ID TRI13_HUMAN Reviewed; 407 AA. AC O60858; B2RB49; Q5UBW0; Q5W0U8; Q5W0U9; Q9BQ47; Q9C021; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 16-JAN-2019, entry version 175. DE RecName: Full=E3 ubiquitin-protein ligase TRIM13; DE EC=2.3.2.27; DE AltName: Full=B-cell chronic lymphocytic leukemia tumor suppressor Leu5; DE AltName: Full=Leukemia-associated protein 5; DE AltName: Full=Putative tumor suppressor RFP2; DE AltName: Full=RING finger protein 77; DE AltName: Full=RING-type E3 ubiquitin transferase TRIM13 {ECO:0000305}; DE AltName: Full=Ret finger protein 2; DE AltName: Full=Tripartite motif-containing protein 13; GN Name=TRIM13; Synonyms=LEU5, RFP2, RNF77; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-355. RC TISSUE=Leukemia; RX PubMed=9599022; DOI=10.1016/S0014-5793(98)00357-3; RA Kapanadze B., Kashuba V., Baranova A., Rasool O., van Everdink W.J., RA Liu Y., Syomov A., Corcoran M., Poltaraus A., Brodyansky V., RA Syomova N., Kazakov A., Ibbotson R., van den Berg A., Gizatullin R., RA Fedorova L., Sulimova G., Zelenin A., Deaven L., Lehrach H., RA Grander D., Buys C., Oscier D., Zabarovsky E.R., Einhorn S., RA Yankovsky N.; RT "A cosmid and cDNA fine physical map of a human chromosome 13q14 RT region frequently lost in B-cell chronic lymphocytic leukemia and RT identification of a new putative tumor suppressor gene, Leu5."; RL FEBS Lett. 426:266-270(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM RP 1). RX PubMed=11264177; DOI=10.1182/blood.V97.7.2098; RA Migliazza A., Bosch F., Komatsu H., Cayanis E., Martinotti S., RA Toniato E., Guccione E., Qu X., Chien M., Murty V.V., Gaidano G., RA Inghirami G., Zhang P., Fischer S., Kalachikov S.M., Russo J., RA Edelman I., Efstratiadis A., Dalla-Favera R.; RT "Nucleotide sequence, transcription map, and mutation analysis of the RT 13q14 chromosomal region deleted in B-cell chronic lymphocytic RT leukemia."; RL Blood 97:2098-2104(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT THR-355. 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., RA Minucci S., Pelicci P.G., Ballabio A.; RT "The tripartite motif family identifies cell compartments."; RL EMBO J. 20:2140-2151(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=14499696; DOI=10.1016/S0165-4608(03)00126-2; RA van Everdink W.J., Baranova A., Lummen C., Tyazhelova T., Looman M.W., RA Ivanov D., Verlind E., Pestova A., Faber H., van der Veen A.Y., RA Yankovsky N., Vellenga E., Buys C.H.; RT "RFP2, c13ORF1, and FAM10A4 are the most likely tumor suppressor gene RT candidates for B-cell chronic lymphocytic leukemia."; RL Cancer Genet. Cytogenet. 146:48-57(2003). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT RP THR-355. RA Baranova A.V., Sangfelt O., Ivanov D.V., Borodina T.A., RA Yankovsky N.K.; RT "RFP2 putative tumor suppressor gene: genomic organization, multiple RT mRNA isoforms and evaluation as a B-cell chronic lymphocytic leukaemia RT candidate."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Corcoran M.M., Hammarsund M., Grander D., Oscier D., Kapanadze B., RA Einhorn S., Sangfelt O.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Corcoran M.M., Lerner M., Sangfelt O.; RT "Alternative isoform of candidate tumor suppressor RFP2."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-355. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Blood, and Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR RP LOCATION, MUTAGENESIS OF CYS-13, IDENTIFICATION BY MASS SPECTROMETRY, RP AND INTERACTION WITH VCP. RX PubMed=17314412; DOI=10.1091/mbc.E06-03-0248; RA Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R., RA Ponten F., Uhlen M., Hober S., Grander D., Sangfelt O.; RT "The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin RT ligase involved in ERAD."; RL Mol. Biol. Cell 18:1670-1682(2007). RN [13] RP FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR RP LOCATION, MUTAGENESIS OF CYS-13, IDENTIFICATION BY MASS SPECTROMETRY, RP AND INTERACTION WITH MDM2 AND AKT1. RX PubMed=21333377; DOI=10.1016/j.ejcb.2010.12.001; RA Joo H.M., Kim J.Y., Jeong J.B., Seong K.M., Nam S.Y., Yang K.H., RA Kim C.S., Kim H.S., Jeong M., An S., Jin Y.W.; RT "Ret finger protein 2 enhances ionizing radiation-induced apoptosis RT via degradation of AKT and MDM2."; RL Eur. J. Cell Biol. 90:420-431(2011). RN [14] RP FUNCTION, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF RP CYS-13, AND INTERACTION WITH SQSTM1. RX PubMed=22178386; DOI=10.1016/j.bbamcr.2011.11.015; RA Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.; RT "TRIM13 regulates ER stress induced autophagy and clonogenic ability RT of the cells."; RL Biochim. Biophys. Acta 1823:316-326(2012). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IKBKG. RX PubMed=25152375; DOI=10.1016/j.cellsig.2014.08.008; RA Tomar D., Singh R.; RT "TRIM13 regulates ubiquitination and turnover of NEMO to suppress TNF RT induced NF-kappaB activation."; RL Cell. Signal. 26:2606-2613(2014). RN [16] RP FUNCTION. RX PubMed=25088585; DOI=10.1016/j.biocel.2014.07.012; RA Hatchi E.M., Poalas K., Cordeiro N., N'Debi M., Gavard J., Bidere N.; RT "Participation of the E3-ligase TRIM13 in NF-kappaB p65 activation and RT NFAT-dependent activation of c-Rel upon T-cell receptor engagement."; RL Int. J. Biochem. Cell Biol. 54:217-222(2014). RN [17] RP FUNCTION, AND INTERACTION WITH TRAF6. RX PubMed=28087809; DOI=10.1124/mol.116.106716; RA Huang B., Baek S.H.; RT "Trim13 potentiates toll-like receptor 2-mediated nuclear factor RT kappaB activation via K29-linked polyubiquitination of tumor necrosis RT factor receptor-associated factor 6."; RL Mol. Pharmacol. 91:307-316(2017). CC -!- FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase CC involved in the retrotranslocation and turnover of membrane and CC secretory proteins from the ER through a set of processes named CC ER-associated degradation (ERAD). This process acts on misfolded CC proteins as well as in the regulated degradation of correctly CC folded proteins. Enhances ionizing radiation-induced p53/TP53 CC stability and apoptosis via ubiquitinating MDM2 and AKT1 and CC decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal CC degradation. Regulates ER stress-induced autophagy, and may act as CC a tumor suppressor (PubMed:22178386). Plays also a role in innate CC immune response by stimulating NF-kappa-B activity in the TLR2 CC signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked CC polyubiquitination chain resulting in NF-kappa-B activation CC (PubMed:28087809). Participates as well in T-cell receptor- CC mediated NF-kappa-B activation (PubMed:25088585). In the presence CC of TNF, modulates the IKK complex by regulating IKBKG/NEMO CC ubiquitination leading to the repression of NF-kappa-B CC (PubMed:25152375). {ECO:0000269|PubMed:17314412, CC ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386, CC ECO:0000269|PubMed:25088585, ECO:0000269|PubMed:25152375, CC ECO:0000269|PubMed:28087809}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts CC with AKT1; the interaction ubiquitinates AKT1 and leads to its CC proteasomal degradation. Interacts with MDM2; the interaction CC ubiquitinates AKT1 and leads to its proteasomal degradation. CC Interacts with p62/SQSTM1. Interacts with TRAF6 (PubMed:28087809). CC Interacts with IKBKG/NEMO (PubMed:25152375). CC {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, CC ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:28087809}. CC -!- INTERACTION: CC Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-9867345, EBI-10172181; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, CC ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25152375}; Single- CC pass membrane protein {ECO:0000269|PubMed:17314412, CC ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}. CC Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at CC the perinuclear endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Alpha; CC IsoId=O60858-1; Sequence=Displayed; CC Name=2; Synonyms=Beta; CC IsoId=O60858-2; Sequence=VSP_005746, VSP_005747; CC Name=3; CC IsoId=O60858-3; Sequence=VSP_038142; CC -!- DOMAIN: The coiled-coil domain is required for the induction of CC autophagy during endoplasmic reticulum (ER) stress. CC -!- DOMAIN: The RING-type zinc finger is required for auto- CC polyubiquitination. CC -!- DOMAIN: The C-terminal domain transmembrane domain is CC indispensable for the localization to the ER. CC -!- PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto- CC polyubiquitination leads to proteasomal degradation. CC {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, CC ECO:0000269|PubMed:22178386}. CC -!- MISCELLANEOUS: Located on chromosome 13 within the minimal CC deletion region for B-cell chronic lymphocytic leukemia. 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; AJ224819; CAA12136.1; -; mRNA. DR EMBL; AF279660; AAK13059.1; -; Genomic_DNA. DR EMBL; AF220127; AAG53500.1; -; mRNA. DR EMBL; AF220128; AAG53501.1; -; mRNA. DR EMBL; AY191002; AAO38979.1; -; mRNA. DR EMBL; AF241849; AAK51624.1; -; Genomic_DNA. DR EMBL; AF241850; AAF91315.1; -; mRNA. DR EMBL; AY455758; AAR31110.1; -; mRNA. DR EMBL; AY764035; AAV51406.1; -; mRNA. DR EMBL; AK314496; BAG37096.1; -; mRNA. DR EMBL; AL137060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08844.1; -; Genomic_DNA. DR EMBL; CH471075; EAX08845.1; -; Genomic_DNA. DR EMBL; BC003579; AAH03579.1; -; mRNA. DR EMBL; BC063407; AAH63407.1; -; mRNA. DR CCDS; CCDS41888.1; -. [O60858-3] DR CCDS; CCDS9423.1; -. [O60858-1] DR RefSeq; NP_001007279.1; NM_001007278.2. [O60858-3] DR RefSeq; NP_005789.2; NM_005798.4. [O60858-1] DR RefSeq; NP_434698.1; NM_052811.3. [O60858-1] DR RefSeq; NP_998755.1; NM_213590.2. [O60858-1] DR UniGene; Hs.436922; -. DR ProteinModelPortal; O60858; -. DR SMR; O60858; -. DR BioGrid; 115501; 31. DR IntAct; O60858; 8. DR STRING; 9606.ENSP00000298772; -. DR DrugBank; DB01565; Dihydromorphine. DR DrugBank; DB01548; Diprenorphine. DR DrugBank; DB01497; Etorphine. DR iPTMnet; O60858; -. DR PhosphoSitePlus; O60858; -. DR BioMuta; TRIM13; -. DR EPD; O60858; -. DR jPOST; O60858; -. DR MaxQB; O60858; -. DR PaxDb; O60858; -. DR PeptideAtlas; O60858; -. DR PRIDE; O60858; -. DR ProteomicsDB; 49630; -. DR ProteomicsDB; 49631; -. [O60858-2] DR ProteomicsDB; 49632; -. [O60858-3] DR DNASU; 10206; -. DR Ensembl; ENST00000356017; ENSP00000348299; ENSG00000204977. [O60858-3] DR Ensembl; ENST00000378182; ENSP00000367424; ENSG00000204977. [O60858-1] DR Ensembl; ENST00000420995; ENSP00000412943; ENSG00000204977. [O60858-1] DR Ensembl; ENST00000457662; ENSP00000399206; ENSG00000204977. [O60858-1] DR GeneID; 10206; -. DR KEGG; hsa:10206; -. DR UCSC; uc001vdp.2; human. [O60858-1] DR CTD; 10206; -. DR DisGeNET; 10206; -. DR EuPathDB; HostDB:ENSG00000204977.9; -. DR GeneCards; TRIM13; -. DR HGNC; HGNC:9976; TRIM13. DR HPA; HPA000367; -. DR MIM; 605661; gene. DR neXtProt; NX_O60858; -. DR OpenTargets; ENSG00000204977; -. DR PharmGKB; PA162406947; -. DR eggNOG; ENOG410ITG5; Eukaryota. DR eggNOG; ENOG410YH9X; LUCA. DR GeneTree; ENSGT00940000159715; -. DR HOVERGEN; HBG056536; -. DR InParanoid; O60858; -. DR KO; K12003; -. DR OMA; SPFKCPT; -. DR OrthoDB; 635534at2759; -. DR PhylomeDB; O60858; -. DR TreeFam; TF331669; -. DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC). DR UniPathway; UPA00143; -. DR GenomeRNAi; 10206; -. DR PRO; PR:O60858; -. DR Proteomes; UP000005640; Chromosome 13. DR Bgee; ENSG00000204977; Expressed in 231 organ(s), highest expression level in testis. DR CleanEx; HS_TRIM13; -. DR ExpressionAtlas; O60858; baseline and differential. DR Genevisible; O60858; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB. DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB. DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB. DR GO; GO:0016239; P:positive regulation of macroautophagy; IDA:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0010332; P:response to gamma radiation; IEP:UniProtKB. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB. DR CDD; cd00021; BBOX; 1. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR027370; Znf-RING_LisH. 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 Pfam; PF00643; zf-B_box; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR SMART; SM00336; BBOX; 1. DR SMART; SM00184; RING; 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 Alternative splicing; Coiled coil; Complete proteome; KW Endoplasmic reticulum; Immunity; Innate immunity; Membrane; KW Metal-binding; Polymorphism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 407 E3 ubiquitin-protein ligase TRIM13. FT /FTId=PRO_0000056028. FT TRANSMEM 317 337 Helical. {ECO:0000255}. FT ZN_FING 10 58 RING-type. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT ZN_FING 89 131 B box-type. {ECO:0000255|PROSITE- FT ProRule:PRU00024}. FT COILED 172 200 {ECO:0000255}. FT VAR_SEQ 1 1 M -> MDVM (in isoform 3). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_038142. FT VAR_SEQ 175 175 L -> D (in isoform 2). FT {ECO:0000303|PubMed:11331580}. FT /FTId=VSP_005746. FT VAR_SEQ 176 407 Missing (in isoform 2). FT {ECO:0000303|PubMed:11331580}. FT /FTId=VSP_005747. FT VARIANT 355 355 S -> T (in dbSNP:rs1056543). FT {ECO:0000269|PubMed:11331580, FT ECO:0000269|PubMed:15057823, FT ECO:0000269|PubMed:9599022, FT ECO:0000269|Ref.5}. FT /FTId=VAR_013512. FT MUTAGEN 13 13 C->A: Absence of polyubiquitination. FT Stability of protein increased. No FT enhanced apoptosis on ionizing radiation FT induction. No ubiquitination of AKT1 or FT MDM2. Decreased p53/TP53 stability. No FT effect on induction of autophagy during FT ER stress. {ECO:0000269|PubMed:17314412, FT ECO:0000269|PubMed:21333377, FT ECO:0000269|PubMed:22178386}. SQ SEQUENCE 407 AA; 46988 MW; 94B624345124AEBF CRC64; MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC LSNFSSYLTK TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF VCKYKLL //