TRI13_HUMAN
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 03-AUG-2022, entry version 195.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Syomova N.,
RA Kazakov A., Ibbotson R., van den Berg A., Gizatullin R., Fedorova L.,
RA Sulimova G., Zelenin A., Deaven L., Lehrach H., Grander D., Buys C.,
RA Oscier D., Zabarovsky E.R., Einhorn S., Yankovsky N.;
RT "A cosmid and cDNA fine physical map of a human chromosome 13q14 region
RT frequently lost in B-cell chronic lymphocytic leukemia and identification
RT 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 1).
RX PubMed=11264177; DOI=10.1182/blood.v97.7.2098;
RA Migliazza A., Bosch F., Komatsu H., Cayanis E., Martinotti S., Toniato E.,
RA Guccione E., Qu X., Chien M., Murty V.V., Gaidano G., Inghirami G.,
RA Zhang P., Fischer S., Kalachikov S.M., Russo J., Edelman I.,
RA Efstratiadis A., Dalla-Favera R.;
RT "Nucleotide sequence, transcription map, and mutation analysis of the 13q14
RT chromosomal region deleted in B-cell chronic lymphocytic 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., Minucci S.,
RA 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 THR-355.
RA Baranova A.V., Sangfelt O., Ivanov D.V., Borodina T.A., Yankovsky N.K.;
RT "RFP2 putative tumor suppressor gene: genomic organization, multiple mRNA
RT 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., 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 [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., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., 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., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., 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., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA 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., 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 (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 project:
RT 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, AND
RP 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., Ponten F.,
RA 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, AND
RP 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., Kim C.S.,
RA Kim H.S., Jeong M., An S., Jin Y.W.;
RT "Ret finger protein 2 enhances ionizing radiation-induced apoptosis via
RT degradation of AKT and MDM2.";
RL Eur. J. Cell Biol. 90:420-431(2011).
RN [14]
RP FUNCTION, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-13,
RP 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 of the
RT 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 kappaB
RT activation via K29-linked polyubiquitination of tumor necrosis factor
RT 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 ER-
CC associated degradation (ERAD). This process acts on misfolded proteins
CC as well as in the regulated degradation of correctly folded proteins.
CC Enhances ionizing radiation-induced p53/TP53 stability and apoptosis
CC via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity
CC through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-
CC induced autophagy, and may act as a tumor suppressor (PubMed:22178386).
CC Also plays a role in innate immune response by stimulating NF-kappa-B
CC activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the
CC 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B
CC activation (PubMed:28087809). Participates as well in T-cell receptor-
CC mediated NF-kappa-B activation (PubMed:25088585). In the presence of
CC TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination
CC leading to the repression of NF-kappa-B (PubMed:25152375).
CC {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377,
CC ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25088585,
CC ECO:0000269|PubMed:25152375, ECO:0000269|PubMed:28087809}.
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 (via C-terminal domain) with VCP. Interacts with
CC AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal
CC degradation. Interacts with MDM2; the interaction ubiquitinates AKT1
CC and leads to its proteasomal degradation. Interacts with p62/SQSTM1.
CC Interacts with TRAF6 (PubMed:28087809). Interacts with IKBKG/NEMO
CC (PubMed:25152375). {ECO:0000269|PubMed:17314412,
CC ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386,
CC ECO:0000269|PubMed:28087809}.
CC -!- INTERACTION:
CC O60858; 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-pass
CC 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 the
CC 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 indispensable for
CC 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 deletion
CC region for B-cell chronic lymphocytic leukemia.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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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 AlphaFoldDB; O60858; -.
DR SMR; O60858; -.
DR BioGRID; 115501; 135.
DR IntAct; O60858; 18.
DR MINT; O60858; -.
DR STRING; 9606.ENSP00000348299; -.
DR DrugBank; DB01565; Dihydromorphine.
DR DrugBank; DB01548; Diprenorphine.
DR DrugBank; DB01497; Etorphine.
DR GlyGen; O60858; 1 site.
DR iPTMnet; O60858; -.
DR PhosphoSitePlus; O60858; -.
DR BioMuta; TRIM13; -.
DR EPD; O60858; -.
DR jPOST; O60858; -.
DR MassIVE; O60858; -.
DR MaxQB; O60858; -.
DR PaxDb; O60858; -.
DR PeptideAtlas; O60858; -.
DR PRIDE; O60858; -.
DR ProteomicsDB; 49630; -. [O60858-1]
DR ProteomicsDB; 49631; -. [O60858-2]
DR ProteomicsDB; 49632; -. [O60858-3]
DR Antibodypedia; 638; 238 antibodies from 27 providers.
DR DNASU; 10206; -.
DR Ensembl; ENST00000356017.8; ENSP00000348299.4; ENSG00000204977.10. [O60858-3]
DR Ensembl; ENST00000378182.4; ENSP00000367424.3; ENSG00000204977.10. [O60858-1]
DR Ensembl; ENST00000420995.6; ENSP00000412943.2; ENSG00000204977.10. [O60858-1]
DR Ensembl; ENST00000457662.2; ENSP00000399206.2; ENSG00000204977.10. [O60858-1]
DR GeneID; 10206; -.
DR KEGG; hsa:10206; -.
DR MANE-Select; ENST00000378182.4; ENSP00000367424.3; NM_213590.3; NP_998755.1.
DR UCSC; uc001vdp.2; human. [O60858-1]
DR CTD; 10206; -.
DR DisGeNET; 10206; -.
DR GeneCards; TRIM13; -.
DR HGNC; HGNC:9976; TRIM13.
DR HPA; ENSG00000204977; Low tissue specificity.
DR MIM; 605661; gene.
DR neXtProt; NX_O60858; -.
DR OpenTargets; ENSG00000204977; -.
DR PharmGKB; PA162406947; -.
DR VEuPathDB; HostDB:ENSG00000204977; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159715; -.
DR InParanoid; O60858; -.
DR OMA; NLQVNYS; -.
DR PhylomeDB; O60858; -.
DR TreeFam; TF331669; -.
DR PathwayCommons; O60858; -.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; O60858; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10206; 7 hits in 1115 CRISPR screens.
DR ChiTaRS; TRIM13; human.
DR GenomeRNAi; 10206; -.
DR Pharos; O60858; Tbio.
DR PRO; PR:O60858; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O60858; protein.
DR Bgee; ENSG00000204977; Expressed in sperm and 205 other tissues.
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:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
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: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: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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEP:UniProtKB.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
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; Endoplasmic reticulum; Immunity;
KW Innate immunity; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..407
FT /note="E3 ubiquitin-protein ligase TRIM13"
FT /id="PRO_0000056028"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 89..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 172..200
FT /evidence="ECO:0000255"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1
FT /note="M -> MDVM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_038142"
FT VAR_SEQ 175
FT /note="L -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005746"
FT VAR_SEQ 176..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005747"
FT VARIANT 355
FT /note="S -> T (in dbSNP:rs1056543)"
FT /evidence="ECO:0000269|PubMed:11331580,
FT ECO:0000269|PubMed:15057823, ECO:0000269|PubMed:9599022,
FT ECO:0000269|Ref.5"
FT /id="VAR_013512"
FT MUTAGEN 13
FT /note="C->A: Absence of polyubiquitination. Stability of
FT protein increased. No enhanced apoptosis on ionizing
FT radiation induction. No ubiquitination of AKT1 or MDM2.
FT Decreased p53/TP53 stability. No effect on induction of
FT autophagy during ER stress."
FT /evidence="ECO:0000269|PubMed:17314412,
FT ECO:0000269|PubMed:21333377, 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
