ID TRM6_HUMAN Reviewed; 497 AA. AC Q9UJA5; B4DUV6; Q76P92; Q9BQV5; Q9ULR7; Q9Y2Z8; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-SEP-2017, entry version 131. DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6; DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6; DE Short=tRNA(m1A58)MTase subunit TRM6; GN Name=TRMT6; Synonyms=KIAA1153, TRM6; ORFNames=CGI-09; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=10574461; DOI=10.1093/dnares/6.5.329; RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.; RT "Characterization of cDNA clones selected by the GeneMark analysis RT from size-fractionated cDNA libraries from human brain."; RL DNA Res. 6:329-336(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP GLY-299. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP GLY-299. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, AND SUBUNIT. RX PubMed=16043508; DOI=10.1261/rna.5040605; RA Ozanick S., Krecic A., Andersland J., Anderson J.T.; RT "The bipartite structure of the tRNA m1A58 methyltransferase from S. RT cerevisiae is conserved in humans."; RL RNA 11:1281-1290(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] 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., RA Buerckstuemmer T., 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-305, AND RP IDENTIFICATION BY 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 [10] {ECO:0000244|PDB:5CCB, ECO:0000244|PDB:5CCX, ECO:0000244|PDB:5CD1} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH TRMT61A. RX PubMed=26470919; DOI=10.1016/j.jmb.2015.10.005; RA Finer-Moore J., Czudnochowski N., O'Connell J.D. III, Wang A.L., RA Stroud R.M.; RT "Crystal structure of the human tRNA m(1)A58 methyltransferase- RT tRNA(3)(Lys) complex: refolding of substrate tRNA allows access to the RT methylation target."; RL J. Mol. Biol. 427:3862-3876(2015). CC -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)- CC methyltransferase, which catalyzes the formation of N(1)- CC methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. CC {ECO:0000269|PubMed:16043508}. CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two CC copies of TRMT61A. {ECO:0000269|PubMed:26470919, CC ECO:0000305|PubMed:16043508}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UJA5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJA5-2; Sequence=VSP_018025; CC Name=3; CC IsoId=Q9UJA5-3; Sequence=VSP_031100, VSP_031101; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q9UJA5-4; Sequence=VSP_054740; CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, testis and ovary. CC {ECO:0000269|PubMed:10574461}. CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86467.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=BAA86467.1; Type=Frameshift; Positions=319; Evidence={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; AB032979; BAA86467.1; ALT_INIT; mRNA. DR EMBL; AF132943; AAD27718.1; ALT_FRAME; mRNA. DR EMBL; AK000613; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK300812; BAG62468.1; -; mRNA. DR EMBL; AL035461; CAB55274.1; -; Genomic_DNA. DR EMBL; BC001262; AAH01262.1; -; mRNA. DR CCDS; CCDS13093.1; -. [Q9UJA5-1] DR CCDS; CCDS63225.1; -. [Q9UJA5-4] DR RefSeq; NP_001268396.1; NM_001281467.1. [Q9UJA5-4] DR RefSeq; NP_057023.2; NM_015939.4. [Q9UJA5-1] DR UniGene; Hs.128791; -. DR PDB; 5CCB; X-ray; 2.00 A; B=1-497. DR PDB; 5CCX; X-ray; 2.10 A; B=1-497. DR PDB; 5CD1; X-ray; 3.60 A; B/E=1-497. DR PDBsum; 5CCB; -. DR PDBsum; 5CCX; -. DR PDBsum; 5CD1; -. DR ProteinModelPortal; Q9UJA5; -. DR SMR; Q9UJA5; -. DR BioGrid; 119634; 54. DR IntAct; Q9UJA5; 14. DR MINT; MINT-5005724; -. DR STRING; 9606.ENSP00000203001; -. DR iPTMnet; Q9UJA5; -. DR PhosphoSitePlus; Q9UJA5; -. DR DMDM; 74753354; -. DR EPD; Q9UJA5; -. DR PaxDb; Q9UJA5; -. DR PeptideAtlas; Q9UJA5; -. DR PRIDE; Q9UJA5; -. DR DNASU; 51605; -. DR Ensembl; ENST00000203001; ENSP00000203001; ENSG00000089195. [Q9UJA5-1] DR Ensembl; ENST00000453074; ENSP00000392070; ENSG00000089195. [Q9UJA5-4] DR GeneID; 51605; -. DR KEGG; hsa:51605; -. DR UCSC; uc002wmh.3; human. [Q9UJA5-1] DR CTD; 51605; -. DR DisGeNET; 51605; -. DR EuPathDB; HostDB:ENSG00000089195.14; -. DR GeneCards; TRMT6; -. DR HGNC; HGNC:20900; TRMT6. DR HPA; HPA047032; -. DR HPA; HPA050408; -. DR neXtProt; NX_Q9UJA5; -. DR OpenTargets; ENSG00000089195; -. DR PharmGKB; PA162407063; -. DR eggNOG; KOG1416; Eukaryota. DR eggNOG; ENOG410XSXD; LUCA. DR GeneTree; ENSGT00390000008327; -. DR HOGENOM; HOG000232007; -. DR HOVERGEN; HBG061231; -. DR InParanoid; Q9UJA5; -. DR KO; K03256; -. DR OMA; RKCPESD; -. DR OrthoDB; EOG091G095O; -. DR PhylomeDB; Q9UJA5; -. DR TreeFam; TF314835; -. DR BRENDA; 2.1.1.220; 2681. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR GenomeRNAi; 51605; -. DR PRO; PR:Q9UJA5; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000089195; -. DR CleanEx; HS_TRMT6; -. DR Genevisible; Q9UJA5; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IEA:InterPro. DR GO; GO:0006400; P:tRNA modification; TAS:Reactome. DR InterPro; IPR017423; TRM6. DR PANTHER; PTHR12945; PTHR12945; 1. DR Pfam; PF04189; Gcd10p; 1. DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; tRNA processing. FT CHAIN 1 497 tRNA (adenine(58)-N(1))-methyltransferase FT non-catalytic subunit TRM6. FT /FTId=PRO_0000233098. FT REGION 94 104 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT REGION 145 154 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT REGION 175 182 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT REGION 415 423 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT REGION 434 441 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT BINDING 349 349 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT BINDING 377 377 Substrate. {ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919}. FT MOD_RES 107 107 Phosphothreonine. FT {ECO:0000244|PubMed:17525332}. FT MOD_RES 298 298 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 305 305 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT VAR_SEQ 1 170 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054740. FT VAR_SEQ 344 365 QEKQRRQEEQRKRHLEAAALLS -> SGKNRGRQGRSSGKD FT FWGCRFA (in isoform 3). FT {ECO:0000303|PubMed:10810093}. FT /FTId=VSP_031100. FT VAR_SEQ 366 497 Missing (in isoform 3). FT {ECO:0000303|PubMed:10810093}. FT /FTId=VSP_031101. FT VAR_SEQ 372 497 LIVASRFHPTPLLLSLLDFVAPSRPFVVYCQYKEPLLECYT FT KLRERGGVINLRLSETWLRNYQVLPDRSHPKLLMSGGGGYL FT LSGFTVAMDNLKADTSLKSNASTLESHETEEPAAKKRKCPE FT SDS -> CVDGRRQETPQCMWALLQTDWHSLSPCL (in FT isoform 2). FT {ECO:0000303|PubMed:10574461}. FT /FTId=VSP_018025. FT VARIANT 293 293 E -> K (in dbSNP:rs6139876). FT /FTId=VAR_053789. FT VARIANT 299 299 E -> G (in dbSNP:rs451571). FT {ECO:0000269|PubMed:10810093, FT ECO:0000269|PubMed:14702039}. FT /FTId=VAR_053790. FT VARIANT 333 333 P -> L (in dbSNP:rs35203742). FT /FTId=VAR_053791. FT STRAND 25 30 {ECO:0000244|PDB:5CCB}. FT STRAND 33 38 {ECO:0000244|PDB:5CCB}. FT STRAND 44 46 {ECO:0000244|PDB:5CCB}. FT STRAND 51 53 {ECO:0000244|PDB:5CCB}. FT HELIX 54 56 {ECO:0000244|PDB:5CCB}. FT STRAND 59 61 {ECO:0000244|PDB:5CCB}. FT STRAND 64 74 {ECO:0000244|PDB:5CCX}. FT HELIX 108 116 {ECO:0000244|PDB:5CCB}. FT HELIX 122 130 {ECO:0000244|PDB:5CCB}. FT STRAND 132 134 {ECO:0000244|PDB:5CCB}. FT HELIX 135 137 {ECO:0000244|PDB:5CCB}. FT HELIX 140 154 {ECO:0000244|PDB:5CCB}. FT STRAND 159 161 {ECO:0000244|PDB:5CCB}. FT HELIX 165 175 {ECO:0000244|PDB:5CCB}. FT HELIX 177 180 {ECO:0000244|PDB:5CCB}. FT HELIX 185 194 {ECO:0000244|PDB:5CCB}. FT STRAND 202 207 {ECO:0000244|PDB:5CCB}. FT HELIX 212 221 {ECO:0000244|PDB:5CCB}. FT STRAND 225 232 {ECO:0000244|PDB:5CCB}. FT HELIX 239 243 {ECO:0000244|PDB:5CCB}. FT HELIX 248 251 {ECO:0000244|PDB:5CCB}. FT STRAND 254 258 {ECO:0000244|PDB:5CCB}. FT HELIX 259 261 {ECO:0000244|PDB:5CCB}. FT HELIX 262 267 {ECO:0000244|PDB:5CCB}. FT HELIX 342 365 {ECO:0000244|PDB:5CCB}. FT STRAND 369 375 {ECO:0000244|PDB:5CCB}. FT HELIX 380 387 {ECO:0000244|PDB:5CCB}. FT HELIX 388 390 {ECO:0000244|PDB:5CCB}. FT STRAND 396 404 {ECO:0000244|PDB:5CCB}. FT HELIX 405 417 {ECO:0000244|PDB:5CCB}. FT STRAND 420 434 {ECO:0000244|PDB:5CCB}. FT STRAND 441 446 {ECO:0000244|PDB:5CCB}. FT STRAND 448 450 {ECO:0000244|PDB:5CCB}. FT STRAND 452 458 {ECO:0000244|PDB:5CCB}. SQ SEQUENCE 497 AA; 55799 MW; 920800D0722A6CBB CRC64; MEGSGEQPGP QPQHPGDHRI RDGDFVVLKR EDVFKAVQVQ RRKKVTFEKQ WFYLDNVIGH SYGTAFEVTS GGSLQPKKKR EEPTAETKEA GTDNRNIVDD GKSQKLTQDD IKALKDKGIK GEEIVQQLIE NSTTFRDKTE FAQDKYIKKK KKKYEAIITV VKPSTRILSI MYYAREPGKI NHMRYDTLAQ MLTLGNIRAG NKMIVMETCA GLVLGAMMER MGGFGSIIQL YPGGGPVRAA TACFGFPKSF LSGLYEFPLN KVDSLLHGTF SAKMLSSEPK DSALVEESNG TLEEKQASEQ ENEDSMAEAP ESNHPEDQET METISQDPEH KGPKERGSKK DYIQEKQRRQ EEQRKRHLEA AALLSERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVA MDNLKADTSL KSNASTLESH ETEEPAAKKR KCPESDS //