TRM6_MOUSE
ID TRM6_MOUSE Reviewed; 497 AA.
AC Q8CE96; Q3TJZ8; Q3TME7; Q6ZPW8; Q80Y59; Q8CEU0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6;
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6 {ECO:0000250|UniProtKB:Q9UJA5};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE Short=tRNA(m1A58)MTase subunit TRM6;
GN Name=Trmt6; Synonyms=Kiaa1153, Trm6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Blastocyst;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA. Together with the
CC TRMT61A catalytic subunit, part of a mRNA N(1)-methyltransferase
CC complex that mediates methylation of adenosine residues at the N(1)
CC position of a small subset of mRNAs: N(1) methylation takes place in
CC tRNA T-loop-like structures of mRNAs and is only present at low
CC stoichiometries. {ECO:0000250|UniProtKB:Q9UJA5}.
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000250|UniProtKB:Q9UJA5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CE96-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8CE96-3; Sequence=VSP_018026;
CC Name=4;
CC IsoId=Q8CE96-4; Sequence=VSP_018026, VSP_018027, VSP_018028;
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98110.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98110.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK129300; BAC98110.1; ALT_SEQ; mRNA.
DR EMBL; AK014359; BAC25432.1; -; mRNA.
DR EMBL; AK165976; BAE38495.1; -; mRNA.
DR EMBL; AK167222; BAE39347.1; -; mRNA.
DR EMBL; AK028755; BAC26100.1; -; mRNA.
DR EMBL; BC049083; AAH49083.1; -; mRNA.
DR EMBL; BC052648; AAH52648.1; -; mRNA.
DR CCDS; CCDS50728.1; -. [Q8CE96-1]
DR RefSeq; NP_780322.2; NM_175113.3. [Q8CE96-1]
DR RefSeq; XP_006500115.1; XM_006500052.2.
DR AlphaFoldDB; Q8CE96; -.
DR SMR; Q8CE96; -.
DR BioGRID; 211814; 10.
DR STRING; 10090.ENSMUSP00000044687; -.
DR iPTMnet; Q8CE96; -.
DR PhosphoSitePlus; Q8CE96; -.
DR EPD; Q8CE96; -.
DR MaxQB; Q8CE96; -.
DR PaxDb; Q8CE96; -.
DR PeptideAtlas; Q8CE96; -.
DR PRIDE; Q8CE96; -.
DR ProteomicsDB; 258851; -. [Q8CE96-1]
DR ProteomicsDB; 258852; -. [Q8CE96-3]
DR ProteomicsDB; 258853; -. [Q8CE96-4]
DR Antibodypedia; 23943; 93 antibodies from 19 providers.
DR DNASU; 66926; -.
DR Ensembl; ENSMUST00000039554; ENSMUSP00000044687; ENSMUSG00000037376. [Q8CE96-1]
DR GeneID; 66926; -.
DR KEGG; mmu:66926; -.
DR UCSC; uc008mng.1; mouse. [Q8CE96-1]
DR CTD; 51605; -.
DR MGI; MGI:1914176; Trmt6.
DR VEuPathDB; HostDB:ENSMUSG00000037376; -.
DR eggNOG; KOG1416; Eukaryota.
DR GeneTree; ENSGT00390000008327; -.
DR HOGENOM; CLU_010916_0_1_1; -.
DR InParanoid; Q8CE96; -.
DR OMA; TFHNRTE; -.
DR OrthoDB; 543764at2759; -.
DR PhylomeDB; Q8CE96; -.
DR TreeFam; TF314835; -.
DR BioGRID-ORCS; 66926; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Trmt6; mouse.
DR PRO; PR:Q8CE96; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CE96; protein.
DR Bgee; ENSMUSG00000037376; Expressed in metanephric ureteric bud and 233 other tissues.
DR Genevisible; Q8CE96; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; ISO:MGI.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISO:MGI.
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 Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..497
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit TRM6"
FT /id="PRO_0000233099"
FT REGION 81..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..105
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 146..155
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 176..183
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 275..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..423
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 434..441
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 474..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018026"
FT VAR_SEQ 343..358
FT /note="IQEKQRRQEEQRKRHL -> VSMSRVIILVIASEPR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018027"
FT VAR_SEQ 359..497
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018028"
FT CONFLICT 9
FT /note="P -> Q (in Ref. 2; BAE38495)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="S -> P (in Ref. 2; BAE38495)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="V -> I (in Ref. 2; BAE38495)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> N (in Ref. 2; BAE38495)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="R -> H (in Ref. 2; BAE39347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55518 MW; F6F16FE689DB514B CRC64;
MEASAAEQPS SPPPPLGDHC IHDGDFVVLK REDVFKAVQV QRRKKVTFEK QWFYLDNAIG
HSYGSAFDVS SGGSLQLRKK LEEPASETKE AGTDNRNIVD DGKSQKLTQD DIKALKDKGI
KGEEIVQQLI ENSTTFRDKT EFAQDKYIKK KKKKYEAIVT ILKPSTRILS IMYYAREPGK
INHMRYDTLA QMLTLGNIRA GNKMIVMETC SGLVLGAMME RMGGFGSIIQ LYPGDGPVRA
ATACFGFPKS FLSGLYEFPL NKVNSLLNGT FSAEMLSSEP KDSTPVEESN GELEEKEIAE
QADEDNIVDA AENNSGEQRP MEIVPGDPEN KEPKEKRSKR DYIQEKQRRQ EEQRKRHLEA
AALLGERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV
INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVV SDSLRADPSL KSCTGALDPH
KAEEPAAKKQ KCMESAS
