TRM2A_HUMAN
ID TRM2A_HUMAN Reviewed; 625 AA.
AC Q8IZ69; D3DX25; Q32P57; Q96ME6; Q9H732;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=tRNA (uracil-5-)-methyltransferase homolog A {ECO:0000305};
DE EC=2.1.1.35 {ECO:0000269|PubMed:31361898, ECO:0000269|PubMed:33799331};
DE AltName: Full=mRNA (uracil-5-)-methyltransferase TRMT2A {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:34123281};
GN Name=TRMT2A {ECO:0000303|PubMed:31361898, ECO:0000312|HGNC:HGNC:24974};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, Colon, and Kidney;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, 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 [11]
RP VARIANT [LARGE SCALE ANALYSIS] SER-604.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=31361898; DOI=10.1093/nar/gkz658;
RA Carter J.M., Emmett W., Mozos I.R., Kotter A., Helm M., Ule J., Hussain S.;
RT "FICC-Seq: a method for enzyme-specified profiling of methyl-5-uridine in
RT cellular RNA.";
RL Nucleic Acids Res. 47:e113-e113(2019).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34123281; DOI=10.1039/c9sc05094a;
RA Cheng Q.Y., Xiong J., Ma C.J., Dai Y., Ding J.H., Liu F.L., Yuan B.F.,
RA Feng Y.Q.;
RT "Chemical tagging for sensitive determination of uridine modifications in
RT RNA.";
RL Chem. Sci. 11:1878-1891(2020).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33799331; DOI=10.3390/ijms22062941;
RA Pereira M., Ribeiro D.R., Pinheiro M.M., Ferreira M., Kellner S.,
RA Soares A.R.;
RT "m5U54 tRNA hypomodification by lack of TRMT2A drives the generation of
RT tRNA-derived small RNAs.";
RL Int. J. Mol. Sci. 22:0-0(2021).
RN [15]
RP FUNCTION.
RX PubMed=34556860; DOI=10.1038/s41589-021-00874-8;
RA Dai W., Li A., Yu N.J., Nguyen T., Leach R.W., Wuehr M., Kleiner R.E.;
RT "Activity-based RNA-modifying enzyme probing reveals DUS3L-mediated
RT dihydrouridylation.";
RL Nat. Chem. Biol. 17:1178-1187(2021).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes the formation of 5-methyl-uridine in tRNAs and some mRNAs
CC (PubMed:31361898, PubMed:33799331, PubMed:34556860). Mainly catalyzes
CC the methylation of uridine at position 54 (m5U54) in cytosolic tRNAs
CC (PubMed:31361898, PubMed:33799331). Also able to mediate the formation
CC of 5-methyl-uridine in some mRNAs (PubMed:34123281).
CC {ECO:0000269|PubMed:31361898, ECO:0000269|PubMed:33799331,
CC ECO:0000269|PubMed:34123281, ECO:0000269|PubMed:34556860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC Evidence={ECO:0000269|PubMed:33799331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42713;
CC Evidence={ECO:0000269|PubMed:33799331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA + S-adenosyl-L-methionine = a 5-
CC methyluridine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69863, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17793,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447;
CC Evidence={ECO:0000269|PubMed:34123281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69864;
CC Evidence={ECO:0000269|PubMed:34123281};
CC -!- INTERACTION:
CC Q8IZ69; Q92624: APPBP2; NbExp=3; IntAct=EBI-2515774, EBI-743771;
CC Q8IZ69; P23508: MCC; NbExp=3; IntAct=EBI-2515774, EBI-307531;
CC Q8IZ69; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2515774, EBI-16439278;
CC Q8IZ69; Q14696: MESD; NbExp=3; IntAct=EBI-2515774, EBI-6165891;
CC Q8IZ69; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2515774, EBI-79165;
CC Q8IZ69; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2515774, EBI-11741437;
CC Q8IZ69; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-2515774, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:31361898}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZ69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ69-2; Sequence=VSP_011322, VSP_011323;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; CR456354; CAG30240.1; -; mRNA.
DR EMBL; AK025106; BAB15067.1; -; mRNA.
DR EMBL; AK057029; BAB71349.1; -; mRNA.
DR EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471176; EAX02996.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02997.1; -; Genomic_DNA.
DR EMBL; BC013352; AAH13352.2; -; mRNA.
DR EMBL; BC017184; AAH17184.2; -; mRNA.
DR EMBL; BC108251; AAI08252.1; -; mRNA.
DR CCDS; CCDS13774.1; -. [Q8IZ69-1]
DR CCDS; CCDS58793.1; -. [Q8IZ69-2]
DR RefSeq; NP_001244923.1; NM_001257994.1. [Q8IZ69-2]
DR RefSeq; NP_073564.3; NM_022727.5. [Q8IZ69-1]
DR RefSeq; NP_892029.2; NM_182984.4. [Q8IZ69-1]
DR PDB; 7NTN; X-ray; 2.02 A; A=69-147.
DR PDB; 7NTO; X-ray; 1.23 A; A=69-147.
DR PDBsum; 7NTN; -.
DR PDBsum; 7NTO; -.
DR AlphaFoldDB; Q8IZ69; -.
DR SMR; Q8IZ69; -.
DR BioGRID; 117968; 176.
DR IntAct; Q8IZ69; 61.
DR MINT; Q8IZ69; -.
DR STRING; 9606.ENSP00000252136; -.
DR GlyGen; Q8IZ69; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZ69; -.
DR PhosphoSitePlus; Q8IZ69; -.
DR BioMuta; TRMT2A; -.
DR DMDM; 51316479; -.
DR EPD; Q8IZ69; -.
DR jPOST; Q8IZ69; -.
DR MassIVE; Q8IZ69; -.
DR MaxQB; Q8IZ69; -.
DR PaxDb; Q8IZ69; -.
DR PeptideAtlas; Q8IZ69; -.
DR PRIDE; Q8IZ69; -.
DR ProteomicsDB; 71283; -. [Q8IZ69-1]
DR ProteomicsDB; 71284; -. [Q8IZ69-2]
DR Antibodypedia; 250; 340 antibodies from 26 providers.
DR DNASU; 27037; -.
DR Ensembl; ENST00000252136.12; ENSP00000252136.7; ENSG00000099899.15. [Q8IZ69-1]
DR Ensembl; ENST00000403707.7; ENSP00000385807.3; ENSG00000099899.15. [Q8IZ69-1]
DR Ensembl; ENST00000404751.7; ENSP00000384968.3; ENSG00000099899.15. [Q8IZ69-2]
DR GeneID; 27037; -.
DR KEGG; hsa:27037; -.
DR MANE-Select; ENST00000252136.12; ENSP00000252136.7; NM_022727.6; NP_073564.3.
DR UCSC; uc002zrk.3; human. [Q8IZ69-1]
DR CTD; 27037; -.
DR DisGeNET; 27037; -.
DR GeneCards; TRMT2A; -.
DR HGNC; HGNC:24974; TRMT2A.
DR HPA; ENSG00000099899; Low tissue specificity.
DR MIM; 611151; gene.
DR neXtProt; NX_Q8IZ69; -.
DR OpenTargets; ENSG00000099899; -.
DR PharmGKB; PA164726751; -.
DR VEuPathDB; HostDB:ENSG00000099899; -.
DR eggNOG; KOG2187; Eukaryota.
DR GeneTree; ENSGT00530000063723; -.
DR HOGENOM; CLU_014689_4_2_1; -.
DR InParanoid; Q8IZ69; -.
DR PhylomeDB; Q8IZ69; -.
DR TreeFam; TF314569; -.
DR BRENDA; 2.1.1.35; 2681.
DR PathwayCommons; Q8IZ69; -.
DR SignaLink; Q8IZ69; -.
DR BioGRID-ORCS; 27037; 22 hits in 1075 CRISPR screens.
DR ChiTaRS; TRMT2A; human.
DR GenomeRNAi; 27037; -.
DR Pharos; Q8IZ69; Tbio.
DR PRO; PR:Q8IZ69; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8IZ69; protein.
DR Bgee; ENSG00000099899; Expressed in granulocyte and 130 other tissues.
DR ExpressionAtlas; Q8IZ69; baseline and differential.
DR Genevisible; Q8IZ69; HS.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0008169; F:C-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12439; RRM_TRMT2A; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_euk.
DR InterPro; IPR034262; TRMT2A_RRM.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904; PTHR45904; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Methyltransferase; mRNA processing; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..625
FT /note="tRNA (uracil-5-)-methyltransferase homolog A"
FT /id="PRO_0000081614"
FT DOMAIN 73..146
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..209
FT /evidence="ECO:0000255"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT ACT_SITE 581
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23003"
FT BINDING 411
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 461
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 510
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 550..562
FT /note="LCRAPSNRVKGIP -> APLFPPQPLQSPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011322"
FT VAR_SEQ 563..625
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011323"
FT VARIANT 602
FT /note="S -> R (in dbSNP:rs447017)"
FT /id="VAR_033721"
FT VARIANT 604
FT /note="P -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035482"
FT CONFLICT 498
FT /note="S -> G (in Ref. 2; BAB71349)"
FT /evidence="ECO:0000305"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:7NTO"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:7NTO"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:7NTO"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:7NTO"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:7NTO"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:7NTO"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7NTO"
SQ SEQUENCE 625 AA; 68726 MW; 2D310E521D846E06 CRC64;
MSENLDNEGP KPMESCGQES SSALSCPTVS VPPAAPAALE EVEKEGAGAA TGPGPQPGLY
SYIRDDLFTS EIFKLELQNV PRHASFSDVR RFLGRFGLQP HKTKLFGQPP CAFVTFRSAA
ERDKALRVLH GALWKGRPLS VRLARPKADP MARRRRQEGE SEPPVTRVAD VVTPLWTVPY
AEQLERKQLE CEQVLQKLAK EIGSTNRALL PWLLEQRHKH NKACCPLEGV RPSPQQTEYR
NKCEFLVGVG VDGEDNTVGC RLGKYKGGTC AVAAPFDTVH IPEATKQVVK AFQEFIRSTP
YSAYDPETYT GHWKQLTVRT SRRHQAMAIA YFHPQKLSPE ELAELKTSLA QHFTAGPGRA
SGVTCLYFVE EGQRKTPSQE GLPLEHVAGD RCIHEDLLGL TFRISPHAFF QVNTPAAEVL
YTVIQDWAQL DAGSMVLDVC CGTGTIGLAL ARKVKRVIGV ELCPEAVEDA RVNAQDNELS
NVEFHCGRAE DLVPTLVSRL ASQHLVAILD PPRAGLHSKV ILAIRRAKNL RRLLYVSCNP
RAAMGNFVDL CRAPSNRVKG IPFRPVKAVA VDLFPQTPHC EMLILFERVE HPNGTGVLGP
HSPPAQPTPG PPDNTLQETG TFPSS
