -.
DR PRIDE; Q86WT6; -.
DR ProteomicsDB; 70201; -. [Q86WT6-1]
DR ProteomicsDB; 70202; -. [Q86WT6-2]
DR ProteomicsDB; 70203; -. [Q86WT6-3]
DR ProteomicsDB; 70204; -. [Q86WT6-4]
DR TopDownProteomics; Q86WT6-2; -. [Q86WT6-2]
DR Antibodypedia; 24281; 326 antibodies from 35 providers.
DR DNASU; 140691; -.
DR Ensembl; ENST00000329464.9; ENSP00000332284.3; ENSG00000185880.13. [Q86WT6-1]
DR Ensembl; ENST00000338264.8; ENSP00000342922.4; ENSG00000185880.13. [Q86WT6-2]
DR Ensembl; ENST00000558329.5; ENSP00000453332.1; ENSG00000185880.13. [Q86WT6-4]
DR Ensembl; ENST00000559390.5; ENSP00000453177.1; ENSG00000185880.13. [Q86WT6-1]
DR Ensembl; ENST00000560442.5; ENSP00000453549.1; ENSG00000185880.13. [Q86WT6-3]
DR Ensembl; ENST00000618398.2; ENSP00000479720.1; ENSG00000278211.4. [Q86WT6-2]
DR Ensembl; ENST00000631740.1; ENSP00000488341.1; ENSG00000278211.4. [Q86WT6-4]
DR Ensembl; ENST00000633106.1; ENSP00000488084.1; ENSG00000278211.4. [Q86WT6-3]
DR GeneID; 140691; -.
DR KEGG; hsa:140691; -.
DR MANE-Select; ENST00000329464.9; ENSP00000332284.3; NM_182985.5; NP_892030.3.
DR UCSC; uc001zuf.3; human. [Q86WT6-1]
DR CTD; 140691; -.
DR DisGeNET; 140691; -.
DR GeneCards; TRIM69; -.
DR HGNC; HGNC:17857; TRIM69.
DR HPA; ENSG00000185880; Tissue enriched (testis).
DR MIM; 616017; gene.
DR neXtProt; NX_Q86WT6; -.
DR OpenTargets; ENSG00000185880; -.
DR PharmGKB; PA162407010; -.
DR VEuPathDB; HostDB:ENSG00000185880; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160707; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q86WT6; -.
DR OMA; GNYVEMN; -.
DR OrthoDB; 631080at2759; -.
DR PhylomeDB; Q86WT6; -.
DR TreeFam; TF342569; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q86WT6; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q86WT6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140691; 3 hits in 1109 CRISPR screens.
DR ChiTaRS; TRIM69; human.
DR GenomeRNAi; 140691; -.
DR Pharos; Q86WT6; Tbio.
DR PRO; PR:Q86WT6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q86WT6; protein.
DR Bgee; ENSG00000185880; Expressed in granulocyte and 111 other tissues.
DR ExpressionAtlas; Q86WT6; baseline and differential.
DR Genevisible; Q86WT6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..500
FT /note="E3 ubiquitin-protein ligase TRIM69"
FT /id="PRO_0000278236"
FT DOMAIN 305..500
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 41..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..152
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT COILED 161..255
FT /evidence="ECO:0000255"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BK82"
FT VAR_SEQ 1..204
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023200"
FT VAR_SEQ 3..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023201"
FT VAR_SEQ 255..271
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023202"
FT VARIANT 12
FT /note="D -> N (in dbSNP:rs2444007)"
FT /id="VAR_057226"
FT VARIANT 15
FT /note="D -> N (in dbSNP:rs2470911)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057227"
FT VARIANT 31
FT /note="V -> A (in dbSNP:rs3759880)"
FT /id="VAR_030704"
FT VARIANT 104
FT /note="K -> R (in dbSNP:rs17588988)"
FT /id="VAR_057228"
FT VARIANT 161
FT /note="T -> M (in dbSNP:rs3100139)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057229"
FT VARIANT 190
FT /note="A -> V (in dbSNP:rs3759880)"
FT /id="VAR_057230"
FT MUTAGEN 61
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity;
FT when associated with A-64."
FT /evidence="ECO:0000269|PubMed:23131556"
FT MUTAGEN 64
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity;
FT when associated with A-61."
FT /evidence="ECO:0000269|PubMed:23131556"
FT CONFLICT 469
FT /note="S -> G (in Ref. 3; AAQ75551)"
FT /evidence="ECO:0000305"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:6YXE"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6YXE"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6YXE"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6YXE"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6YXE"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:6YXE"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6YXE"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6YXE"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:6YXE"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:4NQJ"
FT HELIX 153..260
FT /evidence="ECO:0007829|PDB:4NQJ"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:4NQJ"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:4NQJ"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:4NQJ"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:4NQJ"
SQ SEQUENCE 500 AA; 57419 MW; E9957652895213B3 CRC64;
MEVSTNPSSN IDPGDYVEMN DSITHLPSKV VIQDITMELH CPLCNDWFRD PLMLSCGHNF
CEACIQDFWR LQAKETFCPE CKMLCQYNNC TFNPVLDKLV EKIKKLPLLK GHPQCPEHGE
NLKLFSKPDG KLICFQCKDA RLSVGQSKEF LQISDAVHFF TEELAIQQGQ LETTLKELQT
LRNMQKEAIA AHKENKLHLQ QHVSMEFLKL HQFLHSKEKD ILTELREEGK ALNEEMELNL
SQLQEQCLLA KDMLVSIQAK TEQQNSFDFL KDITTLLHSL EQGMKVLATR ELISRKLNLG
QYKGPIQYMV WREMQDTLCP GLSPLTLDPK TAHPNLVLSK SQTSVWHGDI KKIMPDDPER
FDSSVAVLGS RGFTSGKWYW EVEVAKKTKW TVGVVRESII RKGSCPLTPE QGFWLLRLRN
QTDLKALDLP SFSLTLTNNL DKVGIYLDYE GGQLSFYNAK TMTHIYTFSN TFMEKLYPYF
CPCLNDGGEN KEPLHILHPQ
