TRM9B_MOUSE
ID TRM9B_MOUSE Reviewed; 447 AA.
AC Q80WQ4; Q5DTX8; Q8CA94; Q8CAM3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable tRNA methyltransferase 9B;
DE AltName: Full=Probable tRNA methyltransferase 9-like protein;
DE EC=2.1.1.-;
GN Name=Trmt9b; Synonyms=Kiaa1456, Trmt9l;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Hypothalamus, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 SER-212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: May modifie wobble uridines in specific arginine and glutamic
CC acid tRNAs. Acts as a tumor suppressor by promoting the expression of
CC LIN9 (By similarity). {ECO:0000250|UniProtKB:Q9P272}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80WQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WQ4-2; Sequence=VSP_032795;
CC Name=3;
CC IsoId=Q80WQ4-3; Sequence=VSP_032796, VSP_032797;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK038497; BAC30018.1; -; mRNA.
DR EMBL; AK039253; BAC30293.1; -; mRNA.
DR EMBL; AK141601; BAE24758.1; -; mRNA.
DR EMBL; AK220392; BAD90446.1; ALT_INIT; mRNA.
DR EMBL; BC052184; AAH52184.1; -; mRNA.
DR CCDS; CCDS22248.1; -. [Q80WQ4-1]
DR RefSeq; NP_795926.2; NM_176952.4. [Q80WQ4-1]
DR RefSeq; XP_006509196.1; XM_006509133.2.
DR RefSeq; XP_006509198.1; XM_006509135.2.
DR RefSeq; XP_006509199.1; XM_006509136.3. [Q80WQ4-1]
DR AlphaFoldDB; Q80WQ4; -.
DR SMR; Q80WQ4; -.
DR STRING; 10090.ENSMUSP00000119912; -.
DR iPTMnet; Q80WQ4; -.
DR PhosphoSitePlus; Q80WQ4; -.
DR PaxDb; Q80WQ4; -.
DR PeptideAtlas; Q80WQ4; -.
DR PRIDE; Q80WQ4; -.
DR ProteomicsDB; 298231; -. [Q80WQ4-1]
DR ProteomicsDB; 298232; -. [Q80WQ4-2]
DR ProteomicsDB; 298233; -. [Q80WQ4-3]
DR Antibodypedia; 58596; 59 antibodies from 16 providers.
DR DNASU; 319582; -.
DR Ensembl; ENSMUST00000147525; ENSMUSP00000119912; ENSMUSG00000039620. [Q80WQ4-1]
DR Ensembl; ENSMUST00000152039; ENSMUSP00000119288; ENSMUSG00000039620. [Q80WQ4-3]
DR Ensembl; ENSMUST00000171777; ENSMUSP00000127875; ENSMUSG00000039620. [Q80WQ4-1]
DR GeneID; 319582; -.
DR KEGG; mmu:319582; -.
DR UCSC; uc009llk.1; mouse. [Q80WQ4-1]
DR CTD; 57604; -.
DR MGI; MGI:2442328; Trmt9b.
DR VEuPathDB; HostDB:ENSMUSG00000039620; -.
DR eggNOG; KOG1331; Eukaryota.
DR GeneTree; ENSGT00940000160373; -.
DR HOGENOM; CLU_029501_0_0_1; -.
DR InParanoid; Q80WQ4; -.
DR OMA; HGNWCIV; -.
DR OrthoDB; 996085at2759; -.
DR PhylomeDB; Q80WQ4; -.
DR TreeFam; TF316056; -.
DR BioGRID-ORCS; 319582; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q80WQ4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80WQ4; protein.
DR Bgee; ENSMUSG00000039620; Expressed in cerebellar cortex and 105 other tissues.
DR ExpressionAtlas; Q80WQ4; baseline and differential.
DR Genevisible; Q80WQ4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; ISO:MGI.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032873; Trm9.
DR PANTHER; PTHR13069:SF21; PTHR13069:SF21; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..447
FT /note="Probable tRNA methyltransferase 9B"
FT /id="PRO_0000328793"
FT REGION 274..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032795"
FT VAR_SEQ 110
FT /note="V -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032796"
FT VAR_SEQ 111..447
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032797"
FT CONFLICT 184
FT /note="R -> T (in Ref. 2; BAD90446)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> G (in Ref. 2; BAD90446)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="G -> E (in Ref. 2; BAD90446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50277 MW; 831CE496E09C7165 CRC64;
MDPEAVELEK RHVHSVYENT APYFTDLQSK AWPRVRQFLQ DQKPGSLVAD IGCGTGKYLK
VNSQVHTLGC DYCGPLVEIA RNRGCEVMVC DNLNLPFRDQ GFDAIISIGV IHHFSTKERR
IRAIKEMARV LAPGGQLMIY VWAMEQKNRR FEKQDVLVPW NRALCSRLLS ESHQSWGHHC
EHPRSRGFQG PGSVCGCAVC FKGRCDSKRS HSMDYGSAVA RTCCEAISKE GERENGLYSN
FGKSFRSWFF SRSLDESTLR KQIERVRPMK IPEAWANSTV SQQPSRHPSL DLHAPEPFST
KGPNLDEVFV DTSSQRHLGW LRTPGTSDNF SGHKGGGSRR KEGGNFLDIT DTGDSVAASN
SSDPSARKIL RRVSAFDSND SNSEDSSFLE AQRDATDSKA FMRYYHVFRE GELSSLLQES
VSELQVLSSG NDHGNWCIIA EKKRSWD
