ID   TRM1_HUMAN              Reviewed;         659 AA.
AC   Q9NXH9; O76103; Q548Y5; Q8WVA6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   07-JUL-2009, entry version 71.
DE   RecName: Full=N(2),N(2)-dimethylguanosine tRNA methyltransferase;
DE            EC=2.1.1.32;
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
GN   Name=TRMT1;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   MEDLINE=20440386; PubMed=10982862; DOI=10.1093/nar/28.18.3445;
RA   Liu J., Straby K.B.;
RT   "The human tRNA(m22G26)dimethyltransferase: functional expression and
RT   characterization of a cloned hTRM1 gene.";
RL   Nucleic Acids Res. 28:3445-3451(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon mucosa;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Cervix, and Colon;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 AND
RP   THR-646, AND MASS SPECTROMETRY.
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   [8]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of
CC       most tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC       groups.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing N(2)-methylguanine.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NXH9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NXH9-2; Sequence=VSP_016720;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
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DR   EMBL; AF196479; AAG28495.1; -; mRNA.
DR   EMBL; AK000251; BAA91031.1; -; mRNA.
DR   EMBL; AC005546; AAC33150.1; -; Genomic_DNA.
DR   EMBL; BC002492; AAH02492.1; -; mRNA.
DR   EMBL; BC018302; AAH18302.1; -; mRNA.
DR   EMBL; BC040126; AAH40126.1; -; mRNA.
DR   IPI; IPI00020508; -.
DR   IPI; IPI00178861; -.
DR   RefSeq; NP_001129507.1; -.
DR   RefSeq; NP_001136026.1; -.
DR   RefSeq; NP_060192.1; -.
DR   UniGene; Hs.515169; -.
DR   IntAct; Q9NXH9; 1.
DR   PhosphoSite; Q9NXH9; -.
DR   PRIDE; Q9NXH9; -.
DR   Ensembl; ENSG00000104907; Homo sapiens.
DR   GeneID; 55621; -.
DR   KEGG; hsa:55621; -.
DR   UCSC; uc002mwj.1; human.
DR   UCSC; uc002mwk.1; human.
DR   GeneCards; GC19M013077; -.
DR   H-InvDB; HIX0014819; -.
DR   HGNC; HGNC:25980; TRMT1.
DR   MIM; 611669; gene.
DR   PharmGKB; PA134867808; -.
DR   HOGENOM; Q9NXH9; -.
DR   HOVERGEN; Q9NXH9; -.
DR   OMA; Q9NXH9; AAMENGT.
DR   BRENDA; 2.1.1.32; 247.
DR   NextBio; 60228; -.
DR   ArrayExpress; Q9NXH9; -.
DR   Bgee; Q9NXH9; -.
DR   CleanEx; HS_TRMT1; -.
DR   GermOnline; ENSG00000104907; Homo sapiens.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR002905; TRM_MeTrfase.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR10631; TRM_mtfrase; 1.
DR   Pfam; PF02005; TRM; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   TIGRFAMs; TIGR00308; TRM1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Metal-binding;
KW   Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing; Zinc; Zinc-finger.
FT   CHAIN         1    659       N(2),N(2)-dimethylguanosine tRNA
FT                                methyltransferase.
FT                                /FTId=PRO_0000147671.
FT   ZN_FING     600    627       C3H1-type.
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     625    625       Phosphoserine.
FT   MOD_RES     628    628       Phosphothreonine.
FT   MOD_RES     646    646       Phosphothreonine.
FT   VAR_SEQ     340    368       Missing (in isoform 2).
FT                                /FTId=VSP_016720.
FT   CONFLICT    500    503       RCWE -> Q (in Ref. 3; AAC33150).
SQ   SEQUENCE   659 AA;  72234 MW;  E4F0F2B740B44387 CRC64;
     MQGSSLWLSL TFRSARVLSR ARFFEWQSPG LPNTAAMENG TGPYGEERPR EVQETTVTEG
     AAKIAFPSAN EVFYNPVQEF NRDLTCAVIT EFARIQLGAK GIQIKVPGEK DTQKVVVDLS
     EQEEEKVELK ESENLASGDQ PRTAAVGEIC EEGLHVLEGL AASGLRSIRF ALEVPGLRSV
     VANDASTRAV DLIRRNVQLN DVAHLVQPSQ ADARMLMYQH QRVSERFDVI DLDPYGSPAT
     FLDAAVQAVS EGGLLCVTCT DMAVLAGNSG ETCYSKYGAM ALKSRACHEM ALRIVLHSLD
     LRANCYQRFV VPLLSISADF YVRVFVRVFT GQAKVKASAS KQALVFQCVG CGAFHLQRLG
     KASGVPSGRA KFSAACGPPV TPECEHCGQR HQLGGPMWAE PIHDLDFVGR VLEAVSANPG
     RFHTSERIRG VLSVITEELP DVPLYYTLDQ LSSTIHCNTP SLLQLRSALL HADFRVSLSH
     ACKNAVKTDA PASALWDIMR CWEKECPVKR ERLSETSPAF RILSVEPRLQ ANFTIREDAN
     PSSRQRGLKR FQANPEANWG PRPRARPGGK AADEAMEERR RLLQNKRKEP PEDVAQRAAR
     LKTFPCKRFK EGTCQRGDQC CYSHSPPTPR VSADAAPDCP ETSNQTPPGP GAAAGPGID
//