ID TRIM9_HUMAN Reviewed; 710 AA. AC Q9C026; D3DSB7; D3DSB8; Q92557; Q96D24; Q96NI4; Q9C025; Q9C027; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 28-JAN-2026, entry version 216. DE RecName: Full=E3 ubiquitin-protein ligase TRIM9; DE EC=2.3.2.27 {ECO:0000269|PubMed:20085810}; DE AltName: Full=RING finger protein 91; DE AltName: Full=RING-type E3 ubiquitin transferase TRIM9 {ECO:0000305}; DE AltName: Full=Tripartite motif-containing protein 9; GN Name=TRIM9; Synonyms=KIAA0282, RNF91; 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), AND VARIANT PHE-653. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-653. RC TISSUE=Brain; RX PubMed=9179496; DOI=10.1093/dnares/4.1.53; RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., RA Nomura N.; RT "Construction and characterization of human brain cDNA libraries suitable RT for analysis of cDNA clones encoding relatively large proteins."; RL DNA Res. 4:53-59(1997). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Fetal brain; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND VARIANT RP PHE-653. RC TISSUE=Brain, and Uterus; 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCALIZATION, TISSUE RP SPECIFICITY, AND AUTOUBIQUITINATION. RX PubMed=20085810; DOI=10.1016/j.nbd.2010.01.007; RA Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K.; RT "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the RT brain of Parkinson's disease and dementia with Lewy bodies."; RL Neurobiol. Dis. 38:210-218(2010). RN [8] RP STRUCTURE BY NMR OF 437-534. RG RIKEN structural genomics initiative (RSGI); RT "Solution structures of the FN3 domain of human tripartite motif protein RT 9."; RL Submitted (JUN-2006) to the PDB data bank. CC -!- FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in CC cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting CC signal for proteasomal degradation. May play a role in regulation of CC neuronal functions and may also participate in the formation or CC breakdown of abnormal inclusions in neurodegenerative disorders. May CC act as a regulator of synaptic vesicle exocytosis by controlling the CC availability of SNAP25 for the SNARE complex formation. CC {ECO:0000269|PubMed:20085810}. 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:20085810}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:20085810}. CC -!- SUBUNIT: Interacts with SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}. CC -!- INTERACTION: CC Q9C026; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-720828, EBI-2371151; CC Q9C026; P05067: APP; NbExp=3; IntAct=EBI-720828, EBI-77613; CC Q9C026; P54253: ATXN1; NbExp=6; IntAct=EBI-720828, EBI-930964; CC Q9C026; B7Z3H4: BTRC; NbExp=3; IntAct=EBI-720828, EBI-16429269; CC Q9C026; Q9Y297: BTRC; NbExp=8; IntAct=EBI-720828, EBI-307461; CC Q9C026; P48730: CSNK1D; NbExp=3; IntAct=EBI-720828, EBI-751621; CC Q9C026; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-720828, EBI-5453285; CC Q9C026; Q9UI08: EVL; NbExp=3; IntAct=EBI-720828, EBI-346653; CC Q9C026; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-720828, EBI-6448852; CC Q9C026; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-720828, EBI-11986315; CC Q9C026; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-720828, EBI-6658203; CC Q9C026; Q969S9: GFM2; NbExp=3; IntAct=EBI-720828, EBI-2371750; CC Q9C026; O60333-2: KIF1B; NbExp=3; IntAct=EBI-720828, EBI-10975473; CC Q9C026; Q969V5: MUL1; NbExp=3; IntAct=EBI-720828, EBI-744120; CC Q9C026; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-720828, EBI-10271199; CC Q9C026; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-720828, EBI-741158; CC Q9C026; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-720828, EBI-742688; CC Q9C026; Q13148: TARDBP; NbExp=6; IntAct=EBI-720828, EBI-372899; CC Q9C026; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-720828, EBI-3918381; CC Q9C026; Q68CQ4: UTP25; NbExp=3; IntAct=EBI-720828, EBI-747711; CC Q9C026; P50552: VASP; NbExp=4; IntAct=EBI-720828, EBI-748201; CC Q9C026; P62258: YWHAE; NbExp=2; IntAct=EBI-720828, EBI-356498; CC Q9C026-5; A0A0S2Z507: BTRC; NbExp=3; IntAct=EBI-16437499, EBI-16429247; CC Q9C026-5; B7Z3H4: BTRC; NbExp=3; IntAct=EBI-16437499, EBI-16429269; CC Q9C026-5; Q9Y297: BTRC; NbExp=4; IntAct=EBI-16437499, EBI-307461; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20085810}. Cell CC projection, dendrite {ECO:0000269|PubMed:20085810}. Cytoplasmic CC vesicle, secretory vesicle, synaptic vesicle CC {ECO:0000250|UniProtKB:Q91ZY8}. Synapse {ECO:0000250|UniProtKB:Q91ZY8}. CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZY8}. Note=Enriched CC at synaptic terminals where it exists in a soluble form and a synaptic CC vesicle-associated form. Associated with the cytoskeleton (By CC similarity). Found in proximal dendrites of pyramidal neurons in the CC cerebral cortex and hippocampus, and Purkinje cells in the cerebellum CC (PubMed:20085810). {ECO:0000250|UniProtKB:Q91ZY8, CC ECO:0000269|PubMed:20085810}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Beta; CC IsoId=Q9C026-1; Sequence=Displayed; CC Name=4; CC IsoId=Q9C026-4; Sequence=VSP_007922, VSP_007923, VSP_007924; CC Name=5; CC IsoId=Q9C026-5; Sequence=VSP_007925, VSP_007926; CC -!- TISSUE SPECIFICITY: Brain. Highly expressed in the cerebral cortex (at CC protein level). Severely decreased in the affected brain areas in CC Parkinson disease and dementia with Lewy bodies. CC {ECO:0000269|PubMed:20085810}. CC -!- DOMAIN: The coiled coil domain mediates the interaction with the N- CC terminal t-SNARE domain of SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}. CC -!- PTM: Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas CC it is monoubiquitinated in vitro. {ECO:0000269|PubMed:20085810}. CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a competing donor splice CC site, to exon inclusion and to intron retention. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG53490.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG53492.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA13398.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA13398.2; Type=Frameshift; 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; AF220036; AAG53490.1; ALT_FRAME; mRNA. DR EMBL; AF220037; AAG53491.1; -; mRNA. DR EMBL; AF220038; AAG53492.1; ALT_FRAME; mRNA. DR EMBL; D87458; BAA13398.2; ALT_SEQ; mRNA. DR EMBL; AK055388; BAB70913.1; -; mRNA. DR EMBL; CH471078; EAW65680.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65681.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65682.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65684.1; -; Genomic_DNA. DR EMBL; BC013414; AAH13414.1; -; mRNA. DR EMBL; BC063872; AAH63872.1; -; mRNA. DR CCDS; CCDS45105.1; -. [Q9C026-5] DR CCDS; CCDS9703.1; -. [Q9C026-1] DR RefSeq; NP_055978.4; NM_015163.5. [Q9C026-1] DR RefSeq; NP_443210.1; NM_052978.5. [Q9C026-5] DR RefSeq; XP_011534691.1; XM_011536389.3. [Q9C026-4] DR RefSeq; XP_054231290.1; XM_054375315.1. [Q9C026-4] DR RefSeq; XP_054231294.1; XM_054375319.1. [Q9C026-1] DR RefSeq; XP_054231300.1; XM_054375325.1. [Q9C026-5] DR PDB; 2DB8; NMR; -; A=439-534. DR PDB; 7B2S; X-ray; 1.50 A; A=535-710. DR PDBsum; 2DB8; -. DR PDBsum; 7B2S; -. DR AlphaFoldDB; Q9C026; -. DR BMRB; Q9C026; -. DR SMR; Q9C026; -. DR BioGRID; 125280; 412. DR FunCoup; Q9C026; 729. DR IntAct; Q9C026; 65. DR MINT; Q9C026; -. DR STRING; 9606.ENSP00000298355; -. DR iPTMnet; Q9C026; -. DR PhosphoSitePlus; Q9C026; -. DR BioMuta; TRIM9; -. DR DMDM; 33516964; -. DR REPRODUCTION-2DPAGE; Q9C026; -. DR jPOST; Q9C026; -. DR MassIVE; Q9C026; -. DR PaxDb; 9606-ENSP00000298355; -. DR PeptideAtlas; Q9C026; -. DR ProteomicsDB; 79943; -. [Q9C026-1] DR ProteomicsDB; 79944; -. [Q9C026-4] DR ProteomicsDB; 79945; -. [Q9C026-5] DR Pumba; Q9C026; -. DR Antibodypedia; 10667; 507 antibodies from 25 providers. DR DNASU; 114088; -. DR Ensembl; ENST00000298355.7; ENSP00000298355.3; ENSG00000100505.15. [Q9C026-1] DR Ensembl; ENST00000338969.9; ENSP00000342970.5; ENSG00000100505.15. [Q9C026-4] DR Ensembl; ENST00000360392.4; ENSP00000353561.4; ENSG00000100505.15. [Q9C026-5] DR GeneID; 114088; -. DR KEGG; hsa:114088; -. DR UCSC; uc001wyx.5; human. [Q9C026-1] DR AGR; HGNC:16288; -. DR ClinPGx; PA38116; -. DR CTD; 114088; -. DR DisGeNET; 114088; -. DR GeneCards; TRIM9; -. DR HGNC; HGNC:16288; TRIM9. DR HPA; ENSG00000100505; Tissue enriched (brain). DR MIM; 606555; gene. DR OpenTargets; ENSG00000100505; -. DR VEuPathDB; HostDB:ENSG00000100505; -. DR eggNOG; KOG4367; Eukaryota. DR GeneTree; ENSGT00940000154071; -. DR HOGENOM; CLU_013137_19_2_1; -. DR InParanoid; Q9C026; -. DR OMA; PDTICTI; -. DR OrthoDB; 295536at2759; -. DR PAN-GO; Q9C026; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9C026; -. DR PathwayCommons; Q9C026; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9C026; -. DR SIGNOR; Q9C026; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000100505; -. DR BioGRID-ORCS; 114088; 32 hits in 1186 CRISPR screens. DR ChiTaRS; TRIM9; human. DR EvolutionaryTrace; Q9C026; -. DR GeneWiki; TRIM9; -. DR GenomeRNAi; 114088; -. DR Pharos; Q9C026; Tbio. DR PRO; PR:Q9C026; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9C026; protein. DR Bgee; ENSG00000100505; Expressed in right hemisphere of cerebellum and 145 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR CDD; cd19843; Bbox1_TRIM9_C-I; 1. DR CDD; cd19826; Bbox2_TRIM9_C-I; 1. DR CDD; cd00063; FN3; 1. DR CDD; cd16755; RING-HC_TRIM9; 1. DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1. DR FunFam; 2.60.120.920:FF:000009; E3 ubiquitin-protein ligase TRIM9 isoform X1; 1. DR FunFam; 2.60.40.10:FF:000178; E3 ubiquitin-protein ligase TRIM9 isoform X1; 1. DR FunFam; 3.30.40.10:FF:000168; E3 ubiquitin-protein ligase TRIM9 isoform X1; 1. DR FunFam; 4.10.830.40:FF:000001; E3 ubiquitin-protein ligase TRIM9 isoform X1; 1. DR FunFam; 3.30.160.60:FF:000329; E3 ubiquitin-protein ligase TRIM9 isoform X2; 1. DR FunFam; 1.20.5.170:FF:000017; Putative E3 ubiquitin-protein ligase TRIM9; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 2.60.120.920; -; 1. DR Gene3D; 4.10.830.40; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR003649; Bbox_C. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR017903; COS_domain. DR InterPro; IPR050617; E3_ligase_FN3/SPRY. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003877; SPRY_dom. DR InterPro; IPR049582; TRIM9_Bbox1. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1. DR PANTHER; PTHR24099:SF13; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1. DR Pfam; PF22586; ANCHR-like_BBOX; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 2. DR SMART; SM00060; FN3; 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; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS51262; COS; 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50119; ZF_BBOX; 2. 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; Cell projection; Coiled coil; KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Metal-binding; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW Synapse; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..710 FT /note="E3 ubiquitin-protein ligase TRIM9" FT /id="PRO_0000056208" FT DOMAIN 374..432 FT /note="COS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586" FT DOMAIN 440..535 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 533..702 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT ZN_FING 10..50 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 163..212 FT /note="B box-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT ZN_FING 224..266 FT /note="B box-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT COILED 273..340 FT /evidence="ECO:0000255" FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 193 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 232 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT MOD_RES 41 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8C7M3" FT MOD_RES 44 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C7M3" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C7M3" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C7M3" FT VAR_SEQ 436..439 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_007922" FT VAR_SEQ 534 FT /note="E -> EDTDSEEQTLPFPVPSERLPLRRMSPFSSTLNLQPSFPGRSYFDFRS FT SPHQLSLHSSLQSLNAPGCNFETQSAPYSQLVDIKKLLA (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_007923" FT VAR_SEQ 535..550 FT /note="VAWFAFDPGSAHSDII -> GKALQQYPSERELRGI (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007925" FT VAR_SEQ 551..710 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007926" FT VAR_SEQ 692..710 FT /note="TLHTGLPVPDFYSSRASIA -> STLPLRLNSCCWLPVQRLPRAVQSNRREG FT S (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_007924" FT VARIANT 653 FT /note="L -> F (in dbSNP:rs2275462)" FT /evidence="ECO:0000269|PubMed:11331580, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9179496" FT /id="VAR_016202" FT CONFLICT 314 FT /note="A -> V (in Ref. 2; BAB70913)" FT /evidence="ECO:0000305" FT CONFLICT 384 FT /note="Q -> R (in Ref. 2; BAB70913)" FT /evidence="ECO:0000305" FT STRAND 454..460 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 473..479 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 488..494 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 498..501 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:2DB8" FT STRAND 510..516 FT /evidence="ECO:0007829|PDB:2DB8" FT HELIX 542..544 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 549..552 FT /evidence="ECO:0007829|PDB:7B2S" FT TURN 553..556 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 557..564 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 566..571 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 576..588 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 595..599 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 622..629 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 632..638 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 646..652 FT /evidence="ECO:0007829|PDB:7B2S" FT TURN 653..656 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 657..662 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 679..685 FT /evidence="ECO:0007829|PDB:7B2S" FT STRAND 689..694 FT /evidence="ECO:0007829|PDB:7B2S" SQ SEQUENCE 710 AA; 79177 MW; AEAB24807C89D0E2 CRC64; MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA //