ID TRI14_HUMAN Reviewed; 442 AA.
AC Q14142; A8K9W0; E7EQC4; F8W956; Q548W9; Q5TBQ8; Q6ZWL7; Q9BRD8; Q9C020;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 27-MAR-2024, entry version 195.
DE RecName: Full=Tripartite motif-containing protein 14;
GN Name=TRIM14; Synonyms=KIAA0129;
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 BETA AND 3).
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 3).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 4).
RC TISSUE=Testis, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Eye;
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 INDUCTION BY INTERFERONS.
RX PubMed=22711689; DOI=10.1002/hep.25908;
RA Metz P., Dazert E., Ruggieri A., Mazur J., Kaderali L., Kaul A., Zeuge U.,
RA Trippler M., Lohmann V., Binder M., Frese M., Bartenschlager R.;
RT "Identification of type I and type II interferon-induced effectors
RT controlling hepatitis C virus replication.";
RL Hepatology 56:2082-2093(2012).
RN [8]
RP FUNCTION, INTERACTION WITH MAVS, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP LYS-365, AND UBIQUITINATION.
RX PubMed=24379373; DOI=10.1073/pnas.1316941111;
RA Zhou Z., Jia X., Xue Q., Dou Z., Ma Y., Zhao Z., Jiang Z., He B., Jin Q.,
RA Wang J.;
RT "TRIM14 is a mitochondrial adaptor that facilitates retinoic acid-inducible
RT gene-I-like receptor-mediated innate immune response.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E245-E254(2014).
RN [9]
RP FUNCTION, AND INTERACTION WITH CGAS AND USP14.
RX PubMed=27666593; DOI=10.1016/j.molcel.2016.08.025;
RA Chen M., Meng Q., Qin Y., Liang P., Tan P., He L., Zhou Y., Chen Y.,
RA Huang J., Wang R.F., Cui J.;
RT "TRIM14 inhibits cGAS degradation mediated by selective autophagy receptor
RT p62 to promote innate immune responses.";
RL Mol. Cell 64:105-119(2016).
RN [10]
RP FUNCTION, MUTAGENESIS OF LYS-365, AND INTERACTION WITH HEPATITIS C VIRUS
RP PROTEIN NS5A (MICROBIAL INFECTION).
RX PubMed=27578425; DOI=10.1038/srep32336;
RA Wang S., Chen Y., Li C., Wu Y., Guo L., Peng C., Huang Y., Cheng G.,
RA Qin F.X.;
RT "TRIM14 inhibits hepatitis C virus infection by SPRY domain-dependent
RT targeted degradation of the viral NS5A protein.";
RL Sci. Rep. 6:32336-32336(2016).
RN [11]
RP FUNCTION, INTERACTION WITH WRNIP1 AND PPP6C, AND SUBCELLULAR LOCATION.
RX PubMed=29053956; DOI=10.1016/j.molcel.2017.09.035;
RA Tan P., He L., Cui J., Qian C., Cao X., Lin M., Zhu Q., Li Y., Xing C.,
RA Yu X., Wang H.Y., Wang R.F.;
RT "Assembly of the WHIP-TRIM14-PPP6C mitochondrial complex promotes RIG-I-
RT mediated antiviral signaling.";
RL Mol. Cell 68:293-307(2017).
RN [12]
RP UBIQUITINATION BY RNF125, AND SUBCELLULAR LOCATION.
RX PubMed=28476934; DOI=10.4049/jimmunol.1601322;
RA Jia X., Zhou H., Wu C., Wu Q., Ma S., Wei C., Cao Y., Song J., Zhong H.,
RA Zhou Z., Wang J.;
RT "The Ubiquitin Ligase RNF125 Targets Innate Immune Adaptor Protein TRIM14
RT for Ubiquitination and Degradation.";
RL J. Immunol. 198:4652-4658(2017).
RN [13]
RP FUNCTION, INDUCTION BY TYPE I INTERFERON, AND INTERACTION WITH HEPATITIS B
RP VIRUS PROTEIN HBX (MICROBIAL INFECTION).
RX PubMed=30150992; DOI=10.3389/fimmu.2018.01872;
RA Tan G., Xu F., Song H., Yuan Y., Xiao Q., Ma F., Qin F.X., Cheng G.;
RT "Identification of TRIM14 as a Type I IFN-Stimulated Gene Controlling
RT Hepatitis B Virus Replication by Targeting HBx.";
RL Front. Immunol. 9:1872-1872(2018).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CGAS AND TBK1.
RX PubMed=32404352; DOI=10.4049/jimmunol.1901511;
RA Hoffpauir C.T., Bell S.L., West K.O., Jing T., Wagner A.R., Torres-Odio S.,
RA Cox J.S., West A.P., Li P., Patrick K.L., Watson R.O.;
RT "TRIM14 Is a Key Regulator of the Type I IFN Response during Mycobacterium
RT tuberculosis Infection.";
RL J. Immunol. 205:153-167(2020).
RN [15]
RP FUNCTION, INTERACTION WITH KDM4D AND USP14, AND SUBCELLULAR LOCATION.
RX PubMed=35145029; DOI=10.1073/pnas.2113454119;
RA Liu D., Zhao Z., She Y., Zhang L., Chen X., Ma L., Cui J.;
RT "TRIM14 inhibits OPTN-mediated autophagic degradation of KDM4D to
RT epigenetically regulate inflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
RN [16]
RP FUNCTION, AND INTERACTION WITH EBOLAVIRUS PROTEIN NP (MICROBIAL INFECTION).
RX PubMed=37562033; DOI=10.1093/infdis/jiad325;
RA Kuroda M., Halfmann P.J., Thackray L.B., Diamond M.S., Feldmann H.,
RA Marzi A., Kawaoka Y.;
RT "An antiviral role for TRIM14 in Ebola virus infection.";
RL J. Infect. Dis. 0:0-0(2023).
CC -!- FUNCTION: Plays an essential role in the innate immune defense against
CC viruses and bacteria (PubMed:30150992, PubMed:32404352). Promotes the
CC 'Lys-48'-linked ubiquitination and subsequent degradation of hepatitis
CC C virus NS5A leading to the inhibition of viral replication
CC (PubMed:27578425). Plays also a role in the inhibition of ebolavirus
CC infection by enhancing IFN-beta and NF-kappa-B activation after binding
CC to the viral protein NP (PubMed:37562033). Facilitates the type I IFN
CC response by interacting with MAVS at the outer mitochondria membrane
CC and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the
CC MAVS signalosome, leading to the activation of both the IFN regulatory
CC factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively
CC regulates the CGAS-induced type I interferon signaling pathway by
CC stabilizing CGAS and inhibiting its autophagic degradation
CC (PubMed:27666593). Acts as a scaffold between TBK1 and STAT3 to promote
CC phosphorylation of STAT3 and resolve interferon-stimulated gene (ISG)
CC expression (PubMed:32404352). Inhibits the transcriptional activity of
CC SPI1 in a dose-dependent manner (By similarity). Inhibits also OPTN-
CC mediated selective autophagic degradation of KDM4D and thereby
CC negatively regulates H3K9me2 and H3K9me3. Mechanistically, recruits
CC USP14 to remove the 'Lys-63'-linked ubiquitination of KDM4D, preventing
CC its recognition by OPTN and subsequent degradation (PubMed:35145029).
CC {ECO:0000250|UniProtKB:Q8BVW3, ECO:0000269|PubMed:24379373,
CC ECO:0000269|PubMed:27578425, ECO:0000269|PubMed:27666593,
CC ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:30150992,
CC ECO:0000269|PubMed:32404352, ECO:0000269|PubMed:35145029,
CC ECO:0000269|PubMed:37562033}.
CC -!- SUBUNIT: Interacts with MAVS (PubMed:24379373). Interacts with WRNIP1
CC and PPP6C; these interactions positively regulate the RIGI signaling
CC pathway (PubMed:29053956). Interacts with CGAS; this interaction
CC stabilizes CGAS and promotes type I interferon production
CC (PubMed:27666593, PubMed:32404352). Interacts with USP14; this
CC interaction mediates the cleavage of 'Lys-48'-linked ubiquitination of
CC CGAS (PubMed:27666593). Interacts with TBK1 (PubMed:32404352).
CC Interacts with SPI1 (By similarity). Interacts with KDM4D and USP14
CC (PubMed:35145029). {ECO:0000250|UniProtKB:Q8BVW3,
CC ECO:0000269|PubMed:24379373, ECO:0000269|PubMed:27666593,
CC ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:32404352,
CC ECO:0000269|PubMed:35145029}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus HBX;
CC this interaction inhibits formation of the HBX-DDB1 complex, thus
CC inhibiting viral replication. {ECO:0000269|PubMed:30150992}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus protein
CC NS5A; this interaction promotes NS5A degradation, thus inhibiting viral
CC replication. {ECO:0000269|PubMed:27578425}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein NP.
CC {ECO:0000269|PubMed:37562033}.
CC -!- INTERACTION:
CC Q14142; P58397-3: ADAMTS12; NbExp=3; IntAct=EBI-2820256, EBI-12048761;
CC Q14142; Q13895: BYSL; NbExp=3; IntAct=EBI-2820256, EBI-358049;
CC Q14142; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-2820256, EBI-11530605;
CC Q14142; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-2820256, EBI-11977221;
CC Q14142; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2820256, EBI-10961624;
CC Q14142; Q16204: CCDC6; NbExp=3; IntAct=EBI-2820256, EBI-1045350;
CC Q14142; Q96Q77: CIB3; NbExp=3; IntAct=EBI-2820256, EBI-10292696;
CC Q14142; P61024: CKS1B; NbExp=3; IntAct=EBI-2820256, EBI-456371;
CC Q14142; P19447: ERCC3; NbExp=3; IntAct=EBI-2820256, EBI-1183307;
CC Q14142; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-2820256, EBI-742102;
CC Q14142; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-2820256, EBI-742802;
CC Q14142; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2820256, EBI-618309;
CC Q14142; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2820256, EBI-5916454;
CC Q14142; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-2820256, EBI-14103818;
CC Q14142; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-2820256, EBI-5460660;
CC Q14142; P52597: HNRNPF; NbExp=3; IntAct=EBI-2820256, EBI-352986;
CC Q14142; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-2820256, EBI-8638439;
CC Q14142; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2820256, EBI-14069005;
CC Q14142; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2820256, EBI-739832;
CC Q14142; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-2820256, EBI-726739;
CC Q14142; O15160: POLR1C; NbExp=3; IntAct=EBI-2820256, EBI-1055079;
CC Q14142; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-2820256, EBI-11320284;
CC Q14142; O43741: PRKAB2; NbExp=3; IntAct=EBI-2820256, EBI-1053424;
CC Q14142; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-2820256, EBI-1567797;
CC Q14142; Q16825: PTPN21; NbExp=3; IntAct=EBI-2820256, EBI-2860264;
CC Q14142; O75771: RAD51D; NbExp=3; IntAct=EBI-2820256, EBI-1055693;
CC Q14142; Q8IX21: SLF2; NbExp=3; IntAct=EBI-2820256, EBI-2682240;
CC Q14142; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-2820256, EBI-742688;
CC Q14142; Q12933: TRAF2; NbExp=3; IntAct=EBI-2820256, EBI-355744;
CC Q14142; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2820256, EBI-744794;
CC Q14142; P08670: VIM; NbExp=3; IntAct=EBI-2820256, EBI-353844;
CC Q14142; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-2820256, EBI-10183064;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24379373, ECO:0000269|PubMed:28476934,
CC ECO:0000269|PubMed:29053956}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:32404352}. Nucleus {ECO:0000269|PubMed:35145029}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=Q14142-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q14142-2; Sequence=VSP_000510, VSP_000511;
CC Name=3;
CC IsoId=Q14142-3; Sequence=VSP_044099;
CC Name=4;
CC IsoId=Q14142-4; Sequence=VSP_044097, VSP_044098, VSP_044099;
CC -!- TISSUE SPECIFICITY: Highest expression in liver; undetectable in
CC skeletal muscle.
CC -!- INDUCTION: By interferons alpha and gamma in a STAT1-dependent way.
CC {ECO:0000269|PubMed:22711689, ECO:0000269|PubMed:30150992}.
CC -!- DOMAIN: The B-box zinc finger is responsible for inhibition of SPI1-
CC mediated transcriptional activation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated (PubMed:24379373). Undergoes 'Lys-63'-linked
CC polyubiquitination; this modification allows IKBKG/NEMO recruitment to
CC MAVS. Undergoes 'Lys-48'-linked polyubiquitination by RNF125; this
CC modification mediates its degradation via the ubiquitin-proteasome
CC pathway (PubMed:28476934). {ECO:0000269|PubMed:24379373,
CC ECO:0000269|PubMed:28476934}.
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; AF220130; AAG53503.1; -; mRNA.
DR EMBL; AF220131; AAG53504.1; -; mRNA.
DR EMBL; D50919; BAA09478.1; -; mRNA.
DR EMBL; AK097480; BAC05071.1; -; mRNA.
DR EMBL; AK292825; BAF85514.1; -; mRNA.
DR EMBL; AL137073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58870.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58877.1; -; Genomic_DNA.
DR EMBL; BC006333; AAH06333.1; -; mRNA.
DR CCDS; CCDS6734.1; -. [Q14142-1]
DR RefSeq; NP_055603.2; NM_014788.3. [Q14142-1]
DR RefSeq; NP_150088.1; NM_033219.2. [Q14142-1]
DR RefSeq; XP_005252377.1; XM_005252320.3. [Q14142-1]
DR RefSeq; XP_016870841.1; XM_017015352.1.
DR RefSeq; XP_016870842.1; XM_017015353.1. [Q14142-1]
DR PDB; 6JBM; X-ray; 2.10 A; A/B/C/D=249-442.
DR PDBsum; 6JBM; -.
DR AlphaFoldDB; Q14142; -.
DR SMR; Q14142; -.
DR BioGRID; 115168; 382.
DR IntAct; Q14142; 39.
DR STRING; 9606.ENSP00000344208; -.
DR iPTMnet; Q14142; -.
DR PhosphoSitePlus; Q14142; -.
DR BioMuta; TRIM14; -.
DR DMDM; 20141957; -.
DR EPD; Q14142; -.
DR jPOST; Q14142; -.
DR MassIVE; Q14142; -.
DR MaxQB; Q14142; -.
DR PaxDb; 9606-ENSP00000344208; -.
DR PeptideAtlas; Q14142; -.
DR ProteomicsDB; 30266; -.
DR ProteomicsDB; 59847; -. [Q14142-1]
DR ProteomicsDB; 59848; -. [Q14142-2]
DR ProteomicsDB; 62556; -.
DR Pumba; Q14142; -.
DR Antibodypedia; 14448; 159 antibodies from 24 providers.
DR DNASU; 9830; -.
DR Ensembl; ENST00000341469.7; ENSP00000344208.2; ENSG00000106785.15. [Q14142-1]
DR Ensembl; ENST00000342043.3; ENSP00000343990.3; ENSG00000106785.15. [Q14142-1]
DR Ensembl; ENST00000375098.7; ENSP00000364239.3; ENSG00000106785.15. [Q14142-1]
DR GeneID; 9830; -.
DR KEGG; hsa:9830; -.
DR MANE-Select; ENST00000341469.7; ENSP00000344208.2; NM_014788.4; NP_055603.2.
DR UCSC; uc004ayg.3; human. [Q14142-1]
DR AGR; HGNC:16283; -.
DR CTD; 9830; -.
DR DisGeNET; 9830; -.
DR GeneCards; TRIM14; -.
DR HGNC; HGNC:16283; TRIM14.
DR HPA; ENSG00000106785; Low tissue specificity.
DR MalaCards; TRIM14; -.
DR MIM; 606556; gene.
DR neXtProt; NX_Q14142; -.
DR OpenTargets; ENSG00000106785; -.
DR PharmGKB; PA38113; -.
DR VEuPathDB; HostDB:ENSG00000106785; -.
DR eggNOG; ENOG502QTZS; Eukaryota.
DR GeneTree; ENSGT00940000161010; -.
DR HOGENOM; CLU_013137_1_0_1; -.
DR InParanoid; Q14142; -.
DR OMA; WWIGAAY; -.
DR OrthoDB; 5342123at2759; -.
DR PhylomeDB; Q14142; -.
DR TreeFam; TF351014; -.
DR PathwayCommons; Q14142; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q14142; -.
DR BioGRID-ORCS; 9830; 18 hits in 1194 CRISPR screens.
DR ChiTaRS; TRIM14; human.
DR GenomeRNAi; 9830; -.
DR Pharos; Q14142; Tbio.
DR PRO; PR:Q14142; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q14142; Protein.
DR Bgee; ENSG00000106785; Expressed in palpebral conjunctiva and 180 other cell types or tissues.
DR ExpressionAtlas; Q14142; baseline and differential.
DR Genevisible; Q14142; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProt.
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:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd13738; SPRY_PRY_TRIM14; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic 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; IPR044116; SPRY_PRY_TRIM14.
DR InterPro; IPR000315; Znf_B-box.
DR PANTHER; PTHR25465:SF11; B BOX-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 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 PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW Immunity; Innate immunity; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Reference proteome; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..442
FT /note="Tripartite motif-containing protein 14"
FT /id="PRO_0000220370"
FT DOMAIN 249..442
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 19..61
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 76..109
FT /evidence="ECO:0000255"
FT COILED 135..156
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044097"
FT VAR_SEQ 232..253
FT /note="KESINCQLSDPSSTKPGTLLKT -> SPTNHAYSALKVSSPRLVSNRP (in
FT isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_000510"
FT VAR_SEQ 254..442
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_000511"
FT VAR_SEQ 265..380
FT /note="YARTPTLDPDTMHARLRLSADRLTVRCGLLGSLGPVPVLRFDALWQVLARDC
FT FATGRHYWEVDVQEAGAGWWVGAAYASLRRRGASAAARLGCNRQSWCLKRYDLEYWAFH
FT DGQRS -> SCWAAWGPCPCCGSTRSGKCWLVTASPPAATTGRLTCRRRAPAGGWARPT
FT PPFGAAGPRPPPAWAATASPGASSATTLSTGPSTTASAA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044098"
FT VAR_SEQ 381..442
FT /note="RLRPRDDLDRLGVFLDYEAGVLAFYDVTGGMSHLHTFRATFQEPLYPALRLW
FT EGAISIPRLP -> ACGPATTSTGSASSWTTRPASSPSTT (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:8590280"
FT /id="VSP_044099"
FT VARIANT 219
FT /note="V -> M (in dbSNP:rs2296079)"
FT /id="VAR_048399"
FT MUTAGEN 365
FT /note="K->R: More than 50% loss of interaction with MAVS.
FT However it has equal potency in inhibiting HCV replication
FT that the wild type."
FT /evidence="ECO:0000269|PubMed:24379373,
FT ECO:0000269|PubMed:27578425"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6JBM"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6JBM"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6JBM"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:6JBM"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:6JBM"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:6JBM"
FT STRAND 425..437
FT /evidence="ECO:0007829|PDB:6JBM"
FT CONFLICT Q14142-4:106..108
FT /note="LKS -> PIA (in Ref. 3; BAC05071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49773 MW; 68990B2B57F1D083 CRC64;
MAGAATGSRT PGRSELVEGC GWRCPEHGDR VAELFCRRCR RCVCALCPVL GAHRGHPVGL
ALEAAVHVQK LSQECLKQLA IKKQQHIDNI TQIEDATEKL KANAESSKTW LKGKFTELRL
LLDEEEALAK KFIDKNTQLT LQVYREQADS CREQLDIMND LSNRVWSISQ EPDPVQRLQA
YTATEQEMQQ QMSLGELCHP VPLSFEPVKS FFKGLVEAVE STLQTPLDIR LKESINCQLS
DPSSTKPGTL LKTSPSPERS LLLKYARTPT LDPDTMHARL RLSADRLTVR CGLLGSLGPV
PVLRFDALWQ VLARDCFATG RHYWEVDVQE AGAGWWVGAA YASLRRRGAS AAARLGCNRQ
SWCLKRYDLE YWAFHDGQRS RLRPRDDLDR LGVFLDYEAG VLAFYDVTGG MSHLHTFRAT
FQEPLYPALR LWEGAISIPR LP
//
