MOD5_HUMAN
ID MOD5_HUMAN Reviewed; 467 AA.
AC Q9H3H1; A1A4X7; Q3T7B5; Q5QPK5; Q5QPK6; Q6IAC9; Q96FJ3; Q96L45; Q9NXT7;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=tRNA dimethylallyltransferase;
DE EC=2.5.1.75 {ECO:0000269|PubMed:24901367};
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE Short=IPP transferase;
DE Short=IPPT;
DE AltName: Full=hGRO1;
DE AltName: Full=tRNA isopentenyltransferase 1;
DE Short=IPTase;
DE Flags: Precursor;
GN Name=TRIT1; Synonyms=IPT, MOD5;
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 FUNCTION.
RX PubMed=11111046; DOI=10.1016/s0378-1119(00)00421-2;
RA Golovko A., Hjalm G., Sitbon F., Nicander B.;
RT "Cloning of a human tRNA isopentenyl transferase.";
RL Gene 258:85-93(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND ALTERNATIVE SPLICING.
RC TISSUE=Lung;
RX PubMed=15870694; DOI=10.1038/sj.onc.1208687;
RA Spinola M., Galvan A., Pignatiello C., Conti B., Pastorino U., Nicander B.,
RA Paroni R., Dragani T.A.;
RT "Identification and functional characterization of the candidate tumor
RT suppressor gene TRIT1 in human lung cancer.";
RL Oncogene 24:5502-5509(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Peters J.L., Yan Q., Guan M.X.;
RT "Human MOD5 cDNA sequence.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 7-467 (ISOFORM 5), AND VARIANT LEU-202.
RC TISSUE=Kidney, 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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-467 (ISOFORM 4).
RX PubMed=11560893; DOI=10.1093/genetics/159.1.147;
RA Lemieux J., Lakowski B., Webb A., Meng Y., Ubach A., Bussiere F.,
RA Barnes T., Hekimi S.;
RT "Regulation of physiological rates in Caenorhabditis elegans by a tRNA-
RT modifying enzyme in the mitochondria.";
RL Genetics 159:147-157(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24126054; DOI=10.1128/mcb.01041-13;
RA Lamichhane T.N., Mattijssen S., Maraia R.J.;
RT "Human cells have a limited set of tRNA anticodon loop substrates of the
RT tRNA isopentenyltransferase TRIT1 tumor suppressor.";
RL Mol. Cell. Biol. 33:4900-4908(2013).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN COXPD35,
RP VARIANT COXPD35 GLN-323, AND CHARACTERIZATION OF VARIANT COXPD35 GLN-323.
RX PubMed=24901367; DOI=10.1371/journal.pgen.1004424;
RA Yarham J.W., Lamichhane T.N., Pyle A., Mattijssen S., Baruffini E.,
RA Bruni F., Donnini C., Vassilev A., He L., Blakely E.L., Griffin H.,
RA Santibanez-Koref M., Bindoff L.A., Ferrero I., Chinnery P.F., McFarland R.,
RA Maraia R.J., Taylor R.W.;
RT "Defective i6A37 modification of mitochondrial and cytosolic tRNAs results
RT from pathogenic mutations in TRIT1 and its substrate tRNA.";
RL PLoS Genet. 10:E1004424-E1004424(2014).
RN [16]
RP INVOLVEMENT IN COXPD35.
RX PubMed=32088416; DOI=10.1016/j.ejmg.2020.103882;
RA Forde K.M., Molloy B., Conroy J., Green A.J., King M.D., Buckley P.G.,
RA Ryan S., Gorman K.M.;
RT "Expansion of the phenotype of biallelic variants in TRIT1.";
RL Eur. J. Med. Genet. 63:103882-103882(2020).
RN [17]
RP FUNCTION.
RX PubMed=34774131; DOI=10.1016/j.molcel.2021.10.018;
RA Schoeller E., Marks J., Marchand V., Bruckmann A., Powell C.A.,
RA Reichold M., Mutti C.D., Dettmer K., Feederle R., Huettelmaier S., Helm M.,
RA Oefner P., Minczuk M., Motorin Y., Hafner M., Meister G.;
RT "Balancing of mitochondrial translation through METTL8-mediated m3C
RT modification of mitochondrial tRNAs.";
RL Mol. Cell 81:4810-4825(2021).
RN [18]
RP INVOLVEMENT IN COXPD35, AND VARIANTS COXPD35 8-ARG--VAL-467 DEL; SER-283;
RP GLU-286; 402-ARG--VAL-467 DEL AND PRO-419.
RX PubMed=28185376; DOI=10.1002/humu.23196;
RG Care4Rare Consortium;
RA Kernohan K.D., Dyment D.A., Pupavac M., Cramer Z., McBride A., Bernard G.,
RA Straub I., Tetreault M., Hartley T., Huang L., Sell E., Majewski J.,
RA Rosenblatt D.S., Shoubridge E., Mhanni A., Myers T., Proud V., Vergano S.,
RA Spangler B., Farrow E., Kussman J., Safina N., Saunders C., Boycott K.M.,
RA Thiffault I.;
RT "Matchmaking facilitates the diagnosis of an autosomal-recessive
RT mitochondrial disease caused by biallelic mutation of the tRNA
RT isopentenyltransferase (TRIT1) gene.";
RL Hum. Mutat. 38:511-516(2017).
RN [19]
RP VARIANT COXPD35 LYS-409.
RX PubMed=32948376; DOI=10.1016/j.braindev.2020.08.016;
RA Yoo S., Kim Y.A., Yoon J.Y., Seo G.H., Keum C., Cheon C.K.;
RT "The first Korean cases of combined oxidative phosphorylation deficiency 35
RT with two novel TRIT1 mutations in two siblings confirmed by clinical and
RT molecular investigation.";
RL Brain Dev. 43:325-330(2021).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 of both cytosolic and mitochondrial tRNAs,
CC leading to the formation of N6-(dimethylallyl)adenosine (i6A37)
CC (PubMed:11111046, PubMed:24126054, PubMed:24901367, PubMed:34774131).
CC Mediates modification of a limited subset of tRNAs: tRNA(Ser)(AGA),
CC tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial modification of the
CC selenocysteine tRNA(Ser)(UCA) (PubMed:24126054). TRIT1 is therefore
CC required for selenoprotein expression (PubMed:24126054).
CC {ECO:0000269|PubMed:11111046, ECO:0000269|PubMed:24126054,
CC ECO:0000269|PubMed:24901367, ECO:0000269|PubMed:34774131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC Evidence={ECO:0000269|PubMed:24126054, ECO:0000269|PubMed:24901367};
CC -!- INTERACTION:
CC Q9H3H1-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25932209, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:24901367}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9H3H1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3H1-2; Sequence=VSP_010719;
CC Name=3;
CC IsoId=Q9H3H1-3; Sequence=VSP_010719, VSP_010720;
CC Name=4;
CC IsoId=Q9H3H1-4; Sequence=VSP_010721;
CC Name=5;
CC IsoId=Q9H3H1-5; Sequence=VSP_012415, VSP_010720;
CC Name=6;
CC IsoId=Q9H3H1-6; Sequence=VSP_053746, VSP_053747;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 35 (COXPD35)
CC [MIM:617873]: An autosomal recessive disorder caused by defective
CC mitochondrial metabolism and deficiencies of mitochondrial respiratory
CC enzyme complexes. Clinical manifestations include global developmental
CC delay, intellectual disability, microcephaly, and early-onset seizures.
CC {ECO:0000269|PubMed:24901367, ECO:0000269|PubMed:28185376,
CC ECO:0000269|PubMed:32088416, ECO:0000269|PubMed:32948376}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AF074918; AAG31324.1; -; Transcribed_RNA.
DR EMBL; AY702944; AAW63405.1; -; mRNA.
DR EMBL; AY702945; AAW63406.1; -; mRNA.
DR EMBL; AY303390; AAP60111.1; -; mRNA.
DR EMBL; AK000068; BAA90923.1; -; mRNA.
DR EMBL; CR457226; CAG33507.1; -; mRNA.
DR EMBL; AL033527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010741; AAH10741.2; -; mRNA.
DR EMBL; BC107569; AAI07570.1; -; mRNA.
DR EMBL; BC128155; AAI28156.1; -; mRNA.
DR EMBL; AY052768; AAL14107.1; -; mRNA.
DR CCDS; CCDS30681.1; -. [Q9H3H1-1]
DR CCDS; CCDS81302.1; -. [Q9H3H1-5]
DR CCDS; CCDS81303.1; -. [Q9H3H1-4]
DR RefSeq; NP_001299620.1; NM_001312691.1. [Q9H3H1-4]
DR RefSeq; NP_001299621.1; NM_001312692.1. [Q9H3H1-5]
DR RefSeq; NP_060116.2; NM_017646.5. [Q9H3H1-1]
DR RefSeq; XP_006710769.1; XM_006710706.1. [Q9H3H1-2]
DR AlphaFoldDB; Q9H3H1; -.
DR SMR; Q9H3H1; -.
DR BioGRID; 120161; 13.
DR IntAct; Q9H3H1; 7.
DR MINT; Q9H3H1; -.
DR STRING; 9606.ENSP00000321810; -.
DR iPTMnet; Q9H3H1; -.
DR MetOSite; Q9H3H1; -.
DR PhosphoSitePlus; Q9H3H1; -.
DR BioMuta; TRIT1; -.
DR DMDM; 56405066; -.
DR EPD; Q9H3H1; -.
DR jPOST; Q9H3H1; -.
DR MassIVE; Q9H3H1; -.
DR MaxQB; Q9H3H1; -.
DR PaxDb; Q9H3H1; -.
DR PeptideAtlas; Q9H3H1; -.
DR PRIDE; Q9H3H1; -.
DR ProteomicsDB; 61872; -.
DR ProteomicsDB; 80709; -. [Q9H3H1-1]
DR ProteomicsDB; 80710; -. [Q9H3H1-2]
DR ProteomicsDB; 80711; -. [Q9H3H1-3]
DR ProteomicsDB; 80712; -. [Q9H3H1-4]
DR ProteomicsDB; 80713; -. [Q9H3H1-5]
DR Antibodypedia; 17887; 137 antibodies from 22 providers.
DR DNASU; 54802; -.
DR Ensembl; ENST00000316891.10; ENSP00000321810.5; ENSG00000043514.17. [Q9H3H1-1]
DR Ensembl; ENST00000372818.5; ENSP00000361905.1; ENSG00000043514.17. [Q9H3H1-4]
DR Ensembl; ENST00000441669.6; ENSP00000388333.2; ENSG00000043514.17. [Q9H3H1-5]
DR Ensembl; ENST00000537440.5; ENSP00000437700.1; ENSG00000043514.17. [Q9H3H1-6]
DR GeneID; 54802; -.
DR KEGG; hsa:54802; -.
DR MANE-Select; ENST00000316891.10; ENSP00000321810.5; NM_017646.6; NP_060116.2.
DR UCSC; uc001cem.5; human. [Q9H3H1-1]
DR CTD; 54802; -.
DR DisGeNET; 54802; -.
DR GeneCards; TRIT1; -.
DR HGNC; HGNC:20286; TRIT1.
DR HPA; ENSG00000043514; Low tissue specificity.
DR MalaCards; TRIT1; -.
DR MIM; 617840; gene.
DR MIM; 617873; phenotype.
DR neXtProt; NX_Q9H3H1; -.
DR OpenTargets; ENSG00000043514; -.
DR PharmGKB; PA134943037; -.
DR VEuPathDB; HostDB:ENSG00000043514; -.
DR eggNOG; KOG1384; Eukaryota.
DR GeneTree; ENSGT00390000015214; -.
DR HOGENOM; CLU_032616_2_2_1; -.
DR InParanoid; Q9H3H1; -.
DR OMA; NGDAMQM; -.
DR PhylomeDB; Q9H3H1; -.
DR TreeFam; TF315069; -.
DR BRENDA; 2.5.1.75; 2681.
DR PathwayCommons; Q9H3H1; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR SignaLink; Q9H3H1; -.
DR BioGRID-ORCS; 54802; 180 hits in 1082 CRISPR screens.
DR ChiTaRS; TRIT1; human.
DR GeneWiki; TRIT1; -.
DR GenomeRNAi; 54802; -.
DR Pharos; Q9H3H1; Tbio.
DR PRO; PR:Q9H3H1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H3H1; protein.
DR Bgee; ENSG00000043514; Expressed in oocyte and 202 other tissues.
DR ExpressionAtlas; Q9H3H1; baseline and differential.
DR Genevisible; Q9H3H1; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070900; P:mitochondrial tRNA modification; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR030666; IPP_transferase_euk.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PIRSF; PIRSF039110; IPP_transferase; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Disease variant;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Transferase;
KW Transit peptide; tRNA processing; Zinc; Zinc-finger.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..467
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000019023"
FT ZN_FING 395..425
FT /note="Matrin-type"
FT REGION 55..58
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 183..187
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 221..230
FT /note="Core aggregation region"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 233..255
FT /note="Interaction with isopentenylpyrophosphate
FT transferase"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 281..283
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 313..331
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 429..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..37
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT SITE 122
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT SITE 206
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_010719"
FT VAR_SEQ 1..5
FT /note="MASVA -> MFRKI (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15870694"
FT /id="VSP_053746"
FT VAR_SEQ 6..309
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15870694"
FT /id="VSP_053747"
FT VAR_SEQ 59..138
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012415"
FT VAR_SEQ 235..236
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_010720"
FT VAR_SEQ 311..336
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11560893"
FT /id="VSP_010721"
FT VARIANT 8..467
FT /note="Missing (in COXPD35)"
FT /evidence="ECO:0000269|PubMed:28185376"
FT /id="VAR_080745"
FT VARIANT 202
FT /note="F -> L (in dbSNP:rs3738671)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020486"
FT VARIANT 283
FT /note="I -> S (in COXPD35; unknown pathological
FT significance; dbSNP:rs199622789)"
FT /evidence="ECO:0000269|PubMed:28185376"
FT /id="VAR_080746"
FT VARIANT 286
FT /note="K -> E (in COXPD35; unknown pathological
FT significance; dbSNP:rs1060505019)"
FT /evidence="ECO:0000269|PubMed:28185376"
FT /id="VAR_080747"
FT VARIANT 323
FT /note="R -> Q (in COXPD35; reduced tRNA
FT dimethylallyltransferase activity; dbSNP:rs1047420796)"
FT /evidence="ECO:0000269|PubMed:24901367"
FT /id="VAR_080748"
FT VARIANT 402..467
FT /note="Missing (in COXPD35; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28185376"
FT /id="VAR_080749"
FT VARIANT 409
FT /note="E -> K (in COXPD35; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32948376"
FT /id="VAR_085917"
FT VARIANT 419
FT /note="H -> P (in COXPD35; unknown pathological
FT significance; dbSNP:rs566435653)"
FT /evidence="ECO:0000269|PubMed:28185376"
FT /id="VAR_080750"
FT CONFLICT 303
FT /note="S -> G (in Ref. 5; CAG33507)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="H -> Y (in Ref. 8; AAL14107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52725 MW; 634469919D7F56A5 CRC64;
MASVAAARAV PVGSGLRGLQ RTLPLVVILG ATGTGKSTLA LQLGQRLGGE IVSADSMQVY
EGLDIITNKV SAQEQRICRH HMISFVDPLV TNYTVVDFRN RATALIEDIF ARDKIPIVVG
GTNYYIESLL WKVLVNTKPQ EMGTEKVIDR KVELEKEDGL VLHKRLSQVD PEMAAKLHPH
DKRKVARSLQ VFEETGISHS EFLHRQHTEE GGGPLGGPLK FSNPCILWLH ADQAVLDERL
DKRVDDMLAA GLLEELRDFH RRYNQKNVSE NSQDYQHGIF QSIGFKEFHE YLITEGKCTL
ETSNQLLKKG IEALKQVTKR YARKQNRWVK NRFLSRPGPI VPPVYGLEVS DVSKWEESVL
EPALEIVQSF IQGHKPTATP IKMPYNEAEN KRSYHLCDLC DRIIIGDREW AAHIKSKSHL
NQLKKRRRLD SDAVNTIESQ SVSPDHNKEP KEKGSPGQND QELKCSV
